Cited by 79Chemical Synthesis and AnalysisProtein Degradation and InhibitorsComputational Drug Discovery Methods

Small molecule modulators of protein-protein interactions: selected case studies

Aeluri, Madhu, Chamakuri, Srinivas, Dasari, Bhanudas, Guduru, Shiva Krishna Reddy, Jimmidi, Ravikumar, Jogula, Srinivas, Arya, Prabhat·2014·Chemical Reviews

Abstract

ADVERTISEMENT RETURN TO ISSUEPREVReviewNEXTSmall Molecule Modulators of Protein–Protein Interactions: Selected Case StudiesMadhu Aeluri, Srinivas Chamakuri, Bhanudas Dasari, Shiva Krishna Reddy Guduru, Ravikumar Jimmidi, Srinivas Jogula, and Prabhat Arya*View Author Information Dr. Reddy's Institute of Life Sciences (DRILS), University of Hyderabad Campus Gachibowli, Hyderabad 500046, India*Phone: (+91) (40) 6657 1500. E mail: [email protected]Cite this: Chem. Rev. 2014, 114, 9, 4640–4694Publication Date (Web):March 27, 2014Publication History Received25 July 2013Published online27 March 2014Published inissue 14 May 2014https://pubs.acs.org/doi/10.1021/cr4004049https://doi.org/10.1021/cr4004049review-articleACS PublicationsCopyright © 2014 American Chemical SocietyRequest reuse permissionsArticle Views6379Altmetric-Citations70LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose SUBJECTS:Apoptosis,Cells,Inhibitors,Peptides and proteins,Small molecules Get e-Alerts

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  • Analysis of crystal structure of MDM2-p53 complex showed interaction primarily mediated by three hydrophobic residues Phe19, Trp23, Leu26 of p53 peptide and a small deep hydrophobic cleft in MDM2.

    “Analysis of the crystal structure of the MDM2-p53 complex showed that the interaction between MDM2 and its transcriptional factor p53 was primarily mediated by three hydrophobic residues, namely Phe19, Trp23, and Leu26 of a p53 peptide and a small deep hydrophobic cleft in MDM2 [38].”

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Authors
Aeluri, M., Chamakuri, S., Dasari, B., Guduru, S. K. R., Jimmidi, R., Jogula, S., & Arya, P.
Affiliations
University of Hyderabad (IN)
Corresponding author
Arya, Prabhat
Venue
Chemical Reviews
Published
2014-03-27
Volume
114
Issue
9
Pages
4640-4694
ISSN
  • 0009-2665 (ISSN-L)
  • 1520-6890
OpenAlex
W2312443521
Cited by
79
References
525
Citations by year
2026: 3 · 2025: 1 · 2024: 3 · 2023: 3 · 2022: 3 · 2021: 3 · 2020: 3 · 2019: 7 · 2018: 12 · 2017: 7 · 2016: 16 · 2015: 15 · 2014: 3
FWCI
1.32
Type
journal article
Language
en
Open access
closed
Locations
  • Chemical Reviews (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chemical Synthesis and Analysis
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
  • Physical Sciences › Computer Science › Computational Theory and Mathematics › Computational Drug Discovery Methods
Keywords
small molecule modulators, protein-protein interaction, small molecule inhibitors, peptides and proteins
MeSH terms
Animals, Humans, Protein Binding, Proteins, Tubulin, HSP90 Heat-Shock Proteins, Proto-Oncogene Proteins c-bcl-2, 14-3-3 Proteins, Apoptosis Regulatory Proteins, Small Molecule Libraries

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