Procollagen triple helix assembly: an unconventional chaperone-assisted folding paradigm.
about
A missense mutation in the SERPINH1 gene in Dachshunds with osteogenesis imperfectaMolecular basis for the action of the collagen-specific chaperone Hsp47/SERPINH1 and its structure-specific client recognitionTacrolimus (FK506) prevents early stages of ethanol induced hepatic fibrosis by targeting LARP6 dependent mechanism of collagen synthesisIntracellular mechanisms of molecular recognition and sorting for transport of large extracellular matrix moleculesMutations in the gene encoding the RER protein FKBP65 cause autosomal-recessive osteogenesis imperfecta.Role of heat shock protein 47 in transdifferentiation of human tenon's fibroblasts to myofibroblasts.Chaperoning osteogenesis: new protein-folding disease paradigms.The rough endoplasmic reticulum-resident FK506-binding protein FKBP65 is a molecular chaperone that interacts with collagens.Molecular Consequences of the SERPINH1/HSP47 Mutation in the Dachshund Natural Model of Osteogenesis Imperfecta.Intracellularly-retained decorin lacking the C-terminal ear repeat causes ER stress: a cell-based etiological mechanism for congenital stromal corneal dystrophy.Hepatic lipase maturation: a partial proteome of interacting factorsThe collagen family.Faithful chaperones.Recessive osteogenesis imperfecta: clinical, radiological, and molecular findings.Matrix metalloproteinase collagenolysis in health and disease.Neonatal Respiratory Failure with Retarded Perinatal Lung Maturation in Mice Caused by Reticulocalbin 3 Disruption.Sodium 4-phenylbutyrate ameliorates the effects of cataract-causing mutant gammaD-crystallin in cultured cells.Biochemical characterization of the prolyl 3-hydroxylase 1.cartilage-associated protein.cyclophilin B complex.Mutation in cyclophilin B that causes hyperelastosis cutis in American Quarter Horse does not affect peptidylprolyl cis-trans isomerase activity but shows altered cyclophilin B-protein interactions and affects collagen foldingStructural heterogeneity of type I collagen triple helix and its role in osteogenesis imperfecta.
P2860
Q21092456-B24C22FE-29F1-41E5-98EA-382F02D54738Q24616550-E7EF3FF2-FE96-4634-BD12-46C06019CCACQ28533607-29C0814A-6CCF-4238-A43F-90E55F7D2EC0Q30008858-796CFDC8-899E-44FC-9427-7B0132A12031Q33772970-7116FF6A-0EC4-41E7-BFE3-516B979C15ACQ34411209-9AD85884-0E7E-48B3-A6AC-456F4044F415Q34672644-827B5362-8FC2-4218-8034-5FC07F6BE0E2Q34825879-0F117B35-BB66-4F06-B857-55A2C1EF6E60Q35859447-784EA06F-6D00-44DC-8C25-A66E82D161F6Q36986486-0CB12C24-EA89-47FE-B3C5-D058A3A0ACF7Q37190381-09A6089D-346B-4251-9A1B-CB169660CE19Q37855335-9D28E18C-0AE0-4286-9D49-9BFAEFC66EFDQ37886778-24A75E90-3160-4E25-B477-CA1F6B879409Q38025998-F13999CD-0EA1-4AED-AF4C-5D0005A25AA5Q38431602-41A7DDDE-16D1-4E08-A792-CBA47874BE15Q38845521-D63C6417-6FF4-42D6-A0AA-BE283635E975Q41345156-D27AAE38-9AE8-4742-A0C5-1DD8D7AD3B6FQ41860665-89127590-D352-43DA-96EA-9ABE9D9FC6A6Q42033519-6205165A-8108-4D2F-92F3-0082E6FE4C93Q46855555-91559B3C-6873-4DD0-8D3A-0978E1759403
P2860
Procollagen triple helix assembly: an unconventional chaperone-assisted folding paradigm.
description
2007 nî lūn-bûn
@nan
2007 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Procollagen triple helix assembly: an unconventional chaperone-assisted folding paradigm.
@ast
Procollagen triple helix assembly: an unconventional chaperone-assisted folding paradigm.
@en
Procollagen triple helix assembly: an unconventional chaperone-assisted folding paradigm.
@nl
type
label
Procollagen triple helix assembly: an unconventional chaperone-assisted folding paradigm.
@ast
Procollagen triple helix assembly: an unconventional chaperone-assisted folding paradigm.
@en
Procollagen triple helix assembly: an unconventional chaperone-assisted folding paradigm.
@nl
prefLabel
Procollagen triple helix assembly: an unconventional chaperone-assisted folding paradigm.
@ast
Procollagen triple helix assembly: an unconventional chaperone-assisted folding paradigm.
@en
Procollagen triple helix assembly: an unconventional chaperone-assisted folding paradigm.
@nl
P2860
P1433
P1476
Procollagen triple helix assembly: an unconventional chaperone-assisted folding paradigm.
@en
P2093
Elena Makareeva
P2860
P356
10.1371/JOURNAL.PONE.0001029
P407
P577
2007-10-10T00:00:00Z