scholarly journals Kaleidoscopic protein–protein interactions in the life and death of ataxin-1: new strategies against protein aggregation

2014 ◽  
Vol 37 (4) ◽  
pp. 211-218 ◽  
Author(s):  
Cesira de Chiara ◽  
Annalisa Pastore
Keyword(s):  
Protein Aggregation ◽  
Protein Interactions ◽  
Protein Protein Interactions ◽  
Life And Death ◽  
New Strategies

scholarly journals 26th Annual GP2A Medicinal Chemistry Conference & 32nd Journées Franco-Belges de Pharmacochimie

2019 ◽  
Vol 12 (2) ◽  
pp. 73
Author(s):  
Patrick Dallemagne ◽  
Christophe Rochais ◽  
Pascal Marchand ◽  
Thierry Besson
Keyword(s):  
Drug Design ◽  
Natural Product ◽  
Protein Interactions ◽  
Medicinal Chemistry ◽  
Young Researcher ◽  
Protein Protein Interactions ◽  
Computer Aided Drug Design ◽  
Computer Aided ◽  
Wide Group ◽  
New Strategies

As a joint meeting, the 26th Medicinal Chemistry Conference of GP2A and 32nd Journées Franco-Belges de Pharmacochimie took place between 13th and 15th June at Asnelles sur Mer (Normandie, France), providing a unique opportunity for a wide group of European medicinal chemists to engage. Topics included chemical tools for medicinal chemistry, protein-protein interactions, epigenetics, natural product-inspired molecules, computer-aided drug design, and new strategies for the design and development of drugs. Abstracts of invited lectures, proffered young researcher communications, flash communications and posters presented during the meeting are collected in this report.

Evolutionary selection for protein aggregation

2012 ◽  
Vol 40 (5) ◽  
pp. 1032-1037 ◽  
Author(s):  
Natalia Sanchez de Groot ◽  
Marc Torrent ◽  
Anna Villar-Piqué ◽  
Benjamin Lang ◽  
Salvador Ventura ◽  
...  
Keyword(s):  
Protein Aggregation ◽  
Protein Interactions ◽  
Current Knowledge ◽  
Protein Aggregates ◽  
Cellular Systems ◽  
Aggregation Process ◽  
Loss Of Function ◽  
Protein Protein Interactions ◽  
Wide Range ◽  
Range Of Functions

Protein aggregation is being found to be associated with an increasing number of human diseases. Aggregation can lead to a loss of function (lack of active protein) or to a toxic gain of function (cytotoxicity associated with protein aggregates). Although potentially harmful, protein sequences predisposed to aggregation seem to be ubiquitous in all kingdoms of life, which suggests an evolutionary advantage to having such segments in polypeptide sequences. In fact, aggregation-prone segments are essential for protein folding and for mediating certain protein–protein interactions. Moreover, cells use protein aggregates for a wide range of functions. Against this background, life has adapted to tolerate the presence of potentially dangerous aggregation-prone sequences by constraining and counteracting the aggregation process. In the present review, we summarize the current knowledge of the advantages associated with aggregation-prone stretches in proteomes and the strategies that cellular systems have developed to control the aggregation process.

P3-295: Breaking protein-protein interactions: A combined chemical and computational approach to develop a new class of protein aggregation inhibitors

2009 ◽  
Vol 5 (4S_Part_14) ◽  
pp. P429-P430
Author(s):  
Isabella Graef ◽  
Mamoun M. Alhamadsheh ◽  
Alexandra Esteras-Chopo ◽  
Kim Branson ◽  
Mohua Bose ◽  
...  
Keyword(s):  
Protein Aggregation ◽  
Protein Interactions ◽  
Computational Approach ◽  
Protein Protein Interactions ◽  
New Class ◽  
Aggregation Inhibitors

Protein-protein interactions of the p53 family with the Bcl-2 family in hepatocellular carcinoma

2011 ◽  
Vol 49 (08) ◽  
Author(s):  
LC König ◽  
M Meinhard ◽  
C Sandig ◽  
MH Bender ◽  
A Lovas ◽  
...  
Keyword(s):  
Hepatocellular Carcinoma ◽  
Protein Interactions ◽  
Protein Protein Interactions ◽  
P53 Family
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