Molecular tweezers modulate 14-3-3 protein–protein interactions

Supramolecular chemistry has recently emerged as a promising way to modulate protein functions, but devising molecules that will interact with a protein in the desired manner is difficult as many competing interactions exist in a biological environment (with solvents, salts or different sites for th...

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Bibliographic Details
Published in:	Nature chemistry Vol. 5; no. 3; pp. 234 - 239
Main Authors:	Bier, David, Rose, Rolf, Bravo-Rodriguez, Kenny, Bartel, Maria, Ramirez-Anguita, Juan Manuel, Dutt, Som, Wilch, Constanze, Klärner, Frank-Gerrit, Sanchez-Garcia, Elsa, Schrader, Thomas, Ottmann, Christian
Format:	Journal Article
Language:	English
Published:	London Nature Publishing Group UK 01.03.2013 Nature Publishing Group
Subjects:	14-3-3 protein 14-3-3 Proteins - chemistry 14-3-3 Proteins - genetics 14-3-3 Proteins - metabolism 639/638/541 639/638/92/96 Adapter proteins Adapters ADP Ribose Transferases - chemistry ADP Ribose Transferases - metabolism Amino acids Analytical Chemistry Bacterial Toxins - chemistry Bacterial Toxins - metabolism Binding Biochemistry Biology Biomimetic Materials - chemistry Biomimetic Materials - metabolism Biomolecules Chemistry Chemistry/Food Science Computer simulation Crystallography Enzymes Humans Inorganic Chemistry Kinases Ligands Lysine Mathematical models Mechanics Models, Molecular Molecular Conformation Organic Chemistry Phosphates Phosphorylation Physical Chemistry Physiology Protein Binding Protein interaction Proteins Proto-Oncogene Proteins c-raf - chemistry Proto-Oncogene Proteins c-raf - metabolism Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Salts Solvents Structural analysis Germany
ISSN:	1755-4330, 1755-4349, 1755-4349
Online Access:	Get full text
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