Cited by 263

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

Cloning of cDNAs for cellular proteins that bind to the retinoblastoma gene product

Defeo-Jones, Deborah, Huang, Pearl S., Jones, Raymond E., Haskell, Kathleen M., Vuocolo, Gerald A., Hanobik, Michelle G., Huber, Hans E., Oliff, Alien·1991·Nature

Abstract

The E7 transforming protein of human papilloma virus-16 binds to the retinoblastoma gene product (pRb) through a nine-amino-acid segment of E7 (21-29). This segment of E7 is homologous to the pRb-binding domains of the simian virus 40 large T and adenovirus E1A transforming proteins. Each of these viral transforming proteins bind to the same region of pRb. To isolate cellular proteins that interact with this viral protein-binding domain on pRb, we used recombinant pRb to screen a human complementary DNA expression library. Two cDNAs were isolated that encode retinoblastoma binding proteins (RBP-1 and RBP-2). We report here that these RBP genes exist in separate loci and produce discrete messenger RNAs. The predicted amino-acid sequence of these genes showed no homology to known proteins, but both RBPs contain the pRb binding motif conserved between E7, large T and E1A14. In vitro expression of the RBP cDNAs yielded proteins that specifically bound to pRb. Recombinant E7 protein, the E7 21-29 peptide and the homologous RBP-1 peptide inhibited RBP-pRb binding. Mutations introduced into the putative pRb-binding segment in RBP-1 impaired its binding activity. These studies indicate that the cellular RBP-1, RBP-2 and viral E7 proteins interact with pRb through similar domains.

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Crossref · 10.1038/352251a0

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Citations

Cites

Research works printed but not linked: 24

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Cited by

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Metadata

Authors
Defeo-Jones, D., Huang, P. S., Jones, R. E., Haskell, K. M., Vuocolo, G. A., Hanobik, M. G., Huber, H. E., & Oliff, A.
Venue
Nature
Published
1991-07
Volume
352
Issue
6332
Pages
251-254
ISSN
  • 0028-0836
  • 1476-4687
Cited by
263
References
2
Language
en

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