Identification of specific sites involved in ligand binding by photoaffinity labeling of the receptor for the urokinase-type plasminogen activator. Residues located at equivalent positions in uPAR domains I and III participate in the assembly of a c

Identification of specific sites involved in ligand binding by photoaffinity labeling of the receptor for the urokinase-type plasminogen activator. Residues located at equivalent positions in uPAR domains I and III participate in the assembly of a c

Item
http://www.wikidata.org/entity/Q31960282
Crystal structure of the human urokinase plasminogen activator receptor bound to an antagonist peptideDirect binding of occupied urokinase receptor (uPAR) to LDL receptor-related protein is required for endocytosis of uPAR and regulation of cell surface urokinase activityThe urokinase receptor (uPAR) and the uPAR-associated protein (uPARAP/Endo180): membrane proteins engaged in matrix turnover during tissue remodelingPhotoaffinity labeling combined with mass spectrometric approaches as a tool for structural proteomics.Mapping the topographic epitope landscape on the urokinase plasminogen activator receptor (uPAR) by surface plasmon resonance and X-ray crystallographyRandom peptide bacteriophage display as a probe for urokinase receptor ligands.Mapping of the vitronectin-binding site on the urokinase receptor: involvement of a coherent receptor interface consisting of residues from both domain I and the flanking interdomain linker region.The acidic domain of GPIHBP1 is important for the binding of lipoprotein lipase and chylomicrons.Molecular and functional interdependence of the urokinase-type plasminogen activator system with integrins.Therapeutic potential of siRNA-mediated targeting of urokinase plasminogen activator, its receptor, and matrix metalloproteinases.Highly conserved cysteines within the Ly6 domain of GPIHBP1 are crucial for the binding of lipoprotein lipase.Cyr61 and YB-1 are novel interacting partners of uPAR and elevate the malignancy of triple-negative breast cancer.Structure-driven design of radionuclide tracers for non-invasive imaging of uPAR and targeted radiotherapy. The tale of a synthetic peptide antagonist.Mapping part of the functional epitope for ligand binding on the receptor for urokinase-type plasminogen activator by site-directed mutagenesis.The receptor for urokinase-plasminogen activator (uPAR) controls plasticity of cancer cell movement in mesenchymal and amoeboid migration style.uPA/uPAR system activation drives a glycolytic phenotype in melanoma cells.Differential binding of urokinase and peptide antagonists to the urokinase receptor: evidence from characterization of the receptor in four primate species.
P2860

Identification of specific sites involved in ligand binding by photoaffinity labeling of the receptor for the urokinase-type plasminogen activator. Residues located at equivalent positions in uPAR domains I and III participate in the assembly of a c

Item
http://www.wikidata.org/entity/Q31960282
description
1998 nî lūn-bûn
@nan
1998 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Identification of specific sit ...... icipate in the assembly of a c
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Identification of specific sit ...... icipate in the assembly of a c
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type
label
Identification of specific sit ...... icipate in the assembly of a c
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Identification of specific sit ...... icipate in the assembly of a c
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prefLabel
Identification of specific sit ...... icipate in the assembly of a c
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Identification of specific sit ...... icipate in the assembly of a c
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P1433
P1476
P2093
P304
P31
P356
P407
P433
P478
P50
P577
P698
P921
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P1433
P1476
Identification of specific sit ...... composite ligand-binding site
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P2093
P304
P31
P356
P407
P433
P478
P50
P577
P698
P921