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Cited by 229

The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.

Catalysis of cis/trans isomerization in native HIV-1 capsid by human cyclophilin A

Open access
Bosco, Daryl A., Eisenmesser, Elan Z., Pochapsky, Susan, Sundquist, Wesley I., Kern, Dorothee·2002·Proceedings of the National Academy of Sciences

Abstract

Packaging of cyclophilin A (CypA) into HIV-1 virions is essential for efficient replication; however, the reason for this is unknown. Incorporation is mediated through binding to the Gly-89–Pro-90 peptide bond of the N-terminal domain of HIV-1 capsid (CA N ). Despite the fact that CypA is a peptidyl-prolyl cis/trans isomerase, catalytic activity on CA N has not been observed previously. We show here, using NMR exchange spectroscopy, that CypA does not only bind to CA N but also catalyzes efficiently the cis/trans isomerization of the Gly-89–Pro-90 peptide bond. In addition, conformational changes in CA N distal to the CypA binding loop are observed on CypA binding and catalysis. The results provide experimental evidence for efficient CypA catalysis on a natively folded and biologically relevant protein substrate.

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Metadata

Authors
Bosco, D. A., Eisenmesser, E. Z., Pochapsky, S., Sundquist, W. I., & Kern, D.
Venue
Proceedings of the National Academy of Sciences
Published
2002-04-02
Volume
99
Issue
8
Pages
5247-5252
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W1975534778
Cited by
229
References
5
FWCI
4.32
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Catalysis of cis/trans isomerization in native HIV-1 capsid by human cyclophilin A. https://app.cochat.ai/papers/10.1073/pnas.082100499
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Bosco, D. A., Eisenmesser, E. Z., Pochapsky, S., Sundquist, W. I., & Kern, D. (2002). Catalysis of cis/trans isomerization in native HIV-1 capsid by human cyclophilin A. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.082100499

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