Leucine Zipper Dimerization
Leucine Zipper Dimerization is a protein dimerization mechanism characterized by the association of two alpha-helical regions containing regularly spaced leucine residues that interlock in a coiled-coil structure, thereby facilitating sequence-specific DNA binding or protein-protein interactions in transcription factors.
336
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403
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2017–2026
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336
A Switch Between Two-, Three-, and Four-stranded Coiled Coils in GCN4 Leucine Zipper Mutants
Pehr B. Harbury, Tao Zhang, Peter S. Kim et al. · Science · 1993 · 1.5K citations
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Whitehead Institute for Biomedical Research, United States
6 publications · 3.1K citations
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Howard Hughes Medical Institute
Chevy Chase, United States
16 h-index
35 publications
7.2K citations
Harvard University
Cambridge, United States
15 h-index
45 publications
11.7K citations
National Institutes of Health
Bethesda, United States
12 h-index
47 publications
6.1K citations
Massachusetts Institute of Technology
Cambridge, United States
10 h-index
31 publications
6.4K citations
National Cancer Institute
Bethesda, United States
9 h-index
35 publications
6.4K citations

Centre National de la Recherche Scientifique
Paris, France
9 h-index
32 publications
953 citations
Yale University
New Haven, United States
7 h-index
22 publications
1.8K citations
New York University
New York, United States
7 h-index
19 publications
5.1K citations
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JBC · 43 publications · 3K citations
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MCB · 34 publications · 2.8K citations
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23 publications · 1.1K citations
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PNAS · 23 publications · 3.3K citations
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JVI · 16 publications · 768 citations
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