Defective folding and stable association with protein disulfide isomerase/prolyl hydroxylase of type I procollagen with a deletion in the pro alpha 2(I) chain that preserves the Gly-X-Y repeat pattern
about
sameAs
TRAM2 protein interacts with endoplasmic reticulum Ca2+ pump Serca2b and is necessary for collagen type I synthesisPost-translational hydroxylation at the N-terminus of the prion protein reveals presence of PPII structure in vivoIs protein disulfide isomerase a redox-dependent molecular chaperone?Thiol-independent interaction of protein disulphide isomerase with type X collagen during intra-cellular folding and assemblyThe deletion of six amino acids at the C-terminus of the alpha 1 (II) chain causes overmodification of type II and type XI collagen: further evidence for the association between small deletions in COL2A1 and Kniest dysplasiaSpecific inhibition of eIF-5A and collagen hydroxylation by a single agent. Antiproliferative and fibrosuppressive effects on smooth muscle cells from human coronary arteries.Expression, in cartilage, of a 7-amino-acid deletion in type II collagen from two unrelated individuals with Kniest dysplasia.A novel transgenic mouse model of growth plate dysplasia reveals that decreased chondrocyte proliferation due to chronic ER stress is a key factor in reduced bone growth.R992C (p.R1192C) Substitution in collagen II alters the structure of mutant molecules and induces the unfolded protein response.Proteomic analysis of circulating monocytes in Chinese premenopausal females with extremely discordant bone mineral density.Insufficient folding of type IV collagen and formation of abnormal basement membrane-like structure in embryoid bodies derived from Hsp47-null embryonic stem cells.Membrane topology influences N-glycosylation of the prion protein.An intramolecular disulfide bridge between Cys-7 and Cys61 determines the structure of the secretory core gene product (e antigen) of hepatitis B virus.Reconstitution of the folding pathway of collagen in a cell-free system: formation of correctly aligned and hydroxylated triple helices.The final stage of gene expression: chaperones and the regulation of protein fate.Type-III procollagen assembly in semi-intact cells: chain association, nucleation and triple-helix folding do not require formation of inter-chain disulphide bonds but triple-helix nucleation does require hydroxylation.The C-propeptide domain of procollagen can be replaced with a transmembrane domain without affecting trimer formation or collagen triple helix folding during biosynthesis.The chondrodystrophy, nanomelia: biosynthesis and processing of the defective aggrecan precursor.
P2860
Q24306604-C2ACB547-38A8-4A3E-8E9E-BF0C1382BD48Q28141258-ADA9317B-076F-4819-A912-4DB3CB1FD768Q28217860-E270AF0A-498C-4E09-8F80-7D68D4F9FFD2Q28608949-689DC58F-D312-408C-8B0B-C4CD70203530Q33677641-B8E67354-428A-4C61-AB55-E308D4B22710Q34198618-6F2EBBB3-B4D4-4178-90A5-BB1C8F8F2730Q35889820-63E26C25-BA09-43D3-BAFA-32D302EA909BQ37287446-50BB3D99-FFDC-43E5-BD40-C9EAC1CE0FD9Q37358545-05667C6F-48A9-4C51-9348-A7F04308B2BCQ37385051-BBF82E4D-DC8C-4A9A-82ED-E6B58332F177Q37537942-2F293CCF-29F6-4128-8731-7C5CF44FCEFDQ39714529-86251891-6CCB-4BFE-BBA6-A61D6B09EBA8Q40046109-3CDEC68F-F214-4FBA-9B2F-364DA09C9259Q41510838-574B6A23-258C-4DDB-ABE5-1FE5738DE802Q41602460-C51F5489-6DE4-409E-897E-157EACC0FAF0Q41937550-9317A27A-9354-4BDB-A0EA-C47CEFA99D6EQ42235754-0789AD26-57EE-4549-95C4-A42B85A263B5Q42828489-51C6BF12-1ADB-41A1-8FB6-C5BA0D92F622
P2860
Defective folding and stable association with protein disulfide isomerase/prolyl hydroxylase of type I procollagen with a deletion in the pro alpha 2(I) chain that preserves the Gly-X-Y repeat pattern
description
1992 nî lūn-bûn
@nan
1992 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
Defective folding and stable a ...... ves the Gly-X-Y repeat pattern
@ast
Defective folding and stable a ...... ves the Gly-X-Y repeat pattern
@en
Defective folding and stable a ...... ves the Gly-X-Y repeat pattern
@nl
type
label
Defective folding and stable a ...... ves the Gly-X-Y repeat pattern
@ast
Defective folding and stable a ...... ves the Gly-X-Y repeat pattern
@en
Defective folding and stable a ...... ves the Gly-X-Y repeat pattern
@nl
prefLabel
Defective folding and stable a ...... ves the Gly-X-Y repeat pattern
@ast
Defective folding and stable a ...... ves the Gly-X-Y repeat pattern
@en
Defective folding and stable a ...... ves the Gly-X-Y repeat pattern
@nl
P1476
Defective folding and stable a ...... ves the Gly-X-Y repeat pattern
@en
P2093
S D Chessler
P304
P407
P577
1992-04-15T00:00:00Z