---
_id: '14795'
abstract:
- lang: eng
text: Metazoan development relies on the formation and remodeling of cell-cell contacts.
Dynamic reorganization of adhesion receptors and the actomyosin cell cortex in
space and time plays a central role in cell-cell contact formation and maturation.
Nevertheless, how this process is mechanistically achieved when new contacts are
formed remains unclear. Here, by building a biomimetic assay composed of progenitor
cells adhering to supported lipid bilayers functionalized with E-cadherin ectodomains,
we show that cortical F-actin flows, driven by the depletion of myosin-2 at the
cell contact center, mediate the dynamic reorganization of adhesion receptors
and cell cortex at the contact. E-cadherin-dependent downregulation of the small
GTPase RhoA at the forming contact leads to both a depletion of myosin-2 and a
decrease of F-actin at the contact center. At the contact rim, in contrast, myosin-2
becomes enriched by the retraction of bleb-like protrusions, resulting in a cortical
tension gradient from the contact rim to its center. This tension gradient, in
turn, triggers centrifugal F-actin flows, leading to further accumulation of F-actin
at the contact rim and the progressive redistribution of E-cadherin from the contact
center to the rim. Eventually, this combination of actomyosin downregulation and
flows at the contact determines the characteristic molecular organization, with
E-cadherin and F-actin accumulating at the contact rim, where they are needed
to mechanically link the contractile cortices of the adhering cells.
acknowledged_ssus:
- _id: Bio
- _id: PreCl
acknowledgement: "We are grateful to Edwin Munro for their feedback and help with
the single particle analysis. We thank members of the Heisenberg and Loose labs
for their help and feedback on the manuscript, notably Xin Tong for making the PCS2-mCherry-AHPH
plasmid. Finally, we thank the Aquatics and Imaging & Optics facilities of ISTA
for their continuous support, especially Yann Cesbron for assistance with the laser
cutter. This work was supported by an ERC\r\nAdvanced Grant (MECSPEC) to C.-P.H."
article_processing_charge: Yes (via OA deal)
article_type: original
author:
- first_name: Feyza N
full_name: Arslan, Feyza N
id: 49DA7910-F248-11E8-B48F-1D18A9856A87
last_name: Arslan
orcid: 0000-0001-5809-9566
- first_name: Edouard B
full_name: Hannezo, Edouard B
id: 3A9DB764-F248-11E8-B48F-1D18A9856A87
last_name: Hannezo
orcid: 0000-0001-6005-1561
- first_name: Jack
full_name: Merrin, Jack
id: 4515C308-F248-11E8-B48F-1D18A9856A87
last_name: Merrin
orcid: 0000-0001-5145-4609
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
- first_name: Carl-Philipp J
full_name: Heisenberg, Carl-Philipp J
id: 39427864-F248-11E8-B48F-1D18A9856A87
last_name: Heisenberg
orcid: 0000-0002-0912-4566
citation:
ama: Arslan FN, Hannezo EB, Merrin J, Loose M, Heisenberg C-PJ. Adhesion-induced
cortical flows pattern E-cadherin-mediated cell contacts. Current Biology.
2024;34(1):171-182.e8. doi:10.1016/j.cub.2023.11.067
apa: Arslan, F. N., Hannezo, E. B., Merrin, J., Loose, M., & Heisenberg, C.-P.
