---
APC_amount: 1395,61 EUR
DOAJ_listed: '1'
OA_place: publisher
OA_type: gold
PlanS_conform: '1'
_id: '20370'
abstract:
- lang: eng
  text: The Huntingtin protein (HTT), named for its role in Huntington’s disease,
    has been best understood as a scaffolding protein that promotes vesicle transport
    by molecular motors along microtubules. Here, we show that HTT also interacts
    with the actin cytoskeleton, and its loss of function disturbs the morphology
    and function of the axonal growth cone. We demonstrate that HTT organizes F-actin
    into bundles. Cryo–electron tomography (cryo-ET) and subtomogram averaging (STA)
    structural analyses reveal that HTT’s N-terminal HEAT and Bridge domains wrap
    around F-actin, while the C-terminal HEAT domain is displaced; furthermore, HTT
    dimerizes via the N-HEAT domain to bridge parallel actin filaments separated by
    ~20 nanometers. Our study provides the structural basis for understanding how
    HTT interacts with and organizes the actin cytoskeleton.
acknowledgement: 'We thank C. Cuveillier, J. Delaroche, T. Ferraro, and A. Zanchi
  for help with TIRF experiments, electron microscopy preparation, data analysis,
  and cell cultures, respectively; A. Antkowiak, C. Bosc, C. Fassier, A. Fourest-Lieuvin,
  and V. Brandt for helpful discussions. We acknowledge the contribution of the Photonic
  Imaging Center of Grenoble Institute Neuroscience which is part of the ISdV core
  facility and certified by the IBiSA label and ICM.Quant (RRID:SCR_026393) core facility
  of the Paris Brain Institute (ICM); the AniRA lentivector production facility from
  the CELPHEDIA Infrastructure and SFR Biosciences (UAR3444/CNRS, US8/Inserm, ENS
  de Lyon, UCBL); the Scientific Service Units (SSUs) of ISTA through resources provided
  by Scientific Computing (SciComp, A. Schloegl and S. Elefante); and the Electron
  Microscopy Facility (EMF, V.V. Hodirnau). The software programs used for the processing
  were supported by SBGrid (www.sbgrid.org). This work was supported by the Agence
  Nationale pour la Recherche (AXYON: ANR-18-CE16-0009-01, S.H.), Austrian Science
  Fund (FWF) grants (P33367, F.K.M.S.; E435, J.M.H.), ChanZuckerberg Initiative (CZI)
  grant (DAF2021-234754, F.K.M.S.), Hereditary Disease Foundation Research Grant (HDF
  990846, M.C.), European Union (ERC: ActinID 101076260, F.K.M.S.), Fondation pour
  la Recherche Médicale (FRM: équipe labellisée DEQ202203014675, S.H.; PhD fellowship,
  FDT202001010865, R.C.), Korea Health Industry Development Institute (KHIDI) (Korea-Switzerland
  global research support grant: RS-2023-00266300, J.-J.S.), National Research Foundation
  (NRF) of Korea (Korea-Austria collaborative grant NRF-2019K1A3A1A181160, J.-J.S.
  and F.K.M.S.; NRF-2020R1A2B5B03001517 and RS-2024-00333346 and RS-2024-00436173,
  J.-J.S.; 2021R1C1C1006700, D.K.).'
article_number: eadw4124
article_processing_charge: Yes
article_type: original
author:
- first_name: Rémi
  full_name: Carpentier, Rémi
  last_name: Carpentier
- first_name: Jaesung
  full_name: Kim, Jaesung
  last_name: Kim
- first_name: Mariacristina
  full_name: Capizzi, Mariacristina
  last_name: Capizzi
- first_name: Hyeongju
  full_name: Kim, Hyeongju
  last_name: Kim
- first_name: Florian
  full_name: Fäßler, Florian
  id: 404F5528-F248-11E8-B48F-1D18A9856A87
  last_name: Fäßler
  orcid: 0000-0001-7149-769X
- first_name: Jesse
  full_name: Hansen, Jesse
  id: 1063c618-6f9b-11ec-9123-f912fccded63
  last_name: Hansen
  orcid: 0000-0001-7967-2085
- first_name: Min Jeong
  full_name: Kim, Min Jeong
  last_name: Kim
- first_name: Eric
  full_name: Denarier, Eric
  last_name: Denarier
- first_name: Béatrice
  full_name: Blot, Béatrice
  last_name: Blot
- first_name: Marine
  full_name: Degennaro, Marine
  last_name: Degennaro
- first_name: Sophia
  full_name: Labou, Sophia
  last_name: Labou
- first_name: Isabelle
  full_name: Arnal, Isabelle
  last_name: Arnal
- first_name: Maria J.
