Structural interactions of fibroblast growth factor receptor with its ligands - Wikidata - wikimedia - TriplyDB

Structural interactions of fibroblast growth factor receptor with its ligands

Structural interactions of fibroblast growth factor receptor with its ligands

http://www.wikidata.org/entity/Q22011005

about

Structural basis for fibroblast growth factor receptor 2 activation in Apert syndrome Structural basis by which alternative splicing confers specificity in fibroblast growth factor receptors Gentisic acid, a compound associated with plant defense and a metabolite of aspirin, heads a new class of in vivo fibroblast growth factor inhibitors Insights into the molecular basis for fibroblast growth factor receptor autoinhibition and ligand-binding promiscuity Fibroblast growth factor (FGF) homologous factors share structural but not functional homology with FGFs FGF-10 and its receptor exhibit bidirectional paracrine targeting to urothelial and smooth muscle cells in the lower urinary tract Identification of receptor and heparin binding sites in fibroblast growth factor 4 by structure-based mutagenesis Analysis of mutations in fibroblast growth factor (FGF) and a pathogenic mutation in FGF receptor (FGFR) provides direct evidence for the symmetric two-end model for FGFR dimerization Cell signaling by receptor tyrosine kinases The alternatively spliced acid box region plays a key role in FGF receptor autoinhibition Fibroblast growth factor homologous factors are intracellular signaling proteins Exploring mechanisms of FGF signalling through the lens of structural biology Structure of the active core of human stem cell factor and analysis of binding to its receptor Kit Alternative type I and I' turn conformations in the beta8/beta9 beta-hairpin of human acidic fibroblast growth factor Structure and stability of an acidic fibroblast growth factor from Notophthalmus viridescens Structure of the extracellular domains of the human interleukin-6 receptor alpha -chain Homodimerization Controls the Fibroblast Growth Factor 9 Subfamily's Receptor Binding and Heparan Sulfate-Dependent Diffusion in the Extracellular Matrix Engineering an improved crystal contact across a solvent-mediated interface of human fibroblast growth factor 1.Plasticity in Interactions of Fibroblast Growth Factor 1 (FGF1) N Terminus with FGF Receptors Underlies Promiscuity of FGF1 Fibroblast growth factor signaling in Caenorhabditis elegans Molecular mechanisms of fibroblast growth factor signaling in physiology and pathology Genomic screening of fibroblast growth-factor receptor 2 reveals a wide spectrum of mutations in patients with syndromic craniosynostosis Identification of rare partially unfolded states in equilibrium with the native conformation in an all beta-barrel protein.Virtual screening on an α-helix to β-strand switchable region of the FGFR2 extracellular domain revealed positive and negative modulators.Development of a high throughput screening assay for inhibitors of fibroblast growth factor-receptor-heparin interactions.A light scattering study of the interaction of fibroblast growth factor (FGF) with its receptor Chemical Tumor Biology of Heparan Sulfate Proteoglycans.Interrogating protein interaction networks through structural biology Biochemical analysis of pathogenic ligand-dependent FGFR2 mutations suggests distinct pathophysiological mechanisms for craniofacial and limb abnormalities.Potential use of non-classical pathways for the transport of macromolecular drugs.Protein-protein interactions in receptor activation and intracellular signalling.Molecular diversity of heparan sulfate.FIGC, a novel FGF-induced ubiquitin-protein ligase in gastric cancers.Signaling by fibroblast growth factors: the inside story.Structural basis for activation of fibroblast growth factor signaling by sucrose octasulfate Heparan sulfate proteoglycans and human breast cancer epithelial cell tumorigenicity.FGFs, their receptors, and human limb malformations: clinical and molecular correlations.Perlecan and tumor angiogenesis.2-O Heparan Sulfate Sulfation by Hs2st Is Required for Erk/Mapk Signalling Activation at the Mid-Gestational Mouse Telencephalic Midline.Mechanistic diversity of cytokine receptor signaling across cell membranes.

