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Inhibition of basal FGF receptor signaling by dimeric Grb2
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scholarly article
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title
Inhibition of basal FGF receptor signaling by dimeric Grb2
(English)
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main subject
Growth factor receptor bound protein 2
1 reference
stated in
GOA release 2020-03-11
identical protein binding
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stated in
GOA release 2020-03-11
author
John E. Ladbury
series ordinal
9
object named as
John E Ladbury
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Stefan T Arold
object named as
Stefan T Arold
series ordinal
7
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author name string
Chi-Chuan Lin
series ordinal
1
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Fernando A Melo
series ordinal
2
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Ragini Ghosh
series ordinal
3
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Kin M Suen
series ordinal
4
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Loren J Stagg
series ordinal
5
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John Kirkpatrick
series ordinal
6
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Zamal Ahmed
series ordinal
8
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language of work or name
English
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publication date
22 June 2012
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published in
Cell
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volume
149
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page(s)
1514-24
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issue
7
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cites work
Phosphorylation and lipid raft association of fibroblast growth factor receptor-2 in oligodendrocytes
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Crossref
reference URL
https://api.crossref.org/works/10.1016%2FJ.CELL.2012.04.033
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7 January 2021
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Solution structure of Grb2 reveals extensive flexibility necessary for target recognition
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https://api.crossref.org/works/10.1016%2FJ.CELL.2012.04.033
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7 January 2021
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NMRPipe: a multidimensional spectral processing system based on UNIX pipes
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reference URL
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Grb2 adaptor undergoes conformational change upon dimerization
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reference URL
https://api.crossref.org/works/10.1016%2FJ.CELL.2012.04.033
retrieved
7 January 2021
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Prediction of hydrodynamic and other solution properties of rigid proteins from atomic- and residue-level models
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Crossref
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7 January 2021
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An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor
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7 January 2021
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Cell signaling by receptor tyrosine kinases
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reference URL
https://api.crossref.org/works/10.1016%2FJ.CELL.2012.04.033
retrieved
7 January 2021
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Direct binding of Grb2 SH3 domain to FGFR2 regulates SHP2 function
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https://api.crossref.org/works/10.1016%2FJ.CELL.2012.04.033
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Autophosphorylation of FGFR1 kinase is mediated by a sequential and precisely ordered reaction.
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reference URL
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Macromolecular TLS refinement in REFMAC at moderate resolutions
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RTK mutations and human syndromeswhen good receptors turn bad.
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Solution structure and ligand-binding site of the carboxy-terminal SH3 domain of GRB2
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Sensing the heat: the application of isothermal titration calorimetry to thermodynamic studies of biomolecular interactions
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Topography for independent binding of alpha-helical and PPII-helical ligands to a peroxisomal SH3 domain
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Structural basis for recruitment of the adaptor protein APS to the activated insulin receptor
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HADDOCK: a protein-protein docking approach based on biochemical or biophysical information
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The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSos1
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Guanine-nucleotide-releasing factor hSos1 binds to Grb2 and links receptor tyrosine kinases to Ras signalling
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reference URL
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Fibroblast growth factor signalling: from development to cancer
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The FGF family: biology, pathophysiology and therapy
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Oligomerization of signaling complexes by the multipoint binding of GRB2 to both LAT and SOS1
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Frequent activating FGFR2 mutations in endometrial carcinomas parallel germline mutations associated with craniosynostosis and skeletal dysplasia syndromes
1 reference
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Imaging proteins in vivo using fluorescence lifetime microscopy
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Extracellular point mutations in FGFR2 elicit unexpected changes in intracellular signalling
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Crossref
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Fibroblast growth factors and their receptors in cancer
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Aberrant receptor internalization and enhanced FRS2-dependent signaling contribute to the transforming activity of the fibroblast growth factor receptor 2 IIIb C3 isoform
1 reference
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Novel Src homology 3 domain-binding motifs identified from proteomic screen of a Pro-rich region
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Signaling by fibroblast growth factors (FGF) and fibroblast growth factor receptor 2 (FGFR2)-activating mutations blocks mineralization and induces apoptosis in osteoblasts
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Molecular interaction studies using microscale thermophoresis
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The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling
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Tyrosine phosphorylation of Grb2 by Bcr/Abl and epidermal growth factor receptor: a novel regulatory mechanism for tyrosine kinase signaling
1 reference
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Rosetta FlexPepDock web server--high resolution modeling of peptide-protein interactions
1 reference
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Crossref
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Coot: model-building tools for molecular graphics
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Crossref
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Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
1 reference
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Crystal structure of the mammalian Grb2 adaptor
1 reference
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Crossref
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https://api.crossref.org/works/10.1016%2FJ.CELL.2012.04.033
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Tyrosine phosphorylation of Grb2: role in prolactin/epidermal growth factor cross talk in mammary epithelial cell growth and differentiation.
1 reference
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Crossref
reference URL
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7 January 2021
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A truncated K-sam product lacking the distal carboxyl-terminal portion provides a reduced level of autophosphorylation and greater resistance against induction of differentiation
1 reference
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Crossref
reference URL
https://api.crossref.org/works/10.1016%2FJ.CELL.2012.04.033
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7 January 2021
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FGFR2-amplified gastric cancer cell lines require FGFR2 and Erbb3 signaling for growth and survival
1 reference
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Crossref
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7 January 2021
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AZD2171 shows potent antitumor activity against gastric cancer over-expressing fibroblast growth factor receptor 2/keratinocyte growth factor receptor
1 reference
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Monoclonal antibodies to fibroblast growth factor receptor 2 effectively inhibit growth of gastric tumor xenografts
1 reference
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Involvement of fibroblast growth factor receptor 2 isoform switching in mammary oncogenesis
1 reference
stated in
Crossref
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https://api.crossref.org/works/10.1016%2FJ.CELL.2012.04.033
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7 January 2021
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Loss-of-function fibroblast growth factor receptor-2 mutations in melanoma
1 reference
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Crossref
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https://api.crossref.org/works/10.1016%2FJ.CELL.2012.04.033
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Identifiers
DOI
10.1016/J.CELL.2012.04.033
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2440549
OpenCitations bibliographic resource ID
2440549
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2440549
PubMed ID
22726438
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2440549
ResearchGate publication ID
228060552
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