New functional roles for non-collagenous domains of basement membrane collagens - Test2 - elhamkhani - TriplyDB

New functional roles for non-collagenous domains of basement membrane collagens

New functional roles for non-collagenous domains of basement membrane collagens

http://www.wikidata.org/entity/Q34958987

about

Cleavage of the matricellular protein SPARC by matrix metalloproteinase 3 produces polypeptides that influence angiogenesis Physiological levels of tumstatin, a fragment of collagen IV alpha3 chain, are generated by MMP-9 proteolysis and suppress angiogenesis via alphaV beta3 integrin Topical Collagen-Based Biomaterials for Chronic Wounds: Rationale and Clinical Application Collagens.Bacterial collagen-like proteins that form triple-helical structures Basement membrane zone collagens XV and XVIII/proteoglycans mediate leukocyte influx in renal ischemia/reperfusion Esophageal muscle physiology and morphogenesis require assembly of a collagen XIX-rich basement membrane zone Matrix metalloproteinases and the regulation of tissue remodelling The extracellular matrix in development and morphogenesis: a dynamic view.Muscle-derived collagen XIII regulates maturation of the skeletal neuromuscular junction.Recombinant non-collagenous domain of alpha2(IV) collagen causes involution of choroidal neovascularization by inducing apoptosis.Extracellular matrix and its role in spermatogenesis Inhibitory effects of arresten on bFGF-induced proliferation, migration, and matrix metalloproteinase-2 activation in mouse retinal endothelial cells Characterization of a non-fibrillar-related collagen in the mollusc Haliotis tuberculata and its biological activity on human dermal fibroblasts.A local autocrine axis in the testes that regulates spermatogenesis.Hormonal and local control of mammary branching morphogenesis Collagen XIX is expressed by interneurons and contributes to the formation of hippocampal synapses.Synthetic disulfide-bridged cyclic peptides mimic the anti-angiogenic actions of chondromodulin-I.Molecular cloning, expression and purification of recombinant soluble mouse endostatin as an anti-angiogenic protein in Escherichia coli.Collagen type IV at the fetal-maternal interface.Recombinant alpha2(IV)NC1 domain inhibits tumor cell-extracellular matrix interactions, induces cellular senescence, and inhibits tumor growth in vivo.Inhibition of experimental metastasis by targeting the HUIV26 cryptic epitope in collagen.Lamstatin--a novel inhibitor of lymphangiogenesis derived from collagen IV Recessive mutations in the α3 (VI) collagen gene COL6A3 cause early-onset isolated dystonia.Regulation of matrix biology by matrix metalloproteinases.Type I collagen gene suppresses tumor growth and invasion of malignant human glioma cells L-arginine mediated renaturation enhances yield of human, α6 Type IV collagen non-collagenous domain from bacterial inclusion bodies.Enzymatic processing of collagen IV by MMP-2 (gelatinase A) affects neutrophil migration and it is modulated by extracatalytic domains.Two Bioactive Molecular Weight Fractions of a Conditioned Medium Enhance RPE Cell Survival on Age-Related Macular Degeneration and Aged Bruch's Membrane NC1 domain of collagen α3(IV) derived from the basement membrane regulates Sertoli cell blood-testis barrier dynamics.Preparation and characterization of a biologic scaffold from esophageal mucosa MIG-17/ADAMTS controls cell migration by recruiting nidogen to the basement membrane in C. elegans.Cathepsin B Regulates Collagen Expression by Fibroblasts via Prolonging TLR2/NF-κB Activation MT2-MMP-dependent release of collagen IV NC1 domains regulates submandibular gland branching morphogenesis.Contribution of host MMP-2 and MMP-9 to promote tumor vascularization and invasion of malignant keratinocytes.Lack of collagen XV is protective after ischemic stroke in mice.Extracellular matrix signaling in morphogenesis and repair.Salivary gland development: a template for regeneration.Age-related macular degeneration and changes in the extracellular matrix.Vastatin, an Endogenous Antiangiogenesis Polypeptide That Is Lost in Hepatocellular Carcinoma, Effectively Inhibits Tumor Metastasis.