P2860

2f12ca9a60519a4424405e7f35e967b0d03c11e2 72f1395e211c298db27887767224fdb01efafe22

P248

Q24291302-098439C4-B138-449A-A034-6DD91BA7F0A9 Q24294933-6490A87B-AF73-414E-A380-FA3D7454162F Q24298832-DC71B231-1AE1-430E-9129-4A9E4E80B781 Q24305380-69E13A1B-089D-414A-A8D8-6E51A9AB8AFA Q24305543-99E3E5D5-F281-4A6A-B8A7-850185984982 Q24314647-9ED122BC-69BE-46D8-955F-7E3FD15F4CB9 Q24550863-D0F14E02-2724-40F3-9F1B-54AD06823C40 Q24557572-F317D823-FCDA-4E94-949B-17CB77ED4A47 Q24598357-EF23CBC2-0587-44C4-B5A6-BA0F63B7B2A2 Q24602026-F9535692-D4A0-4CB5-A91D-A82CDBC91B07 Q24628289-13842B8C-C557-4F46-9D8E-E6F7E9522AC0 Q27015054-F1F27941-F0C6-4235-85FA-4C56A0B066BD Q27625176-26EA21AA-072B-4F97-A5D7-F50B72880E99 Q27637812-38B6BFDD-414E-4B47-A284-67E570128AA8 Q27639562-44EBA1FF-FF75-49E9-B30D-12DAD3E05796 Q27640083-DB875349-3855-4218-8D14-C1FEFCB15806 Q27646372-A86D7B8A-6664-4211-BF43-B2C83E347555 Q27658256-6617DA05-8BD3-43F8-8D84-AD4952FAD4E2 Q27675418-F8688800-17B0-48CD-AF5A-BD81D64E2C7A Q28211519-C02D1140-28C2-4F27-A847-01DC84E0F085 Q28291993-14ED72C6-87F9-4ACD-B78E-AF3A4FB0B07E Q28344714-821C2EA9-5A4D-43AB-B4EE-349FFD065857 Q30165309-D0D58F4A-E794-4E05-9598-E29CB9D8B3F5 Q30365357-98FE73A0-E021-4F5E-8E78-4B8040C59B43 Q30760295-9B2A1DEB-0BDC-4D08-8E67-EAA80999F460 Q33321817-C4989F4D-7A85-4844-8A36-3A44278377A7 Q33944132-FF8A9FB1-C901-4138-8E3E-069A6E195F28 Q34027140-9A33614E-D5D3-4127-8E89-3541444EAE1A Q34074836-A07CC102-0313-4D2D-A39E-2629DEC5A8BA Q34075054-A2618A1C-0FE5-4D3A-BDF2-55BEA5083C8C Q34081480-DD5E3FA6-3175-46E5-BD65-5AF2D73715D9 Q34310374-C0D8F517-36EF-4B05-82AC-605A16B4CDBB Q34373899-83C3F7AD-7807-42BE-9DBF-AA74D7823C25 Q34425256-119A28C7-6126-4AF2-BD6D-AD10A9FDB376 Q34442255-6BD034B3-CCCC-4046-9282-77E1BAB01379 Q34475894-B3A829A8-6BD6-4B9C-81D0-C00682FEB407 Q34926833-85EDDA94-B948-4DCB-884A-E24CD2201E86 Q35562693-543DDA94-0214-40AC-BB46-C4D40E796280 Q35663605-B367A495-2E56-4F27-A97F-F12E669CF094 Q35764259-A4EA6992-6B5D-42E6-841E-2C6778E1E7D4

P2860

Structural interactions of fibroblast growth factor receptor with its ligands

http://www.wikidata.org/entity/Q22011005

description

2000 nî lūn-bûn

@nan

2000 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2000 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2000年の論文

