---
_id: '12131'
abstract:
- lang: eng
  text: Replication-incompetent adenoviral vectors have been extensively used as a
    platform for vaccine design, with at least four anti-COVID-19 vaccines authorized
    to date. These vaccines elicit neutralizing antibody responses directed against
    SARS-CoV-2 Spike protein and confer significant level of protection against SARS-CoV-2
    infection. Immunization with adenovirus-vectored vaccines is known to be accompanied
    by the production of anti-vector antibodies, which may translate into reduced
    efficacy of booster or repeated rounds of revaccination. Here, we used blood samples
    from patients who received an adenovirus-based Gam-COVID-Vac vaccine to address
    the question of whether anti-vector antibodies may influence the magnitude of
    SARS-CoV-2-specific humoral response after booster vaccination. We observed that
    rAd26-based prime vaccination with Gam-COVID-Vac induced the development of Ad26-neutralizing
    antibodies, which persisted in circulation for at least 9 months. Our analysis
    further indicates that high pre-boost Ad26 neutralizing antibody titers do not
    appear to affect the humoral immunogenicity of the Gam-COVID-Vac boost. The titers
    of anti-SARS-CoV-2 RBD IgGs and antibodies, which neutralized both the wild type
    and the circulating variants of concern of SARS-CoV-2 such as Delta and Omicron,
    were independent of the pre-boost levels of Ad26-neutralizing antibodies. Thus,
    our results support the development of repeated immunization schedule with adenovirus-based
    COVID-19 vaccines.
acknowledgement: We thank Sergey Kulemzin, Grigory Efimov, Yuri Lebedin, Alexander
  Taranin and Rudolf Valenta for providing reagents. Figures were created with the
  help of BioRender.com. This work was supported by the Russian Science Foundation
  (Project 21-15-00286). Byazrova M.G. was supported by the RUDN University Strategic
  Academic Leadership Program.
article_number: '145'
article_processing_charge: No
article_type: original
author:
- first_name: Maria G.
  full_name: Byazrova, Maria G.
  last_name: Byazrova
- first_name: Ekaterina A.
  full_name: Astakhova, Ekaterina A.
  last_name: Astakhova
- first_name: Aygul
  full_name: Minnegalieva, Aygul
  id: 87DF77F0-1D9A-11EA-B6AE-CE443DDC885E
  last_name: Minnegalieva
- first_name: Maria M.
  full_name: Sukhova, Maria M.
  last_name: Sukhova
- first_name: Artem A.
  full_name: Mikhailov, Artem A.
  last_name: Mikhailov
- first_name: Alexey G.
  full_name: Prilipov, Alexey G.
  last_name: Prilipov
- first_name: Andrey A.
  full_name: Gorchakov, Andrey A.
  last_name: Gorchakov
- first_name: Alexander V.
  full_name: Filatov, Alexander V.
  last_name: Filatov
citation:
  ama: Byazrova MG, Astakhova EA, Minnegalieva A, et al. Anti-Ad26 humoral immunity
    does not compromise SARS-COV-2 neutralizing antibody responses following Gam-COVID-Vac
    booster vaccination. <i>npj Vaccines</i>. 2022;7. doi:<a href="https://doi.org/10.1038/s41541-022-00566-x">10.1038/s41541-022-00566-x</a>
  apa: Byazrova, M. G., Astakhova, E. A., Minnegalieva, A., Sukhova, M. M., Mikhailov,
    A. A., Prilipov, A. G., … Filatov, A. V. (2022). Anti-Ad26 humoral immunity does
    not compromise SARS-COV-2 neutralizing antibody responses following Gam-COVID-Vac
    booster vaccination. <i>Npj Vaccines</i>. Springer Nature. <a href="https://doi.org/10.1038/s41541-022-00566-x">https://doi.org/10.1038/s41541-022-00566-x</a>
  chicago: Byazrova, Maria G., Ekaterina A. Astakhova, Aygul Minnegalieva, Maria M.
    Sukhova, Artem A. Mikhailov, Alexey G. Prilipov, Andrey A. Gorchakov, and Alexander
    V. Filatov. “Anti-Ad26 Humoral Immunity Does Not Compromise SARS-COV-2 Neutralizing
    Antibody Responses Following Gam-COVID-Vac Booster Vaccination.” <i>Npj Vaccines</i>.
