Correlation of the Phosphorylation States of pp60c-src with Tyrosine Kinase Activity: The Intramolecular pY530−SH2 Complex Retains Significant Activity If Y419 Is Phosphorylated-Reference-Cited by-同舟云学术

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Correlation of the Phosphorylation States of pp60c-src with Tyrosine Kinase Activity: The Intramolecular pY530−SH2 Complex Retains Significant Activity If Y419 Is Phosphorylated

Published:1996-01-01 Issue:29 Volume:35 Page:9519-9525
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Boerner Renee J.¹,Kassel Daniel B.¹,Barker Sean C.¹,Ellis Byron¹,DeLacy Pam¹,Knight Wilson B.¹

Affiliation:

1. Departments of Biochemistry and Bioanalytical Chemistry, Glaxo Wellcome Inc., Research Triangle Park, North Carolina 27709

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi960248u

Reference27 articles.

Cited by 90 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. The priming phosphorylation of KaiC is activated by the release of its autokinase autoinhibition;2024-03-23

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

3. Phosphorylation of tyrosine 90 in SH3 domain is a new regulatory switch controlling Src kinase;eLife;2023-07-10

4. An allosteric switch between the activation loop and a c-terminal palindromic phospho-motif controls c-Src function;2022-10-16

5. Phosphorylation of tyrosine 90 in SH3 domain is a new regulatory switch controlling Src kinase;2022-08-24

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