A short sequence in the N-terminal region is required for the trimerization of type XIII collagen and is conserved in other collagenous transmembrane proteins.
about
Evolution of collagensCLAC: a novel Alzheimer amyloid plaque component derived from a transmembrane precursor, CLAC-P/collagen type XXVThe type XIII collagen ectodomain is a 150-nm rod and capable of binding to fibronectin, nidogen-2, perlecan, and heparinCharacterization of the Alzheimer's disease-associated CLAC protein and identification of an amyloid beta-peptide-binding siteCrystal Structure of Human Collagen XVIII Trimerization Domain: A Novel Collagen Trimerization FoldCrystal structure of the human collagen XV trimerization domain: A potent trimerizing unit common to multiplexin collagensType XXVI collagen, a new member of the collagen family, is specifically expressed in the testis and ovaryType XXIII collagen, a new transmembrane collagen identified in metastatic tumor cellsCleavage and oligomerization of gliomedin, a transmembrane collagen required for node of ranvier formationShedding of Collagen XVII/BP180: STRUCTURAL MOTIFS INFLUENCE CLEAVAGE FROM CELL SURFACEMuscle-derived collagen XIII regulates maturation of the skeletal neuromuscular junction.The amino-terminal heptad repeats of the coiled-coil neck domain of pulmonary surfactant protein d are necessary for the assembly of trimeric subunits and dodecamers.Type XIII collagen and some other transmembrane collagens contain two separate coiled-coil motifs, which may function as independent oligomerization domains.Collagens and collagen-related diseases.Collagenous transmembrane proteins: recent insights into biology and pathology.The NC16A domain of collagen XVII plays a role in triple helix assembly and stabilityVariation in extracellular matrix genes is associated with weight regain after weight loss in a sex-specific mannerMolecular recognition in the assembly of collagens: terminal noncollagenous domains are key recognition modules in the formation of triple helical protomers.Abnormal adherence junctions in the heart and reduced angiogenesis in transgenic mice overexpressing mutant type XIII collagen.Transmembrane collagen XVII, an epithelial adhesion protein, is shed from the cell surface by ADAMs.The role of disulfide bonds and alpha-helical coiled-coils in the biosynthesis of type XIII collagen and other collagenous transmembrane proteins.Modulation of the cellular cholesterol level affects shedding of the type XIII collagen ectodomain.Sorting of furin in polarized epithelial and endothelial cells: expression beyond the Golgi apparatus.The shed ectodomain of type XIII collagen affects cell behaviour in a matrix-dependent manner.The cell adhesion domain of type XVII collagen promotes integrin-mediated cell spreading by a novel mechanism.Template-tethered collagen mimetic peptides for studying heterotrimeric triple-helical interactions.The shed ectodomain of type XIII collagen associates with the fibrillar fibronectin matrix and may interfere with its assembly in vitro.Collagen XIII secures pre- and postsynaptic integrity of the neuromuscular synapse.Lack of cytosolic and transmembrane domains of type XIII collagen results in progressive myopathy.Transformation of the mechanism of triple-helix peptide folding in the absence of a C-terminal nucleation domain and its implications for mutations in collagen disorders.Autoimmune antibodies to collagen XIII in myasthenia gravis patients.Collagen type XIII ectodomain sheddingType XIII Collagen Strongly Affects Bone Formation in Transgenic Mice
P2860
Q22337422-C5325F87-A815-4054-81CB-94987D0C7F53Q24292980-CC195822-C26A-4F22-ABC3-EB86032D6670Q24294514-0515E316-D735-4804-82AC-12BEFFFC9DBEQ24310810-AFB581FC-18D3-4CDD-B218-93BAD78B8B63Q27656720-F6707C63-6215-49AD-8E0D-0704CF6C0C92Q27664951-D6D03E1A-8585-46B8-9443-A0377B2EF0ABQ28216210-36887D19-9E3A-4089-B60D-73B7E9C2A374Q28568589-972360D6-655E-4B7A-8B14-7EA4940D7AFBQ28588337-F1452A61-389B-40CC-B2CC-76B1504D2FB1Q29013483-2D6242AD-A065-45C3-8D6D-3244DC6CDCF6Q30497006-EDE1C46F-F5C2-4B75-BCA9-E8D6642945B0Q33940594-1C68FA48-D28F-4C14-A597-796CE05044DFQ34209723-975929EA-8F61-4371-8047-4D79CF6DAC54Q34224267-5EAB2AFE-4EAF-41E9-87D7-C7158A875F29Q34370620-B6058285-5F21-46D4-8107-EDC69B0EE300Q35742074-15CA149D-D494-4965-BD05-49EC63AB5BB5Q36300111-842B7612-2B62-4797-B001-710142168F35Q36643333-79C68489-EA33-452B-8514-28DB22C31A44Q39645757-80570378-EA30-45F9-BC54-BC0DF4F9F2BAQ39658973-9A6DB92E-F1BB-43EE-9D8A-55CF891F8C5EQ40162042-CAB0D4CB-9AAB-42EC-89E5-79BD3B6D4EB7Q40236626-45809F3A-E63C-4D8C-A2E5-DBA703C0D414Q40564413-FAF8E57D-6132-4741-8E4D-76DF82185C81Q40581317-BA2772C0-9830-42D4-9B4F-EF07BB12E300Q40784980-8D53AB53-CCBE-40F1-99DE-6AB09675A2BAQ41317774-49A4584A-7C96-4BCC-B0ED-9B9D2C8AEB61Q41894627-06A18943-7922-4DB8-AFE7-23C3619F52D8Q42508002-9AA179F7-EB25-4CBA-9E4C-BB920AE66FC9Q42856204-F51F7ADE-9886-4EE3-A3AD-047C35AB6B84Q45010258-41D757FA-8A95-400C-BFC7-9803C52AC95AQ47834883-165D4C31-7A99-4346-AB82-E9DDAB540796Q50289956-F53ECB4A-ADC0-47AC-BB69-522AACF6D0DEQ58008527-B6B39114-257B-437C-B1EB-9DAAA1CA0012
P2860
A short sequence in the N-terminal region is required for the trimerization of type XIII collagen and is conserved in other collagenous transmembrane proteins.
description
2000 nî lūn-bûn
@nan
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
2000年论文
@zh
2000年论文
@zh-cn
name
A short sequence in the N-term ...... genous transmembrane proteins.
@en
type
label
A short sequence in the N-term ...... genous transmembrane proteins.
@en
prefLabel
A short sequence in the N-term ...... genous transmembrane proteins.
@en
P2093
P2860
P356
P1433
P1476
A short sequence in the N-term ...... genous transmembrane proteins.
@en
P2093
P2860
P304
P356
10.1093/EMBOJ/19.19.5051
P407
P577
2000-10-01T00:00:00Z