    Springer Nature, 2022. <a href="https://doi.org/10.1038/s41541-022-00566-x">https://doi.org/10.1038/s41541-022-00566-x</a>.
  ieee: M. G. Byazrova <i>et al.</i>, “Anti-Ad26 humoral immunity does not compromise
    SARS-COV-2 neutralizing antibody responses following Gam-COVID-Vac booster vaccination,”
    <i>npj Vaccines</i>, vol. 7. Springer Nature, 2022.
  ista: Byazrova MG, Astakhova EA, Minnegalieva A, Sukhova MM, Mikhailov AA, Prilipov
    AG, Gorchakov AA, Filatov AV. 2022. Anti-Ad26 humoral immunity does not compromise
    SARS-COV-2 neutralizing antibody responses following Gam-COVID-Vac booster vaccination.
    npj Vaccines. 7, 145.
  mla: Byazrova, Maria G., et al. “Anti-Ad26 Humoral Immunity Does Not Compromise
    SARS-COV-2 Neutralizing Antibody Responses Following Gam-COVID-Vac Booster Vaccination.”
    <i>Npj Vaccines</i>, vol. 7, 145, Springer Nature, 2022, doi:<a href="https://doi.org/10.1038/s41541-022-00566-x">10.1038/s41541-022-00566-x</a>.
  short: M.G. Byazrova, E.A. Astakhova, A. Minnegalieva, M.M. Sukhova, A.A. Mikhailov,
    A.G. Prilipov, A.A. Gorchakov, A.V. Filatov, Npj Vaccines 7 (2022).
date_created: 2023-01-12T12:02:54Z
date_published: 2022-11-15T00:00:00Z
date_updated: 2023-08-04T08:52:40Z
day: '15'
ddc:
- '570'
department:
- _id: FyKo
doi: 10.1038/s41541-022-00566-x
external_id:
  isi:
  - '000884278600004'
  pmid:
  - '36379998'
file:
- access_level: open_access
  checksum: ddaac096381565b2b4b7dcc34cdbc4ee
  content_type: application/pdf
  creator: dernst
  date_created: 2023-01-23T11:22:09Z
  date_updated: 2023-01-23T11:22:09Z
  file_id: '12347'
  file_name: 2022_njpVaccines_Byazrova.pdf
  file_size: 1856046
  relation: main_file
  success: 1
file_date_updated: 2023-01-23T11:22:09Z
has_accepted_license: '1'
intvolume: '         7'
isi: 1
keyword:
- Pharmacology (medical)
- Infectious Diseases
- Pharmacology
- Immunology
- SARS-COV-2
- COVID
language:
- iso: eng
license: https://creativecommons.org/licenses/by/4.0/
month: '11'
oa: 1
oa_version: Published Version
pmid: 1
publication: npj Vaccines
publication_identifier:
  issn:
  - 2059-0105
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: Anti-Ad26 humoral immunity does not compromise SARS-COV-2 neutralizing antibody
  responses following Gam-COVID-Vac booster vaccination
tmp:
  image: /images/cc_by.png
  legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
  name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
  short: CC BY (4.0)
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 7
year: '2022'
...
---
_id: '11447'
abstract:
- lang: eng
  text: Empirical essays of fitness landscapes suggest that they may be rugged, that
    is having multiple fitness peaks. Such fitness landscapes, those that have multiple
    peaks, necessarily have special local structures, called reciprocal sign epistasis
    (Poelwijk et al. in J Theor Biol 272:141–144, 2011). Here, we investigate the
    quantitative relationship between the number of fitness peaks and the number of
    reciprocal sign epistatic interactions. Previously, it has been shown (Poelwijk
    et al. in J Theor Biol 272:141–144, 2011) that pairwise reciprocal sign epistasis
    is a necessary but not sufficient condition for the existence of multiple peaks.
