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Perlecan protein core interacts with extracellular matrix protein 1 (ECM1), a glycoprotein involved in bone formation and angiogenesisMolecular cloning of a human melanoma-associated chondroitin sulfate proteoglycanPerlecan maintains the integrity of cartilage and some basement membranesChondrogenic activity of the heparan sulfate proteoglycan perlecan maps to the N-terminal domain IThe protein core of the proteoglycan perlecan binds specifically to fibroblast growth factor-7Tropoelastin binding to fibulins, nidogen-2 and other extracellular matrix proteinsChanges in the cytologic distribution of heparin/heparan sulfate interacting protein/ribosomal protein L29 (HIP/RPL29) during in vivo and in vitro mouse mammary epithelial cell expression and differentiationBinding of the NG2 proteoglycan to type VI collagen and other extracellular matrix moleculesStructural and functional characterization of the human perlecan gene promoter. Transcriptional activation by transforming growth factor-beta via a nuclear factor 1-binding elementMetastasis suppressor genes at the interface between the environment and tumor cell growthWARP is a novel multimeric component of the chondrocyte pericellular matrix that interacts with perlecanStructural determinants of antiproliferative activity of heparin on pulmonary artery smooth muscle cells.Specific inhibition of eIF-5A and collagen hydroxylation by a single agent. Antiproliferative and fibrosuppressive effects on smooth muscle cells from human coronary arteries.Role of endothelial heparanase in delayed-type hypersensitivity.An amino-terminal extension is required for the secretion of chick agrin and its binding to extracellular matrix.Agrin can mediate acetylcholine receptor gene expression in muscle by aggregation of muscle-derived neuregulins.Proteolytic disruption of laminin-integrin complexes on muscle cells during synapse formationEndostatin and endorepellin: A common route of action for similar angiostatic cancer avengersStructural characterization of the complete human perlecan gene and its promoter.alpha1 and alpha2 integrins mediate invasive activity of mouse mammary carcinoma cells through regulation of stromelysin-1 expression.Evidence for the role of proteoglycans in cation-mediated gene transfer.Identification of a novel family of laminin N-terminal alternate splice isoforms: structural and functional characterization.Structural and functional analysis of the globular domain IVa of the laminin alpha 1 chain and its impact on an adjacent RGD site.The Reproductive System.Adaptation of Sindbis virus to BHK cells selects for use of heparan sulfate as an attachment receptor.Perlecan domain V of Drosophila melanogaster. Sequence, recombinant analysis and tissue expression.Recombinant domain IV of perlecan binds to nidogens, laminin-nidogen complex, fibronectin, fibulin-2 and heparin.Structural properties of recombinant domain III-3 of perlecan containing a globular domain inserted into an epidermal-growth-factor-like motif.Recombinant domain III of perlecan promotes cell attachment through its RGDS sequence.Binding of the G domains of laminin alpha1 and alpha2 chains and perlecan to heparin, sulfatides, alpha-dystroglycan and several extracellular matrix proteins.The biology of perlecan: the multifaceted heparan sulphate proteoglycan of basement membranes and pericellular matrices.Lectin-binding sites and silver affinity of the macula densa basement membranes in the rabbit kidney.Structural characterization of recombinant domain II of the basement membrane proteoglycan perlecan.Characterization of recombinant perlecan domain I and its substitution by glycosaminoglycans and oligosaccharides.Effects of glycosaminoglycans and glycosphingolipids on cytosolic phospholipases A2 from bovine brainBiosensing of arteriosclerotic nanoplaque formation and interaction with an HMG-CoA reductase inhibitor.Evidence for the existence of multiple heparan sulfate proteoglycans in the human glomerular basement membrane and mesangial matrix.Perlecan participates in proliferation activation of quiescent Drosophila neuroblasts.The shape of thrombomodulin and interactions with thrombin as determined by electron microscopy.
P2860
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P2860
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年学术文章
@wuu
1993年学术文章
@zh-cn
1993年学术文章
@zh-hans
1993年学术文章
@zh-my
1993年学术文章
@zh-sg
1993年學術文章
@yue
1993年學術文章
@zh
1993年學術文章
@zh-hant
name
Proteoglycans of basement membranes.
@en
type
label
Proteoglycans of basement membranes.
@en
prefLabel
Proteoglycans of basement membranes.
@en
P2860
P356
P1433
P1476
Proteoglycans of basement membranes.
@en
P2093
P2860
P304
P356
10.1007/BF01923586
P577
1993-05-01T00:00:00Z