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Cited by 804

The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.

Structure of the C-Terminal Region of p21WAF1/CIP1 Complexed with Human PCNA

Open access
Gulbis, Jacqueline M, Kelman, Zvi, Hurwitz, Jerard, O'Donnell, Mike, Kuriyan, John·1996·Cell

Abstract

The crystal structure of the human DNA polymerase delta processivity factor PCNA (proliferating cell nuclear antigen) complexed with a 22 residue peptide derived from the C-terminus of the cell-cycle checkpoint protein p21(WAF1/CIP1) has been determined at 2.6 angstrom resolution. p21 binds to PCNA in a 1:1 stoichiometry with an extensive array of interactions that include the formation of a beta sheet with the interdomain connector loop of PCNA. An intact trimeric ring is maintained in the structure of the p21-PCNA complex, with a central hole available for DNA interaction. The ability of p21 to inhibit the action of PCNA is therefore likely to be due to its masking of elements on PCNA that are required for the binding of other components of the polymerase assembly.

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Metadata

Authors
Gulbis, J. M., Kelman, Z., Hurwitz, J., O'Donnell, M., & Kuriyan, J.
Venue
Cell
Publisher
Elsevier BV
Published
1996-10
Volume
87
Issue
2
Pages
297-306
ISSN
0092-8674 (ISSN-L)
OpenAlex
W2116537286
Cited by
804
References
8
FWCI
10.82
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Structure of the C-Terminal Region of p21WAF1/CIP1 Complexed with Human PCNA. https://app.cochat.ai/papers/10.1016/s0092-8674(00)81347-1
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Gulbis, J. M., Kelman, Z., Hurwitz, J., O'Donnell, M., & Kuriyan, J. (1996). Structure of the C-Terminal Region of p21WAF1/CIP1 Complexed with Human PCNA. Cell. https://doi.org/10.1016/s0092-8674(00)81347-1

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

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