    Applying discrete Morse theory, which to our knowledge has never been used in
    this context, we extend this result by giving the minimal number of reciprocal
    sign epistatic interactions required to create a given number of peaks.
acknowledgement: We are grateful to Herbert Edelsbrunner and Jeferson Zapata for helpful
  discussions. Open access funding provided by Austrian Science Fund (FWF). Partially
  supported by the ERC Consolidator (771209–CharFL) and the FWF Austrian Science Fund
  (I5127-B) grants to FAK.
article_number: '74'
article_processing_charge: Yes (via OA deal)
article_type: original
author:
- first_name: Raimundo J
  full_name: Saona Urmeneta, Raimundo J
  id: BD1DF4C4-D767-11E9-B658-BC13E6697425
  last_name: Saona Urmeneta
  orcid: 0000-0001-5103-038X
- first_name: Fyodor
  full_name: Kondrashov, Fyodor
  id: 44FDEF62-F248-11E8-B48F-1D18A9856A87
  last_name: Kondrashov
  orcid: 0000-0001-8243-4694
- first_name: Kseniia
  full_name: Khudiakova, Kseniia
  id: 4E6DC800-AE37-11E9-AC72-31CAE5697425
  last_name: Khudiakova
  orcid: 0000-0002-6246-1465
citation:
  ama: Saona Urmeneta RJ, Kondrashov F, Khudiakova K. Relation between the number
    of peaks and the number of reciprocal sign epistatic interactions. <i>Bulletin
    of Mathematical Biology</i>. 2022;84(8). doi:<a href="https://doi.org/10.1007/s11538-022-01029-z">10.1007/s11538-022-01029-z</a>
  apa: Saona Urmeneta, R. J., Kondrashov, F., &#38; Khudiakova, K. (2022). Relation
    between the number of peaks and the number of reciprocal sign epistatic interactions.
    <i>Bulletin of Mathematical Biology</i>. Springer Nature. <a href="https://doi.org/10.1007/s11538-022-01029-z">https://doi.org/10.1007/s11538-022-01029-z</a>
  chicago: Saona Urmeneta, Raimundo J, Fyodor Kondrashov, and Kseniia Khudiakova.
    “Relation between the Number of Peaks and the Number of Reciprocal Sign Epistatic
    Interactions.” <i>Bulletin of Mathematical Biology</i>. Springer Nature, 2022.
    <a href="https://doi.org/10.1007/s11538-022-01029-z">https://doi.org/10.1007/s11538-022-01029-z</a>.
  ieee: R. J. Saona Urmeneta, F. Kondrashov, and K. Khudiakova, “Relation between
    the number of peaks and the number of reciprocal sign epistatic interactions,”
    <i>Bulletin of Mathematical Biology</i>, vol. 84, no. 8. Springer Nature, 2022.
  ista: Saona Urmeneta RJ, Kondrashov F, Khudiakova K. 2022. Relation between the
    number of peaks and the number of reciprocal sign epistatic interactions. Bulletin
    of Mathematical Biology. 84(8), 74.
  mla: Saona Urmeneta, Raimundo J., et al. “Relation between the Number of Peaks and
    the Number of Reciprocal Sign Epistatic Interactions.” <i>Bulletin of Mathematical
    Biology</i>, vol. 84, no. 8, 74, Springer Nature, 2022, doi:<a href="https://doi.org/10.1007/s11538-022-01029-z">10.1007/s11538-022-01029-z</a>.
  short: R.J. Saona Urmeneta, F. Kondrashov, K. Khudiakova, Bulletin of Mathematical
    Biology 84 (2022).
