(Q34413697)

English

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

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scholarly article

1 reference

Europe PubMed Central

2 August 2017

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

1 reference

Europe PubMed Central

2 August 2017

author name string

Ronald J Hause

1

1 reference

Europe PubMed Central

2 August 2017

Kin K Leung

2

1 reference

Europe PubMed Central

2 August 2017

John L Barkinge

3

1 reference

Europe PubMed Central

2 August 2017

Mark F Ciaccio

4

1 reference

Europe PubMed Central

2 August 2017

Chih-Pin Chuu

5

1 reference

Europe PubMed Central

2 August 2017

Richard B Jones

6

1 reference

Europe PubMed Central

2 August 2017

language of work or name

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publication date

4 September 2012

1 reference

Europe PubMed Central

2 August 2017

1 reference

Europe PubMed Central

2 August 2017

7

1 reference

Europe PubMed Central

2 August 2017

e44471

1 reference

Europe PubMed Central

2 August 2017

9

1 reference

Europe PubMed Central

2 August 2017

copyright license

Creative Commons Attribution 4.0 International

4 September 2012

1 reference

April 2022 Public Data File from Crossref

copyright status

0 references

Phospho.ELM: a database of phosphorylation sites--update 2011

1 reference

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Cell death or survival promoted by alternative isoforms of ErbB4

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3433420

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SH2 Domains Recognize Contextual Peptide Sequence Information to Determine Selectivity

1 reference

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1 reference

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ErbB3/HER3 intracellular domain is competent to bind ATP and catalyze autophosphorylation

1 reference

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Systems analysis of EGF receptor signaling dynamics with microwestern arrays

1 reference

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ErbB receptors and signaling pathways in cancer

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6 July 2018

System-wide investigation of ErbB4 reveals 19 sites of Tyr phosphorylation that are unusually selective in their recruitment properties

1 reference

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A quantitative study of the recruitment potential of all intracellular tyrosine residues on EGFR, FGFR1 and IGF1R.

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Defining the specificity space of the human SRC homology 2 domain

1 reference

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Src: more than the sum of its parts

1 reference

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PDZ domain binding selectivity is optimized across the mouse proteome

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The EGF receptor family: spearheading a merger of signaling and therapeutics

1 reference

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6 July 2018

Global, in vivo, and site-specific phosphorylation dynamics in signaling networks

1 reference

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Effects of HER2 overexpression on cell signaling networks governing proliferation and migration

1 reference

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6 July 2018

The human and mouse complement of SH2 domain proteins-establishing the boundaries of phosphotyrosine signaling

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3433420

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Uncovering quantitative protein interaction networks for mouse PDZ domains using protein microarrays

1 reference

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6 July 2018

A quantitative protein interaction network for the ErbB receptors using protein microarrays

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3433420

6 July 2018

Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules

1 reference

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ERBB receptors and cancer: the complexity of targeted inhibitors

1 reference

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The ERBB4/HER4 receptor tyrosine kinase regulates gene expression by functioning as a STAT5A nuclear chaperone

1 reference

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Phospho.ELM: a database of experimentally verified phosphorylation sites in eukaryotic proteins

1 reference

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PhosphoSite: A bioinformatics resource dedicated to physiological protein phosphorylation

1 reference

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Development of human protein reference database as an initial platform for approaching systems biology in humans

1 reference

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SH2 and PTB domains in tyrosine kinase signaling

1 reference

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Structural and Thermodynamic Basis for the Interaction of the Src SH2 Domain with the Activated Form of the PDGF β-receptor

1 reference

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SH2 domains, interaction modules and cellular wiring

1 reference

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1 reference

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1 reference

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1 reference

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Physiological requirement for both SH2 domains for phospholipase C-gamma1 function and interaction with platelet-derived growth factor receptors

1 reference

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Analysis of Grb7 recruitment by heregulin-activated erbB receptors reveals a novel target selectivity for erbB3

1 reference

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ErbB-2, the preferred heterodimerization partner of all ErbB receptors, is a mediator of lateral signaling

1 reference

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A fluorescence polarization based Src-SH2 binding assay

1 reference

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Diversification of Neu differentiation factor and epidermal growth factor signaling by combinatorial receptor interactions

1 reference

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Interactions between SH2 domains and tyrosine-phosphorylated platelet-derived growth factor beta-receptor sequences: analysis of kinetic parameters by a novel biosensor-based approach

1 reference

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Heregulin induces tyrosine phosphorylation of HER4/p180erbB4

1 reference

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SH2 domains recognize specific phosphopeptide sequences

1 reference

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SH2 domains exhibit high-affinity binding to tyrosine-phosphorylated peptides yet also exhibit rapid dissociation and exchange

1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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12 December 2020

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Identifiers

10.1371/JOURNAL.PONE.0044471

1 reference

Europe PubMed Central

2 August 2017

2012PLoSO...744471H

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1 reference

Europe PubMed Central

2 August 2017

1 reference

Europe PubMed Central

2 August 2017

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