(Q28609650)

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Ligand-independent activation of fibroblast growth factor receptors by point mutations in the extracellular, transmembrane, and kinase domains

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scholarly article

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PubMed publication ID

3 February 2017

Ligand-independent activation of fibroblast growth factor receptors by point mutations in the extracellular, transmembrane, and kinase domains (English)

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PubMed publication ID

3 February 2017

transmembrane protein

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author name string

K. M. Neilson

1

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PubMed publication ID

3 February 2017

R. Friesel

2

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PubMed publication ID

3 February 2017

language of work or name

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publication date

4 October 1996

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PubMed publication ID

3 February 2017

Journal of Biological Chemistry

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PubMed publication ID

3 February 2017

271

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PubMed publication ID

3 February 2017

40

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PubMed publication ID

3 February 2017

25049–25057

1 reference

PubMed publication ID

3 February 2017

Receptor tyrosine kinases: genetic evidence for their role in Drosophila and mouse development

1 reference

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Combined deficiencies of Src, Fyn, and Yes tyrosine kinases in mutant mice.

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Expression of a dominant negative mutant of the FGF receptor disrupts mesoderm formation in Xenopus embryos

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Oncogenes and signal transduction

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Functions of fibroblast growth factors and their receptors

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The human fibroblast growth factor receptor genes: a common structural arrangement underlies the mechanisms for generating receptor forms that differ in their third immunoglobulin domain

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High-affinity binding sites for related fibroblast growth factor ligands reside within different receptor immunoglobulin-like domains

1 reference

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Determination of ligand-binding specificity by alternative splicing: two distinct growth factor receptors encoded by a single gene

1 reference

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Unique expression pattern of the FGF receptor 3 gene during mouse organogenesis

1 reference

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Requirement of FGF-4 for postimplantation mouse development

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Fibroblast growth factor receptor 3 is a negative regulator of bone growth

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Mutations in the transmembrane domain of FGFR3 cause the most common genetic form of dwarfism, achondroplasia

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Mutations in the gene encoding fibroblast growth factor receptor-3 in achondroplasia

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Thanatophoric dysplasia (types I and II) caused by distinct mutations in fibroblast growth factor receptor 3.

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A recurrent mutation in the tyrosine kinase domain of fibroblast growth factor receptor 3 causes hypochondroplasia

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A common mutation in the fibroblast growth factor receptor 1 gene in Pfeiffer syndrome

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Identical mutations in the FGFR2 gene cause both Pfeiffer and Crouzon syndrome phenotypes

1 reference

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Mutations in the fibroblast growth factor receptor 2 gene cause Crouzon syndrome

1 reference

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Apert syndrome results from localized mutations of FGFR2 and is allelic with Crouzon syndrome

1 reference

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Jackson-Weiss and Crouzon syndromes are allelic with mutations in fibroblast growth factor receptor 2

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Production of recombinant Xenopus fibroblast growth factor receptor-1 using a baculovirus expression system

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Rapid and efficient site-specific mutagenesis without phenotypic selection

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cDNA cloning and developmental expression of fibroblast growth factor receptors from Xenopus laevis

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Constitutive Activation of Fibroblast Growth Factor Receptor-2 by a Point Mutation Associated with Crouzon Syndrome

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Single-Step Method of RNA Isolation by Acid Guanidinium Thiocyanate–Phenol–Chloroform Extraction

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Raf-1 kinase is essential for early Xenopus development and mediates the induction of mesoderm by FGF

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Involvement of p21ras in Xenopus mesoderm induction

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Multiple independent activations of the neu oncogene by a point mutation altering the transmembrane domain of p185.

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Crystal structure of the tyrosine kinase domain of the human insulin receptor

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Active and inactive protein kinases: structural basis for regulation

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Alternately spliced NH2-terminal immunoglobulin-like Loop I in the ectodomain of the fibroblast growth factor (FGF) receptor 1 lowers affinity for both heparin and FGF-1.

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Neu receptor dimerization

1 reference

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Identifiers

10.1074/JBC.271.40.25049

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PubMed publication ID

1 reference

PubMed publication ID

3 February 2017

ResearchGate publication ID

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