---
_id: '12652'
abstract:
- lang: eng
text: We explore the robustness and transferability of parameterizations of cloud
radiative forcing used in glacier melt models at two sites in the Swiss Alps.
We also look at the rationale behind some of the most commonly used approaches,
and explore the relationship between cloud transmittance and several standard
meteorological variables. The 2 m air-temperature diurnal range is the best predictor
of variations in cloud transmittance. However, linear and exponential parameterizations
can only explain 30–50% of the observed variance in computed cloud transmittance
factors. We examine the impact of modelled cloud transmittance factors on both
solar radiation and ablation rates computed with an enhanced temperature-index
model. The melt model performance decreases when modelled radiation is used, the
reduction being due to an underestimation of incoming solar radiation on clear-sky
days. The model works well under overcast conditions. We also seek alternatives
to the use of in situ ground data. However, outputs from an atmospheric model
(2.2 km horizontal resolution) do not seem to provide an alternative to the parameterizations
of cloud radiative forcing based on observations of air temperature at glacier
automatic weather stations. Conversely, the correct definition of overcast conditions
is important.
article_processing_charge: No
article_type: original
author:
- first_name: Francesca
full_name: Pellicciotti, Francesca
id: b28f055a-81ea-11ed-b70c-a9fe7f7b0e70
last_name: Pellicciotti
orcid: 0000-0002-5554-8087
- first_name: Thomas
full_name: Raschle, Thomas
last_name: Raschle
- first_name: Thomas
full_name: Huerlimann, Thomas
last_name: Huerlimann
- first_name: Marco
full_name: Carenzo, Marco
last_name: Carenzo
- first_name: Paolo
full_name: Burlando, Paolo
last_name: Burlando
citation:
ama: 'Pellicciotti F, Raschle T, Huerlimann T, Carenzo M, Burlando P. Transmission
of solar radiation through clouds on melting glaciers: A comparison of parameterizations
and their impact on melt modelling. Journal of Glaciology. 2011;57(202):367-381.
doi:10.3189/002214311796406013'
apa: 'Pellicciotti, F., Raschle, T., Huerlimann, T., Carenzo, M., & Burlando,
P. (2011). Transmission of solar radiation through clouds on melting glaciers:
A comparison of parameterizations and their impact on melt modelling. Journal
of Glaciology. Cambridge University Press. https://doi.org/10.3189/002214311796406013'
chicago: 'Pellicciotti, Francesca, Thomas Raschle, Thomas Huerlimann, Marco Carenzo,
and Paolo Burlando. “Transmission of Solar Radiation through Clouds on Melting
Glaciers: A Comparison of Parameterizations and Their Impact on Melt Modelling.”
Journal of Glaciology. Cambridge University Press, 2011. https://doi.org/10.3189/002214311796406013.'
ieee: 'F. Pellicciotti, T. Raschle, T. Huerlimann, M. Carenzo, and P. Burlando,
“Transmission of solar radiation through clouds on melting glaciers: A comparison
of parameterizations and their impact on melt modelling,” Journal of Glaciology,
vol. 57, no. 202. Cambridge University Press, pp. 367–381, 2011.'
ista: 'Pellicciotti F, Raschle T, Huerlimann T, Carenzo M, Burlando P. 2011. Transmission
of solar radiation through clouds on melting glaciers: A comparison of parameterizations
and their impact on melt modelling. Journal of Glaciology. 57(202), 367–381.'
mla: 'Pellicciotti, Francesca, et al. “Transmission of Solar Radiation through Clouds
on Melting Glaciers: A Comparison of Parameterizations and Their Impact on Melt
Modelling.” Journal of Glaciology, vol. 57, no. 202, Cambridge University
Press, 2011, pp. 367–81, doi:10.3189/002214311796406013.'
short: F. Pellicciotti, T. Raschle, T. Huerlimann, M. Carenzo, P. Burlando, Journal
of Glaciology 57 (2011) 367–381.
date_created: 2023-02-20T08:18:21Z
date_published: 2011-03-01T00:00:00Z
date_updated: 2024-10-14T12:00:58Z
day: '01'
doi: 10.3189/002214311796406013
extern: '1'
intvolume: ' 57'
issue: '202'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.3189/002214311796406013
month: '03'
oa: 1
oa_version: Published Version
page: 367-381
publication: Journal of Glaciology
publication_identifier:
eissn:
- 1727-5652
issn:
- 0022-1430
publication_status: published
publisher: Cambridge University Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: 'Transmission of solar radiation through clouds on melting glaciers: A comparison
of parameterizations and their impact on melt modelling'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 57
year: '2011'
...
---
_id: '1299'
abstract:
- lang: eng
text: Recent experiments have shown that motion detection in Drosophila starts with
splitting the visual input into two parallel channels encoding brightness increments
(ON) or decrements (OFF). This suggests the existence of either two (ON-ON, OFF-OFF)
or four (for all pairwise interactions) separate motion detectors. To decide between
these possibilities, we stimulated flies using sequences of ON and OFF brightness
pulses while recording from motion-sensitive tangential cells. We found direction-selective
responses to sequences of same sign (ON-ON, OFF-OFF), but not of opposite sign
(ON-OFF, OFF-ON), refuting the existence of four separate detectors. Based on
further measurements, we propose a model that reproduces a variety of additional
experimental data sets, including ones that were previously interpreted as support
for four separate detectors. Our experiments and the derived model mark an important
step in guiding further dissection of the fly motion detection circuit.
author:
- first_name: Hubert
full_name: Eichner, Hubert
last_name: Eichner
- first_name: Maximilian A
full_name: Maximilian Jösch
id: 2BD278E6-F248-11E8-B48F-1D18A9856A87
last_name: Jösch
orcid: 0000-0002-3937-1330
- first_name: Bettina
full_name: Schnell, Bettina
last_name: Schnell
- first_name: Dierk
full_name: Reiff, Dierk F
last_name: Reiff
- first_name: Alexander
full_name: Borst, Alexander
last_name: Borst
citation:
ama: Eichner H, Jösch MA, Schnell B, Reiff D, Borst A. Internal structure of the
fly elementary motion detector. Neuron. 2011;70(6):1155-1164. doi:10.1016/j.neuron.2011.03.028
apa: Eichner, H., Jösch, M. A., Schnell, B., Reiff, D., & Borst, A. (2011).
Internal structure of the fly elementary motion detector. Neuron. Elsevier.
https://doi.org/10.1016/j.neuron.2011.03.028
chicago: Eichner, Hubert, Maximilian A Jösch, Bettina Schnell, Dierk Reiff, and
Alexander Borst. “Internal Structure of the Fly Elementary Motion Detector.” Neuron.
Elsevier, 2011. https://doi.org/10.1016/j.neuron.2011.03.028.
ieee: H. Eichner, M. A. Jösch, B. Schnell, D. Reiff, and A. Borst, “Internal structure
of the fly elementary motion detector,” Neuron, vol. 70, no. 6. Elsevier,
pp. 1155–1164, 2011.
ista: Eichner H, Jösch MA, Schnell B, Reiff D, Borst A. 2011. Internal structure
of the fly elementary motion detector. Neuron. 70(6), 1155–1164.
mla: Eichner, Hubert, et al. “Internal Structure of the Fly Elementary Motion Detector.”
Neuron, vol. 70, no. 6, Elsevier, 2011, pp. 1155–64, doi:10.1016/j.neuron.2011.03.028.
short: H. Eichner, M.A. Jösch, B. Schnell, D. Reiff, A. Borst, Neuron 70 (2011)
1155–1164.
date_created: 2018-12-11T11:51:14Z
date_published: 2011-06-23T00:00:00Z
date_updated: 2021-01-12T06:49:43Z
day: '23'
doi: 10.1016/j.neuron.2011.03.028
extern: 1
intvolume: ' 70'
issue: '6'
month: '06'
page: 1155 - 1164
publication: Neuron
publication_status: published
publisher: Elsevier
publist_id: '5969'
quality_controlled: 0
status: public
title: Internal structure of the fly elementary motion detector
type: journal_article
volume: 70
year: '2011'
...
---
_id: '1985'
abstract:
- lang: eng
text: |2-
In Escherichia coli, the pole-to-pole oscillation of the Min proteins directs septum formation to midcell, which is required for symmetric cell division. In vitro, protein waves emerge from the self-organization of MinD, a membrane-binding ATPase, and its activator MinE. For wave propagation, the proteins need to cycle through states of collective membrane binding and unbinding. Although MinD presumably undergoes cooperative membrane attachment, it is unclear how synchronous detachment is coordinated. We used confocal and single-molecule microscopy to elucidate the order of events during Min wave propagation. We propose that protein detachment at the rear of the wave, and the formation of the E-ring, are accomplished by two complementary processes: first, local accumulation of MinE due to rapid rebinding, leading to dynamic instability; and second, a structural change induced by membrane-interaction of MinE in an equimolar MinD-MinE (MinDE) complex, which supports the robustness of pattern formation.
acknowledgement: This work was also supported by the Max Planck Society (M.L., E.F.-F.,
P.S.).
author:
- first_name: Martin
full_name: Martin Loose
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
- first_name: Elisabeth
full_name: Fischer-Friedrich, Elisabeth
last_name: Fischer Friedrich
- first_name: Christoph
full_name: Herold, Christoph
last_name: Herold
- first_name: Karsten
full_name: Kruse, Karsten
last_name: Kruse
- first_name: Petra
full_name: 'Schwille, Petra '
last_name: Schwille
citation:
ama: Loose M, Fischer Friedrich E, Herold C, Kruse K, Schwille P. Min protein patterns
emerge from rapid rebinding and membrane interaction of MinE. Nature Structural
and Molecular Biology. 2011;18(5):577-583. doi:10.1038/nsmb.2037
apa: Loose, M., Fischer Friedrich, E., Herold, C., Kruse, K., & Schwille, P.
