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Cited by 246

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

Detecting and Measuring Cotranslational Protein Degradation in Vivo

Turner, Glenn C., Varshavsky, Alexander·2000·Science

Abstract

Nascent polypeptides emerging from the ribosome and not yet folded may at least transiently present degradation signals similar to those recognized by the ubiquitin system in misfolded proteins. The ubiquitin sandwich technique was used to detect and measure cotranslational protein degradation in living cells. More than 50 percent of nascent protein molecules bearing an amino-terminal degradation signal can be degraded cotranslationally, never reaching their mature size before their destruction by processive proteolysis. Thus, the folding of nascent proteins, including abnormal ones, may be in kinetic competition with pathways that target these proteins for degradation cotranslationally.

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Metadata

Authors
Turner, G. C., & Varshavsky, A.
Venue
Science
Published
2000-09-22
Volume
289
Issue
5487
Pages
2117-2120
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2071847586
Cited by
246
References
2
FWCI
5.29
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Detecting and Measuring Cotranslational Protein Degradation in Vivo. https://app.cochat.ai/papers/10.1126/science.289.5487.2117
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Turner, G. C., & Varshavsky, A. (2000). Detecting and Measuring Cotranslational Protein Degradation in Vivo. Science. https://doi.org/10.1126/science.289.5487.2117

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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.