J. (2024). Adhesion-induced cortical flows pattern E-cadherin-mediated cell contacts.
Current Biology. Elsevier. https://doi.org/10.1016/j.cub.2023.11.067
chicago: Arslan, Feyza N, Edouard B Hannezo, Jack Merrin, Martin Loose, and Carl-Philipp
J Heisenberg. “Adhesion-Induced Cortical Flows Pattern E-Cadherin-Mediated Cell
Contacts.” Current Biology. Elsevier, 2024. https://doi.org/10.1016/j.cub.2023.11.067.
ieee: F. N. Arslan, E. B. Hannezo, J. Merrin, M. Loose, and C.-P. J. Heisenberg,
“Adhesion-induced cortical flows pattern E-cadherin-mediated cell contacts,” Current
Biology, vol. 34, no. 1. Elsevier, p. 171–182.e8, 2024.
ista: Arslan FN, Hannezo EB, Merrin J, Loose M, Heisenberg C-PJ. 2024. Adhesion-induced
cortical flows pattern E-cadherin-mediated cell contacts. Current Biology. 34(1),
171–182.e8.
mla: Arslan, Feyza N., et al. “Adhesion-Induced Cortical Flows Pattern E-Cadherin-Mediated
Cell Contacts.” Current Biology, vol. 34, no. 1, Elsevier, 2024, p. 171–182.e8,
doi:10.1016/j.cub.2023.11.067.
short: F.N. Arslan, E.B. Hannezo, J. Merrin, M. Loose, C.-P.J. Heisenberg, Current
Biology 34 (2024) 171–182.e8.
date_created: 2024-01-14T23:00:56Z
date_published: 2024-01-08T00:00:00Z
date_updated: 2024-01-17T08:20:40Z
day: '08'
ddc:
- '570'
department:
- _id: CaHe
- _id: EdHa
- _id: MaLo
- _id: NanoFab
doi: 10.1016/j.cub.2023.11.067
ec_funded: 1
file:
- access_level: open_access
checksum: 51220b76d72a614208f84bdbfbaf9b72
content_type: application/pdf
creator: dernst
date_created: 2024-01-16T10:53:31Z
date_updated: 2024-01-16T10:53:31Z
file_id: '14813'
file_name: 2024_CurrentBiology_Arslan.pdf
file_size: 5183861
relation: main_file
success: 1
file_date_updated: 2024-01-16T10:53:31Z
has_accepted_license: '1'
intvolume: ' 34'
issue: '1'
language:
- iso: eng
month: '01'
oa: 1
oa_version: Published Version
page: 171-182.e8
project:
- _id: 260F1432-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '742573'
name: Interaction and feedback between cell mechanics and fate specification in
vertebrate gastrulation
publication: Current Biology
publication_identifier:
eissn:
- 1879-0445
issn:
- 0960-9822
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Adhesion-induced cortical flows pattern E-cadherin-mediated cell contacts
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: 34
year: '2024'
...
---
_id: '15018'
abstract:
- lang: eng
text: The epitaxial growth of a strained Ge layer, which is a promising candidate
for the channel material of a hole spin qubit, has been demonstrated on 300 mm
Si wafers using commercially available Si0.3Ge0.7 strain relaxed buffer (SRB)
layers. The assessment of the layer and the interface qualities for a buried strained
Ge layer embedded in Si0.3Ge0.7 layers is reported. The XRD reciprocal space mapping
confirmed that the reduction of the growth temperature enables the 2-dimensional
growth of the Ge layer fully strained with respect to the Si0.3Ge0.7. Nevertheless,
dislocations at the top and/or bottom interface of the Ge layer were observed
by means of electron channeling contrast imaging, suggesting the importance of
the careful dislocation assessment. The interface abruptness does not depend on
the selection of the precursor gases, but it is strongly influenced by the growth
temperature which affects the coverage of the surface H-passivation. The mobility
of 2.7 × 105 cm2/Vs is promising, while the low percolation density of 3 × 1010
/cm2 measured with a Hall-bar device at 7 K illustrates the high quality of the
heterostructure thanks to the high Si0.3Ge0.7 SRB quality.
acknowledgement: The Ge project received funding from the European Union's Horizon
Europe programme under the Grant Agreement 101069515 – IGNITE. Siltronic AG is acknowledged
for providing the SRB wafers. This work was supported by Imec's Industrial Affiliation
Program on Quantum Computing.