corr_author: '1'
date_created: 2022-06-17T16:16:15Z
date_published: 2022-06-17T00:00:00Z
date_updated: 2026-05-27T06:26:08Z
day: '17'
ddc:
- '510'
- '570'
department:
- _id: GradSch
- _id: NiBa
- _id: JaMa
doi: 10.1007/s11538-022-01029-z
ec_funded: 1
external_id:
  isi:
  - '000812509800001'
  pmid:
  - '35713756'
file:
- access_level: open_access
  checksum: 05a1fe7d10914a00c2bca9b447993a65
  content_type: application/pdf
  creator: dernst
  date_created: 2022-06-20T07:51:32Z
  date_updated: 2022-06-20T07:51:32Z
  file_id: '11455'
  file_name: 2022_BulletinMathBiology_Saona.pdf
  file_size: 463025
  relation: main_file
  success: 1
file_date_updated: 2022-06-20T07:51:32Z
has_accepted_license: '1'
intvolume: '        84'
isi: 1
issue: '8'
keyword:
- Computational Theory and Mathematics
- General Agricultural and Biological Sciences
- Pharmacology
- General Environmental Science
- General Biochemistry
- Genetics and Molecular Biology
- General Mathematics
- Immunology
- General Neuroscience
language:
- iso: eng
month: '06'
oa: 1
oa_version: Published Version
pmid: 1
project:
- _id: 26580278-B435-11E9-9278-68D0E5697425
  call_identifier: H2020
  grant_number: '771209'
  name: Characterizing the fitness landscape on population and global scales
- _id: 34e076d6-11ca-11ed-8bc3-aec76c41a181
  grant_number: I05127
  name: Evolutionary analysis of gene regulation
publication: Bulletin of Mathematical Biology
publication_identifier:
  eissn:
  - 1522-9602
  issn:
  - 0092-8240
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
related_material:
  link:
  - relation: erratum
    url: https://doi.org/10.1007/s11538-022-01118-z
  record:
  - id: '21918'
    relation: popular_science
    status: private
scopus_import: '1'
status: public
title: Relation between the number of peaks and the number of reciprocal sign epistatic
  interactions
tmp:
  image: /images/cc_by.png
  legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
  name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
  short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 84
year: '2022'
...
---
_id: '9018'
abstract:
- lang: eng
  text: Anti-silencing function 1 (ASF1) is a conserved H3-H4 histone chaperone involved
    in histone dynamics during replication, transcription, and DNA repair. Overexpressed
    in proliferating tissues including many tumors, ASF1 has emerged as a promising
    therapeutic target. Here, we combine structural, computational, and biochemical
    approaches to design peptides that inhibit the ASF1-histone interaction. Starting
    from the structure of the human ASF1-histone complex, we developed a rational
    design strategy combining epitope tethering and optimization of interface contacts
    to identify a potent peptide inhibitor with a dissociation constant of 3 nM. When
    introduced into cultured cells, the inhibitors impair cell proliferation, perturb
    cell-cycle progression, and reduce cell migration and invasion in a manner commensurate
    with their affinity for ASF1. Finally, we find that direct injection of the most
    potent ASF1 peptide inhibitor in mouse allografts reduces tumor growth. Our results
    open new avenues to use ASF1 inhibitors as promising leads for cancer therapy.
article_processing_charge: No
article_type: original
author:
- first_name: May M
  full_name: Bakail, May M
  id: FB3C3F8E-522F-11EA-B186-22963DDC885E
  last_name: Bakail
  orcid: 0000-0002-9592-1587
- first_name: Albane
  full_name: Gaubert, Albane
  last_name: Gaubert
- first_name: Jessica
  full_name: Andreani, Jessica
  last_name: Andreani
- first_name: Gwenaëlle
  full_name: Moal, Gwenaëlle
  last_name: Moal
- first_name: Guillaume
  full_name: Pinna, Guillaume
  last_name: Pinna
- first_name: Ekaterina
  full_name: Boyarchuk, Ekaterina
  last_name: Boyarchuk
- first_name: Marie-Cécile
  full_name: Gaillard, Marie-Cécile
  last_name: Gaillard
- first_name: Regis
  full_name: Courbeyrette, Regis
  last_name: Courbeyrette
- first_name: Carl
  full_name: Mann, Carl
  last_name: Mann
- first_name: Jean-Yves
  full_name: Thuret, Jean-Yves
  last_name: Thuret
- first_name: Bérengère
  full_name: Guichard, Bérengère
  last_name: Guichard
- first_name: Brice
  full_name: Murciano, Brice
  last_name: Murciano
- first_name: Nicolas
  full_name: Richet, Nicolas
  last_name: Richet
- first_name: Adeline
  full_name: Poitou, Adeline
  last_name: Poitou
- first_name: Claire
  full_name: Frederic, Claire
  last_name: Frederic
- first_name: Marie-Hélène
  full_name: Le Du, Marie-Hélène
  last_name: Le Du
- first_name: Morgane
  full_name: Agez, Morgane
  last_name: Agez
- first_name: Caroline
  full_name: Roelants, Caroline
  last_name: Roelants
- first_name: Zachary A.
  full_name: Gurard-Levin, Zachary A.