P2860

Q24309124-BA9DEFFF-A511-48BD-907D-C85C87D44CCA Q24641850-38CB4055-A919-4D0B-ACC5-4F71E6930D8F Q26767417-23CC6C28-8D08-48F5-B176-9B9BB367BB12 Q27967659-C0DEF5DC-D9B8-4B13-B1B5-A6B96E51F529 Q28390080-8AD88AE9-E767-4DBF-93FE-11763B2BD195 Q28542782-F18DB8AF-2FDD-4CFD-B549-DB86D793DE39 Q28585359-8502C7DD-9CDD-4712-B061-D9C0132EF30C Q29618747-35EE405A-A12B-48E9-B65A-4AB51712D9F0 Q30432483-3A611256-8AE9-4B47-92F9-BDC9268213B6 Q30497006-0140F722-0446-439D-853F-7B0F8BA6419C Q33237435-F9A683FE-07F9-43D2-8688-330A1F7D0C64 Q33674054-F9880D23-DE4F-4B8D-BCA4-494A2FAC9E1E Q33685500-97284440-3E7E-4880-82DF-ABB74C75B330 Q33805033-30568299-82C9-4C20-978E-DEB0DB60A3E9 Q33841603-939CC537-2F12-4A97-BAC3-95389345F02F Q33845036-167E5A9D-B042-445B-9C6A-5E8A62EC7112 Q34035023-4C77EEA3-DDAD-4A15-BD00-D05C3ACB8E29 Q34262295-260991C8-DC4F-4B01-B839-C20D46CA6366 Q34446517-6F751ABC-FFD4-4F28-95F6-89D4103FC3B1 Q34996675-29D7BFCD-07DF-46AF-A67D-054D82AAD013 Q35083731-F09D5238-10A9-4174-9658-767FDE75C019 Q35088252-445A13DA-9018-4F24-B63A-33BFB37D10F9 Q35370419-1AFFC5D0-683E-4DE8-9EBE-9543E1EA76EB Q35689799-2B571E46-25C4-45F4-B423-30085793F932 Q35885655-25842D16-D078-43E9-81D1-45DCE6A7F4C3 Q35902328-F4FCC0A4-0027-44CA-B10C-DC65D8B81915 Q36203315-F51B0DD5-B5F2-4936-90FD-6C967B94E583 Q36458187-483EDC1C-A71A-4650-9303-2F2227AD2262 Q36630592-2BFD6892-9162-456B-BD30-280EAD52AB66 Q37008685-99943EA2-2FEE-43CC-87FF-AEE963F04D7E Q37055796-0AA46DAC-BC05-4205-9AB5-2930F63F0DC8 Q37081729-EF88502A-74DC-4947-9C83-10981CE3DA4D Q37246551-C26FC286-C01F-4B99-85C7-4A31A7F77949 Q37401941-13526450-3DC2-4268-BA18-F993A792B2A9 Q37407293-D703CC95-0524-4283-A3F8-6C5526648D41 Q37744900-C4786FCE-1D29-4545-9BC6-95C721DB2801 Q38111039-E6ACCB43-9560-4B57-9650-ACA8FD265EE5 Q38170923-5DB8B4D3-BED1-4F5B-A682-1567955EB03D Q38221023-8F851F69-40D4-4394-ABFE-E1F6FB119C5C Q38787495-00C2343C-4B42-4751-9EF6-97974C67A044

