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Cited by 850

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

Evidence That the Leucine Zipper Is a Coiled Coil

O'Shea, Erin K., Rutkowski, Rheba, Kim, Peter S.·1989·Science

Abstract

Recently, a hypothetical structure called a leucine zipper was proposed that defines a new class of DNA binding proteins. The common feature of these proteins is a region spanning approximately 30 amino acids that contains a periodic repeat of leucines every seven residues. A peptide corresponding to the leucine zipper region of the yeast transcriptional activator GCN4 was synthesized and characterized. This peptide associates in the micromolar concentration range to form a very stable dimer of α helices with a parallel orientation. Although some features of the leucine zipper model are supported by our experimental data, the peptide has the characteristics of a coiled coil.

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Metadata

Authors
O'Shea, E. K., Rutkowski, R., & Kim, P. S.
Venue
Science
Published
1989-01-27
Volume
243
Issue
4890
Pages
538-542
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W1975511017
Cited by
850
References
2
FWCI
31.24
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Evidence That the Leucine Zipper Is a Coiled Coil. https://app.cochat.ai/papers/10.1126/science.2911757
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O'Shea, E. K., Rutkowski, R., & Kim, P. S. (1989). Evidence That the Leucine Zipper Is a Coiled Coil. Science. https://doi.org/10.1126/science.2911757

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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.