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The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.

Virus membrane-fusion proteins: more than one way to make a hairpin

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Kielian, Margaret, Rey, Félix A.·2006·Nature Reviews Microbiology

Abstract

Structure–function studies have defined two classes of viral membrane-fusion proteins that have radically different architectures but adopt a similar overall 'hairpin' conformation to induce fusion of the viral and cellular membranes and therefore initiate infection. In both classes, the hairpin conformation is achieved after a conformational change is triggered by interaction with the target cell. This review will focus in particular on the properties of the more recently described class II proteins.

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Metadata

Authors
Kielian, M., & Rey, F. A.
Venue
Nature Reviews Microbiology
Published
2006-01-01
Volume
4
Issue
1
Pages
67-76
ISSN
  • 1740-1526 (ISSN-L)
  • 1740-1534
OpenAlex
W2091001172
Cited by
570
References
3
FWCI
3.87
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Virus membrane-fusion proteins: more than one way to make a hairpin. https://app.cochat.ai/papers/10.1038/nrmicro1326
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Kielian, M., & Rey, F. A. (2006). Virus membrane-fusion proteins: more than one way to make a hairpin. Nature Reviews Microbiology. https://doi.org/10.1038/nrmicro1326

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.