Journal article
Crystal structure of the Herpesvirus nuclear egress complex provides insights into inner nuclear membrane remodeling.
- Abstract:
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Although nucleo-cytoplasmic transport is typically mediated through nuclear pore complexes, herpesvirus capsids exit the nucleus via a unique vesicular pathway. Together, the conserved herpesvirus proteins pUL31 and pUL34 form the heterodimeric nuclear egress complex (NEC), which, in turn, mediates the formation of tight-fitting membrane vesicles around capsids at the inner nuclear membrane. Here, we present the crystal structure of the pseudorabies virus NEC. The structure revealed that a zi...
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- Publication status:
- Published
- Peer review status:
- Peer reviewed
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(Version of record, pdf, 3.4MB)
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- Publisher copy:
- 10.1016/j.celrep.2015.11.008
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Authors
Funding
São Paulo Research Foundation
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Max Planck Society
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Bibliographic Details
- Publisher:
- Elsevier Publisher's website
- Journal:
- Cell reports Journal website
- Volume:
- 13
- Issue:
- 12
- Pages:
- 2645-2652
- Publication date:
- 2015-12-16
- DOI:
- EISSN:
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2211-1247
- ISSN:
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2211-1247
- Source identifiers:
-
587363
Item Description
- Language:
- English
- Pubs id:
-
pubs:587363
- UUID:
-
uuid:c2748706-a680-4788-b66c-da69bd008cb6
- Local pid:
- pubs:587363
- Deposit date:
- 2016-02-01
Terms of use
- Copyright holder:
- Zeev-Ben-Mordehai et al
- Copyright date:
- 2015
- Notes:
- Copyright © 2015 The Authors. Published by Elsevier Inc. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
- Licence:
- CC Attribution (CC BY)
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