Alpha 1(XVIII), a collagen chain with frequent interruptions in the collagenous sequence, a distinct tissue distribution, and homology with type XV collagen
about
Proteoglycan form and function: A comprehensive nomenclature of proteoglycansComplete exon-intron organization of the human gene for the alpha1 chain of type XV collagen (COL15A1) and comparison with the homologous COL18A1 geneCrystal structure of the angiogenesis inhibitor endostatin at 1.5 A resolutionIsolation and sequencing of cDNAs for proteins with multiple domains of Gly-Xaa-Yaa repeats identify a distinct family of collagenous proteinsSecreted cathepsin L generates endostatin from collagen XVIIIZinc-dependent dimers observed in crystals of human endostatinLocation of type XV collagen in human tissues and its accumulation in the interstitial matrix of the fibrotic kidneyCorneal neovascularization and the utility of topical VEGF inhibition: ranibizumab (Lucentis) vs bevacizumab (Avastin)A cryptic frizzled module in cell surface collagen 18 inhibits Wnt/beta-catenin signalingCrystal Structure of Human Collagen XVIII Trimerization Domain: A Novel Collagen Trimerization FoldCrystal structure of the human collagen XV trimerization domain: A potent trimerizing unit common to multiplexin collagensLack of collagen XVIII/endostatin results in eye abnormalitiesBasement membrane zone collagens XV and XVIII/proteoglycans mediate leukocyte influx in renal ischemia/reperfusionMouse Col18a1 is expressed in a tissue-specific manner as three alternative variants and is localized in basement membrane zonesGeneration and degradation of human endostatin proteins by various proteinasesCollagen XVIII is a basement membrane heparan sulfate proteoglycan.Homeostatic control of angiogenesis: A newly identified function of the liver?Structure, function and tissue forms of the C-terminal globular domain of collagen XVIII containing the angiogenesis inhibitor endostatin.Basement membrane zone type XV collagen is a disulfide-bonded chondroitin sulfate proteoglycan in human tissues and cultured cells.Endostatin regulates branching morphogenesis of renal epithelial cells and ureteric bud.Still more complexity in mammalian basement membranes.[Matrikines: a new anticancer therapeutic strategy].Elective orthopedic and cardiopulmonary bypass surgery causes a reduction in serum endostatin levels.Lack of collagen XVIII long isoforms affects kidney podocytes, whereas the short form is needed in the proximal tubular basement membrane.New functional roles for non-collagenous domains of basement membrane collagensLipid raft redox signaling: molecular mechanisms in health and disease.Genotype analysis of the human endostatin variant p.D104N in benign and malignant adrenocortical tumors.Distribution of type XV collagen transcripts in human tissue and their production by muscle cells and fibroblasts.Endostatin lowers blood pressure via nitric oxide and prevents hypertension associated with VEGF inhibition.The NC1/endostatin domain of Caenorhabditis elegans type XVIII collagen affects cell migration and axon guidance.Oligomerization-dependent regulation of motility and morphogenesis by the collagen XVIII NC1/endostatin domainMutations in collagen 18A1 and their relevance to the human phenotype.Collagen type XVIII/endostatin is differentially expressed in primary and metastatic colorectal cancers and ovarian carcinomasThe extracellular matrix and blood vessel formation: not just a scaffold.Endostatin and transglutaminase 2 are involved in fibrosis of the aging kidney.Critical role of lipid raft redox signaling platforms in endostatin-induced coronary endothelial dysfunction.Molecular analysis of collagen XVIII reveals novel mutations, presence of a third isoform, and possible genetic heterogeneity in Knobloch syndromeExercise increases serum endostatin levels in female and male patients with diabetes and controls.Mining the extracellular matrix for tissue engineering applications.Overview of extracellular matrix.
P2860
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P2860
Alpha 1(XVIII), a collagen chain with frequent interruptions in the collagenous sequence, a distinct tissue distribution, and homology with type XV collagen
description
1994 nî lūn-bûn
@nan
1994 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
Alpha 1(XVIII), a collagen cha ...... homology with type XV collagen
@ast
Alpha 1(XVIII), a collagen cha ...... homology with type XV collagen
@en
type
label
Alpha 1(XVIII), a collagen cha ...... homology with type XV collagen
@ast
Alpha 1(XVIII), a collagen cha ...... homology with type XV collagen
@en
prefLabel
Alpha 1(XVIII), a collagen cha ...... homology with type XV collagen
@ast
Alpha 1(XVIII), a collagen cha ...... homology with type XV collagen
@en
P2860
P356
P1476
Alpha 1(XVIII), a collagen cha ...... homology with type XV collagen
@en
P2093
Pihlajaniemi T
P2860
P304
P356
10.1073/PNAS.91.10.4234
P407
P577
1994-05-01T00:00:00Z