The solution structure of the N-terminal domain of hepatocyte growth factor reveals a potential heparin-binding site
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Targeted disruption of heparan sulfate interaction with hepatocyte and vascular endothelial growth factors blocks normal and oncogenic signalingCrystal structures of NK1-heparin complexes reveal the basis for NK1 activity and enable engineering of potent agonists of the MET receptor.Noncoding mutations of HGF are associated with nonsyndromic hearing loss, DFNB39.Fell-Muir Lecture: Heparan sulphate and the art of cell regulation: a polymer chain conducts the protein orchestra.DMT-MM mediated functionalisation of the non-reducing end of glycosaminoglycans.Homologous plasminogen N-terminal and plasminogen-related gene A and B peptides. Characterization of cDNAs and recombinant fusion proteins.The PAN module: the N-terminal domains of plasminogen and hepatocyte growth factor are homologous with the apple domains of the prekallikrein family and with a novel domain found in numerous nematode proteins.The unique architecture and function of cellulose-interacting proteins in oomycetes revealed by genomic and structural analysesStructural basis of hepatocyte growth factor/scatter factor and MET signalling.In-vitro suppression of IL-6 and IL-8 release from human pulmonary epithelial cells by non-anticoagulant fraction of enoxaparinHeparan sulfate in angiogenesis: a target for therapy.Hepatocyte growth factor/scatter factor binds to small heparin-derived oligosaccharides and stimulates the proliferation of human HaCaT keratinocytes.Interactions of signaling proteins, growth factors and other proteins with heparan sulfate: mechanisms and mysteries.Interaction of hepatocyte growth factor with gelatin as the carrier material.Dissociation of heparan sulfate and receptor binding domains of hepatocyte growth factor reveals that heparan sulfate-c-met interaction facilitates signaling.Thiocarbamate-linked polysulfonate-peptide conjugates as selective hepatocyte growth factor receptor binders.Evidence that the conformation of unliganded human plasminogen is maintained via an intramolecular interaction between the lysine-binding site of kringle 5 and the N-terminal peptide.The N-terminal domain of hepatocyte growth factor inhibits the angiogenic behavior of endothelial cells independently from binding to the c-met receptor.Structural interpretation of 42 mutations causing factor XI deficiency using homology modeling.Insights into the structure of hepatocyte growth factor/scatter factor (HGF/SF) and implications for receptor activation.
P2860
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P2860
The solution structure of the N-terminal domain of hepatocyte growth factor reveals a potential heparin-binding site
description
1998 nî lūn-bûn
@nan
1998 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
name
The solution structure of the ...... potential heparin-binding site
@ast
The solution structure of the ...... potential heparin-binding site
@en
The solution structure of the ...... potential heparin-binding site
@nl
type
label
The solution structure of the ...... potential heparin-binding site
@ast
The solution structure of the ...... potential heparin-binding site
@en
The solution structure of the ...... potential heparin-binding site
@nl
prefLabel
The solution structure of the ...... potential heparin-binding site
@ast
The solution structure of the ...... potential heparin-binding site
@en
The solution structure of the ...... potential heparin-binding site
@nl
P2093
P1433
P1476
The solution structure of the ...... potential heparin-binding site
@en
P2093
D P Bottaro
J D Kaufman
M J Mazzulla
P T Wingfield
P304
P356
10.1016/S0969-2126(98)00012-4
P577
1998-01-01T00:00:00Z