article_number: '108231'
article_processing_charge: No
article_type: original
author:
- first_name: Yosuke
full_name: Shimura, Yosuke
last_name: Shimura
- first_name: Clement
full_name: Godfrin, Clement
last_name: Godfrin
- first_name: Andriy
full_name: Hikavyy, Andriy
last_name: Hikavyy
- first_name: Roy
full_name: Li, Roy
last_name: Li
- first_name: Juan L
full_name: Aguilera Servin, Juan L
id: 2A67C376-F248-11E8-B48F-1D18A9856A87
last_name: Aguilera Servin
orcid: 0000-0002-2862-8372
- first_name: Georgios
full_name: Katsaros, Georgios
id: 38DB5788-F248-11E8-B48F-1D18A9856A87
last_name: Katsaros
orcid: 0000-0001-8342-202X
- first_name: Paola
full_name: Favia, Paola
last_name: Favia
- first_name: Han
full_name: Han, Han
last_name: Han
- first_name: Danny
full_name: Wan, Danny
last_name: Wan
- first_name: Kristiaan
full_name: de Greve, Kristiaan
last_name: de Greve
- first_name: Roger
full_name: Loo, Roger
last_name: Loo
citation:
ama: Shimura Y, Godfrin C, Hikavyy A, et al. Compressively strained epitaxial Ge
layers for quantum computing applications. Materials Science in Semiconductor
Processing. 2024;174(5). doi:10.1016/j.mssp.2024.108231
apa: Shimura, Y., Godfrin, C., Hikavyy, A., Li, R., Aguilera Servin, J. L., Katsaros,
G., … Loo, R. (2024). Compressively strained epitaxial Ge layers for quantum computing
applications. Materials Science in Semiconductor Processing. Elsevier.
https://doi.org/10.1016/j.mssp.2024.108231
chicago: Shimura, Yosuke, Clement Godfrin, Andriy Hikavyy, Roy Li, Juan L Aguilera
Servin, Georgios Katsaros, Paola Favia, et al. “Compressively Strained Epitaxial
Ge Layers for Quantum Computing Applications.” Materials Science in Semiconductor
Processing. Elsevier, 2024. https://doi.org/10.1016/j.mssp.2024.108231.
ieee: Y. Shimura et al., “Compressively strained epitaxial Ge layers for
quantum computing applications,” Materials Science in Semiconductor Processing,
vol. 174, no. 5. Elsevier, 2024.
ista: Shimura Y, Godfrin C, Hikavyy A, Li R, Aguilera Servin JL, Katsaros G, Favia
P, Han H, Wan D, de Greve K, Loo R. 2024. Compressively strained epitaxial Ge
layers for quantum computing applications. Materials Science in Semiconductor
Processing. 174(5), 108231.
mla: Shimura, Yosuke, et al. “Compressively Strained Epitaxial Ge Layers for Quantum
Computing Applications.” Materials Science in Semiconductor Processing,
vol. 174, no. 5, 108231, Elsevier, 2024, doi:10.1016/j.mssp.2024.108231.
short: Y. Shimura, C. Godfrin, A. Hikavyy, R. Li, J.L. Aguilera Servin, G. Katsaros,
P. Favia, H. Han, D. Wan, K. de Greve, R. Loo, Materials Science in Semiconductor
Processing 174 (2024).
date_created: 2024-02-22T14:10:40Z
date_published: 2024-02-20T00:00:00Z
date_updated: 2024-02-26T10:36:35Z
day: '20'
ddc:
- '530'
department:
- _id: GeKa
- _id: NanoFab
doi: 10.1016/j.mssp.2024.108231
has_accepted_license: '1'
intvolume: ' 174'
issue: '5'
keyword:
- Mechanical Engineering
- Mechanics of Materials
- Condensed Matter Physics
- General Materials Science
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.mssp.2024.108231
month: '02'
oa: 1
oa_version: Published Version
project:
- _id: 34c0acea-11ca-11ed-8bc3-8775e10fd452
grant_number: '101069515'
name: Integrated GermaNIum quanTum tEchnology
publication: Materials Science in Semiconductor Processing
publication_identifier:
issn:
- 1369-8001
publication_status: epub_ahead
publisher: Elsevier
quality_controlled: '1'
status: public
title: Compressively strained epitaxial Ge layers for quantum computing applications
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: 174
year: '2024'
...