  full_name: Marcaida, Maria J.
  last_name: Marcaida
- first_name: Matteo Dal
  full_name: Peraro, Matteo Dal
  last_name: Peraro
- first_name: Doory
  full_name: Kim, Doory
  last_name: Kim
- first_name: Florian KM
  full_name: Schur, Florian KM
  id: 48AD8942-F248-11E8-B48F-1D18A9856A87
  last_name: Schur
  orcid: 0000-0003-4790-8078
- first_name: Ji-Joon
  full_name: Song, Ji-Joon
  last_name: Song
- first_name: Sandrine
  full_name: Humbert, Sandrine
  last_name: Humbert
citation:
  ama: Carpentier R, Kim J, Capizzi M, et al. Structure of the Huntingtin F-actin
    complex reveals its role in cytoskeleton organization. <i>Science Advances</i>.
    2025;11(38). doi:<a href="https://doi.org/10.1126/sciadv.adw4124">10.1126/sciadv.adw4124</a>
  apa: Carpentier, R., Kim, J., Capizzi, M., Kim, H., Fäßler, F., Hansen, J., … Humbert,
    S. (2025). Structure of the Huntingtin F-actin complex reveals its role in cytoskeleton
    organization. <i>Science Advances</i>. AAAS. <a href="https://doi.org/10.1126/sciadv.adw4124">https://doi.org/10.1126/sciadv.adw4124</a>
  chicago: Carpentier, Rémi, Jaesung Kim, Mariacristina Capizzi, Hyeongju Kim, Florian
    Fäßler, Jesse Hansen, Min Jeong Kim, et al. “Structure of the Huntingtin F-Actin
    Complex Reveals Its Role in Cytoskeleton Organization.” <i>Science Advances</i>.
    AAAS, 2025. <a href="https://doi.org/10.1126/sciadv.adw4124">https://doi.org/10.1126/sciadv.adw4124</a>.
  ieee: R. Carpentier <i>et al.</i>, “Structure of the Huntingtin F-actin complex
    reveals its role in cytoskeleton organization,” <i>Science Advances</i>, vol.
    11, no. 38. AAAS, 2025.
  ista: Carpentier R, Kim J, Capizzi M, Kim H, Fäßler F, Hansen J, Kim MJ, Denarier
    E, Blot B, Degennaro M, Labou S, Arnal I, Marcaida MJ, Peraro MD, Kim D, Schur
    FK, Song J-J, Humbert S. 2025. Structure of the Huntingtin F-actin complex reveals
    its role in cytoskeleton organization. Science Advances. 11(38), eadw4124.
  mla: Carpentier, Rémi, et al. “Structure of the Huntingtin F-Actin Complex Reveals
    Its Role in Cytoskeleton Organization.” <i>Science Advances</i>, vol. 11, no.
    38, eadw4124, AAAS, 2025, doi:<a href="https://doi.org/10.1126/sciadv.adw4124">10.1126/sciadv.adw4124</a>.
  short: R. Carpentier, J. Kim, M. Capizzi, H. Kim, F. Fäßler, J. Hansen, M.J. Kim,
