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Cited by 290

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

Insights into SARS-CoV transcription and replication from the structure of the nsp7–nsp8 hexadecamer

Open access
Zhai, Yujia, Sun, Fei, Li, Xuemei, Pang, Hai, Xu, Xiaoling, Bartlam, Mark, Rao, Zihe·2005·Nature Structural & Molecular Biology

Abstract

Coronavirus replication and transcription machinery involves multiple virus-encoded nonstructural proteins (nsp). We report the crystal structure of the hexadecameric nsp7–nsp8 supercomplex from the severe acute respiratory syndrome coronavirus at 2.4-Å resolution. nsp8 has a novel 'golf-club' fold with two conformations. The supercomplex is a unique hollow, cylinder-like structure assembled from eight copies of nsp8 and held tightly together by eight copies of nsp7. With an internal diameter of ∼30 Å, the central channel has dimensions and positive electrostatic properties favorable for nucleic acid binding, implying that its role is to confer processivity on RNA-dependent RNA polymerase.

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Metadata

Authors
Zhai, Y., Sun, F., Li, X., Pang, H., Xu, X., Bartlam, M., & Rao, Z.
Venue
Nature Structural & Molecular Biology
Published
2005-10-16
Volume
12
Issue
11
Pages
980-986
ISSN
  • 1545-9985 (ISSN-L)
  • 1545-9993
OpenAlex
W2134092129
Cited by
290
References
3
FWCI
10.20
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Insights into SARS-CoV transcription and replication from the structure of the nsp7–nsp8 hexadecamer. https://app.cochat.ai/papers/10.1038/nsmb999
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Zhai, Y., Sun, F., Li, X., Pang, H., Xu, X., Bartlam, M., & Rao, Z. (2005). Insights into SARS-CoV transcription and replication from the structure of the nsp7–nsp8 hexadecamer. Nature Structural & Molecular Biology. https://doi.org/10.1038/nsmb999

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