Genomic organization of the sequence coding for fibrillin, the defective gene product in Marfan syndrome.
about
The evolution of extracellular fibrillins and their functional domainsLatent transforming growth factor beta-binding protein-3 and fibulin-1C interact with the extracellular domain of the heparin-binding EGF-like growth factor precursorIsolation and characterization of EMILIN-2, a new component of the growing EMILINs family and a member of the EMI domain-containing superfamilyFurther characterization of proteins associated with elastic fiber microfibrils including the molecular cloning of MAGP-2 (MP25)Structure of the integrin binding fragment from fibrillin-1 gives new insights into microfibril organizationStructure and expression of fibrillin-2, a novel microfibrillar component preferentially located in elastic matricesStructure and interdomain interactions of a hybrid domain: a disulphide-rich module of the fibrillin/LTBP superfamily of matrix proteinsFibrillin: from microfibril assembly to biomechanical functionCorneal stroma microfibrilsSolution structure and dynamics of a calcium binding epidermal growth factor-like domain pair from the neonatal region of human fibrillin-1Structure of the Fibrillin-1 N-Terminal Domains Suggests that Heparan Sulfate Regulates the Early Stages of Microfibril AssemblyalphaVbeta6 is a novel receptor for human fibrillin-1. Comparative studies of molecular determinants underlying integrin-rgd affinity and specificityMAGP-2 has multiple binding regions on fibrillins and has covalent periodic association with fibrillin-containing microfibrilsCell adhesion to fibrillin-1 molecules and microfibrils is mediated by alpha 5 beta 1 and alpha v beta 3 integrinsMicrofibril-associated glycoprotein-1 (MAGP-1) binds to the pepsin-resistant domain of the alpha3(VI) chain of type VI collagenFibrillin-1 and fibulin-2 interact and are colocalized in some tissuesDevelopmental expression of fibrillin genes suggests heterogeneity of extracellular microfibrilsIsolation of a novel latent transforming growth factor-beta binding protein gene (LTBP-3)Cell adhesion and integrin binding to recombinant human fibrillin-1Fibrillin degradation by matrix metalloproteinases: implications for connective tissue remodellingFibrillin degradation by matrix metalloproteinases: identification of amino- and carboxy-terminal cleavage sitesMouse fibulin-2 gene. Complete exon-intron organization and promoter characterization.Quantification of single nucleotide polymorphisms: a novel method that combines primer extension assay and capillary electrophoresis.Defining elastic fiber interactions by molecular fishing: an affinity purification and mass spectrometry approach.A new missense mutation of fibrillin in a patient with Marfan syndrome.Marfan syndrome: new clues to genotype-phenotype correlations.EMI, a novel cysteine-rich domain of EMILINs and other extracellular proteins, interacts with the gC1q domains and participates in multimerization.Cysteine substitutions in epidermal growth factor-like domains of fibrillin-1: distinct effects on biochemical and clinical phenotypes.Ligament-derived matrix stimulates a ligamentous phenotype in human adipose-derived stem cellsA mutation in FBN1 disrupts profibrillin processing and results in isolated skeletal features of the Marfan syndrome.An extra cysteine in one of the non-calcium-binding epidermal growth factor-like motifs of the FBN1 polypeptide is connected to a novel variant of Marfan syndrome.The calcium binding properties and molecular organization of epidermal growth factor-like domains in human fibrillin-1.Multiple molecular mechanisms underlying subdiagnostic variants of Marfan syndrome.Recurrence of Marfan syndrome as a result of parental germ-line mosaicism for an FBN1 mutation.Fibrillin-1 mutations causing Weill-Marchesani syndrome and acromicric and geleophysic dysplasias disrupt heparan sulfate interactionsFibrillin-1 interactions with fibulins depend on the first hybrid domain and provide an adaptor function to tropoelastin.Inactivation of Fam20C in cells expressing type I collagen causes periodontal disease in mice.Marfan Database (third edition): new mutations and new routines for the software.The microfibrillar proteins MAGP-1 and fibrillin-1 form a ternary complex with the chondroitin sulfate proteoglycan decorinMarfan syndrome in the third Millennium.
