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Cited by 395

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

Intracellular Targeting and Structural Conservation of a Prohormone-Processing Endoprotease

Fuller, Robert S., Brake, Anthony J., Thorner, Jeremy·1989·Science

Abstract

The prohormone-processing endoprotease ( KEX2 gene product) of the yeast Saccharomyces cerevisiae is a membrane-bound, 135,000-dalton glycoprotein, which contains both asparagine-linked and serine- and threonine-linked oligosaccharide and resides in a secretory compartment. Analysis of mutant kex2 genes truncated at their 3′ end indicates that carboxyl terminal domains of the enzyme are required for its proper localization within the cell. A human gene product, "furin," shares 50% identity with the catalytic domain of Kex2 protease and is, therefore, a candidate for a human prohormone-processing enzyme.

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Crossref · 10.1126/science.2683070

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Metadata

Authors
Fuller, R. S., Brake, A. J., & Thorner, J.
Venue
Science
Published
1989-10-27
Volume
246
Issue
4929
Pages
482-486
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2012020894
Cited by
395
References
1
FWCI
14.01
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Intracellular Targeting and Structural Conservation of a Prohormone-Processing Endoprotease. https://app.cochat.ai/papers/10.1126/science.2683070
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Fuller, R. S., Brake, A. J., & Thorner, J. (1989). Intracellular Targeting and Structural Conservation of a Prohormone-Processing Endoprotease. Science. https://doi.org/10.1126/science.2683070

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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.