Proteolytic modification of laminins: functional consequences.
about
Uncoordinated production of Laminin-5 chains in airways epithelium of allergic asthmatics.Regulated synthesis and functions of laminin 5 in polarized madin-darby canine kidney epithelial cellsAutocrine transforming growth factor-{beta}1 activation mediated by integrin {alpha}V{beta}3 regulates transcriptional expression of laminin-332 in Madin-Darby canine kidney epithelial cellsThe basement membrane matrix in malignancy.SIKVAV, a laminin alpha1-derived peptide, interacts with integrins and increases protease activity of a human salivary gland adenoid cystic carcinoma cell line through the ERK 1/2 signaling pathway.Immobilization of Cell-Adhesive Laminin Peptides in Degradable PEGDA Hydrogels Influences Endothelial Cell Tubulogenesis.Laminin 5 regulates polycystic kidney cell proliferation and cyst formation.Membrane type 1 matrix metalloprotease cleaves laminin-10 and promotes prostate cancer cell migration.Recombinant human laminin-5 domains. Effects of heterotrimerization, proteolytic processing, and N-glycosylation on alpha3beta1 integrin binding.Function of laminins and laminin-binding integrins in gingival epithelial cell adhesion.Expression and localization of laminin 5, laminin 10, type IV collagen, and amelotin in adult murine gingiva.A comparative quantitative analysis of laminin-5 in the basement membrane of normal, hyperplastic, and malignant oral mucosa by confocal immunofluorescence imaging.Overexpression of laminin alpha1 chain in colonic cancer cells induces an increase in tumor growth.The junctional epithelium around murine teeth differs from gingival epithelium in its basement membrane composition.
P2860
Q24814617-F1AFD76E-5DC0-4126-A674-FDD71412AA99Q30445851-82724616-578A-40A3-8DF5-E9C40944D016Q34249176-642FD525-38EC-4F3B-BAD5-4D91118B7569Q35170435-7FC05864-EC82-4018-8A6A-C9D75A272071Q35928179-1701A766-459E-4A35-A93C-77073F40E978Q37064945-85B7AD6F-404D-49C8-8FB6-CC2D823BD4E6Q40251122-2E0ABE42-D308-4927-BE3D-068958E33DB8Q40407110-BA8D0DCD-0610-4666-89D4-2FFE3CB9E224Q40617498-428E44B3-B40A-4B7B-BCBA-FE75B5628494Q40714810-164A3077-2530-4A3D-BEA7-CE40C57A093CQ42451000-050ECD5A-9F14-48A0-8B36-6CAAD76C1B32Q42510257-94C5E587-DEF3-4155-8B30-E51962711FD9Q42511742-399DA2EF-0763-4462-9C4C-B82F4ACF83D4Q42516252-EB8971CE-9DB7-4927-B843-FAF88A8398E8
P2860
Proteolytic modification of laminins: functional consequences.
description
2000 nî lūn-bûn
@nan
2000 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Proteolytic modification of laminins: functional consequences.
@ast
Proteolytic modification of laminins: functional consequences.
@en
Proteolytic modification of laminins: functional consequences.
@nl
type
label
Proteolytic modification of laminins: functional consequences.
@ast
Proteolytic modification of laminins: functional consequences.
@en
Proteolytic modification of laminins: functional consequences.
@nl
prefLabel
Proteolytic modification of laminins: functional consequences.
@ast
Proteolytic modification of laminins: functional consequences.
@en
Proteolytic modification of laminins: functional consequences.
@nl
P2860
P1476
Proteolytic modification of laminins: functional consequences.
@en
P2093
P2860
P304
P356
10.1002/1097-0029(20001101)51:3<238::AID-JEMT4>3.0.CO;2-3
P577
2000-11-01T00:00:00Z