Biogenesis of extracellular microfibrils: Multimerization of the fibrillin-1 C terminus into bead-like structures enables self-assembly
about
Fibrillin-1 and -2 differentially modulate endogenous TGF-β and BMP bioavailability during bone formationHeparin/heparan sulfate controls fibrillin-1, -2 and -3 self-interactions in microfibril assemblyFunctional consequences of homocysteinylation of the elastic fiber proteins fibrillin-1 and tropoelastinStructure and interdomain interactions of a hybrid domain: a disulphide-rich module of the fibrillin/LTBP superfamily of matrix proteinsCorneal stroma microfibrilsStructure of the Fibrillin-1 N-Terminal Domains Suggests that Heparan Sulfate Regulates the Early Stages of Microfibril AssemblyADAMTSL-6 is a novel extracellular matrix protein that binds to fibrillin-1 and promotes fibrillin-1 fibril formationBiogenesis and function of fibrillin assemblies.C-terminal propeptide is required for fibrillin-1 secretion and blocks premature assembly through linkage to domains cbEGF41-43.Fibrillin assemblies: extracellular determinants of tissue formation and fibrosisComparative immunolocalisation of fibrillin-1 and perlecan in the human foetal, and HS-deficient hspg2 exon 3 null mutant mouse intervertebral disc.Fibrillin-1 mutations causing Weill-Marchesani syndrome and acromicric and geleophysic dysplasias disrupt heparan sulfate interactionsHomocysteine modifies structural and functional properties of fibronectin and interferes with the fibronectin-fibrillin-1 interaction.ADAMTSL6β protein rescues fibrillin-1 microfibril disorder in a Marfan syndrome mouse model through the promotion of fibrillin-1 assembly.Complex contributions of fibronectin to initiation and maturation of microfibrilsFibrillin-containing microfibrils are key signal relay stations for cell function.Fibrillin assembly requires fibronectin.Revisiting the mystery of fibronectin multimers: the fibronectin matrix is composed of fibronectin dimers cross-linked by non-covalent bonds.Extracellular microfibrils: contextual platforms for TGFbeta and BMP signaling.TB domain proteins: evolutionary insights into the multifaceted roles of fibrillins and LTBPs.Homocysteine in renovascular complications: hydrogen sulfide is a modulator and plausible anaerobic ATP generator¹H, ¹³C and ¹⁵N assignments of the four N-terminal domains of human fibrillin-1.Classical and neonatal Marfan syndrome mutations in fibrillin-1 cause differential protease susceptibilities and protein function.Assembly of fibrillin microfibrils governs extracellular deposition of latent TGF beta.Independent multimerization of Latent TGFβ Binding Protein-1 stabilized by cross-linking and enhanced by heparan sulfate.Fell-Muir Lecture: Fibrillin microfibrils: structural tensometers of elastic tissues?Early fibrillin-1 assembly monitored through a modifiable recombinant cell approach.FBN1 isoform expression varies in a tissue and development-specific fashion.Truncated C-terminus of fibrillin-1 induces Marfanoid-progeroid-lipodystrophy (MPL) syndrome in rabbit.Multiscale Imaging Reveals the Hierarchical Organization of Fibrillin Microfibrils
P2860
Q24300318-8D2AAB03-5411-4D9C-AF50-2A3A3847E7A3Q24300895-94BE0DED-EA6A-46A1-B96C-565434EC50C4Q24651294-678E6F26-F5E7-4326-B83C-0D9F77A7C787Q24654634-7AEFC855-69C8-4395-B4E3-3FDAAE164644Q26996228-C9A5F5B4-F731-4F24-9F74-CD62E0D71E41Q27679940-1B2C7B06-A597-4ACA-A489-A5958361DBEEQ28508725-29A9C10D-13B3-4154-A1D5-1D59FB0D4655Q33641386-63DBF0F6-5775-48A3-8BB9-06CC1175055CQ33925885-14203E6E-44AC-4FE6-94F4-02D904076CA1Q34447925-283C23EB-7304-4FDF-B9D2-517D69A610E9Q34458888-F7E1AFD8-5E85-476C-A2E7-23B927B2BBFFQ34469801-FB59D7A0-9030-41CD-B688-6B4C365F97F9Q35038315-5C7C7C8F-3BFF-434D-86B0-C228EAEDF1A2Q35515879-E5416CFF-6910-4A16-9821-DD2307B0DEEFQ35997870-52A089B0-C146-47C7-BE34-AD3A0A38B696Q36470965-6DE37823-90A8-4B46-B99B-E3B6ED299DC6Q37078574-2221C636-01A2-45F2-9D98-395C31D2576CQ37195085-F53BB297-3D74-472A-89FC-D95C7D7289BBQ37399313-93E20284-5787-42F0-B050-7D432FE89306Q37822821-C0282BEE-2AC2-408B-8D07-2DE67904E283Q38223130-F62CADF0-6107-4864-B6EA-439B72F846FBQ38284297-7AEF3531-E8C2-40D7-82F9-274CF024D87CQ38421397-6091BC6D-E835-4F1B-A8E2-AB9A9A0AA395Q39668937-E41CCF1F-DBE8-455D-B955-3EE0DAF75FF3Q41203010-C8A3E691-2C33-4ECB-B617-C58F633BC522Q42376279-19874347-CEE8-402D-A032-549B32E9FE84Q42402963-3B84AB3F-1EA0-4FB9-8ADB-019EA9A8332DQ42851321-4E188399-2A1C-4DE9-9876-AA85A17F5DD0Q52431634-7AFFCA1F-911B-4AE8-B54D-B670F94EF3C6Q58723125-79AD85A1-B7A3-4310-8B5F-F421CC841576
P2860
Biogenesis of extracellular microfibrils: Multimerization of the fibrillin-1 C terminus into bead-like structures enables self-assembly
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Biogenesis of extracellular mi ...... ructures enables self-assembly
@ast
Biogenesis of extracellular mi ...... ructures enables self-assembly
@en
type
label
Biogenesis of extracellular mi ...... ructures enables self-assembly
@ast
Biogenesis of extracellular mi ...... ructures enables self-assembly
@en
prefLabel
Biogenesis of extracellular mi ...... ructures enables self-assembly
@ast
Biogenesis of extracellular mi ...... ructures enables self-assembly
@en
P2093
P2860
P921
P356
P1476
Biogenesis of extracellular mi ...... ructures enables self-assembly
@en
P2093
Dirk Hubmacher
Ehab I El-Hallous
Eunice R Lee
Mari T Kaartinen
Valentin Nelea
P2860
P304
P356
10.1073/PNAS.0706335105
P407
P577
2008-04-30T00:00:00Z