P2860
Q21134722-E1736904-C39A-41B9-8A73-91C51D03CD3DQ21284179-342A47AE-4DA8-4086-9620-BF350E068ADAQ24291040-35CAD920-B1A6-434A-8F03-EBE165A8B28EQ24316167-7D16E4CA-5CB1-4F39-942B-2460A2E63DC2Q24323342-86A1FDFA-C574-42E3-A3CB-CB174F1A804CQ24336069-2F84E5D8-3277-4F72-9C26-C494E3A8BE40Q24654634-2DDACE4E-4B55-42C4-86FB-1EBD0679E743Q24676103-5004842C-7FA0-436B-97F3-73E36829710DQ26996228-ACAE46C5-3308-4A48-8FEA-A07BA82B869DQ27640264-5A3E2CBC-6A59-455F-A064-D1FB6DF65BEFQ27679940-CF7858C4-9749-4F66-831E-B5A3A356689DQ28116214-BF9AB14D-A069-442C-BAC3-3A562F70BA9CQ28117523-6A7FE0DA-8B63-440D-9418-AC59D3836EF9Q28118870-FE0FFEEF-A34C-4A1D-9C45-0D0DBFF1A9D8Q28247738-29C19005-2961-4B6E-8C64-FEB763E008E9Q28284384-0C857D7C-5946-4D19-B8E2-AC4C00D44DBEQ28504747-84A2BEDA-CB2C-419F-964B-51FBAB193D03Q28592926-FA6A2B9C-1C63-40C4-9461-5C9C7246794FQ28610091-996FE42B-0C30-46FA-A804-084419354E6BQ28610876-D2482BE0-1B1C-4CF4-8A82-8D294FDB6FBEQ28610878-F673A548-3E15-4CF8-AB9B-9D7A508A8C51Q30734761-F1FFF6D3-F187-433B-9F3C-AE3A33831851Q31033018-A0FE155B-4035-450F-8FF4-96B2A7B1B69CQ33628905-099D69A3-2899-4B85-952A-E4BEEF8420C3Q33673909-21394FC6-3EF2-495E-9DB4-16BCDE328B3DQ33708680-468311EC-3167-43E5-9B41-A2E8BDEDBBEEQ33924479-4FD485C0-600C-4B1B-8546-EABB87D25E71Q34145672-1F56EB0A-279E-488E-93E1-86AEAD82ABA8Q34165801-108A765F-E2BB-4A1D-AA46-DF7FE66A4232Q34219428-906273D0-620A-4CF7-A953-B07FDF839460Q34229237-D8433D3F-BC3E-4B39-92A4-2203ABC3A54AQ34321399-9E920129-6B6C-424B-A808-AB012518692DQ34388195-BB15D92D-A2A5-4776-AAE3-1048B1F231A9Q34389307-1CE478B4-45B9-43A1-9894-40AB36FCEDE6Q34469801-1EB0DE91-79DC-4848-8442-2B8FC6A93F6AQ34606497-DCF3551D-20B6-401B-A7EF-518DE0340AF8Q34640430-E11DF94B-7F3F-48CB-B65A-474781DD0B5BQ34648993-12EA6B33-A739-4D47-8DF0-D9EBA8B31FC1Q34707917-BCDD0F65-6EA3-4C58-B499-EDB8CF67CDCAQ34982429-BBD0E163-C0CE-46D7-9F71-2723127AF844
P2860
Genomic organization of the sequence coding for fibrillin, the defective gene product in Marfan syndrome.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
1993年论文
@zh
1993年论文
@zh-cn
name
Genomic organization of the se ...... ne product in Marfan syndrome.
@ast
Genomic organization of the se ...... ne product in Marfan syndrome.
@en
type
label
Genomic organization of the se ...... ne product in Marfan syndrome.
@ast
Genomic organization of the se ...... ne product in Marfan syndrome.
@en
prefLabel
Genomic organization of the se ...... ne product in Marfan syndrome.
@ast
Genomic organization of the se ...... ne product in Marfan syndrome.
@en
P2093
P356
P1476
Genomic organization of the se ...... ene product in Marfan syndrome
@en
P2093
P304
P356
10.1093/HMG/2.7.961
P577
1993-07-01T00:00:00Z