Autophosphorylation activates c-Src kinase through global structural rearrangements-Reference-Cited by-同舟云学术

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Autophosphorylation activates c-Src kinase through global structural rearrangements

Published:2019-08 Issue:35 Volume:294 Page:13186-13197
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Boczek Edgar E.,Luo Qi,Dehling Marco,Röpke Michael^ORCID,Mader Sophie L.^ORCID,Seidl Andreas,Kaila Ville R.I.^ORCID,Buchner Johannes^ORCID

Funder

Studienstiftung des Deutschen Volkes (Studienstiftung)

China Scholarship Council (CSC)

Gauss Centre for Supercomputing/Leibniz Supercomputing Centre

Deutsche Forschungsgemeinschaft (DFG)

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference51 articles.

1. Insights into protein kinase regulation and inhibition by large scale structural comparison;Eswaran;Biochim. Biophys. Acta,2010

2. Structural coupling of SH2-kinase domains links Fes and Abl substrate recognition and kinase activation;Filippakopoulos;Cell,2008

3. Activation segment dimerization: a mechanism for kinase autophosphorylation of non-consensus sites;Pike;EMBO J,2008

4. Mechanism and consequence of the autoactivation of p38α mitogen-activated protein kinase promoted by TAB1;DeNicola;Nat. Struct. Mol. Biol,2013

5. Structure of the CaMKIIδ/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation;Rellos;PLoS Biol,2010

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3. An allosteric switch between the activation loop and a c-terminal palindromic phospho-motif controls c-Src function;Nature Communications;2023-10-17

4. Uncovering the Early Events Associated with Oligomeric Aβ-Induced Src Activation;Antioxidants;2023-09-16

5. Profiling of drug resistance in Src kinase at scale uncovers a regulatory network coupling autoinhibition and catalytic domain dynamics;Cell Chemical Biology;2023-09

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