Refinement of the structure of human basic fibroblast growth factor at 1.6 A resolution and analysis of presumed heparin binding sites by selenate substitution.
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Gentisic acid, a compound associated with plant defense and a metabolite of aspirin, heads a new class of in vivo fibroblast growth factor inhibitorsRefined crystal structure of the interleukin-1 receptor antagonist. Presence of a disulfide link and a cis-prolineMolecular mapping and functional characterization of the VEGF164 heparin-binding domainFibroblast growth factors 1 and 2 are distinct in oligomerization in the presence of heparin-like glycosaminoglycans.High throughput protein fold identification by using experimental constraints derived from intramolecular cross-links and mass spectrometry.Preferential self-association of basic fibroblast growth factor is stabilized by heparin during receptor dimerization and activation.Syndromic congenital sensorineural deafness, microtia and microdontia resulting from a novel homoallelic mutation in fibroblast growth factor 3 (FGF3).A molecular dynamics-based algorithm for evaluating the glycosaminoglycan mimicking potential of synthetic, homogenous, sulfated small molecules.Molecular characteristics of fibroblast growth factor-fibroblast growth factor receptor-heparin-like glycosaminoglycan complexIdentification of polyoxometalates as inhibitors of basic fibroblast growth factor.Nature of interaction between basic fibroblast growth factor and the antiangiogenic drug 7,7-(Carbonyl-bis[imino-N-methyl-4, 2-pyrrolecarbonylimino[N-methyl-4,2-pyrrole]-carbonylimino] )bis-(1, 3-naphthalene disulfonate).Nature of Interaction between basic fibroblast growth factor and the antiangiogenic drug 7,7-(carbonyl-bis[imino-N-methyl-4,2-pyrrolecarbonylimino[N-methyl-4,2-pyrrole]-carbonylimino])-bis-(1,3-naphtalene disulfonate). II. Removal of polar interactiMonomer complexes of basic fibroblast growth factor and heparan sulfate oligosaccharides are the minimal functional unit for cell activation.Lysine 58 and histidine 66 at the C-terminal alpha-helix of monocyte chemoattractant protein-1 are essential for glycosaminoglycan binding.A new scoring function for protein-protein docking that identifies native structures with unprecedented accuracy.Development of an in vivo method to identify mutants of phage T4 lysozyme of enhanced thermostability.Heparin binding to platelet factor-4. An NMR and site-directed mutagenesis study: arginine residues are crucial for binding.Susceptibility towards intramolecular disulphide-bond formation affects conformational stability and folding of human basic fibroblast growth factor.Molecular modeling and deletion mutagenesis implicate the nuclear translocation sequence in structural integrity of fibroblast growth factor-1.13C-NMR relation study of heparin-disaccharide interactions with tripeptides GRG and GKG.Probing fibroblast growth factor dimerization and role of heparin-like glycosaminoglycans in modulating dimerization and signaling.Glu-96 of basic fibroblast growth factor is essential for high affinity receptor binding. Identification by structure-based site-directed mutagenesis.Cytotoxic Conjugates of Fibroblast Growth Factor 2 (FGF2) with Monomethyl Auristatin E for Effective Killing of Cells Expressing FGF Receptors.
P2860
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P2860
Refinement of the structure of human basic fibroblast growth factor at 1.6 A resolution and analysis of presumed heparin binding sites by selenate substitution.
description
1993 nî lūn-bûn
@nan
1993 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1993 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
name
Refinement of the structure of ...... ites by selenate substitution.
@ast
Refinement of the structure of ...... ites by selenate substitution.
@en
type
label
Refinement of the structure of ...... ites by selenate substitution.
@ast
Refinement of the structure of ...... ites by selenate substitution.
@en
prefLabel
Refinement of the structure of ...... ites by selenate substitution.
@ast
Refinement of the structure of ...... ites by selenate substitution.
@en
P2093
P2860
P356
P1433
P1476
Refinement of the structure of ...... ites by selenate substitution.
@en
P2093
A E Eriksson
B W Matthews
L S Cousens
P2860
P304
P356
10.1002/PRO.5560020810
P577
1993-08-01T00:00:00Z