---
_id: '15048'
abstract:
- lang: eng
text: Embryogenesis results from the coordinated activities of different signaling
pathways controlling cell fate specification and morphogenesis. In vertebrate
gastrulation, both Nodal and BMP signaling play key roles in germ layer specification
and morphogenesis, yet their interplay to coordinate embryo patterning with morphogenesis
is still insufficiently understood. Here, we took a reductionist approach using
zebrafish embryonic explants to study the coordination of Nodal and BMP signaling
for embryo patterning and morphogenesis. We show that Nodal signaling triggers
explant elongation by inducing mesendodermal progenitors but also suppressing
BMP signaling activity at the site of mesendoderm induction. Consistent with this,
ectopic BMP signaling in the mesendoderm blocks cell alignment and oriented mesendoderm
intercalations, key processes during explant elongation. Translating these ex
vivo observations to the intact embryo showed that, similar to explants, Nodal
signaling suppresses the effect of BMP signaling on cell intercalations in the
dorsal domain, thus allowing robust embryonic axis elongation. These findings
suggest a dual function of Nodal signaling in embryonic axis elongation by both
inducing mesendoderm and suppressing BMP effects in the dorsal portion of the
mesendoderm.
acknowledged_ssus:
- _id: Bio
- _id: LifeSc
acknowledgement: "We thank Patrick Müller for sharing the chordintt250 mutant zebrafish
line as well as the plasmid for chrd-GFP, Katherine Rogers for sharing the bmp2b
plasmid and Andrea Pauli for sharing the draculin plasmid. Diana Pinheiro generated
the MZlefty1,2;Tg(sebox::EGFP) line. We are grateful to Patrick Müller, Diana Pinheiro
and Katherine Rogers and members of the Heisenberg lab for discussions, technical
advice and feedback on the manuscript. We also thank Anna Kicheva and Edouard Hannezo
for discussions. We thank the Imaging and Optics Facility as well as the Life Science
facility at IST Austria for support with microscopy and fish maintenance.\r\nThis
work was supported by a European Research Council Advanced Grant\r\n(MECSPEC 742573
to C.-P.H.). A.S. is a recipient of a DOC Fellowship of the Austrian\r\nAcademy
of Sciences at IST Austria. Open Access funding provided by Institute of\r\nScience
and Technology Austria. "
article_processing_charge: Yes (via OA deal)
article_type: original
author:
- first_name: Alexandra
full_name: Schauer, Alexandra
id: 30A536BA-F248-11E8-B48F-1D18A9856A87
last_name: Schauer
orcid: 0000-0001-7659-9142
- first_name: Kornelija
full_name: Pranjic-Ferscha, Kornelija
id: 4362B3C2-F248-11E8-B48F-1D18A9856A87
last_name: Pranjic-Ferscha
- first_name: Robert
full_name: Hauschild, Robert
id: 4E01D6B4-F248-11E8-B48F-1D18A9856A87
last_name: Hauschild
orcid: 0000-0001-9843-3522
- first_name: Carl-Philipp J
full_name: Heisenberg, Carl-Philipp J
id: 39427864-F248-11E8-B48F-1D18A9856A87
last_name: Heisenberg
orcid: 0000-0002-0912-4566
citation:
ama: Schauer A, Pranjic-Ferscha K, Hauschild R, Heisenberg C-PJ. Robust axis elongation
by Nodal-dependent restriction of BMP signaling. Development. 2024;151(4):1-18.
doi:10.1242/dev.202316
apa: Schauer, A., Pranjic-Ferscha, K., Hauschild, R., & Heisenberg, C.-P. J.
