Dimerization-based control of cooperativity-Reference-Cited by-同舟云学术

Dimerization-based control of cooperativity

Published:2014 Issue:7 Volume:10 Page:1824-1832
ISSN:1742-206X
Container-title:Mol. BioSyst.
language:en
Short-container-title:Mol. BioSyst.

Author:

Bouhaddou Mehdi¹²³,Birtwistle Marc R.¹²³

Affiliation:

1. Icahn School of Medicine at Mount Sinai

2. Department of Pharmacology and Systems Therapeutics

3. New York, USA

Abstract

Kinetic modeling reveals that dimerization affinity can increase, eliminate, and even reverse cooperativity imposed by the canonical ligand-affinity mechanism highlighting a novel role for the ubiquitous signaling motif.

Funder

National Institute of General Medical Sciences

National Institutes of Health

Publisher

Royal Society of Chemistry (RSC)

Subject

Molecular Biology,Biotechnology

Link

http://pubs.rsc.org/en/content/articlepdf/2014/MB/C4MB00022F

Reference45 articles.

1. J. M. Matthews and M.Sunde , in Protein dimerization and oligomerization in biology , ed. J. M. Matthews , Landes Bioscience and Springer Science + Business Media , 2012 , ch. 1, pp. 1–18

2. The Subunit Interfaces of Weakly Associated Homodimeric Proteins

3. The power of two: protein dimerization in biology

4. Dimer formation drives the activation of the cell death protease caspase 9

5. The E. coli bio operon: Transcriptional repression by an essential protein modification enzyme

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