Identification of tropoelastin as a ligand for the 65-kD FK506-binding protein, FKBP65, in the secretory pathway.
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Impaired elastic-fiber assembly by fibroblasts from patients with either Morquio B disease or infantile GM1-gangliosidosis is linked to deficiency in the 67-kD spliced variant of beta-galactosidase.Developmental regulation of FKBP65. An ER-localized extracellular matrix binding-proteinOrchestration of secretory protein folding by ER chaperonesDepletion of cyclophilins B and C leads to dysregulation of endoplasmic reticulum redox homeostasisLysosomal sialidase (neuraminidase-1) is targeted to the cell surface in a multiprotein complex that facilitates elastic fiber assemblyMutations in the gene encoding the RER protein FKBP65 cause autosomal-recessive osteogenesis imperfecta.Connective tissue alterations in Fkbp10-/- mice.Developmental regulation and coordinate reexpression of FKBP65 with extracellular matrix proteins after lung injury suggest a specialized function for this endoplasmic reticulum immunophilin.Oxidative and nitrosative modifications of tropoelastin prevent elastic fiber assembly in vitro.The hyperthermia-enhanced association between tropoelastin and its 67-kDa chaperone results in better deposition of elastic fibers.Unique inflammatory RNA profiles of microglia in Creutzfeldt-Jakob disease.The rough endoplasmic reticulum-resident FK506-binding protein FKBP65 is a molecular chaperone that interacts with collagens.Mutations in FKBP10 cause recessive osteogenesis imperfecta and Bruck syndromeEndoplasmic reticulum stress or mutation of an EF-hand Ca(2+)-binding domain directs the FKBP65 rotamase to an ERAD-based proteolysisAbsence of FKBP10 in recessive type XI osteogenesis imperfecta leads to diminished collagen cross-linking and reduced collagen deposition in extracellular matrix.Rare mutations and potentially damaging missense variants in genes encoding fibrillar collagens and proteins involved in their production are candidates for risk for preterm premature rupture of membranesExport of a cysteine-free misfolded secretory protein from the endoplasmic reticulum for degradation requires interaction with protein disulfide isomerase.Mutations in FKBP10, which result in Bruck syndrome and recessive forms of osteogenesis imperfecta, inhibit the hydroxylation of telopeptide lysines in bone collagen.Kuskokwim syndrome, a recessive congenital contracture disorder, extends the phenotype of FKBP10 mutations.Hepatic lipase maturation: a partial proteome of interacting factorsLoss-of-function mutations in ATP6V0A2 impair vesicular trafficking, tropoelastin secretion and cell survivalUnraveling the role of peptidyl-prolyl isomerases in neurodegeneration.Peptidyl-Proline Isomerases (PPIases): Targets for Natural Products and Natural Product-Inspired Compounds.Fkbp10 Deletion in Osteoblasts Leads to Qualitative Defects in Bone.Expression and function of alphabeta1 integrins in pancretic beta (INS-1) cells.Loss of Type I Collagen Telopeptide Lysyl Hydroxylation Causes Musculoskeletal Abnormalities in a Zebrafish Model of Bruck Syndrome.Effect of FKBP65, a putative elastin chaperone, on the coacervation of tropoelastin in vitro.Profibrillin-1 maturation by human dermal fibroblasts: proteolytic processing and molecular chaperones.Chemical synthesis of cross-linked poly(KGGVG), an elastin-like biopolymer.Human FK506 binding protein 65 is associated with colorectal cancer.Mutations in FKBP10 cause both Bruck syndrome and isolated osteogenesis imperfecta in humans
P2860
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P2860
Identification of tropoelastin as a ligand for the 65-kD FK506-binding protein, FKBP65, in the secretory pathway.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
1998年论文
@zh
1998年论文
@zh-cn
name
Identification of tropoelastin ...... P65, in the secretory pathway.
@ast
Identification of tropoelastin ...... P65, in the secretory pathway.
@en
type
label
Identification of tropoelastin ...... P65, in the secretory pathway.
@ast
Identification of tropoelastin ...... P65, in the secretory pathway.
@en
prefLabel
Identification of tropoelastin ...... P65, in the secretory pathway.
@ast
Identification of tropoelastin ...... P65, in the secretory pathway.
@en
P2093
P2860
P356
P1476
Identification of tropoelastin ...... P65, in the secretory pathway.
@en
P2093
R P Mecham
T J Broekelmann
P2860
P304
P356
10.1083/JCB.140.2.295
P407
P577
1998-01-01T00:00:00Z