    E. Denarier, B. Blot, M. Degennaro, S. Labou, I. Arnal, M.J. Marcaida, M.D. Peraro,
    D. Kim, F.K. Schur, J.-J. Song, S. Humbert, Science Advances 11 (2025).
corr_author: '1'
date_created: 2025-09-22T08:00:52Z
date_published: 2025-09-19T00:00:00Z
date_updated: 2026-05-20T08:20:27Z
day: '19'
ddc:
- '570'
department:
- _id: FlSc
doi: 10.1126/sciadv.adw4124
external_id:
  isi:
  - '001575751700013'
  pmid:
  - '40971423'
file:
- access_level: open_access
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  creator: dernst
  date_created: 2025-09-23T07:57:51Z
  date_updated: 2025-09-23T07:57:51Z
  file_id: '20372'
  file_name: 2025_ScienceAdvance_Carpentier.pdf
  file_size: 3599137
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  success: 1
file_date_updated: 2025-09-23T07:57:51Z
has_accepted_license: '1'
intvolume: '        11'
isi: 1
issue: '38'
language:
- iso: eng
month: '09'
oa: 1
oa_version: Published Version
pmid: 1
project:
- _id: 9B954C5C-BA93-11EA-9121-9846C619BF3A
  grant_number: P33367
  name: Structure and isoform diversity of the Arp2/3 complex
- _id: 7bd318a1-9f16-11ee-852c-cc9217763180
  grant_number: E435
  name: In Situ Actin Structures via Hybrid Cryo-electron Microscopy
- _id: 62909c6f-2b32-11ec-9570-e1476aab5308
  grant_number: CZI01
  name: CryoMinflux-guided in-situ molecular census and structure determination
- _id: bd980d18-d553-11ed-ba76-ceaa645c97eb
  grant_number: '101076260'
  name: A molecular atlas of Actin filament IDentities in the cell motility machinery
- _id: 3AC91DDA-15DF-11EA-824D-93A3E7B544D1
  call_identifier: FWF
  name: FWF Open Access Fund
publication: Science Advances
publication_identifier:
  issn:
  - 2375-2548
publication_status: published
publisher: AAAS
quality_controlled: '1'
scopus_import: '1'
status: public
title: Structure of the Huntingtin F-actin complex reveals its role in cytoskeleton
  organization
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: 11
year: '2025'
...
---
APC_amount: 11700 EUR
OA_place: publisher
OA_type: hybrid
_id: '14979'
abstract:
- lang: eng
  text: Poxviruses are among the largest double-stranded DNA viruses, with members
    such as variola virus, monkeypox virus and the vaccination strain vaccinia virus
    (VACV). Knowledge about the structural proteins that form the viral core has remained
    sparse. While major core proteins have been annotated via indirect experimental
    evidence, their structures have remained elusive and they could not be assigned
    to individual core features. Hence, which proteins constitute which layers of
    the core, such as the palisade layer and the inner core wall, has remained enigmatic.
    Here we show, using a multi-modal cryo-electron microscopy (cryo-EM) approach
    in combination with AlphaFold molecular modeling, that trimers formed by the cleavage
    product of VACV protein A10 are the key component of the palisade layer. This
    allows us to place previously obtained descriptions of protein interactions within
    the core wall into perspective and to provide a detailed model of poxvirus core
    architecture. Importantly, we show that interactions within A10 trimers are likely
    generalizable over members of orthopox- and parapoxviruses.
acknowledged_ssus:
- _id: ScienComp
- _id: LifeSc
- _id: EM-Fac
acknowledgement: "We thank A. Bergthaler (Research Center for Molecular Medicine of
  the Austrian Academy of Sciences) for providing VACV WR. We thank A. Nicholas and
  his team at the ISTA proteomics facility, and S. Elefante at the ISTA Scientific
  Computing facility for their support. We also thank F. Fäßler, D. Porley, T. Muthspiel
  and other members of the Schur group for support and helpful discussions. We also
  thank D. Castaño-Díez for support with Dynamo. We thank D. Farrell for his help
  optimizing the Rosetta protocol to refine the atomic model into the cryo-EM map
  with symmetry.\r\n\r\nF.K.M.S. acknowledges support from ISTA and EMBO. F.K.M.S.
  also received support from the Austrian Science Fund (FWF) grant P31445. This publication
  has been made possible in part by CZI grant DAF2021-234754 and grant https://doi.org/10.37921/812628ebpcwg
  from the Chan Zuckerberg Initiative DAF, an advised fund of Silicon Valley Community
  Foundation (funder https://doi.org/10.13039/100014989) awarded to F.K.M.S.\r\n\r\nThis
  research was also supported by the Scientific Service Units (SSUs) of ISTA through
  resources provided by Scientific Computing (SciComp), the Life Science Facility
  (LSF), and the Electron Microscopy Facility (EMF). We also acknowledge the use of
  COSMIC45 and Colabfold46."