(2011). Min protein patterns emerge from rapid rebinding and membrane interaction
of MinE. Nature Structural and Molecular Biology. Nature Publishing Group.
https://doi.org/10.1038/nsmb.2037
chicago: Loose, Martin, Elisabeth Fischer Friedrich, Christoph Herold, Karsten Kruse,
and Petra Schwille. “Min Protein Patterns Emerge from Rapid Rebinding and Membrane
Interaction of MinE.” Nature Structural and Molecular Biology. Nature Publishing
Group, 2011. https://doi.org/10.1038/nsmb.2037.
ieee: M. Loose, E. Fischer Friedrich, C. Herold, K. Kruse, and P. Schwille, “Min
protein patterns emerge from rapid rebinding and membrane interaction of MinE,”
Nature Structural and Molecular Biology, vol. 18, no. 5. Nature Publishing
Group, pp. 577–583, 2011.
ista: Loose M, Fischer Friedrich E, Herold C, Kruse K, Schwille P. 2011. Min protein
patterns emerge from rapid rebinding and membrane interaction of MinE. Nature
Structural and Molecular Biology. 18(5), 577–583.
mla: Loose, Martin, et al. “Min Protein Patterns Emerge from Rapid Rebinding and
Membrane Interaction of MinE.” Nature Structural and Molecular Biology,
vol. 18, no. 5, Nature Publishing Group, 2011, pp. 577–83, doi:10.1038/nsmb.2037.
short: M. Loose, E. Fischer Friedrich, C. Herold, K. Kruse, P. Schwille, Nature
Structural and Molecular Biology 18 (2011) 577–583.
date_created: 2018-12-11T11:55:03Z
date_published: 2011-05-01T00:00:00Z
date_updated: 2021-01-12T06:54:31Z
day: '01'
doi: 10.1038/nsmb.2037
extern: 1
intvolume: ' 18'
issue: '5'
month: '05'
page: 577 - 583
publication: Nature Structural and Molecular Biology
publication_status: published
publisher: Nature Publishing Group
publist_id: '5098'
quality_controlled: 0
status: public
title: Min protein patterns emerge from rapid rebinding and membrane interaction of
MinE
type: journal_article
volume: 18
year: '2011'
...
---
_id: '1986'
abstract:
- lang: eng
text: One of the most fundamental features of biological systems is probably their
ability to self-organize in space and time on different scales. Despite many elaborate
theoretical models of how molecular self-organization can come about, only a few
experimental systems of biological origin have so far been rigorously described,
due mostly to their inherent complexity. The most promising strategy of modern
biophysics is thus to identify minimal biological systems showing self-organized
emergent behavior. One of the best-understood examples of protein self-organization,
which has recently been successfully reconstituted in vitro, is represented by
the oscillations of the Min proteins in Escherichia coli. In this review, we summarize
the current understanding of the mechanism of Min protein self-organization in
vivo and in vitro. We discuss the potential of the Min oscillations to sense the
geometry of the cell and suggest that spontaneous protein waves could be a general
means of intracellular organization. We hypothesize that cooperative membrane
binding and unbinding, e.g., as an energy-dependent switch, may act as an important
regulatory mechanism for protein oscillations and pattern formation in the cell.
author:
- first_name: Martin
full_name: Martin Loose
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
- first_name: Karsten
full_name: Kruse, Karsten
last_name: Kruse
- first_name: Petra
full_name: 'Schwille, Petra '
last_name: Schwille
citation:
ama: 'Loose M, Kruse K, Schwille P. Protein self-organization: Lessons from the
min system. Annual Review of Biophysics. 2011;40(1):315-336. doi:10.1146/annurev-biophys-042910-155332'
apa: 'Loose, M., Kruse, K., & Schwille, P. (2011). Protein self-organization:
Lessons from the min system. Annual Review of Biophysics. Annual Reviews.
https://doi.org/10.1146/annurev-biophys-042910-155332'
chicago: 'Loose, Martin, Karsten Kruse, and Petra Schwille. “Protein Self-Organization:
Lessons from the Min System.” Annual Review of Biophysics. Annual Reviews,
2011. https://doi.org/10.1146/annurev-biophys-042910-155332.'
ieee: 'M. Loose, K. Kruse, and P. Schwille, “Protein self-organization: Lessons
from the min system,” Annual Review of Biophysics, vol. 40, no. 1. Annual
Reviews, pp. 315–336, 2011.'
ista: 'Loose M, Kruse K, Schwille P. 2011. Protein self-organization: Lessons from
the min system. Annual Review of Biophysics. 40(1), 315–336.'
mla: 'Loose, Martin, et al. “Protein Self-Organization: Lessons from the Min System.”
Annual Review of Biophysics, vol. 40, no. 1, Annual Reviews, 2011, pp.
315–36, doi:10.1146/annurev-biophys-042910-155332.'
short: M. Loose, K. Kruse, P. Schwille, Annual Review of Biophysics 40 (2011) 315–336.
date_created: 2018-12-11T11:55:04Z
date_published: 2011-06-09T00:00:00Z
date_updated: 2021-01-12T06:54:31Z
day: '09'
doi: 10.1146/annurev-biophys-042910-155332
extern: 1
intvolume: ' 40'
issue: '1'
month: '06'
page: 315 - 336
publication: Annual Review of Biophysics
publication_status: published
publisher: Annual Reviews
publist_id: '5097'
quality_controlled: 0
status: public
title: 'Protein self-organization: Lessons from the min system'
type: journal_article
volume: 40
year: '2011'
...
---
_id: '2072'
abstract:
- lang: eng
text: Many species have morphologically and genetically differentiated sex chromosomes,
such as the XY pair of mammals. Y chromosomes are often highly degenerated and
carry few functional genes, so that XY males have only one copy of most Xlinked
genes (whereas females have two). As a result, chromosome-wide mechanisms of dosage
compensation, such as the mammalian X-inactivation, often evolve to reestablish
expression balance. A similar phenomenon is expected in femaleheterogametic species,
where ZW females should suffer from imbalances due to W-chromosome degeneration.
However, no global dosage compensation mechanisms have been detected in the two
independent ZW systems that have been studied systematically (birds and silkworm),
leading to the suggestion that lack of global dosage compensation may be a general
feature of female-heterogametic species. However, analyses of other independently
evolved ZW systems are required to test if this is the case. In this study, we
use published genomic and expression data to test for the presence of global dosage
compensation in Schistosoma mansoni, a trematode parasite that causes schistosomiasis
in humans. We find that Z-linked expression is reduced relative to autosomal expression
in females but not males, consistent with incomplete or localized dosage compensation.
This gives further support to the theory that female-heterogametic species may
not require global mechanisms of dosage compensation.
author:
- first_name: Beatriz
full_name: Vicoso, Beatriz
id: 49E1C5C6-F248-11E8-B48F-1D18A9856A87
last_name: Vicoso
orcid: 0000-0002-4579-8306
- first_name: Doris
full_name: Bachtrog, Doris
last_name: Bachtrog
citation:
ama: Vicoso B, Bachtrog D. Lack of global dosage compensation in Schistosoma mansoni,
a female-heterogametic parasite. Genome Biology and Evolution. 2011;3(1):230-235.
doi:10.1093/gbe/evr010
apa: Vicoso, B., & Bachtrog, D. (2011). Lack of global dosage compensation in
Schistosoma mansoni, a female-heterogametic parasite. Genome Biology and Evolution.
Oxford University Press. https://doi.org/10.1093/gbe/evr010
chicago: Vicoso, Beatriz, and Doris Bachtrog. “Lack of Global Dosage Compensation
in Schistosoma Mansoni, a Female-Heterogametic Parasite.” Genome Biology and
Evolution. Oxford University Press, 2011. https://doi.org/10.1093/gbe/evr010.
ieee: B. Vicoso and D. Bachtrog, “Lack of global dosage compensation in Schistosoma
mansoni, a female-heterogametic parasite,” Genome Biology and Evolution,
vol. 3, no. 1. Oxford University Press, pp. 230–235, 2011.
ista: Vicoso B, Bachtrog D. 2011. Lack of global dosage compensation in Schistosoma
mansoni, a female-heterogametic parasite. Genome Biology and Evolution. 3(1),
230–235.
mla: Vicoso, Beatriz, and Doris Bachtrog. “Lack of Global Dosage Compensation in
Schistosoma Mansoni, a Female-Heterogametic Parasite.” Genome Biology and Evolution,
vol. 3, no. 1, Oxford University Press, 2011, pp. 230–35, doi:10.1093/gbe/evr010.
short: B. Vicoso, D. Bachtrog, Genome Biology and Evolution 3 (2011) 230–235.
date_created: 2018-12-11T11:55:33Z
date_published: 2011-02-11T00:00:00Z
date_updated: 2021-01-12T06:55:08Z
day: '11'
ddc:
- '570'
doi: 10.1093/gbe/evr010
extern: '1'
file:
- access_level: open_access
checksum: 7855c134436e4f6a13d63b6606d7e8dd
content_type: application/pdf
creator: dernst
date_created: 2019-05-10T07:41:28Z
date_updated: 2020-07-14T12:45:27Z
file_id: '6395'
file_name: 2011_GBE_Vicoso.pdf
file_size: 212547
relation: main_file
file_date_updated: 2020-07-14T12:45:27Z
has_accepted_license: '1'
intvolume: ' 3'
issue: '1'
language:
- iso: eng
license: https://creativecommons.org/licenses/by-nc/4.0/
month: '02'
oa: 1
oa_version: Published Version
page: 230 - 235
publication: Genome Biology and Evolution
publication_status: published
publisher: Oxford University Press
publist_id: '4966'
quality_controlled: '1'
status: public
title: Lack of global dosage compensation in Schistosoma mansoni, a female-heterogametic
parasite
tmp:
image: /images/cc_by_nc.png
legal_code_url: https://creativecommons.org/licenses/by-nc/4.0/legalcode
name: Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)
short: CC BY-NC (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 3
year: '2011'
...
---
_id: '1973'
abstract:
- lang: eng
text: Complex I is the first and largest enzyme of the respiratory chain, coupling
electron transfer between NADH and ubiquinone to the translocation of four protons
across the membrane. It has a central role in cellular energy production and has
been implicated in many human neurodegenerative diseases. The L-shaped enzyme
consists of hydrophilic and membrane domains. Previously, we determined the structure
of the hydrophilic domain. Here we report the crystal structure of the Esherichia
coli complex I membrane domain at 3.0 Ã. resolution. It includes six subunits,
NuoL, NuoM, NuoN, NuoA, NuoJ and NuoK, with 55 transmembrane helices. The fold
of the homologous antiporter-like subunits L, M and N is novel, with two inverted
structural repeats of five transmembrane helices arranged, unusually, face-to-back.
