about
Isolation and characterization of EMILIN-2, a new component of the growing EMILINs family and a member of the EMI domain-containing superfamilyMolecular cloning and characterization of EndoGlyx-1, an EMILIN-like multisubunit glycoprotein of vascular endotheliumPerlecan protein core interacts with extracellular matrix protein 1 (ECM1), a glycoprotein involved in bone formation and angiogenesisExtracellular Matrix, a Hard Player in AngiogenesisDiagnostic Exome Sequencing Identifies a Novel Gene, EMILIN1, Associated with Autosomal-Dominant Hereditary Connective Tissue DiseaseFibroblast growth factor-binding protein is a novel partner for perlecan protein coreEMILIN-1 deficiency induces elastogenesis and vascular cell defectsThe solution structure of EMILIN1 globular C1q domain reveals a disordered insertion necessary for interaction with the alpha4beta1 integrinEmilin1 gene and essential hypertension: a two-stage association study in northern Han Chinese population.The extracellular matrix protein EMILIN1 silences the RAS-ERK pathway via α4β1 integrin and decreases tumor cell growth.Extracellular matrix molecules: potential targets in pharmacotherapy.Fibulin-4 deposition requires EMILIN-1 in the extracellular matrix of osteoblasts.EMI, a novel cysteine-rich domain of EMILINs and other extracellular proteins, interacts with the gC1q domains and participates in multimerization.beta 1 Integrin-dependent cell adhesion to EMILIN-1 is mediated by the gC1q domain.Metabolic regulation by C1q/TNF-related protein-13 (CTRP13): activation OF AMP-activated protein kinase and suppression of fatty acid-induced JNK signalingEMILIN1-α4/α9 integrin interaction inhibits dermal fibroblast and keratinocyte proliferation.Regulation of the extrinsic apoptotic pathway by the extracellular matrix glycoprotein EMILIN2.Local inhibition of elastase reduces EMILIN1 cleavage reactivating lymphatic vessel function in a mouse lymphoedema modelMultimerin 1.Neutrophil elastase cleavage of the gC1q domain impairs the EMILIN1-α4β1 integrin interaction, cell adhesion and anti-proliferative activityThe EMILIN/Multimerin family.The extracellular matrix glycoprotein elastin microfibril interface located protein 2: a dual role in the tumor microenvironment.EMILIN-3, peculiar member of elastin microfibril interface-located protein (EMILIN) family, has distinct expression pattern, forms oligomeric assemblies, and serves as transforming growth factor β (TGF-β) antagonist.EMILIN-1 regulates the amount of oxytalan fiber formation in periodontal ligaments in vitro.
P2860
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P2860
description
2000 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 2000
@ast
im August 2000 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2000/08/18)
@sk
vědecký článek publikovaný v roce 2000
@cs
wetenschappelijk artikel (gepubliceerd op 2000/08/18)
@nl
наукова стаття, опублікована в серпні 2000
@uk
name
Self-assembly and supramolecular organization of EMILIN
@ast
Self-assembly and supramolecular organization of EMILIN
@en
Self-assembly and supramolecular organization of EMILIN
@nl
type
label
Self-assembly and supramolecular organization of EMILIN
@ast
Self-assembly and supramolecular organization of EMILIN
@en
Self-assembly and supramolecular organization of EMILIN
@nl
prefLabel
Self-assembly and supramolecular organization of EMILIN
@ast
Self-assembly and supramolecular organization of EMILIN
@en
Self-assembly and supramolecular organization of EMILIN
@nl
P2093
P2860
P50
P921
P356
P1476
Self-assembly and supramolecular organization of EMILIN
@en
P2093
G Mungiguerra
M T Mucignat
P2860
P304
25471-25480
P356
10.1074/JBC.M001426200
P407
P577
2000-08-01T00:00:00Z