(2024). Robust axis elongation by Nodal-dependent restriction of BMP signaling.
Development. The Company of Biologists. https://doi.org/10.1242/dev.202316
chicago: Schauer, Alexandra, Kornelija Pranjic-Ferscha, Robert Hauschild, and Carl-Philipp
J Heisenberg. “Robust Axis Elongation by Nodal-Dependent Restriction of BMP Signaling.”
Development. The Company of Biologists, 2024. https://doi.org/10.1242/dev.202316.
ieee: A. Schauer, K. Pranjic-Ferscha, R. Hauschild, and C.-P. J. Heisenberg, “Robust
axis elongation by Nodal-dependent restriction of BMP signaling,” Development,
vol. 151, no. 4. The Company of Biologists, pp. 1–18, 2024.
ista: Schauer A, Pranjic-Ferscha K, Hauschild R, Heisenberg C-PJ. 2024. Robust axis
elongation by Nodal-dependent restriction of BMP signaling. Development. 151(4),
1–18.
mla: Schauer, Alexandra, et al. “Robust Axis Elongation by Nodal-Dependent Restriction
of BMP Signaling.” Development, vol. 151, no. 4, The Company of Biologists,
2024, pp. 1–18, doi:10.1242/dev.202316.
short: A. Schauer, K. Pranjic-Ferscha, R. Hauschild, C.-P.J. Heisenberg, Development
151 (2024) 1–18.
date_created: 2024-03-03T23:00:50Z
date_published: 2024-02-01T00:00:00Z
date_updated: 2024-03-04T07:28:25Z
day: '01'
ddc:
- '570'
department:
- _id: CaHe
- _id: Bio
doi: 10.1242/dev.202316
ec_funded: 1
file:
- access_level: open_access
checksum: 6961ea10012bf0d266681f9628bb8f13
content_type: application/pdf
creator: dernst
date_created: 2024-03-04T07:24:43Z
date_updated: 2024-03-04T07:24:43Z
file_id: '15050'
file_name: 2024_Development_Schauer.pdf
file_size: 14839986
relation: main_file
success: 1
file_date_updated: 2024-03-04T07:24:43Z
has_accepted_license: '1'
intvolume: ' 151'
issue: '4'
language:
- iso: eng
month: '02'
oa: 1
oa_version: Published Version
page: 1-18
project:
- _id: 260F1432-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '742573'
name: Interaction and feedback between cell mechanics and fate specification in
vertebrate gastrulation
- _id: 26B1E39C-B435-11E9-9278-68D0E5697425
grant_number: '25239'
name: 'Mesendoderm specification in zebrafish: The role of extraembryonic tissues'
publication: Development
publication_identifier:
eissn:
- 1477-9129
issn:
- 0950-1991
publication_status: published
publisher: The Company of Biologists
quality_controlled: '1'
related_material:
record:
- id: '14926'
relation: research_data
status: public
scopus_import: '1'
status: public
title: Robust axis elongation by Nodal-dependent restriction of BMP signaling
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: 151
year: '2024'
...
---
_id: '14926'
author:
- first_name: Robert
full_name: Hauschild, Robert
id: 4E01D6B4-F248-11E8-B48F-1D18A9856A87
last_name: Hauschild
orcid: 0000-0001-9843-3522
citation:
ama: Hauschild R. Matlab script for analysis of clone dispersal. 2024. doi:10.15479/AT:ISTA:14926
apa: Hauschild, R. (2024). Matlab script for analysis of clone dispersal. ISTA.
https://doi.org/10.15479/AT:ISTA:14926
chicago: Hauschild, Robert. “Matlab Script for Analysis of Clone Dispersal.” ISTA,
2024. https://doi.org/10.15479/AT:ISTA:14926.