article_processing_charge: Yes (in subscription journal)
article_type: original
author:
- first_name: Julia
  full_name: Datler, Julia
  id: 3B12E2E6-F248-11E8-B48F-1D18A9856A87
  last_name: Datler
  orcid: 0000-0002-3616-8580
- first_name: Jesse
  full_name: Hansen, Jesse
  id: 1063c618-6f9b-11ec-9123-f912fccded63
  last_name: Hansen
  orcid: 0000-0001-7967-2085
- first_name: Andreas
  full_name: Thader, Andreas
  id: 3A18A7B8-F248-11E8-B48F-1D18A9856A87
  last_name: Thader
- first_name: Alois
  full_name: Schlögl, Alois
  id: 45BF87EE-F248-11E8-B48F-1D18A9856A87
  last_name: Schlögl
  orcid: 0000-0002-5621-8100
- first_name: Lukas W
  full_name: Bauer, Lukas W
  id: 0c894dcf-897b-11ed-a09c-8186353224b0
  last_name: Bauer
- first_name: Victor-Valentin
  full_name: Hodirnau, Victor-Valentin
  id: 3661B498-F248-11E8-B48F-1D18A9856A87
  last_name: Hodirnau
  orcid: 0000-0003-3904-947X
- first_name: Florian KM
  full_name: Schur, Florian KM
  id: 48AD8942-F248-11E8-B48F-1D18A9856A87
  last_name: Schur
  orcid: 0000-0003-4790-8078
citation:
  ama: Datler J, Hansen J, Thader A, et al. Multi-modal cryo-EM reveals trimers of
    protein A10 to form the palisade layer in poxvirus cores. <i>Nature Structural
    &#38; Molecular Biology</i>. 2024;31:1114-1123. doi:<a href="https://doi.org/10.1038/s41594-023-01201-6">10.1038/s41594-023-01201-6</a>
  apa: Datler, J., Hansen, J., Thader, A., Schlögl, A., Bauer, L. W., Hodirnau, V.-V.,
    &#38; Schur, F. K. (2024). Multi-modal cryo-EM reveals trimers of protein A10
    to form the palisade layer in poxvirus cores. <i>Nature Structural &#38; Molecular
    Biology</i>. Springer Nature. <a href="https://doi.org/10.1038/s41594-023-01201-6">https://doi.org/10.1038/s41594-023-01201-6</a>
  chicago: Datler, Julia, Jesse Hansen, Andreas Thader, Alois Schlögl, Lukas W Bauer,
    Victor-Valentin Hodirnau, and Florian KM Schur. “Multi-Modal Cryo-EM Reveals Trimers
    of Protein A10 to Form the Palisade Layer in Poxvirus Cores.” <i>Nature Structural
    &#38; Molecular Biology</i>. Springer Nature, 2024. <a href="https://doi.org/10.1038/s41594-023-01201-6">https://doi.org/10.1038/s41594-023-01201-6</a>.
  ieee: J. Datler <i>et al.</i>, “Multi-modal cryo-EM reveals trimers of protein A10
    to form the palisade layer in poxvirus cores,” <i>Nature Structural &#38; Molecular
    Biology</i>, vol. 31. Springer Nature, pp. 1114–1123, 2024.
  ista: Datler J, Hansen J, Thader A, Schlögl A, Bauer LW, Hodirnau V-V, Schur FK.
    2024. Multi-modal cryo-EM reveals trimers of protein A10 to form the palisade
    layer in poxvirus cores. Nature Structural &#38; Molecular Biology. 31, 1114–1123.
  mla: Datler, Julia, et al. “Multi-Modal Cryo-EM Reveals Trimers of Protein A10 to
    Form the Palisade Layer in Poxvirus Cores.” <i>Nature Structural &#38; Molecular
    Biology</i>, vol. 31, Springer Nature, 2024, pp. 1114–23, doi:<a href="https://doi.org/10.1038/s41594-023-01201-6">10.1038/s41594-023-01201-6</a>.
  short: J. Datler, J. Hansen, A. Thader, A. Schlögl, L.W. Bauer, V.-V. Hodirnau,
    F.K. Schur, Nature Structural &#38; Molecular Biology 31 (2024) 1114–1123.
