Structural and Biochemical Characterization of a Cyanobacterial PP2C Phosphatase Reveals Insights into Catalytic Mechanism and Substrate Recognition-Reference-Cited by-同舟云学术

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Structural and Biochemical Characterization of a Cyanobacterial PP2C Phosphatase Reveals Insights into Catalytic Mechanism and Substrate Recognition

Published:2016-04-26 Issue:5 Volume:6 Page:60
ISSN:2073-4344
Container-title:Catalysts
language:en
Short-container-title:Catalysts

Author:

Si Yunlong,Yuan Ye,Wang Yue,Gao Jin,Hu Yanbo,Feng Shiqiong,Su Jiyong

Funder

National Natural Science Foundation of China

Publisher

MDPI AG

Subject

Physical and Theoretical Chemistry,Catalysis

Link

http://www.mdpi.com/2073-4344/6/5/60/pdf

Reference53 articles.

1. Wip1, a novel human protein phosphatase that is induced in response to ionizing radiation in a p53-dependent manner

2. Plant PP2C phosphatases: emerging functions in stress signaling

3. Type 2C Protein Phosphatases in Fungi

4. A PP2C-type phosphatase dephosphorylates the PII signaling protein in the cyanobacterium Synechocystis PCC 6803

5. Determinants for substrate specificity of the bacterial PP2C protein phosphatase tPphA fromThermosynechococcus elongatus

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1. An artificial protein modulator reprogramming neuronal protein functions;Nature Communications;2024-03-06

2. Crystal Structures of Pyrophosphatase from Acinetobacter baumannii: Snapshots of Pyrophosphate Binding and Identification of a Phosphorylated Enzyme Intermediate;International Journal of Molecular Sciences;2019-09-06

3. Structural Insight into the Mechanism of Staphylococcus aureus Stp1 Phosphatase;ACS Infectious Diseases;2019-03-14

4. The inhibitory mechanism of aurintricarboxylic acid targeting serine/threonine phosphatase Stp1 in Staphylococcus aureus: insights from molecular dynamics simulations;Acta Pharmacologica Sinica;2019-02-22

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