  last_name: Gurard-Levin
- first_name: Geneviève
  full_name: Almouzni, Geneviève
  last_name: Almouzni
- first_name: Nadia
  full_name: Cherradi, Nadia
  last_name: Cherradi
- first_name: Raphael
  full_name: Guerois, Raphael
  last_name: Guerois
- first_name: Françoise
  full_name: Ochsenbein, Françoise
  last_name: Ochsenbein
citation:
  ama: Bakail MM, Gaubert A, Andreani J, et al. Design on a rational basis of high-affinity
    peptides inhibiting the histone chaperone ASF1. <i>Cell Chemical Biology</i>.
    2019;26(11):1573-1585.e10. doi:<a href="https://doi.org/10.1016/j.chembiol.2019.09.002">10.1016/j.chembiol.2019.09.002</a>
  apa: Bakail, M. M., Gaubert, A., Andreani, J., Moal, G., Pinna, G., Boyarchuk, E.,
    … Ochsenbein, F. (2019). Design on a rational basis of high-affinity peptides
    inhibiting the histone chaperone ASF1. <i>Cell Chemical Biology</i>. Elsevier.
    <a href="https://doi.org/10.1016/j.chembiol.2019.09.002">https://doi.org/10.1016/j.chembiol.2019.09.002</a>
  chicago: Bakail, May M, Albane Gaubert, Jessica Andreani, Gwenaëlle Moal, Guillaume
    Pinna, Ekaterina Boyarchuk, Marie-Cécile Gaillard, et al. “Design on a Rational
    Basis of High-Affinity Peptides Inhibiting the Histone Chaperone ASF1.” <i>Cell
    Chemical Biology</i>. Elsevier, 2019. <a href="https://doi.org/10.1016/j.chembiol.2019.09.002">https://doi.org/10.1016/j.chembiol.2019.09.002</a>.
  ieee: M. M. Bakail <i>et al.</i>, “Design on a rational basis of high-affinity peptides
    inhibiting the histone chaperone ASF1,” <i>Cell Chemical Biology</i>, vol. 26,
    no. 11. Elsevier, p. 1573–1585.e10, 2019.
  ista: Bakail MM, Gaubert A, Andreani J, Moal G, Pinna G, Boyarchuk E, Gaillard M-C,
    Courbeyrette R, Mann C, Thuret J-Y, Guichard B, Murciano B, Richet N, Poitou A,
    Frederic C, Le Du M-H, Agez M, Roelants C, Gurard-Levin ZA, Almouzni G, Cherradi
    N, Guerois R, Ochsenbein F. 2019. Design on a rational basis of high-affinity
    peptides inhibiting the histone chaperone ASF1. Cell Chemical Biology. 26(11),
    1573–1585.e10.
  mla: Bakail, May M., et al. “Design on a Rational Basis of High-Affinity Peptides
    Inhibiting the Histone Chaperone ASF1.” <i>Cell Chemical Biology</i>, vol. 26,
    no. 11, Elsevier, 2019, p. 1573–1585.e10, doi:<a href="https://doi.org/10.1016/j.chembiol.2019.09.002">10.1016/j.chembiol.2019.09.002</a>.
  short: M.M. Bakail, A. Gaubert, J. Andreani, G. Moal, G. Pinna, E. Boyarchuk, M.-C.
    Gaillard, R. Courbeyrette, C. Mann, J.-Y. Thuret, B. Guichard, B. Murciano, N.
    Richet, A. Poitou, C. Frederic, M.-H. Le Du, M. Agez, C. Roelants, Z.A. Gurard-Levin,
    G. Almouzni, N. Cherradi, R. Guerois, F. Ochsenbein, Cell Chemical Biology 26
    (2019) 1573–1585.e10.
date_created: 2021-01-19T11:04:50Z
date_published: 2019-11-21T00:00:00Z
date_updated: 2023-02-23T13:46:53Z
day: '21'
doi: 10.1016/j.chembiol.2019.09.002
extern: '1'
external_id:
  pmid:
  - '31543461'
intvolume: '        26'
issue: '11'
keyword:
- Clinical Biochemistry
- Molecular Medicine
- Biochemistry
- Molecular Biology
- Pharmacology
- Drug Discovery
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://doi.org/10.1016/j.chembiol.2019.09.002
month: '11'
oa: 1
oa_version: Published Version
page: 1573-1585.e10
pmid: 1
publication: Cell Chemical Biology
publication_identifier:
  issn:
  - 2451-9456
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: Design on a rational basis of high-affinity peptides inhibiting the histone
  chaperone ASF1
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 26
year: '2019'
...