Each repeat includes a discontinuous transmembrane helix and forms half of a channel
across the membrane. A network of conserved polar residues connects the two half-channels,
completing the proton translocation pathway. Unexpectedly, lysines rather than
carboxylate residues act as the main elements of the proton pump in these subunits.
The fourth probable proton-translocation channel is at the interface of subunits
N, K, J and A. The structure indicates that proton translocation in complex I,
uniquely, involves coordinated conformational changes in six symmetrical structural
elements.
acknowledgement: This work was funded by the Medical Research Council.
author:
- first_name: Rouslan
full_name: Efremov, Rouslan G
last_name: Efremov
- first_name: Leonid A
full_name: Leonid Sazanov
id: 338D39FE-F248-11E8-B48F-1D18A9856A87
last_name: Sazanov
orcid: 0000-0002-0977-7989
citation:
ama: Efremov R, Sazanov LA. Structure of the membrane domain of respiratory complex
i. Nature. 2011;476(7361):414-421. doi:10.1038/nature10330
apa: Efremov, R., & Sazanov, L. A. (2011). Structure of the membrane domain
of respiratory complex i. Nature. Nature Publishing Group. https://doi.org/10.1038/nature10330
chicago: Efremov, Rouslan, and Leonid A Sazanov. “Structure of the Membrane Domain
of Respiratory Complex I.” Nature. Nature Publishing Group, 2011. https://doi.org/10.1038/nature10330.
ieee: R. Efremov and L. A. Sazanov, “Structure of the membrane domain of respiratory
complex i,” Nature, vol. 476, no. 7361. Nature Publishing Group, pp. 414–421,
2011.
ista: Efremov R, Sazanov LA. 2011. Structure of the membrane domain of respiratory
complex i. Nature. 476(7361), 414–421.
mla: Efremov, Rouslan, and Leonid A. Sazanov. “Structure of the Membrane Domain
of Respiratory Complex I.” Nature, vol. 476, no. 7361, Nature Publishing
Group, 2011, pp. 414–21, doi:10.1038/nature10330.
short: R. Efremov, L.A. Sazanov, Nature 476 (2011) 414–421.
date_created: 2018-12-11T11:54:59Z
date_published: 2011-08-25T00:00:00Z
date_updated: 2021-01-12T06:54:26Z
day: '25'
doi: 10.1038/nature10330
extern: 1
intvolume: ' 476'
issue: '7361'
month: '08'
page: 414 - 421
publication: Nature
publication_status: published
publisher: Nature Publishing Group
publist_id: '5110'
quality_controlled: 0
status: public
title: Structure of the membrane domain of respiratory complex i
type: journal_article
volume: 476
year: '2011'
...
---
_id: '1974'
abstract:
- lang: eng
text: Complex I is the first enzyme of the respiratory chain and plays a central
role in cellular energy production. It has been implicated in many human neurodegenerative
diseases, as well as in ageing. One of the biggest membrane protein complexes,
it is an L-shaped assembly consisting of hydrophilic and membrane domains. Previously,
we have determined structures of the hydrophilic domain in several redox states.
Last year was marked by fascinating breakthroughs in the understanding of the
complete structure. We described the architecture of the membrane domain and of
the entire bacterial complex I. X-ray analysis of the larger mitochondrial enzyme
has also been published. The core subunits of the bacterial and mitochondrial
enzymes have remarkably similar structures. The proposed mechanism of coupling
between electron transfer and proton translocation involves long-range conformational
changes, coordinated in part by a long α-helix, akin to the coupling rod of a
steam engine.
acknowledgement: The work in authors’ laboratory was funded by the Medical Research
Council.
author:
- first_name: Rouslan
full_name: Efremov, Rouslan G
last_name: Efremov
- first_name: Leonid A
full_name: Leonid Sazanov
id: 338D39FE-F248-11E8-B48F-1D18A9856A87
last_name: Sazanov
orcid: 0000-0002-0977-7989
citation:
ama: 'Efremov R, Sazanov LA. Respiratory complex I: “steam engine” of the cell?
Current Opinion in Structural Biology. 2011;21(4):532-540. doi:10.1016/j.sbi.2011.07.002'
apa: 'Efremov, R., & Sazanov, L. A. (2011). Respiratory complex I: “steam engine”
of the cell? Current Opinion in Structural Biology. Elsevier. https://doi.org/10.1016/j.sbi.2011.07.002'
chicago: 'Efremov, Rouslan, and Leonid A Sazanov. “Respiratory Complex I: ‘steam
Engine’ of the Cell?” Current Opinion in Structural Biology. Elsevier,
2011. https://doi.org/10.1016/j.sbi.2011.07.002.'
ieee: 'R. Efremov and L. A. Sazanov, “Respiratory complex I: ‘steam engine’ of the
cell?,” Current Opinion in Structural Biology, vol. 21, no. 4. Elsevier,
pp. 532–540, 2011.'
ista: 'Efremov R, Sazanov LA. 2011. Respiratory complex I: ‘steam engine’ of the
cell? Current Opinion in Structural Biology. 21(4), 532–540.'
mla: 'Efremov, Rouslan, and Leonid A. Sazanov. “Respiratory Complex I: ‘steam Engine’
of the Cell?” Current Opinion in Structural Biology, vol. 21, no. 4, Elsevier,
2011, pp. 532–40, doi:10.1016/j.sbi.2011.07.002.'
short: R. Efremov, L.A. Sazanov, Current Opinion in Structural Biology 21 (2011)
532–540.
date_created: 2018-12-11T11:54:59Z
date_published: 2011-08-01T00:00:00Z
date_updated: 2021-01-12T06:54:27Z
day: '01'
doi: 10.1016/j.sbi.2011.07.002
extern: 1
intvolume: ' 21'
issue: '4'
month: '08'
page: 532 - 540
publication: Current Opinion in Structural Biology
publication_status: published
publisher: Elsevier
publist_id: '5111'
quality_controlled: 0
status: public
title: 'Respiratory complex I: ''steam engine'' of the cell?'
type: journal_article
volume: 21
year: '2011'
...
---
_id: '1975'
abstract:
- lang: eng
text: 'Modern α-proteobacteria are thought to be closely related to the ancient
symbiont of eukaryotes, an ancestor of mitochondria. Respiratory complex I from
α-proteobacteria and mitochondria is well conserved at the level of the 14 "core"
subunits, consistent with that notion. Mitochondrial complex I contains the core
subunits, present in all species, and up to 31 "supernumerary" subunits,
generally thought to have originated only within eukaryotic lineages. However,
the full protein composition of an α-proteobacterial complex I has not been established
previously. Here, we report the first purification and characterization of complex
I from the α-proteobacterium Paracoccus denitrificans. Single particle electron
microscopy shows that the complex has a well defined L-shape. Unexpectedly, in
addition to the 14 core subunits, the enzyme also contains homologues of three
supernumerary mitochondrial subunits as follows: B17.2, AQDQ/18, and 13 kDa (bovine
nomenclature). This finding suggests that evolution of complex I via addition
of supernumerary or "accessory" subunits started before the original
endosymbiotic event that led to the creation of the eukaryotic cell. It also provides
further confirmation that α-proteobacteria are the closest extant relatives of
mitochondria.'
acknowledgement: 'This work was supported by the Medical Research Council. '
author:
- first_name: Chui
full_name: Yip, Chui Y
last_name: Yip
- first_name: Michael
full_name: Harbour, Michael E
last_name: Harbour
- first_name: Kamburapola
full_name: Jayawardena, Kamburapola G
last_name: Jayawardena
- first_name: Ian
full_name: Fearnley, Ian M
last_name: Fearnley
- first_name: Leonid A
full_name: Leonid Sazanov
id: 338D39FE-F248-11E8-B48F-1D18A9856A87
last_name: Sazanov
orcid: 0000-0002-0977-7989
citation:
ama: Yip C, Harbour M, Jayawardena K, Fearnley I, Sazanov LA. Evolution of respiratory
complex I "Supernumerary" subunits are present in the α-proteobacterial
enzyme. Journal of Biological Chemistry. 2011;286(7):5023-5033. doi:10.1074/jbc.M110.194993
apa: Yip, C., Harbour, M., Jayawardena, K., Fearnley, I., & Sazanov, L. A. (2011).
Evolution of respiratory complex I "Supernumerary" subunits
are present in the α-proteobacterial enzyme. Journal of Biological Chemistry.
American Society for Biochemistry and Molecular Biology. https://doi.org/10.1074/jbc.M110.194993
chicago: Yip, Chui, Michael Harbour, Kamburapola Jayawardena, Ian Fearnley, and
Leonid A Sazanov. “Evolution of Respiratory Complex I "Supernumerary"
Subunits Are Present in the α-Proteobacterial Enzyme.” Journal of Biological
Chemistry. American Society for Biochemistry and Molecular Biology, 2011.
https://doi.org/10.1074/jbc.M110.194993.
ieee: C. Yip, M. Harbour, K. Jayawardena, I. Fearnley, and L. A. Sazanov, “Evolution
of respiratory complex I "Supernumerary" subunits are present
in the α-proteobacterial enzyme,” Journal of Biological Chemistry, vol.