corr_author: '1'
date_created: 2024-02-12T09:59:45Z
date_published: 2024-07-01T00:00:00Z
date_updated: 2026-04-07T12:59:44Z
day: '01'
ddc:
- '570'
department:
- _id: FlSc
- _id: ScienComp
- _id: EM-Fac
doi: 10.1038/s41594-023-01201-6
external_id:
  isi:
  - '001158144600002'
  pmid:
  - '38316877'
file:
- access_level: open_access
  checksum: bda7bf65d81455480efaed8ca293b0db
  content_type: application/pdf
  creator: dernst
  date_created: 2024-07-22T11:27:22Z
  date_updated: 2024-07-22T11:27:22Z
  file_id: '17307'
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  file_size: 17485494
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  success: 1
file_date_updated: 2024-07-22T11:27:22Z
has_accepted_license: '1'
intvolume: '        31'
isi: 1
keyword:
- Molecular Biology
- Structural Biology
language:
- iso: eng
month: '07'
oa: 1
oa_version: Published Version
page: 1114-1123
pmid: 1
project:
- _id: 26736D6A-B435-11E9-9278-68D0E5697425
  call_identifier: FWF
  grant_number: P31445
  name: Structural conservation and diversity in retroviral capsid
publication: Nature Structural & Molecular Biology
publication_identifier:
  eissn:
  - 1545-9985
  issn:
  - 1545-9993
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
related_material:
  link:
  - description: News on ISTA Website
    relation: press_release
    url: https://ista.ac.at/en/news/down-to-the-core-of-poxviruses/
  record:
  - id: '18766'
    relation: dissertation_contains
    status: public
scopus_import: '1'
status: public
title: Multi-modal cryo-EM reveals trimers of protein A10 to form the palisade layer
  in poxvirus cores
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: 317138e5-6ab7-11ef-aa6d-ffef3953e345
volume: 31
year: '2024'
...
---
_id: '15146'
abstract:
- lang: eng
  text: The extracellular matrix (ECM) serves as a scaffold for cells and plays an
    essential role in regulating numerous cellular processes, including cell migration
    and proliferation. Due to limitations in specimen preparation for conventional
    room-temperature electron microscopy, we lack structural knowledge on how ECM
    components are secreted, remodeled, and interact with surrounding cells. We have
    developed a 3D-ECM platform compatible with sample thinning by cryo-focused ion
    beam milling, the lift-out extraction procedure, and cryo-electron tomography.
    Our workflow implements cell-derived matrices (CDMs) grown on EM grids, resulting
    in a versatile tool closely mimicking ECM environments. This allows us to visualize
    ECM for the first time in its hydrated, native context. Our data reveal an intricate
    network of extracellular fibers, their positioning relative to matrix-secreting
    cells, and previously unresolved structural entities. Our workflow and results
    add to the structural atlas of the ECM, providing novel insights into its secretion
    and assembly.
acknowledged_ssus:
- _id: LifeSc
- _id: ScienComp
- _id: EM-Fac
- _id: M-Shop
acknowledgement: "Open Access funding provided by IST Austria. We thank Armel Nicolas
  and his team at the ISTA proteomics facility, Alois Schloegl, Stefano Elefante,
  and colleagues at the ISTA Scientific Computing facility, Tommaso Constanzo and
  Ludek Lovicar at the Electron Microsocpy Facility (EMF), and Thomas Menner at the
  Miba Machine shop for their support. We also thank Wanda Kukulski (University of
  Bern) as well as Darío Porley, Andreas Thader, and other members of the Schur group
  for helpful discussions. Matt Swulius and Jessica Heebner provided great support
  in using Dragonfly. We thank Dorotea Fracciolla (Art & Science) for support in figure
  illustration.\r\n\r\nThis research was supported by the Scientific Service Units
  of ISTA through resources provided by Scientific Computing, the Lab Support Facility,
  and the Electron Microscopy Facility. We acknowledge funding support from the following
  sources: Austrian Science Fund (FWF) grant P33367 (to F.K.M. Schur), the Federation
  of European Biochemical Societies (to F.K.M. Schur), Niederösterreich (NÖ) Fonds
  (to B. Zens), FWF grant E435 (to J.M. Hansen), European Research Council under the
  European Union’s Horizon 2020 research (grant agreement No. 724373) (to M. Sixt),
  and Jenny and Antti Wihuri Foundation (to J. Alanko). This publication has been
  made possible in part by CZI grant DAF2021-234754 and grant DOI https://doi.org/10.37921/812628ebpcwg
  from the Chan Zuckerberg Initiative DAF, an advised fund of Silicon Valley Community
  Foundation (to F.K.M. Schur)."
