Structure of a heparin-linked biologically active dimer of fibroblast growth factor (Q27760195)

1

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I Lax

2

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D I Chen

3

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C M Svahn

4

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M Jaye

5

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J Schlessinger

6

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W A Hendrickson

Fibroblast growth factor receptor tyrosine kinases: molecular analysis and signal transduction

7

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language of work or name

English

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publication date

25 June 1998

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published in

Nature

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volume

393

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issue

6687

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page(s)

812-7

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cites work

1 reference

Signal transduction by allosteric receptor oligomerization

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Heparin-induced oligomerization of FGF molecules is responsible for FGF receptor dimerization, activation, and cell proliferation

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Structural studies of the binding of the anti-ulcer drug sucrose octasulfate to acidic fibroblast growth factor

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FGF binding and FGF receptor activation by synthetic heparan-derived di- and trisaccharides.

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Heparin structure and interactions with basic fibroblast growth factor

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Heparin is required for cell-free binding of basic fibroblast growth factor to a soluble receptor and for mitogenesis in whole cells

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Properly oriented heparin-decasaccharide-induced dimers are the biologically active form of basic fibroblast growth factor.

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Crystal structure at 1.7 A resolution of VEGF in complex with domain 2 of the Flt-1 receptor

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Reduced activation of RAF-1 and MAP kinase by a fibroblast growth factor receptor mutant deficient in stimulation of phosphatidylinositol hydrolysis

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Human endothelial cell growth factor: cloning, nucleotide sequence, and chromosome localization

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AMoRe: an automated package for molecular replacement

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Determination of macromolecular structures from anomalous diffraction of synchrotron radiation

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Improved methods for building protein models in electron density maps and the location of errors in these models

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PROCHECK: a program to check the stereochemical quality of protein structures

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SETOR: hardware-lighted three-dimensional solid model representations of macromolecules

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Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons

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Energetic characterization of the basic fibroblast growth factor-heparin interaction: identification of the heparin binding domain

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7 January 2021

Heparin-induced self-association of fibroblast growth factor-2. Evidence for two oligomerization processes

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7 January 2021

An essential heparin-binding domain in the fibroblast growth factor receptor kinase

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7 January 2021

The CCP4 suite: programs for protein crystallography

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7 January 2021

Dimensions Publication ID

Identifiers

DOI

10.1038/31741

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1033730580

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Fatcat ID

release_nftfh6l26vcwnhjcnpfgma2vji

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/nftfh6l26vcwnhjcnpfgma2vji

24 November 2022