[ASAP] Allosteric Influence of Extremophile Hairpin Motif Mutations on the Protein Splicing Activity of a Hyperthermophilic Intein
Allosteric Influence of Extremophile Hairpin Motif Mutations on the Protein Splicing Activity of a Hyperthermophilic Intein
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.0c00348/20200624/images/medium/bi0c00348_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.0c00348
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06-25-2020 02:58 AM
[ASAP] Substrate Activation of the Low-Molecular Weight Protein Tyrosine Phosphatase from Mycobacterium tuberculosis
Substrate Activation of the Low-Molecular Weight Protein Tyrosine Phosphatase from Mycobacterium tuberculosis
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.0c00059/20200312/images/medium/bi0c00059_0009.gif
Biochemistry
DOI: 10.1021/acs.biochem.0c00059
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03-16-2020 04:59 PM
[ASAP] Optochemical Control of Protein Localization and Activity within Cell-like Compartments
Optochemical Control of Protein Localization and Activity within Cell-like Compartments
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00131/20180418/images/medium/bi-2018-00131e_0006.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00131
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nmrlearner
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04-20-2018 01:59 AM
[NMR paper] NMR reveals the allosteric opening and closing of Abelson tyrosine kinase by ATP-site and myristoyl pocket inhibitors.
NMR reveals the allosteric opening and closing of Abelson tyrosine kinase by ATP-site and myristoyl pocket inhibitors.
Related Articles NMR reveals the allosteric opening and closing of Abelson tyrosine kinase by ATP-site and myristoyl pocket inhibitors.
Proc Natl Acad Sci U S A. 2013 Nov 4;
Authors: Skora L, Mestan J, Fabbro D, Jahnke W, Grzesiek S
Abstract
Successful treatment of chronic myelogenous leukemia is based on inhibitors binding to the ATP site of the deregulated breakpoint cluster region (Bcr)-Abelson tyrosine kinase (Abl)...
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11-06-2013 10:20 PM
[NMR paper] X-ray crystallography and NMR as tools for the study of protein tyrosine phosphatases.
X-ray crystallography and NMR as tools for the study of protein tyrosine phosphatases.
X-ray crystallography and NMR as tools for the study of protein tyrosine phosphatases.
Methods. 2013 Jul 27;
Authors: Elena Gulerez I, Gehring K
Abstract
Protein tyrosine phosphatases (PTPs) are well recognized as key targets in a wide spectrum of diseases, such as diabetes, obesity and cancer. Their roles in these maladies have been successfully characterized by various methods. However, it is only by utilizing the entire gamut of tools and techniques...
nmrlearner
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08-01-2013 12:56 PM
X-ray crystallography and NMR as tools for the study of protein tyrosine phosphatases
X-ray crystallography and NMR as tools for the study of protein tyrosine phosphatases
Publication date: Available online 27 July 2013
Source:Methods</br>
Author(s): Irina Elena Gulerez , Kalle Gehring</br>
Protein tyrosine phosphatases (PTPs) are well recognized as key targets in a wide spectrum of diseases, such as diabetes, obesity and cancer. Their roles in these maladies have been successfully characterized by various methods. However, it is only by utilizing the entire gamut of tools and techniques available that we can build a sufficient knowledge of their...
nmrlearner
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07-28-2013 07:11 AM
[NMR paper] TROSY-NMR studies of the 91kDa TRAP protein reveal allosteric control of a gene regul
TROSY-NMR studies of the 91kDa TRAP protein reveal allosteric control of a gene regulatory protein by ligand-altered flexibility.
Related Articles TROSY-NMR studies of the 91kDa TRAP protein reveal allosteric control of a gene regulatory protein by ligand-altered flexibility.
J Mol Biol. 2002 Oct 25;323(3):463-73
Authors: McElroy C, Manfredo A, Wendt A, Gollnick P, Foster M
The tryptophan biosynthesis genes of several Bacilli are controlled through terminator/anti-terminator transcriptional attenuation. This process is regulated by...
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11-24-2010 08:58 PM
[NMR paper] Insights into tyrosine phosphorylation control of protein-protein association from th
Insights into tyrosine phosphorylation control of protein-protein association from the NMR structure of a band 3 peptide inhibitor bound to glyceraldehyde-3-phosphate dehydrogenase.
Related Articles Insights into tyrosine phosphorylation control of protein-protein association from the NMR structure of a band 3 peptide inhibitor bound to glyceraldehyde-3-phosphate dehydrogenase.
Biochemistry. 1998 Jan 20;37(3):867-77
Authors: Eisenmesser EZ, Post CB
A protein-protein association regulated by phosphorylation of tyrosine is examined by NMR...
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[ASAP] Optogenetic Analysis of Allosteric Control in Protein Tyrosine Phosphatases
Linear Mode