P2860

New functional roles for non-collagenous domains of basement membrane collagens

http://www.wikidata.org/entity/Q34958987

description

2002 nî lūn-bûn

@nan

2002 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

2002年の論文

@ja

2002年論文

@yue

2002年論文

@zh-hant

2002年論文

@zh-hk

2002年論文

@zh-mo

2002年論文

@zh-tw

2002年论文

@wuu

name

New functional roles for non-collagenous domains of basement membrane collagens

@ast

New functional roles for non-collagenous domains of basement membrane collagens

@en

New functional roles for non-collagenous domains of basement membrane collagens

@nl

type

label

New functional roles for non-collagenous domains of basement membrane collagens

@ast

New functional roles for non-collagenous domains of basement membrane collagens

@en

New functional roles for non-collagenous domains of basement membrane collagens

@nl

prefLabel

New functional roles for non-collagenous domains of basement membrane collagens

@ast

New functional roles for non-collagenous domains of basement membrane collagens

@en

New functional roles for non-collagenous domains of basement membrane collagens

@nl

P1433

Q34958987-CFC5FC5A-42E9-472A-9A77-F2854517D1FD

P1476

Q34958987-7D42690A-B8C3-4E70-A82D-E3DDA9D5808C

P2093

Q34958987-00AF7B95-A291-4D08-BC05-597E8E82D837

Q34958987-38798FD2-704E-4233-950C-7A173912FA5E

P2860

Q34958987-03937023-5C03-4AEA-A87E-1AD1E2E1DBE9

Q34958987-03D0C092-5BC6-479E-B124-16BC316C1211

Q34958987-067CB117-A864-42CF-B8F4-9B567A08437E

Q34958987-0B61BA6B-1543-46CD-832F-7C0195102EF2

Q34958987-0C970BA6-E81A-4B43-95B4-B9BE183F3297

Q34958987-0E53EBD3-076D-4A1F-B19A-5176CD6E4B2E

Q34958987-0FD12282-1FEB-41C7-AC2C-2D4256245A9D

Q34958987-14F4D638-88DB-432A-BC0A-D4EA1E6DC029

Q34958987-15770312-5DDD-4631-84ED-1EF6E2864CC9

Q34958987-15F6B04D-7D5C-4364-9584-C6EA65200944

P304

Q34958987-06229003-22B1-4B70-9432-4FC829E9D305

P31

Q34958987-EEC3BDCC-82EF-43A2-B053-02E9C54C087F

P356

Q34958987-97EE5144-EAB2-459F-91F2-259B6D7D202E

P407

Q34958987-45C8E74F-F2DF-434E-90F0-D91647E51B8D

P433

Q34958987-5990F4E2-6248-47D3-BE49-E00B18E8EB78

P478

Q34958987-3C824934-068F-4D09-A00F-EE3197CC3EA9

P50

Q34958987-F6405B4D-3A5A-4E81-BCFF-8A88404876EB

P577

Q34958987-41C54DD0-02D1-4777-84DB-7C28B0CC70E0

P5875

Q34958987-C671CA7B-709C-422C-9AA0-CB5403CE4ED2

P698

Q34958987-6592D1BE-2E7C-4A76-8FC4-777E5F4BA755

P932

Q34958987-F609A9E3-1866-4A94-8B73-EF38D2E11AC6

P356

P1433

Journal of Cell Science

P1476

New functional roles for non-collagenous domains of basement membrane collagens

@en

P2093

Nathalie Ortega

http://www.w3.org/2001/XMLSchema#string

Zena Werb

http://www.w3.org/2001/XMLSchema#string

P2860

Canstatin, a novel matrix-derived inhibitor of angiogenesis and tumor growth

Distinct antitumor properties of a type IV collagen domain derived from basement membrane

Two RGD-independent alpha vbeta 3 integrin binding sites on tumstatin regulate distinct anti-tumor properties

Collagen XVIII, containing an endogenous inhibitor of angiogenesis and tumor growth, plays a critical role in the maintenance of retinal structure and in neural tube closure (Knobloch syndrome)

The 1.9-A crystal structure of the noncollagenous (NC1) domain of human placenta collagen IV shows stabilization via a novel type of covalent Met-Lys cross-link

Identification of mutations in the alpha 3(IV) and alpha 4(IV) collagen genes in autosomal recessive Alport syndrome

Endostatin: an endogenous inhibitor of angiogenesis and tumor growth

Crystal structure of the angiogenesis inhibitor endostatin at 1.5 A resolution

Interaction of endostatin with integrins implicated in angiogenesis

Isolation and sequencing of cDNAs for proteins with multiple domains of Gly-Xaa-Yaa repeats identify a distinct family of collagenous proteins

P304

4201-4214

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1242/JCS.00106

http://www.w3.org/2001/XMLSchema#string

P407

P433

Pt 22

http://www.w3.org/2001/XMLSchema#string

P478

115

http://www.w3.org/2001/XMLSchema#string

P50

P577

2002-11-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

11082743

http://www.w3.org/2001/XMLSchema#string

P698

12376553

http://www.w3.org/2001/XMLSchema#string

P932

2789001

http://www.w3.org/2001/XMLSchema#string