286, no. 7. American Society for Biochemistry and Molecular Biology, pp. 5023–5033,
2011.
ista: Yip C, Harbour M, Jayawardena K, Fearnley I, Sazanov LA. 2011. Evolution of
respiratory complex I "Supernumerary" subunits are present in
the α-proteobacterial enzyme. Journal of Biological Chemistry. 286(7), 5023–5033.
mla: Yip, Chui, et al. “Evolution of Respiratory Complex I "Supernumerary"
Subunits Are Present in the α-Proteobacterial Enzyme.” Journal of Biological
Chemistry, vol. 286, no. 7, American Society for Biochemistry and Molecular
Biology, 2011, pp. 5023–33, doi:10.1074/jbc.M110.194993.
short: C. Yip, M. Harbour, K. Jayawardena, I. Fearnley, L.A. Sazanov, Journal of
Biological Chemistry 286 (2011) 5023–5033.
date_created: 2018-12-11T11:55:00Z
date_published: 2011-02-18T00:00:00Z
date_updated: 2021-01-12T06:54:27Z
day: '18'
doi: 10.1074/jbc.M110.194993
extern: 1
intvolume: ' 286'
issue: '7'
month: '02'
page: 5023 - 5033
publication: Journal of Biological Chemistry
publication_status: published
publisher: American Society for Biochemistry and Molecular Biology
publist_id: '5112'
quality_controlled: 0
status: public
title: Evolution of respiratory complex I "Supernumerary" subunits are present
in the α-proteobacterial enzyme
type: journal_article
volume: 286
year: '2011'
...
---
_id: '10907'
abstract:
- lang: eng
text: This paper presents a method to create a model of an articulated object using
the planar motion in an initialization video. The model consists of rigid parts
connected by points of articulation. The rigid parts are described by the positions
of salient feature-points tracked throughout the video. Following a filtering
step that identifies points that belong to different objects, rigid parts are
found by a grouping process in a graph pyramid. Valid articulation points are
selected by verifying multiple hypotheses for each pair of parts.
acknowledgement: This work has been partially supported by the Austrian Science Fund
under grants S9103-N13 and P18716-N13.
alternative_title:
- LNCS
article_processing_charge: No
author:
- first_name: Nicole M.
full_name: Artner, Nicole M.
last_name: Artner
- first_name: Adrian
full_name: Ion, Adrian
id: 29F89302-F248-11E8-B48F-1D18A9856A87
last_name: Ion
- first_name: Walter G.
full_name: Kropatsch, Walter G.
last_name: Kropatsch
citation:
ama: 'Artner NM, Ion A, Kropatsch WG. Spatio-temporal extraction of articulated
models in a graph pyramid. In: Jiang X, Ferrer M, Torsello A, eds. Graph-Based
Representations in Pattern Recognition. Vol 6658. LNIP. Berlin, Heidelberg:
Springer; 2011:215-224. doi:10.1007/978-3-642-20844-7_22'
apa: 'Artner, N. M., Ion, A., & Kropatsch, W. G. (2011). Spatio-temporal extraction
of articulated models in a graph pyramid. In X. Jiang, M. Ferrer, & A. Torsello
(Eds.), Graph-Based Representations in Pattern Recognition (Vol. 6658,
pp. 215–224). Berlin, Heidelberg: Springer. https://doi.org/10.1007/978-3-642-20844-7_22'
chicago: 'Artner, Nicole M., Adrian Ion, and Walter G. Kropatsch. “Spatio-Temporal
Extraction of Articulated Models in a Graph Pyramid.” In Graph-Based Representations
in Pattern Recognition, edited by Xiaoyi Jiang, Miquel Ferrer, and Andrea
Torsello, 6658:215–24. LNIP. Berlin, Heidelberg: Springer, 2011. https://doi.org/10.1007/978-3-642-20844-7_22.'
ieee: N. M. Artner, A. Ion, and W. G. Kropatsch, “Spatio-temporal extraction of
articulated models in a graph pyramid,” in Graph-Based Representations in Pattern
Recognition, Münster, Germany, 2011, vol. 6658, pp. 215–224.
ista: 'Artner NM, Ion A, Kropatsch WG. 2011. Spatio-temporal extraction of articulated
models in a graph pyramid. Graph-Based Representations in Pattern Recognition.
GbRPR: Graph-based Representations in Pattern RecognitionLNIP, LNCS, vol. 6658,
215–224.'
mla: Artner, Nicole M., et al. “Spatio-Temporal Extraction of Articulated Models
in a Graph Pyramid.” Graph-Based Representations in Pattern Recognition,
edited by Xiaoyi Jiang et al., vol. 6658, Springer, 2011, pp. 215–24, doi:10.1007/978-3-642-20844-7_22.
short: N.M. Artner, A. Ion, W.G. Kropatsch, in:, X. Jiang, M. Ferrer, A. Torsello
(Eds.), Graph-Based Representations in Pattern Recognition, Springer, Berlin,
Heidelberg, 2011, pp. 215–224.
conference:
end_date: 2011-05-20
location: Münster, Germany
name: 'GbRPR: Graph-based Representations in Pattern Recognition'
start_date: 2011-05-18
corr_author: '1'
date_created: 2022-03-21T08:08:35Z
date_published: 2011-06-01T00:00:00Z
date_updated: 2024-10-09T21:02:32Z
day: '01'
department:
- _id: HeEd
doi: 10.1007/978-3-642-20844-7_22
editor:
- first_name: Xiaoyi
full_name: Jiang, Xiaoyi
last_name: Jiang
- first_name: Miquel
full_name: Ferrer, Miquel
last_name: Ferrer
- first_name: Andrea
full_name: Torsello, Andrea
last_name: Torsello
intvolume: ' 6658'
language:
- iso: eng
month: '06'
oa_version: None
page: 215-224
place: Berlin, Heidelberg
publication: Graph-Based Representations in Pattern Recognition
publication_identifier:
eisbn:
- '9783642208447'
eissn:
- 1611-3349
isbn:
- '9783642208430'
issn:
- 0302-9743
publication_status: published
publisher: Springer
quality_controlled: '1'
scopus_import: '1'
series_title: LNIP
status: public
title: Spatio-temporal extraction of articulated models in a graph pyramid
type: conference
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
volume: 6658
year: '2011'
...
---
_id: '11094'
abstract:
- lang: eng
text: Nuclear pore complexes (NPCs) assemble at the end of mitosis during nuclear
envelope (NE) reformation and into an intact NE as cells progress through interphase.
Although recent studies have shown that NPC formation occurs by two different
molecular mechanisms at two distinct cell cycle stages, little is known about
the molecular players that mediate the fusion of the outer and inner nuclear membranes
to form pores. In this paper, we provide evidence that the transmembrane nucleoporin
(Nup), POM121, but not the Nup107–160 complex, is present at new pore assembly
sites at a time that coincides with inner nuclear membrane (INM) and outer nuclear
membrane (ONM) fusion. Overexpression of POM121 resulted in juxtaposition of the
INM and ONM. Additionally, Sun1, an INM protein that is known to interact with
the cytoskeleton, was specifically required for interphase assembly and localized
with POM121 at forming pores. We propose a model in which POM121 and Sun1 interact
transiently to promote early steps of interphase NPC assembly.
article_processing_charge: No
article_type: original
author:
- first_name: Jessica A.
full_name: Talamas, Jessica A.
last_name: Talamas
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: Talamas JA, Hetzer M. POM121 and Sun1 play a role in early steps of interphase
NPC assembly. Journal of Cell Biology. 2011;194(1):27-37. doi:10.1083/jcb.201012154
apa: Talamas, J. A., & Hetzer, M. (2011). POM121 and Sun1 play a role in early
steps of interphase NPC assembly. Journal of Cell Biology. Rockefeller
University Press. https://doi.org/10.1083/jcb.201012154
chicago: Talamas, Jessica A., and Martin Hetzer. “POM121 and Sun1 Play a Role in
Early Steps of Interphase NPC Assembly.” Journal of Cell Biology. Rockefeller
University Press, 2011. https://doi.org/10.1083/jcb.201012154.
ieee: J. A. Talamas and M. Hetzer, “POM121 and Sun1 play a role in early steps of
interphase NPC assembly,” Journal of Cell Biology, vol. 194, no. 1. Rockefeller
University Press, pp. 27–37, 2011.
ista: Talamas JA, Hetzer M. 2011. POM121 and Sun1 play a role in early steps of
interphase NPC assembly. Journal of Cell Biology. 194(1), 27–37.
mla: Talamas, Jessica A., and Martin Hetzer. “POM121 and Sun1 Play a Role in Early
Steps of Interphase NPC Assembly.” Journal of Cell Biology, vol. 194, no.
1, Rockefeller University Press, 2011, pp. 27–37, doi:10.1083/jcb.201012154.
short: J.A. Talamas, M. Hetzer, Journal of Cell Biology 194 (2011) 27–37.
date_created: 2022-04-07T07:52:18Z
date_published: 2011-07-04T00:00:00Z
date_updated: 2024-10-14T11:26:10Z
day: '04'
doi: 10.1083/jcb.201012154
extern: '1'
external_id:
pmid:
- '21727197'
intvolume: ' 194'
issue: '1'
keyword:
- Cell Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1083/jcb.201012154
month: '07'
oa: 1
oa_version: Published Version
page: 27-37
pmid: 1
publication: Journal of Cell Biology
publication_identifier:
eissn:
- 1540-8140
issn:
- 0021-9525
publication_status: published
publisher: Rockefeller University Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: POM121 and Sun1 play a role in early steps of interphase NPC assembly
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 194
year: '2011'
...
---
_id: '11095'
article_processing_charge: No
article_type: letter_note
author:
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
- first_name: Giacomo
full_name: Cavalli, Giacomo
last_name: Cavalli
citation:
ama: Hetzer M, Cavalli G. Editorial overview. Current Opinion in Cell Biology.
2011;23(3):255-257. doi:10.1016/j.ceb.2011.04.013
apa: Hetzer, M., & Cavalli, G. (2011). Editorial overview. Current Opinion
in Cell Biology. Elsevier. https://doi.org/10.1016/j.ceb.2011.04.013
chicago: Hetzer, Martin, and Giacomo Cavalli. “Editorial Overview.” Current Opinion
in Cell Biology. Elsevier, 2011. https://doi.org/10.1016/j.ceb.2011.04.013.
ieee: M. Hetzer and G. Cavalli, “Editorial overview,” Current Opinion in Cell
Biology, vol. 23, no. 3. Elsevier, pp. 255–257, 2011.
ista: Hetzer M, Cavalli G. 2011. Editorial overview. Current Opinion in Cell Biology.
