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Cited by 206

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A new pathway for protein export in Saccharomyces cerevisiae.

Open access
Cleves, A E, Cooper, D N, Barondes, S H, Kelly, R B·1996·The Journal of cell biology

Abstract

Several physiologically important proteins lack a classical secretory signal sequence, yet they are secreted from cells. To investigate the secretion mechanism of such proteins, a representative mammalian protein that is exported by a nonclassical mechanism, galectin-1, has been expressed in yeast. Galectin-1 is exported across the yeast plasma membrane, and this export does not require the classical secretory pathway nor the yeast multidrug resistance-like protein Ste6p, the transporter for the peptide a factor. A screen for components of the export machinery has identified genes that are involved in nonclassical export. These findings demonstrate a new pathway for protein export that is distinct from the classical secretory pathway in yeast.

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Metadata

Authors
Cleves, A. E., Cooper, D. N., Barondes, S. H., & Kelly, R. B.
Venue
The Journal of cell biology
Published
1996-06-01
Volume
133
Issue
5
Pages
1017-1026
ISSN
  • 0021-9525 (ISSN-L)
  • 1540-8140
OpenAlex
W2157839115
Cited by
206
References
0
FWCI
4.29
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: A new pathway for protein export in Saccharomyces cerevisiae. https://app.cochat.ai/papers/10.1083/jcb.133.5.1017
The paper
Cleves, A. E., Cooper, D. N., Barondes, S. H., & Kelly, R. B. (1996). A new pathway for protein export in Saccharomyces cerevisiae. The Journal of cell biology. https://doi.org/10.1083/jcb.133.5.1017

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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.