Dimerization-Induced Folding of MST1 SARAH and the Influence of the Intrinsically Unstructured Inhibitory Domain: Low Thermodynamic Stability of Monomer-Reference-Cited by-同舟云学术

Dimerization-Induced Folding of MST1 SARAH and the Influence of the Intrinsically Unstructured Inhibitory Domain: Low Thermodynamic Stability of Monomer

Published:2011-12-02 Issue:51 Volume:50 Page:10990-11000
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Constantinescu Aruxandei Diana¹,Makbul Cihan¹,Koturenkiene Agne¹,Lüdemann Maik-Borris¹,Herrmann Christian¹

Affiliation:

1. Department of Physical Chemistry I, Ruhr University Bochum, Universitätsstrasse 150, 44780 Bochum, Germany

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi201110h

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2. MST1-JNK promotes apoptosis via caspase-dependent and independent pathways

3. Activation of the c-Jun N-Terminal Kinase Pathway by MST1 Is Essential and Sufficient for the Induction of Chromatin Condensation during Apoptosis

4. MST4, a new Ste20-related kinase that mediates cell growth and transformation via modulating ERK pathway

5. Cloning and Characterization of MST4, a Novel Ste20-like Kinase

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