ieee: R. Hauschild, “Matlab script for analysis of clone dispersal.” ISTA, 2024.
ista: Hauschild R. 2024. Matlab script for analysis of clone dispersal, ISTA, 10.15479/AT:ISTA:14926.
mla: Hauschild, Robert. Matlab Script for Analysis of Clone Dispersal. ISTA,
2024, doi:10.15479/AT:ISTA:14926.
short: R. Hauschild, (2024).
date_created: 2024-02-02T14:42:26Z
date_published: 2024-02-02T00:00:00Z
date_updated: 2024-03-04T07:28:25Z
day: '02'
ddc:
- '570'
department:
- _id: Bio
doi: 10.15479/AT:ISTA:14926
file:
- access_level: open_access
checksum: df7f358ae19a176cf710c0a802ce31b1
content_type: application/octet-stream
creator: rhauschild
date_created: 2024-02-02T14:40:31Z
date_updated: 2024-02-02T14:40:31Z
file_id: '14927'
file_name: README.md
file_size: 736
relation: main_file
success: 1
- access_level: open_access
checksum: 10194cc11619eccd8f4b24472e465b7f
content_type: application/x-zip-compressed
creator: rhauschild
date_created: 2024-02-02T14:40:31Z
date_updated: 2024-02-02T14:40:31Z
file_id: '14928'
file_name: Supplementary_file_1.zip
file_size: 3543
relation: main_file
success: 1
file_date_updated: 2024-02-02T14:40:31Z
has_accepted_license: '1'
license: https://opensource.org/licenses/MIT
month: '02'
oa: 1
publisher: ISTA
related_material:
record:
- id: '15048'
relation: used_in_publication
status: public
status: public
title: Matlab script for analysis of clone dispersal
tmp:
legal_code_url: https://opensource.org/licenses/MIT
name: The MIT License
short: MIT
type: software
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2024'
...
---
_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
- 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
- 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. Nature Structural
& Molecular Biology. 2024. doi:10.1038/s41594-023-01201-6
apa: Datler, J., Hansen, J., Thader, A., Schlögl, A., Bauer, L. W., Hodirnau, V.-V.,
& Schur, F. K. (2024). Multi-modal cryo-EM reveals trimers of protein A10
to form the palisade layer in poxvirus cores. Nature Structural & Molecular
Biology. Springer Nature. https://doi.org/10.1038/s41594-023-01201-6
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.” Nature Structural
& Molecular Biology. Springer Nature, 2024. https://doi.org/10.1038/s41594-023-01201-6.
ieee: J. Datler et al., “Multi-modal cryo-EM reveals trimers of protein A10
to form the palisade layer in poxvirus cores,” Nature Structural & Molecular
Biology. Springer Nature, 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 & Molecular Biology.
mla: Datler, Julia, et al. “Multi-Modal Cryo-EM Reveals Trimers of Protein A10 to
Form the Palisade Layer in Poxvirus Cores.” Nature Structural & Molecular
Biology, Springer Nature, 2024, doi:10.1038/s41594-023-01201-6.
short: J. Datler, J. Hansen, A. Thader, A. Schlögl, L.W. Bauer, V.-V. Hodirnau,
F.K. Schur, Nature Structural & Molecular Biology (2024).
date_created: 2024-02-12T09:59:45Z
date_published: 2024-02-05T00:00:00Z
date_updated: 2024-03-05T09:27:47Z
day: '05'
ddc:
- '570'
department:
- _id: FlSc
- _id: ScienComp
- _id: EM-Fac
doi: 10.1038/s41594-023-01201-6
external_id:
pmid:
- '38316877'
has_accepted_license: '1'
keyword:
- Molecular Biology
- Structural Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1038/s41594-023-01201-6
month: '02'
oa: 1
oa_version: Published Version
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: epub_ahead
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/
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: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2024'
...