23(3), 255–257.
mla: Hetzer, Martin, and Giacomo Cavalli. “Editorial Overview.” Current Opinion
in Cell Biology, vol. 23, no. 3, Elsevier, 2011, pp. 255–57, doi:10.1016/j.ceb.2011.04.013.
short: M. Hetzer, G. Cavalli, Current Opinion in Cell Biology 23 (2011) 255–257.
date_created: 2022-04-07T07:52:27Z
date_published: 2011-06-01T00:00:00Z
date_updated: 2024-10-14T11:26:20Z
day: '01'
doi: 10.1016/j.ceb.2011.04.013
extern: '1'
external_id:
pmid:
- '21592757'
intvolume: ' 23'
issue: '3'
keyword:
- Cell Biology
language:
- iso: eng
month: '06'
oa_version: None
page: 255-257
pmid: 1
publication: Current Opinion in Cell Biology
publication_identifier:
issn:
- 0955-0674
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Editorial overview
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 23
year: '2011'
...
---
_id: '11096'
abstract:
- lang: eng
text: As the gatekeepers of the eukaryotic cell nucleus, nuclear pore complexes
(NPCs) mediate all molecular trafficking between the nucleoplasm and the cytoplasm.
In recent years, transport-independent functions of NPC components, nucleoporins,
have been identified including roles in chromatin organization and gene regulation.
Here, we summarize our current view of the NPC as a dynamic hub for the integration
of chromatin regulation and nuclear trafficking and discuss the functional interplay
between nucleoporins and the nuclear genome.
article_processing_charge: No
article_type: original
author:
- first_name: Yun
full_name: Liang, Yun
last_name: Liang
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: Liang Y, Hetzer M. Functional interactions between nucleoporins and chromatin.
Current Opinion in Cell Biology. 2011;23(1):65-70. doi:10.1016/j.ceb.2010.09.008
apa: Liang, Y., & Hetzer, M. (2011). Functional interactions between nucleoporins
and chromatin. Current Opinion in Cell Biology. Elsevier. https://doi.org/10.1016/j.ceb.2010.09.008
chicago: Liang, Yun, and Martin Hetzer. “Functional Interactions between Nucleoporins
and Chromatin.” Current Opinion in Cell Biology. Elsevier, 2011. https://doi.org/10.1016/j.ceb.2010.09.008.
ieee: Y. Liang and M. Hetzer, “Functional interactions between nucleoporins and
chromatin,” Current Opinion in Cell Biology, vol. 23, no. 1. Elsevier,
pp. 65–70, 2011.
ista: Liang Y, Hetzer M. 2011. Functional interactions between nucleoporins and
chromatin. Current Opinion in Cell Biology. 23(1), 65–70.
mla: Liang, Yun, and Martin Hetzer. “Functional Interactions between Nucleoporins
and Chromatin.” Current Opinion in Cell Biology, vol. 23, no. 1, Elsevier,
2011, pp. 65–70, doi:10.1016/j.ceb.2010.09.008.
short: Y. Liang, M. Hetzer, Current Opinion in Cell Biology 23 (2011) 65–70.
date_created: 2022-04-07T07:52:37Z
date_published: 2011-02-01T00:00:00Z
date_updated: 2024-10-14T11:26:31Z
day: '01'
doi: 10.1016/j.ceb.2010.09.008
extern: '1'
external_id:
pmid:
- '21030234'
intvolume: ' 23'
issue: '1'
keyword:
- Cell Biology
language:
- iso: eng
month: '02'
oa_version: None
page: 65-70
pmid: 1
publication: Current Opinion in Cell Biology
publication_identifier:
issn:
- 0955-0674
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Functional interactions between nucleoporins and chromatin
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 23
year: '2011'
...
---
_id: '11100'
abstract:
- lang: eng
text: Eukaryotic cell function depends on the physical separation of nucleoplasmic
and cytoplasmic components by the nuclear envelope (NE). Molecular communication
between the two compartments involves active, signal-mediated trafficking, a function
that is exclusively performed by nuclear pore complexes (NPCs). The individual
NPC components and the mechanisms that are involved in nuclear trafficking are
well documented and have become textbook knowledge. However, in addition to their
roles as nuclear gatekeepers, NPC components-nucleoporins-have been shown to have
critical roles in chromatin organization and gene regulation. These findings have
sparked new enthusiasm to study the roles of this multiprotein complex in nuclear
organization and explore novel functions that in some cases appear to go beyond
a role in transport. Here, we discuss our present view of NPC biogenesis, which
is tightly linked to proper cell cycle progression and cell differentiation. In
addition, we summarize new data suggesting that NPCs represent dynamic hubs for
the integration of gene regulation and nuclear transport processes.
article_processing_charge: No
article_type: original
author:
- first_name: M.
full_name: Capelson, M.
last_name: Capelson
- first_name: C.
full_name: Doucet, C.
last_name: Doucet
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: 'Capelson M, Doucet C, Hetzer M. Nuclear pore complexes: Guardians of the nuclear
genome. Cold Spring Harbor Symposia on Quantitative Biology. 2011;75:585-597.
doi:10.1101/sqb.2010.75.059'
apa: 'Capelson, M., Doucet, C., & Hetzer, M. (2011). Nuclear pore complexes:
Guardians of the nuclear genome. Cold Spring Harbor Symposia on Quantitative
Biology. Cold Spring Harbor Laboratory Press. https://doi.org/10.1101/sqb.2010.75.059'
chicago: 'Capelson, M., C. Doucet, and Martin Hetzer. “Nuclear Pore Complexes: Guardians
of the Nuclear Genome.” Cold Spring Harbor Symposia on Quantitative Biology.
Cold Spring Harbor Laboratory Press, 2011. https://doi.org/10.1101/sqb.2010.75.059.'
ieee: 'M. Capelson, C. Doucet, and M. Hetzer, “Nuclear pore complexes: Guardians
of the nuclear genome,” Cold Spring Harbor Symposia on Quantitative Biology,
vol. 75. Cold Spring Harbor Laboratory Press, pp. 585–597, 2011.'
ista: 'Capelson M, Doucet C, Hetzer M. 2011. Nuclear pore complexes: Guardians of
the nuclear genome. Cold Spring Harbor Symposia on Quantitative Biology. 75, 585–597.'
mla: 'Capelson, M., et al. “Nuclear Pore Complexes: Guardians of the Nuclear Genome.”
Cold Spring Harbor Symposia on Quantitative Biology, vol. 75, Cold Spring
Harbor Laboratory Press, 2011, pp. 585–97, doi:10.1101/sqb.2010.75.059.'
short: M. Capelson, C. Doucet, M. Hetzer, Cold Spring Harbor Symposia on Quantitative
Biology 75 (2011) 585–597.
date_created: 2022-04-07T07:53:18Z
date_published: 2011-04-18T00:00:00Z
date_updated: 2024-10-14T11:27:48Z
day: '18'
doi: 10.1101/sqb.2010.75.059
extern: '1'
external_id:
pmid:
- '21502404'
intvolume: ' 75'
keyword:
- Genetics
- Molecular Biology
- Biochemistry
language:
- iso: eng
month: '04'
oa_version: None
page: 585-597
pmid: 1
publication: Cold Spring Harbor Symposia on Quantitative Biology
publication_identifier:
isbn:
- '9781936113071'
issn:
- 0091-7451
- 1943-4456
publication_status: published
publisher: Cold Spring Harbor Laboratory Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: 'Nuclear pore complexes: Guardians of the nuclear genome'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 75
year: '2011'
...
---
_id: '112'
abstract:
- lang: eng
text: Particle beams are important tools for probing atomic and molecular interactions.
Here we demonstrate that particle beams also offer a unique opportunity to investigate
interactions in macroscopic systems, such as granular media. Motivated by recent
experiments on streams of grains that exhibit liquid-like breakup into droplets,
we use molecular dynamics simulations to investigate the evolution of a dense
stream of macroscopic spheres accelerating out of an opening at the bottom of
a reservoir. We show how nanoscale details associated with energy dissipation
during collisions modify the stream\'s macroscopic behavior. We find that inelastic
collisions collimate the stream, while the presence of short-range attractive
interactions drives structure formation. Parameterizing the collision dynamics
by the coefficient of restitution (i.e., the ratio of relative velocities before
and after impact) and the strength of the cohesive interaction, we map out a spectrum
of behaviors that ranges from gaslike jets in which all grains drift apart to
liquid-like streams that break into large droplets containing hundreds of grains.
We also find a new, intermediate regime in which small aggregates form by capture
from the gas phase, similar to what can be observed in molecular beams. Our results
show that nearly all aspects of stream behavior are closely related to the velocity
gradient associated with vertical free fall. Led by this observation, we propose
a simple energy balance model to explain the droplet formation process. The qualitative
as well as many quantitative features of the simulations and the model compare
well with available experimental data and provide a first quantitative measure
of the role of attractions in freely cooling granular streams.
acknowledgement: This work was supported by the NSF through CBET-0933242. We acknowledge
use of shared facilities provided by the Keck Facility for Ultrafast Imaging at
the University of Chicago and by the Chicago MRSEC through NSF DMR-0820054. Software
support by Itasca Consulting Group, Inc., under the Itasca Educational Partnership
is gratefully acknowledged. H.G. thanks the German-American Fulbright Commission
for fellowship support during his stay at the University of Chicago.
article_number: '051302'
arxiv: 1
author:
- first_name: Scott R
full_name: Waitukaitis, Scott R
id: 3A1FFC16-F248-11E8-B48F-1D18A9856A87
last_name: Waitukaitis
orcid: 0000-0002-2299-3176
- first_name: Helge
full_name: Grütjen, Helge
last_name: Grütjen
- first_name: John
full_name: Royer, John
last_name: Royer
- first_name: Heinrich
full_name: Jaeger, Heinrich
last_name: Jaeger
citation:
ama: Waitukaitis SR, Grütjen H, Royer J, Jaeger H. Droplet and cluster formation
in freely falling granular streams. Physical Review E. 2011;83(5). doi:10.1103/PhysRevE.83.051302
apa: Waitukaitis, S. R., Grütjen, H., Royer, J., & Jaeger, H. (2011). Droplet
and cluster formation in freely falling granular streams. Physical Review E.