@ja

2000年論文

@yue

2000年論文

@zh-hant

2000年論文

@zh-hk

2000年論文

@zh-mo

2000年論文

@zh-tw

2000年论文

@wuu

name

Structural interactions of fibroblast growth factor receptor with its ligands

@ast

Structural interactions of fibroblast growth factor receptor with its ligands

@en

Structural interactions of fibroblast growth factor receptor with its ligands

@en-gb

Structural interactions of fibroblast growth factor receptor with its ligands

@nl

type

label

Structural interactions of fibroblast growth factor receptor with its ligands

@ast

Structural interactions of fibroblast growth factor receptor with its ligands

@en

Structural interactions of fibroblast growth factor receptor with its ligands

@en-gb

Structural interactions of fibroblast growth factor receptor with its ligands

@nl

prefLabel

Structural interactions of fibroblast growth factor receptor with its ligands

@ast

Structural interactions of fibroblast growth factor receptor with its ligands

@en

Structural interactions of fibroblast growth factor receptor with its ligands

@en-gb

Structural interactions of fibroblast growth factor receptor with its ligands

@nl

P1433

Q22011005-17319B9B-66B0-48F9-B20C-FBA3D6B66D1F

P1476

Q22011005-E41CC978-8B32-462D-84D1-4047741A2C90

P2093

Q22011005-7187B0E3-9E8A-4471-A187-C5D878908A2E

Q22011005-79608AA3-0B5B-4046-A98D-149DB664D127

Q22011005-A7B07BEE-8ECA-41E5-A14A-A384C8B575C7

P2860

Q22011005-027A9AA1-BC04-424F-81FA-BBDBCF29BC90

Q22011005-04CA4500-3C17-4FFD-B4ED-9F1F04BF03E9

Q22011005-0B245771-241E-47E6-BFCD-AAB2477E15A4

Q22011005-0DBEF6AB-BEC6-4D58-AB3C-6DE2F775CA54

Q22011005-10E4BAEF-FE6F-4712-A21F-9ABED805787C

Q22011005-1CB802A4-6B57-4E40-A5A8-D2A512435200

Q22011005-24438CC0-2551-4554-8BB7-EA744B9B1E92

Q22011005-25E13F8C-313E-449C-96BF-0C2BE6723D6F

Q22011005-2E13695A-4A80-4C35-B5E5-6A16586017DD

Q22011005-3709BFB0-DF71-4D51-AADF-A8C63F776092

P304

Q22011005-F3FA2818-C96E-449D-B868-CD38862A409A

P31

Q22011005-815AA927-DAAE-47FE-A660-D45E68047732

P356

Q22011005-41D902D6-2AE5-4449-8D22-8DD7F5563E61

P407

Q22011005-AC1AA365-B68F-4345-AF6F-C5D2B9065263

P433

Q22011005-53EF78B0-090A-405F-A589-BF5004C59394

P478

Q22011005-F8353ED4-8EC0-4ACF-97D0-A253EFC2C089

P577

Q22011005-1A5FCC23-3AFD-4A18-99D8-B33051028441

P5875

Q22011005-8F6EE61C-711C-4908-9CF8-74D07B619EE0

P698

Q22011005-217100C3-8F45-4850-9AC9-3F619088F39B

P932

Q22011005-7ADE0DBC-7695-435D-B083-1420DADF4CEC

P356

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Structural interactions of fibroblast growth factor receptor with its ligands

@en

P2093

A D DiGabriele

http://www.w3.org/2001/XMLSchema#string

D J Stauber

http://www.w3.org/2001/XMLSchema#string

W A Hendrickson

http://www.w3.org/2001/XMLSchema#string

P2860

Efficiency of signalling through cytokine receptors depends critically on receptor orientation

Crystal structure of nerve growth factor in complex with the ligand-binding domain of the TrkA receptor

Structural basis for FGF receptor dimerization and activation

Cloning and expression of two distinct high-affinity receptors cross-reacting with acidic and basic fibroblast growth factors

Human growth hormone and extracellular domain of its receptor: crystal structure of the complex

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

N.m.r. and molecular-modelling studies of the solution conformation of heparin

Atomic structure of the GCSF-receptor complex showing a new cytokine-receptor recognition scheme

X-ray structure determination of telokin, the C-terminal domain of myosin light chain kinase, at 2.8 A resolution

Crystal structure of an integrin-binding fragment of vascular cell adhesion molecule-1 at 1.8 A resolution

P304

49-54

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1073/PNAS.97.1.49

http://www.w3.org/2001/XMLSchema#string

P407

P433

1

http://www.w3.org/2001/XMLSchema#string

P478

97

http://www.w3.org/2001/XMLSchema#string

P577

2000-01-04T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

51363891

http://www.w3.org/2001/XMLSchema#string

P698

10618369

http://www.w3.org/2001/XMLSchema#string

P932

26614

http://www.w3.org/2001/XMLSchema#string