End-capped α-helices as modulators of protein function
Open accessAbstract
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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- 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)
- PMC
- PMC3375709
- 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
- green
- www.ncbi.nlm.nih.gov
- 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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