American Physical Society. https://doi.org/10.1103/PhysRevE.83.051302
chicago: Waitukaitis, Scott R, Helge Grütjen, John Royer, and Heinrich Jaeger. “Droplet
and Cluster Formation in Freely Falling Granular Streams.” Physical Review
E. American Physical Society, 2011. https://doi.org/10.1103/PhysRevE.83.051302.
ieee: S. R. Waitukaitis, H. Grütjen, J. Royer, and H. Jaeger, “Droplet and cluster
formation in freely falling granular streams,” Physical Review E, vol.
83, no. 5. American Physical Society, 2011.
ista: Waitukaitis SR, Grütjen H, Royer J, Jaeger H. 2011. Droplet and cluster formation
in freely falling granular streams. Physical Review E. 83(5), 051302.
mla: Waitukaitis, Scott R., et al. “Droplet and Cluster Formation in Freely Falling
Granular Streams.” Physical Review E, vol. 83, no. 5, 051302, American
Physical Society, 2011, doi:10.1103/PhysRevE.83.051302.
short: S.R. Waitukaitis, H. Grütjen, J. Royer, H. Jaeger, Physical Review E 83 (2011).
date_created: 2018-12-11T11:44:41Z
date_published: 2011-05-12T00:00:00Z
date_updated: 2021-01-12T06:48:25Z
day: '12'
doi: 10.1103/PhysRevE.83.051302
extern: '1'
external_id:
arxiv:
- '1006.1371'
intvolume: ' 83'
issue: '5'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://arxiv.org/abs/1006.1371
month: '05'
oa: 1
oa_version: Preprint
publication: Physical Review E
publication_status: published
publisher: American Physical Society
publist_id: '7942'
quality_controlled: '1'
status: public
title: Droplet and cluster formation in freely falling granular streams
type: journal_article
user_id: 3E5EF7F0-F248-11E8-B48F-1D18A9856A87
volume: 83
year: '2011'
...
---
_id: '10389'
abstract:
- lang: eng
text: We perform numerical simulations to study self-assembly of nanoparticles mediated
by an elastic planar surface. We show how the nontrivial elastic response to deformations
of these surfaces leads to anisotropic interactions between the particles resulting
in aggregates having different geometrical features. The morphology of the patterns
can be controlled by the mechanical properties of the surface and the strength
of the particle adhesion. We use simple scaling arguments to understand the formation
of the different structures, and we show how the adhering particles can cause
the underlying elastic substrate to wrinkle if two of its opposite edges are clamped.
Finally, we discuss the implications of our results and suggest how elastic surfaces
could be used in nanofabrication.
acknowledgement: This work was supported by the National Science Foundation under
Career Grant No. DMR-0846426. We thank Josep C. Pàmies and William L. Miller for
helpful discussions.
article_number: '8324'
article_processing_charge: No
article_type: original
arxiv: 1
author:
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Angelo
full_name: Cacciuto, Angelo
last_name: Cacciuto
citation:
ama: Šarić A, Cacciuto A. Soft elastic surfaces as a platform for particle self-assembly.
Soft Matter. 2011;7(18). doi:10.1039/c1sm05773a
apa: Šarić, A., & Cacciuto, A. (2011). Soft elastic surfaces as a platform for
particle self-assembly. Soft Matter. Royal Society of Chemistry. https://doi.org/10.1039/c1sm05773a
chicago: Šarić, Anđela, and Angelo Cacciuto. “Soft Elastic Surfaces as a Platform
for Particle Self-Assembly.” Soft Matter. Royal Society of Chemistry, 2011.
https://doi.org/10.1039/c1sm05773a.
ieee: A. Šarić and A. Cacciuto, “Soft elastic surfaces as a platform for particle
self-assembly,” Soft Matter, vol. 7, no. 18. Royal Society of Chemistry,
2011.
ista: Šarić A, Cacciuto A. 2011. Soft elastic surfaces as a platform for particle
self-assembly. Soft Matter. 7(18), 8324.
mla: Šarić, Anđela, and Angelo Cacciuto. “Soft Elastic Surfaces as a Platform for
Particle Self-Assembly.” Soft Matter, vol. 7, no. 18, 8324, Royal Society
of Chemistry, 2011, doi:10.1039/c1sm05773a.
short: A. Šarić, A. Cacciuto, Soft Matter 7 (2011).
date_created: 2021-11-29T14:33:18Z
date_published: 2011-08-08T00:00:00Z
date_updated: 2021-11-29T15:12:10Z
day: '08'
doi: 10.1039/c1sm05773a
extern: '1'
external_id:
arxiv:
- '1106.2995'
intvolume: ' 7'
issue: '18'
keyword:
- condensed matter physics
- general chemistry
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://arxiv.org/abs/1106.2995
month: '08'
oa: 1
oa_version: Preprint
publication: Soft Matter
publication_identifier:
eissn:
- 1744-6848
issn:
- 1744-683X
publication_status: published
publisher: Royal Society of Chemistry
quality_controlled: '1'
scopus_import: '1'
status: public
title: Soft elastic surfaces as a platform for particle self-assembly
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 7
year: '2011'
...
---
_id: '1048'
abstract:
- lang: eng
text: We produce an ultracold and dense sample of rovibronic ground state Cs 2 molecules
close to the regime of quantum degeneracy, in a single hyperfine level, in the
presence of an optical lattice. The molecules are individually trapped, in the
motional ground state of an optical lattice well, with a lifetime of 8 s. For
preparation, we start with a zero-temperature atomic Mott-insulator state with
optimized double-site occupancy and efficiently associate weakly-bound dimer molecules
on a Feshbach resonance. Despite extremely weak Franck-Condon wavefunction overlap,
the molecules are subsequently transferred with >50% efficiency to the rovibronic
ground state by a stimulated four-photon process. Our results present a crucial
step towards the generation of Bose-Einstein condensates of ground-state molecules
and, when suitably generalized to polar heteronuclear molecules such as RbCs,
the realization of dipolar many-body quantum-gas phases in periodic potentials.
acknowledgement: "We thank H. Ritsch, N. Bouloufa, O. Dulieu, J. Aldegunde, J. M.
Hutson, H. Salami, T. Bergeman, S. D ̈urr, and K. Bergmann for valuable discussions
and H. Telle, H. Schnatz, B. Lipphardt, and J. Alnis for sharing technical expertise.
We are indebted to R. Grimm for generous support. We gratefully acknowledge funding
by the Austrian Ministry of Science and\r\nResearch (Bundesministerium f ̈ur Wissenschaft
und Forschung) and the Austrian Science Fund\r\n(Fonds zur F ̈orderung der wissenschaftlichen
Forschung) in the form of a START prize grant\r\nand by the European Science Foundation
within the framework of the EuroQUASAR collective\r\nresearch project QuDeGPM (Project
I 153-N16) and within the framework of the EuroQUAM\r\ncollective research project
QuDipMol (Project I 124-N16). R.H. was supported by a Marie Curie\r\nInternational
Incoming Fellowship within the 7th European Community Framework Programme"
article_processing_charge: No
arxiv: 1
author:
- first_name: Hanns
full_name: Nägerl, Hanns
last_name: Nägerl
- first_name: Manfred
full_name: Mark, Manfred
last_name: Mark
- first_name: Elmar
full_name: Haller, Elmar
last_name: Haller
- first_name: Mattias
full_name: Gustavsson, Mattias
last_name: Gustavsson
- first_name: Russell
full_name: Hart, Russell
last_name: Hart
- first_name: Johann G
full_name: Danzl, Johann G
id: 42EFD3B6-F248-11E8-B48F-1D18A9856A87
last_name: Danzl
orcid: 0000-0001-8559-3973
citation:
ama: 'Nägerl H, Mark M, Haller E, Gustavsson M, Hart R, Danzl JG. Ultracold and
dense samples of ground-state molecules in lattice potentials. Journal of Physics:
Conference Series. 2011;264(1). doi:10.1088/1742-6596/264/1/012015'
apa: 'Nägerl, H., Mark, M., Haller, E., Gustavsson, M., Hart, R., & Danzl, J.
G. (2011). Ultracold and dense samples of ground-state molecules in lattice potentials.
Journal of Physics: Conference Series. IOP Publishing Ltd. https://doi.org/10.1088/1742-6596/264/1/012015'
chicago: 'Nägerl, Hanns, Manfred Mark, Elmar Haller, Mattias Gustavsson, Russell
Hart, and Johann G Danzl. “Ultracold and Dense Samples of Ground-State Molecules
in Lattice Potentials.” Journal of Physics: Conference Series. IOP Publishing
Ltd., 2011. https://doi.org/10.1088/1742-6596/264/1/012015.'
ieee: 'H. Nägerl, M. Mark, E. Haller, M. Gustavsson, R. Hart, and J. G. Danzl, “Ultracold
and dense samples of ground-state molecules in lattice potentials,” Journal
of Physics: Conference Series, vol. 264, no. 1. IOP Publishing Ltd., 2011.'
ista: 'Nägerl H, Mark M, Haller E, Gustavsson M, Hart R, Danzl JG. 2011. Ultracold
and dense samples of ground-state molecules in lattice potentials. Journal of
Physics: Conference Series. 264(1).'
mla: 'Nägerl, Hanns, et al. “Ultracold and Dense Samples of Ground-State Molecules
in Lattice Potentials.” Journal of Physics: Conference Series, vol. 264,
no. 1, IOP Publishing Ltd., 2011, doi:10.1088/1742-6596/264/1/012015.'
short: 'H. Nägerl, M. Mark, E. Haller, M. Gustavsson, R. Hart, J.G. Danzl, Journal
of Physics: Conference Series 264 (2011).'
date_created: 2018-12-11T11:49:52Z
date_published: 2011-01-01T00:00:00Z
date_updated: 2021-01-12T06:47:54Z
day: '01'
doi: 10.1088/1742-6596/264/1/012015
extern: '1'
external_id:
arxiv:
- '1011.0179'
intvolume: ' 264'
issue: '1'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://arxiv.org/abs/1011.0179
month: '01'
oa: 1
oa_version: Preprint
publication: 'Journal of Physics: Conference Series'
publication_status: published
publisher: IOP Publishing Ltd.
publist_id: '6340'
status: public
title: Ultracold and dense samples of ground-state molecules in lattice potentials
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 264
year: '2011'
...
