Rational design of protein–protein interaction inhibitors

MedChemComm ◽  
2015 ◽  
Vol 6 (1) ◽  
pp. 51-60 ◽  
Author(s):  
Didier Rognan
Keyword(s):  
Molecular Weight ◽  
Tumor Suppressor ◽  
Protein Interaction ◽  
Rational Design ◽  
Low Molecular Weight ◽  
P53 Tumor Suppressor ◽  
Protein Protein Interaction

Low molecular weight compound competing for the binding of the p53 tumor suppressor to the MDM2 oncoprotein.

scholarly journals Correction: Rational design of a stapled JAZ9 peptide inhibiting protein–protein interaction of a plant transcription factor

2021 ◽  
Author(s):  
Kaho Suzuki ◽  
Yousuke Takaoka ◽  
Minoru Ueda
Keyword(s):  
Transcription Factor ◽  
Protein Interaction ◽  
Rational Design ◽  
Protein Protein Interaction ◽  
Inhibiting Protein

Correction for ‘Rational design of a stapled JAZ9 peptide inhibiting protein–protein interaction of a plant transcription factor’ by Kaho Suzuki et al., RSC Chem. Biol., 2021, DOI: 10.1039/d0cb00204f.

scholarly journals Rational design of a stapled JAZ9 peptide inhibiting protein–protein interaction of a plant transcription factor

2021 ◽  
Author(s):  
Kaho Suzuki ◽  
Yousuke Takaoka ◽  
Minoru Ueda
Keyword(s):  
Arabidopsis Thaliana ◽  
Transcription Factor ◽  
Protein Interaction ◽  
Rational Design ◽  
Master Regulators ◽  
Jasmonate Signaling ◽  
Protein Protein Interaction ◽  
Inhibiting Protein

A rationally designed stapled JAZ peptide selectively inhibited MYCs, master-regulators of the jasmonate signaling in Arabidopsis thaliana. It is proposed as a novel chemical tool for the analysis of MYC related jasmonate signaling.

scholarly journals Oligomerization and Activity of the Helicase Domain of the Tobacco Mosaic Virus 126- and 183-Kilodalton Replicase Proteins

2003 ◽  
Vol 77 (6) ◽  
pp. 3549-3556 ◽  
Author(s):  
Sameer P. Goregaoker ◽  
James N. Culver
Keyword(s):  
Electron Microscopy ◽  
Molecular Weight ◽  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Virus Replication ◽  
Protein Interaction ◽  
Gel Filtration ◽  
Helicase Domain ◽  
Protein Protein Interaction ◽  
Replicase Proteins

ABSTRACT A protein-protein interaction within the helicase domain of the Tobacco mosaic virus (TMV) 126- and 183-kDa replicase proteins was previously implicated in virus replication (S. Goregaoker, D. Lewandowski, and J. Culver, Virology 282:320-328, 2001). To further characterize the interaction, polypeptides covering the interacting portions of the TMV helicase domain were expressed and purified. Biochemical characterizations demonstrated that the helicase domain polypeptides hydrolyzed ATP and bound both single-stranded and duplexed RNA in an ATP-controlled fashion. A TMV helicase polypeptide also was capable of unwinding duplexed RNA, confirming the predicted helicase function of the domain. Biochemically active helicase polypeptides were shown by gel filtration to form high-molecular-weight complexes. Electron microscopy studies revealed the presence of ring-like oligomers that displayed six-sided symmetry. Taken together, these data demonstrate that the TMV helicase domain interacts with itself to produce hexamer-like oligomers. Within the context of the full-length 126- and 183-kDa proteins, these findings suggest that the TMV replicase may form a similar oligomer.

Rational Design of a Low Molecular Weight, Stable, Potent, and Long-Lasting GPR103 Aza-β3-pseudopeptide Agonist

2012 ◽  
Vol 55 (17) ◽  
pp. 7516-7524 ◽  
Author(s):  
Cindy Neveu ◽  
Benjamin Lefranc ◽  
Olivier Tasseau ◽  
Jean-Claude Do-Rego ◽  
Adèle Bourmaud ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Rational Design ◽  
Low Molecular Weight

Rational Design, Synthesis and Evaluation of Coumarin Derivatives as Protein-protein Interaction Inhibitors

2016 ◽  
Vol 35 (8-9) ◽  
pp. 460-473 ◽  
Author(s):  
Laura De Luca ◽  
Fatima E. Agharbaoui ◽  
Rosaria Gitto ◽  
Maria Rosa Buemi ◽  
Frauke Christ ◽  
...  
Keyword(s):  
Protein Interaction ◽  
Rational Design ◽  
Coumarin Derivatives ◽  
Design Synthesis ◽  
Protein Protein Interaction
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