---
_id: '11117'
abstract:
- lang: eng
  text: Over the last years it has become evident that the nuclear envelope (NE) is
    more than a passive membrane barrier that separates the nucleus from the cytoplasm.
    The NE not only controls the trafficking of macromolecules between the nucleoplasm
    and the cytosol, but also provides anchoring sites for chromosomes and cytoskeleton
    to the nuclear periphery. Targeting of chromatin to the NE might actually be part
    of gene expression regulation in eukaryotes. Mutations in certain NE proteins
    are associated with a diversity of human diseases, including muscular dystrophy,
    neuropathy, lipodistrophy, torsion dystonia and the premature aging condition
    progeria. Despite the importance of the NE for cell division and differentiation,
    relatively little is known about its biogenesis and its role in human diseases.
    It is our goal to provide a comprehensive view of the NE and to discuss possible
    implications of NE-associated changes for gene expression, chromatin organization
    and signal transduction.
article_processing_charge: No
article_type: review
author:
- first_name: M. A.
  full_name: D’Angelo, M. A.
  last_name: D’Angelo
- 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: D’Angelo MA, Hetzer M. The role of the nuclear envelope in cellular organization.
    <i>Cellular and Molecular Life Sciences</i>. 2006;63(3):316-332. doi:<a href="https://doi.org/10.1007/s00018-005-5361-3">10.1007/s00018-005-5361-3</a>
  apa: D’Angelo, M. A., &#38; Hetzer, M. (2006). The role of the nuclear envelope
    in cellular organization. <i>Cellular and Molecular Life Sciences</i>. Springer
    Nature. <a href="https://doi.org/10.1007/s00018-005-5361-3">https://doi.org/10.1007/s00018-005-5361-3</a>
  chicago: D’Angelo, M. A., and Martin Hetzer. “The Role of the Nuclear Envelope in
    Cellular Organization.” <i>Cellular and Molecular Life Sciences</i>. Springer
    Nature, 2006. <a href="https://doi.org/10.1007/s00018-005-5361-3">https://doi.org/10.1007/s00018-005-5361-3</a>.
  ieee: M. A. D’Angelo and M. Hetzer, “The role of the nuclear envelope in cellular
    organization,” <i>Cellular and Molecular Life Sciences</i>, vol. 63, no. 3. Springer
    Nature, pp. 316–332, 2006.
  ista: D’Angelo MA, Hetzer M. 2006. The role of the nuclear envelope in cellular
    organization. Cellular and Molecular Life Sciences. 63(3), 316–332.
  mla: D’Angelo, M. A., and Martin Hetzer. “The Role of the Nuclear Envelope in Cellular
    Organization.” <i>Cellular and Molecular Life Sciences</i>, vol. 63, no. 3, Springer
    Nature, 2006, pp. 316–32, doi:<a href="https://doi.org/10.1007/s00018-005-5361-3">10.1007/s00018-005-5361-3</a>.
  short: M.A. D’Angelo, M. Hetzer, Cellular and Molecular Life Sciences 63 (2006)
    316–332.
date_created: 2022-04-07T07:56:22Z
date_published: 2006-01-02T00:00:00Z
date_updated: 2024-10-14T11:30:38Z
day: '02'
doi: 10.1007/s00018-005-5361-3
extern: '1'
external_id:
  pmid:
  - '16389459'
intvolume: '        63'
issue: '3'
keyword:
- Cell Biology
- Cellular and Molecular Neuroscience
- Pharmacology
- Molecular Biology
- Molecular Medicine
language:
- iso: eng
month: '01'
oa_version: None
page: 316-332
pmid: 1
publication: Cellular and Molecular Life Sciences
publication_identifier:
  eissn:
  - 1420-9071
  issn:
  - 1420-682X
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: The role of the nuclear envelope in cellular organization
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 63
year: '2006'
...