---
_id: '1050'
abstract:
- lang: eng
text: We present experimentally derived potential curves 1?and spin-orbit interaction
functions for the strongly perturbed AΣu+ 3?and bΠu states of the cesium dimer.
The results are based on data from several sources. Laser-induced fluorescence
Fourier transform spectroscopy (LIF FTS) was used some time ago in the Laboratoire
Aimé Cotton primarily to study the XΣg+ state. More recent work at Tsinghua University
provides information from moderate 3?resolution spectroscopy on the lowest levels
of the bΠ0u± state as well as additional high-resolution data. From Innsbruck
University, we have precision data obtained with cold Cs2 molecules. Recent data
from Temple University was obtained using the optical-optical double resonance
polarization spectroscopy technique, and finally, a group at the University of
Latvia has added additional LIF FTS data. In the Hamiltonian matrix, we have used
analytic potentials (the expanded Morse oscillator form) with both finite-difference
(FD) coupled-channel and discrete variable representation (DVR) calculations of
the term values. Fitted diagonal and off-diagonal spin-orbit functions are obtained
and compared with ab initio results from Temple and Moscow State universities.
acknowledgement: The work in Temple University was supported by NSF grant no. PHY-0855502.
S.K. acknowledges support from AFOSR and from NSF grant no. PHY-1005453. S.A., C.M.,
and J.H. were supported by NSF grants no. PHY-0652938 and PHY-0968898. The work
at Stony Brook was supported by NSF grants no. PHY-0652459 and PHY-0968905. The
work in Tsinghua University was supported by NSFC of China, under grant no. 20773072.
The Moscow team thanks the Russian Foundation for Basic Researches by the grant
no. 10-03-00195 and MSU Priority Direction 2.3. M.T. and R.F. are grateful to Ilze
Klincare, Olga Nikolayeva, and Artis Kruzins for their help in spectra analysis,
as well as appreciate the support from the ESF 2009/0223/1DP/1.1.1.2.0/09/APIA/VIAA/008
project.
article_processing_charge: No
arxiv: 1
author:
- first_name: Jianmei
full_name: Bai, Jianmei
last_name: Bai
- first_name: Ergin
full_name: Ahmed, Ergin
last_name: Ahmed
- first_name: Bediha
full_name: Beser, Bediha
last_name: Beser
- first_name: Yafei
full_name: Guan, Yafei
last_name: Guan
- first_name: Svetlana
full_name: Kotochigova, Svetlana
last_name: Kotochigova
- first_name: Marjatta
full_name: Lyyra, Marjatta
last_name: Lyyra
- first_name: Seth
full_name: Ashman, Seth
last_name: Ashman
- first_name: Christopher
full_name: Wolfe, Christopher
last_name: Wolfe
- first_name: John
full_name: Huennekens, John
last_name: Huennekens
- first_name: Feng
full_name: Xie, Feng
last_name: Xie
- first_name: Dan
full_name: Li, Dan
last_name: Li
- first_name: Li
full_name: Li, Li
last_name: Li
- first_name: Maris
full_name: Tamanis, Maris
last_name: Tamanis
- first_name: Ruvin
full_name: Ferber, Ruvin
last_name: Ferber
- first_name: Anastasia
full_name: Drozdova, Anastasia
last_name: Drozdova
- first_name: Elena
full_name: Pazyuk, Elena
last_name: Pazyuk
- first_name: Andrey
full_name: Stolyarov, Andrey
last_name: Stolyarov
- first_name: Johann G
full_name: Danzl, Johann G
id: 42EFD3B6-F248-11E8-B48F-1D18A9856A87
last_name: Danzl
orcid: 0000-0001-8559-3973
- first_name: Hanns
full_name: Nägerl, Hanns
last_name: Nägerl
- first_name: Nadia
full_name: Bouloufa, Nadia
last_name: Bouloufa
- first_name: Olivier
full_name: Dulieu, Olivier
last_name: Dulieu
- first_name: Claude
full_name: Amiot, Claude
last_name: Amiot
- first_name: Houssam
full_name: Salami, Houssam
last_name: Salami
- first_name: Thomas
full_name: Bergeman, Thomas
last_name: Bergeman
citation:
ama: Bai J, Ahmed E, Beser B, et al. Global analysis of data on the spin-orbit-coupled
A 1Σu+ and b 3Πu inf states of Cs2. Physical Review A - Atomic, Molecular,
and Optical Physics. 2011;83(3). doi:10.1103/PhysRevA.83.032514
apa: Bai, J., Ahmed, E., Beser, B., Guan, Y., Kotochigova, S., Lyyra, M., … Bergeman,
T. (2011). Global analysis of data on the spin-orbit-coupled A 1Σu+ and b 3Πu
inf states of Cs2. Physical Review A - Atomic, Molecular, and Optical Physics.
American Physical Society. https://doi.org/10.1103/PhysRevA.83.032514
chicago: Bai, Jianmei, Ergin Ahmed, Bediha Beser, Yafei Guan, Svetlana Kotochigova,
Marjatta Lyyra, Seth Ashman, et al. “Global Analysis of Data on the Spin-Orbit-Coupled
A 1Σu+ and b 3Πu Inf States of Cs2.” Physical Review A - Atomic, Molecular,
and Optical Physics. American Physical Society, 2011. https://doi.org/10.1103/PhysRevA.83.032514.
ieee: J. Bai et al., “Global analysis of data on the spin-orbit-coupled A
1Σu+ and b 3Πu inf states of Cs2,” Physical Review A - Atomic, Molecular,
and Optical Physics, vol. 83, no. 3. American Physical Society, 2011.
ista: Bai J, Ahmed E, Beser B, Guan Y, Kotochigova S, Lyyra M, Ashman S, Wolfe C,
Huennekens J, Xie F, Li D, Li L, Tamanis M, Ferber R, Drozdova A, Pazyuk E, Stolyarov
A, Danzl JG, Nägerl H, Bouloufa N, Dulieu O, Amiot C, Salami H, Bergeman T. 2011.
Global analysis of data on the spin-orbit-coupled A 1Σu+ and b 3Πu inf states
of Cs2. Physical Review A - Atomic, Molecular, and Optical Physics. 83(3).
mla: Bai, Jianmei, et al. “Global Analysis of Data on the Spin-Orbit-Coupled A 1Σu+
and b 3Πu Inf States of Cs2.” Physical Review A - Atomic, Molecular, and Optical
Physics, vol. 83, no. 3, American Physical Society, 2011, doi:10.1103/PhysRevA.83.032514.
short: J. Bai, E. Ahmed, B. Beser, Y. Guan, S. Kotochigova, M. Lyyra, S. Ashman,
C. Wolfe, J. Huennekens, F. Xie, D. Li, L. Li, M. Tamanis, R. Ferber, A. Drozdova,
E. Pazyuk, A. Stolyarov, J.G. Danzl, H. Nägerl, N. Bouloufa, O. Dulieu, C. Amiot,
H. Salami, T. Bergeman, Physical Review A - Atomic, Molecular, and Optical Physics
83 (2011).
date_created: 2018-12-11T11:49:53Z
date_published: 2011-03-28T00:00:00Z
date_updated: 2021-01-12T06:47:55Z
day: '28'
doi: 10.1103/PhysRevA.83.032514
extern: '1'
external_id:
arxiv:
- '1101.5412'
intvolume: ' 83'
issue: '3'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://arxiv.org/abs/1101.5412
month: '03'
oa: 1
oa_version: Preprint
publication: ' Physical Review A - Atomic, Molecular, and Optical Physics'
publication_status: published
publisher: American Physical Society
publist_id: '6339'
status: public
title: Global analysis of data on the spin-orbit-coupled A 1Σu+ and b 3Πu inf states
of Cs2
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 83
year: '2011'
...
---
_id: '1051'
abstract:
- lang: eng
text: We demonstrate the temporal Talbot effect for trapped matter waves using ultracold
atoms in an optical lattice. We investigate the phase evolution of an array of
essentially non-interacting matter waves and observe matter-wave collapse and
revival in the form of a Talbot interference pattern. By using long expansion
times, we image momentum space with sub-recoil resolution, allowing us to observe
fractional Talbot fringes up to tenth order.
acknowledgement: We are indebted to R Grimm for generous support and we thank A Daley
for valuable discussions. We gratefully acknowledge funding by the Austrian Science
Fund (FWF) within project I153-N16 and within the framework of the European Science
Foundation (ESF) EuroQUASAR collective research project QuDeGPM.
article_processing_charge: No
author:
- first_name: Manfred
full_name: Mark, Manfred
last_name: Mark
- first_name: Elmar
full_name: Haller, Elmar
last_name: Haller
- first_name: Johann G
full_name: Danzl, Johann G
id: 42EFD3B6-F248-11E8-B48F-1D18A9856A87
last_name: Danzl
orcid: 0000-0001-8559-3973
- first_name: Katharina
full_name: Lauber, Katharina
last_name: Lauber
- first_name: Mattias
full_name: Gustavsson, Mattias
last_name: Gustavsson
- first_name: Hanns
full_name: Nägerl, Hanns
last_name: Nägerl
citation:
ama: Mark M, Haller E, Danzl JG, Lauber K, Gustavsson M, Nägerl H. Demonstration
of the temporal matter-wave Talbot effect for trapped matter waves. New Journal
of Physics. 2011;13. doi:10.1088/1367-2630/13/8/085008
apa: Mark, M., Haller, E., Danzl, J. G., Lauber, K., Gustavsson, M., & Nägerl,
H. (2011). Demonstration of the temporal matter-wave Talbot effect for trapped
matter waves. New Journal of Physics. IOP Publishing Ltd. https://doi.org/10.1088/1367-2630/13/8/085008
chicago: Mark, Manfred, Elmar Haller, Johann G Danzl, Katharina Lauber, Mattias
Gustavsson, and Hanns Nägerl. “Demonstration of the Temporal Matter-Wave Talbot
Effect for Trapped Matter Waves.” New Journal of Physics. IOP Publishing
Ltd., 2011. https://doi.org/10.1088/1367-2630/13/8/085008.
