Cited by 46Chemical Synthesis and AnalysisProtein Structure and DynamicsBiochemical and Structural Characterization

End-capped α-helices as modulators of protein function

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Mahon, Andrew B., Arora, Paramjit S.·2012·Drug Discovery Today: Technologies

Abstract

Examination of complexes of proteins with other biomolecules reveals that proteins tend to interact with partners via folded sub-domains, in which the backbone possesses secondary structure. α-Helices, the largest class of protein secondary structures, play fundamental roles in a multitude of highly specific protein-protein and protein-nucleic acids interactions. Herein, we describe the potential of a helix nucleation strategy to afford modulators of protein-protein interactions.

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Crossref · 10.1016/j.ddtec.2011.07.008

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Authors
Mahon, A. B., & Arora, P. S.
Affiliations
New York University (US)
Corresponding author
Arora, Paramjit S.
Venue
Drug Discovery Today: Technologies
Publisher
Elsevier BV
Published
2012-03
Volume
9
Issue
1
Pages
e57-e62
ISSN
1740-6749 (ISSN-L)
OpenAlex
W2026338075
Cited by
44
References
41
Citations by year
2026: 2 · 2025: 2 · 2024: 4 · 2023: 1 · 2022: 1 · 2021: 2 · 2020: 4 · 2019: 4 · 2017: 6 · 2016: 8 · 2015: 4 · 2014: 3 · 2013: 2 · 2012: 1
FWCI
0.78
Type
journal article
Language
en
Open access
Locations
  • Drug Discovery Today Technologies (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
Funders
  • National Institutes of Health
  • National Institute of General Medical Sciences (R01GM073943)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chemical Synthesis and Analysis
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
Keywords
helix nucleation, protein-protein interaction, protein function modulation, protein secondary structure, protein-nucleic acid interactions, protein folding, small molecule modulators

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