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Cited by 361

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Modulation of Ras and a-Factor Function by Carboxyl-Terminal Proteolysis

Boyartchuk, Victor L., Ashby, Matthew N., Rine, Jasper·1997·Science

Abstract

Prenylated proteins contain a covalently linked cholesterol intermediate near their carboxyl-termini. Maturation of most prenylated proteins involves proteolytic removal of the last three amino acids. Two genes in Saccharomyces cerevisiae , RCE1 and AFC1 , were identified that appear to be responsible for this processing. The Afc1 protein is a zinc protease that participates in the processing of yeast a -factor mating pheromone. The Rce1 protein contributes to the processing of both Ras protein and a -factor. Deletion of both AFC1 and RCE1 resulted in the loss of proteolytic processing of prenylated proteins. Disruption of RCE1 led to defects in Ras localization and signaling and suppressed the activated phenotype associated with the allele RAS2 val19 .

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Crossref · 10.1126/science.275.5307.1796

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Metadata

Authors
Boyartchuk, V. L., Ashby, M. N., & Rine, J.
Venue
Science
Published
1997-03-21
Volume
275
Issue
5307
Pages
1796-1800
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W1964489808
Cited by
361
References
1
FWCI
6.75
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Modulation of Ras and a-Factor Function by Carboxyl-Terminal Proteolysis. https://app.cochat.ai/papers/10.1126/science.275.5307.1796
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Boyartchuk, V. L., Ashby, M. N., & Rine, J. (1997). Modulation of Ras and a-Factor Function by Carboxyl-Terminal Proteolysis. Science. https://doi.org/10.1126/science.275.5307.1796

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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

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.