article_number: e202309125
article_processing_charge: Yes (via OA deal)
article_type: original
author:
- first_name: Bettina
  full_name: Zens, Bettina
  id: 45FD126C-F248-11E8-B48F-1D18A9856A87
  last_name: Zens
  orcid: 0000-0002-9561-1239
- first_name: Florian
  full_name: Fäßler, Florian
  id: 404F5528-F248-11E8-B48F-1D18A9856A87
  last_name: Fäßler
  orcid: 0000-0001-7149-769X
- first_name: Jesse
  full_name: Hansen, Jesse
  id: 1063c618-6f9b-11ec-9123-f912fccded63
  last_name: Hansen
  orcid: 0000-0001-7967-2085
- first_name: Robert
  full_name: Hauschild, Robert
  id: 4E01D6B4-F248-11E8-B48F-1D18A9856A87
  last_name: Hauschild
  orcid: 0000-0001-9843-3522
- first_name: Julia
  full_name: Datler, Julia
  id: 3B12E2E6-F248-11E8-B48F-1D18A9856A87
  last_name: Datler
  orcid: 0000-0002-3616-8580
- first_name: Victor-Valentin
  full_name: Hodirnau, Victor-Valentin
  id: 3661B498-F248-11E8-B48F-1D18A9856A87
  last_name: Hodirnau
  orcid: 0000-0003-3904-947X
- first_name: Vanessa
  full_name: Zheden, Vanessa
  id: 39C5A68A-F248-11E8-B48F-1D18A9856A87
  last_name: Zheden
  orcid: 0000-0002-9438-4783
- first_name: Jonna H
  full_name: Alanko, Jonna H
  id: 2CC12E8C-F248-11E8-B48F-1D18A9856A87
  last_name: Alanko
  orcid: 0000-0002-7698-3061
- first_name: Michael K
  full_name: Sixt, Michael K
  id: 41E9FBEA-F248-11E8-B48F-1D18A9856A87
  last_name: Sixt
  orcid: 0000-0002-6620-9179
- first_name: Florian KM
  full_name: Schur, Florian KM
  id: 48AD8942-F248-11E8-B48F-1D18A9856A87
  last_name: Schur
  orcid: 0000-0003-4790-8078
citation:
  ama: Zens B, Fäßler F, Hansen J, et al. Lift-out cryo-FIBSEM and cryo-ET reveal
    the ultrastructural landscape of extracellular matrix. <i>Journal of Cell Biology</i>.
    2024;223(6). doi:<a href="https://doi.org/10.1083/jcb.202309125">10.1083/jcb.202309125</a>
  apa: Zens, B., Fäßler, F., Hansen, J., Hauschild, R., Datler, J., Hodirnau, V.-V.,
    … Schur, F. K. (2024). Lift-out cryo-FIBSEM and cryo-ET reveal the ultrastructural
    landscape of extracellular matrix. <i>Journal of Cell Biology</i>. Rockefeller
    University Press. <a href="https://doi.org/10.1083/jcb.202309125">https://doi.org/10.1083/jcb.202309125</a>
  chicago: Zens, Bettina, Florian Fäßler, Jesse Hansen, Robert Hauschild, Julia Datler,
    Victor-Valentin Hodirnau, Vanessa Zheden, Jonna H Alanko, Michael K Sixt, and
    Florian KM Schur. “Lift-out Cryo-FIBSEM and Cryo-ET Reveal the Ultrastructural
    Landscape of Extracellular Matrix.” <i>Journal of Cell Biology</i>. Rockefeller
    University Press, 2024. <a href="https://doi.org/10.1083/jcb.202309125">https://doi.org/10.1083/jcb.202309125</a>.
  ieee: B. Zens <i>et al.</i>, “Lift-out cryo-FIBSEM and cryo-ET reveal the ultrastructural
    landscape of extracellular matrix,” <i>Journal of Cell Biology</i>, vol. 223,
    no. 6. Rockefeller University Press, 2024.
  ista: Zens B, Fäßler F, Hansen J, Hauschild R, Datler J, Hodirnau V-V, Zheden V,
    Alanko JH, Sixt MK, Schur FK. 2024. Lift-out cryo-FIBSEM and cryo-ET reveal the
    ultrastructural landscape of extracellular matrix. Journal of Cell Biology. 223(6),
    e202309125.
  mla: Zens, Bettina, et al. “Lift-out Cryo-FIBSEM and Cryo-ET Reveal the Ultrastructural
    Landscape of Extracellular Matrix.” <i>Journal of Cell Biology</i>, vol. 223,
    no. 6, e202309125, Rockefeller University Press, 2024, doi:<a href="https://doi.org/10.1083/jcb.202309125">10.1083/jcb.202309125</a>.
  short: B. Zens, F. Fäßler, J. Hansen, R. Hauschild, J. Datler, V.-V. Hodirnau, V.
    Zheden, J.H. Alanko, M.K. Sixt, F.K. Schur, Journal of Cell Biology 223 (2024).
corr_author: '1'
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title: Lift-out cryo-FIBSEM and cryo-ET reveal the ultrastructural landscape of extracellular
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