(Q30008759)

English

Targeting Self-Binding Peptides as a Novel Strategy To Regulate Protein Activity and Function: A Case Study on the Proto-oncogene Tyrosine Protein Kinase c-Src

scientific article published on 27 March 2017

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scholarly article

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Europe PubMed Central

21 May 2017

Targeting Self-Binding Peptides as a Novel Strategy To Regulate Protein Activity and Function: A Case Study on the Proto-oncogene Tyrosine Protein Kinase c-Src (English)

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Europe PubMed Central

21 May 2017

5

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:28345935%20AND%20SRC:MED&resulttype=core&format=json

3 June 2020

author name string

Zhengya Bai

1

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3 June 2020

Shasha Hou

2

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3 June 2020

Shilei Zhang

3

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3 June 2020

Zhongyan Li

4

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3 June 2020

publication date

27 March 2017

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21 May 2017

Journal of Chemical Information and Modeling

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3 June 2020

57

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3 June 2020

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3 June 2020

835-845

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3 June 2020

Functional diversity of Csk, Chk, and Src SH2 domains due to a single residue variation

1 reference

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SH2 domains recognize specific phosphopeptide sequences

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The structural basis of peptide-protein binding strategies.

1 reference

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Comparison of simple potential functions for simulating liquid water

1 reference

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A two-step binding mechanism for the self-binding peptide recognition of target domains.

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Free Energy Calculations by the Molecular Mechanics Poisson-Boltzmann Surface Area Method

1 reference

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Kinetics of p56lck and p60src Src homology 2 domain binding to tyrosine-phosphorylated peptides determined by a competition assay or surface plasmon resonance

1 reference

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Src autoinhibition: let us count the ways

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Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes

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Self-binding peptides: folding or binding?

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Comprehensive binary interaction mapping of SH2 domains via fluorescence polarization reveals novel functional diversification of ErbB receptors

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Ins and outs of kinase DFG motifs.

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Crystal structures of c-Src reveal features of its autoinhibitory mechanism

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αC helix as a switch in the conformational transition of Src/CDK-like kinase domains

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αC helix displacement as a general approach for allosteric modulation of protein kinases.

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