ieee: M. Mark, E. Haller, J. G. Danzl, K. Lauber, M. Gustavsson, and H. Nägerl,
“Demonstration of the temporal matter-wave Talbot effect for trapped matter waves,”
New Journal of Physics, vol. 13. IOP Publishing Ltd., 2011.
ista: Mark M, Haller E, Danzl JG, Lauber K, Gustavsson M, Nägerl H. 2011. Demonstration
of the temporal matter-wave Talbot effect for trapped matter waves. New Journal
of Physics. 13.
mla: Mark, Manfred, et al. “Demonstration of the Temporal Matter-Wave Talbot Effect
for Trapped Matter Waves.” New Journal of Physics, vol. 13, IOP Publishing
Ltd., 2011, doi:10.1088/1367-2630/13/8/085008.
short: M. Mark, E. Haller, J.G. Danzl, K. Lauber, M. Gustavsson, H. Nägerl, New
Journal of Physics 13 (2011).
date_created: 2018-12-11T11:49:53Z
date_published: 2011-08-01T00:00:00Z
date_updated: 2021-01-12T06:47:56Z
day: '01'
doi: 10.1088/1367-2630/13/8/085008
extern: '1'
intvolume: ' 13'
language:
- iso: eng
month: '08'
oa_version: None
publication: New Journal of Physics
publication_status: published
publisher: IOP Publishing Ltd.
publist_id: '6338'
status: public
title: Demonstration of the temporal matter-wave Talbot effect for trapped matter
waves
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 13
year: '2011'
...
---
_id: '1052'
abstract:
- lang: eng
text: The present paper aims at finding optimal parameters for trapping of Cs 2
molecules in optical lattices, with the perspective of creating a quantum degenerate
gas of ground-state molecules. We have calculated dynamic polarizabilities of
Cs 2 molecules subject to an oscillating electric field, using accurate potential
curves and electronic transition dipole moments. We show that for some particular
wavelengths of the optical lattice, called "magic wavelengths", the
polarizability of the ground-state molecules is equal to the one of a Feshbach
molecule. As the creation of the sample of ground-state molecules relies on an
adiabatic population transfer from weakly-bound molecules created on a Feshbach
resonance, such a coincidence ensures that both the initial and final states are
favorably trapped by the lattice light, allowing optimized transfer in agreement
with the experimental observation.
acknowledgement: "We thank E. Haller for important contributions to the experimental
work and R. Grimm for generous support. We acknowledge funding by the Austrian
\ Science Fund (FWF) within\r\nproject Quantum Gases of Ground-State Molecules,
\ project\r\nnumber P 21555-N20."
article_processing_charge: No
arxiv: 1
author:
- first_name: Romain
full_name: Vexiau, Romain
last_name: Vexiau
- first_name: Nadia
full_name: Bouloufa, Nadia
last_name: Bouloufa
- first_name: Mireille
full_name: Aymar, Mireille
last_name: Aymar
- first_name: Johann G
full_name: Danzl, Johann G
id: 42EFD3B6-F248-11E8-B48F-1D18A9856A87
last_name: Danzl
orcid: 0000-0001-8559-3973
- first_name: Manfred
full_name: Mark, Manfred
last_name: Mark
- first_name: Hanns
full_name: Nägerl, Hanns
last_name: Nägerl
- first_name: Olivier
full_name: Dulieu, Olivier
last_name: Dulieu
citation:
ama: Vexiau R, Bouloufa N, Aymar M, et al. Optimal trapping wavelengths of Cs 2
molecules in an optical lattice. European Physical Journal D. 2011;65(1-2):243-250.
doi:10.1140/epjd/e2011-20085-4
apa: Vexiau, R., Bouloufa, N., Aymar, M., Danzl, J. G., Mark, M., Nägerl, H., &
Dulieu, O. (2011). Optimal trapping wavelengths of Cs 2 molecules in an optical
lattice. European Physical Journal D. Springer. https://doi.org/10.1140/epjd/e2011-20085-4
chicago: Vexiau, Romain, Nadia Bouloufa, Mireille Aymar, Johann G Danzl, Manfred
Mark, Hanns Nägerl, and Olivier Dulieu. “Optimal Trapping Wavelengths of Cs 2
Molecules in an Optical Lattice.” European Physical Journal D. Springer,
2011. https://doi.org/10.1140/epjd/e2011-20085-4.
ieee: R. Vexiau et al., “Optimal trapping wavelengths of Cs 2 molecules in
an optical lattice,” European Physical Journal D, vol. 65, no. 1–2. Springer,
pp. 243–250, 2011.
ista: Vexiau R, Bouloufa N, Aymar M, Danzl JG, Mark M, Nägerl H, Dulieu O. 2011.
Optimal trapping wavelengths of Cs 2 molecules in an optical lattice. European
Physical Journal D. 65(1–2), 243–250.
mla: Vexiau, Romain, et al. “Optimal Trapping Wavelengths of Cs 2 Molecules in an
Optical Lattice.” European Physical Journal D, vol. 65, no. 1–2, Springer,
2011, pp. 243–50, doi:10.1140/epjd/e2011-20085-4.
short: R. Vexiau, N. Bouloufa, M. Aymar, J.G. Danzl, M. Mark, H. Nägerl, O. Dulieu,
European Physical Journal D 65 (2011) 243–250.
date_created: 2018-12-11T11:49:53Z
date_published: 2011-11-01T00:00:00Z
date_updated: 2021-01-12T06:47:56Z
day: '01'
doi: 10.1140/epjd/e2011-20085-4
extern: '1'
external_id:
arxiv:
- '1102.1793'
intvolume: ' 65'
issue: 1-2
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://arxiv.org/abs/1102.1793
month: '11'
oa: 1
oa_version: Preprint
page: 243 - 250
publication: European Physical Journal D
publication_status: published
publisher: Springer
publist_id: '6336'
status: public
title: Optimal trapping wavelengths of Cs 2 molecules in an optical lattice
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 65
year: '2011'
...
---
_id: '1053'
abstract:
- lang: eng
text: We perform precision measurements on a Mott-insulator quantum state of ultracold
atoms with tunable interactions. We probe the dependence of the superfluid-to-Mott-insulator
transition on the interaction strength and explore the limits of the standard
Bose-Hubbard model description. By tuning the on-site interaction energies to
values comparable to the interband separation, we are able to quantitatively measure
number-dependent shifts in the excitation spectrum caused by effective multibody
interactions.
acknowledgement: We are indebted to R. Grimm for generous support. We thank D. Boyanovsky,
H. Büchler, P. Johnson, W. Niedenzu, and E. Tiesinga for fruitful discussions. We
gratefully acknowledge funding by the Austrian Science Fund (FWF) within project
I153-N16 and within the framework of the European Science Foundation (ESF) EuroQUASAR
collective research project QuDeGPM.
article_processing_charge: No
arxiv: 1
author:
- first_name: Manfred
full_name: Mark, Manfred
last_name: Mark
- first_name: Elmar
full_name: Haller, Elmar
last_name: Haller
- first_name: Katharina
full_name: Lauber, Katharina
last_name: Lauber
- first_name: Johann G
full_name: Danzl, Johann G
id: 42EFD3B6-F248-11E8-B48F-1D18A9856A87
last_name: Danzl
orcid: 0000-0001-8559-3973
- first_name: Andrew
full_name: Daley, Andrew
last_name: Daley
- first_name: Hanns
full_name: Nägerl, Hanns
last_name: Nägerl
citation:
ama: Mark M, Haller E, Lauber K, Danzl JG, Daley A, Nägerl H. Precision measurements
on a tunable Mott insulator of ultracold atoms. Physical Review Letters.
2011;107(17). doi:10.1103/PhysRevLett.107.175301
apa: Mark, M., Haller, E., Lauber, K., Danzl, J. G., Daley, A., & Nägerl, H.
(2011). Precision measurements on a tunable Mott insulator of ultracold atoms.
Physical Review Letters. American Physical Society. https://doi.org/10.1103/PhysRevLett.107.175301
chicago: Mark, Manfred, Elmar Haller, Katharina Lauber, Johann G Danzl, Andrew Daley,
and Hanns Nägerl. “Precision Measurements on a Tunable Mott Insulator of Ultracold
Atoms.” Physical Review Letters. American Physical Society, 2011. https://doi.org/10.1103/PhysRevLett.107.175301.
ieee: M. Mark, E. Haller, K. Lauber, J. G. Danzl, A. Daley, and H. Nägerl, “Precision
measurements on a tunable Mott insulator of ultracold atoms,” Physical Review
Letters, vol. 107, no. 17. American Physical Society, 2011.
ista: Mark M, Haller E, Lauber K, Danzl JG, Daley A, Nägerl H. 2011. Precision measurements
on a tunable Mott insulator of ultracold atoms. Physical Review Letters. 107(17).
mla: Mark, Manfred, et al. “Precision Measurements on a Tunable Mott Insulator of
Ultracold Atoms.” Physical Review Letters, vol. 107, no. 17, American Physical
Society, 2011, doi:10.1103/PhysRevLett.107.175301.
short: M. Mark, E. Haller, K. Lauber, J.G. Danzl, A. Daley, H. Nägerl, Physical
Review Letters 107 (2011).
date_created: 2018-12-11T11:49:54Z
date_published: 2011-10-18T00:00:00Z
date_updated: 2021-01-12T06:47:56Z
day: '18'
doi: 10.1103/PhysRevLett.107.175301
extern: '1'
external_id:
arxiv:
- '1107.1803'
intvolume: ' 107'
issue: '17'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://arxiv.org/abs/1107.1803
month: '10'
oa: 1
oa_version: Preprint
publication: Physical Review Letters
publication_status: published
publisher: American Physical Society
publist_id: '6337'
status: public
title: Precision measurements on a tunable Mott insulator of ultracold atoms
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 107
year: '2011'
...