Receptor- and heparin-binding domains of basic fibroblast growth factor.
about
Three-dimensional structure of human basic fibroblast growth factor, a structural homolog of interleukin 1 betaThree-dimensional structure of human basic fibroblast growth factorNonenzymatic glycosylation in vitro and in bovine endothelial cells alters basic fibroblast growth factor activity. A model for intracellular glycosylation in diabetesRecent developments in the cell biology of basic fibroblast growth factorAlternative type I and I' turn conformations in the beta8/beta9 beta-hairpin of human acidic fibroblast growth factorFibroblast growth factors as tissue repair and regeneration therapeutics.Correlation between the 1.6 A crystal structure and mutational analysis of keratinocyte growth factor.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.Identification of FGF receptor-binding peptides for cancer gene therapy.Identification of a heparin binding domain in the N-terminal cleavage site of pro-islet amyloid polypeptide. Implications for islet amyloid formation.Identification of heparin-binding sites in proteins by selective labeling.Preferential self-association of basic fibroblast growth factor is stabilized by heparin during receptor dimerization and activation.FGFs, heparan sulfate and FGFRs: complex interactions essential for development.Basic fibroblast growth factor is a substrate for protein phosphorylation and is phosphorylated by capillary endothelial cells in culture.Instructing cells with programmable peptide DNA hybrids.Identification of a novel domain of fibroblast growth factor 2 controlling its angiogenic properties.Monoclonal antibodies against heparin-binding growth factor II/basic fibroblast growth factor that block its biological activity: invalidity of the antibodies for tumor angiogenesisGrowth factor delivery for bone tissue engineering.Angiogenic effects of extracellular human immunodeficiency virus type 1 Tat protein and its role in the pathogenesis of AIDS-associated Kaposi's sarcoma.Fibroblast growth factors in cancer: therapeutic possibilities.Amyloidogenesis: historical and modern observations point to heparan sulfate proteoglycans as a major culprit.Proteoglycans in cell regulation.The extracellular regulation of growth factor actionThe basic residues of placenta growth factor type 2 retrieve sequestered angiogenic factors into a soluble form: implications for tumor angiogenesis.In Alzheimer's disease the Golgi apparatus of a population of neurons without neurofibrillary tangles is fragmented and atrophic.Heparin binding preference and structures in the fibroblast growth factor family parallel their evolutionary diversification.Cytokines and growth factors cross-link heparan sulfate.Perivascular and intravenous administration of basic fibroblast growth factor: vascular and solid organ deposition.Basic fibroblast growth factor from human keratinocytes is a natural mitogen for melanocytes.Autocrine activities of basic fibroblast growth factor: regulation of endothelial cell movement, plasminogen activator synthesis, and DNA synthesis.Differential effects of heparin, fibronectin, and laminin on the phosphorylation of basic fibroblast growth factor by protein kinase C and the catalytic subunit of protein kinase A.Possible dissociation of the heparin-binding and mitogenic activities of heparin-binding (acidic fibroblast) growth factor-1 from its receptor-binding activities by site-directed mutagenesis of a single lysine residue.A 10-amino acid sequence of fibroblast growth factor 2 is sufficient for its mitogenic activity on neural progenitor cells.Diversification of the structural determinants of fibroblast growth factor-heparin interactions: implications for binding specificityMolecular characteristics of fibroblast growth factor-fibroblast growth factor receptor-heparin-like glycosaminoglycan complexCompartmentalization of PDGF on extracellular binding sites dependent on exon-6-encoded sequences.The fibroblast growth factor receptor is not required for herpes simplex virus type 1 infectionIsolation of peptides that inhibit binding of basic fibroblast growth factor to its receptor from a random phage-epitope libraryHerpes simplex virus infection can occur without involvement of the fibroblast growth factor receptorStructure-function studies of acidic fibroblast growth factor.
P2860
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P2860
Receptor- and heparin-binding domains of basic fibroblast growth factor.
description
1988 nî lūn-bûn
@nan
1988 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1988 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1988年の論文
@ja
1988年論文
@yue
1988年論文
@zh-hant
1988年論文
@zh-hk
1988年論文
@zh-mo
1988年論文
@zh-tw
1988年论文
@wuu
name
Receptor- and heparin-binding domains of basic fibroblast growth factor.
@ast
Receptor- and heparin-binding domains of basic fibroblast growth factor.
@en
Receptor- and heparin-binding domains of basic fibroblast growth factor.
@nl
type
label
Receptor- and heparin-binding domains of basic fibroblast growth factor.
@ast
Receptor- and heparin-binding domains of basic fibroblast growth factor.
@en
Receptor- and heparin-binding domains of basic fibroblast growth factor.
@nl
prefLabel
Receptor- and heparin-binding domains of basic fibroblast growth factor.
@ast
Receptor- and heparin-binding domains of basic fibroblast growth factor.
@en
Receptor- and heparin-binding domains of basic fibroblast growth factor.
@nl
P2093
P2860
P356
P1476
Receptor- and heparin-binding domains of basic fibroblast growth factor.
@en
P2093
P2860
P304
P356
10.1073/PNAS.85.7.2324
P407
P577
1988-04-01T00:00:00Z