Hydroxyproline stabilizes the triple helix of chick tendon collagen.
about
Prolyl 3-hydroxylase: partial characterization of the enzyme from rat kidney cortexThe biosynthesis of basement-membrane collagen by isolated rat glomeruliSpecifically decreased collagen biosynthesis in scurvy dissociated from an effect on proline hydroxylation and correlated with body weight loss. In vitro studies in guinea pig calvarial bones.Collagen-like proteins in pathogenic E. coli strains.An additional function of the rough endoplasmic reticulum protein complex prolyl 3-hydroxylase 1·cartilage-associated protein·cyclophilin B: the CXXXC motif reveals disulfide isomerase activity in vitro.Regulation of collagen synthesis by ascorbic acid.Collagen biosynthesis.Prolyl hydroxylase in the skin of patients with obstructive jaundiceSomatic overgrowth associated with homozygous mutations in both MAN1B1 and SEC23AHydroxyproline-free single composition ABC collagen heterotrimerRole of procollagen mRNA levels in controlling the rate of procollagen synthesis.Ascorbate induction of collagen synthesis as a means for elucidating a mechanism of quantitative control of tissue-specific function.Role of hypoxia-inducible factor 1 alpha in the integrity of articular cartilage in murine knee jointsThe route of secretion of procollagen. The influence of alphaalpha'-bipyridyl, colchicine and antimycin A on the secretory process in embryonic-chick tendon and cartilage cells.Action of rheumatoid synovial collagenase on cartilage collagen. Different susceptibilities of cartilage and tendon collagen to collagenase attack.Engineered recombinant bacterial collagen as an alternative collagen-based biomaterial for tissue engineeringAscorbic acid promotes a TGFβ1-induced myofibroblast phenotype switchThe synthesis and secretion of cartilage procollagen.Influence of ascorbic acid on ribosomal patterns and collagen biosynthesis in healing wounds of scorbutic guinea pigs.Evidence that chick tendon procollagen must be denatured to serve as substrate for proline hydroxylase.The influence of 1-hydroxyethane-1,1-diphosphonate and dichloromethanediphosphonate on lysine hydroxylation and cross-link formation in rat bone, cartilage and skin collagen.Further studies on the effect of the collagen triple-helix formation on the hydroxylation of lysine and the glycosylations of hydroxylysine in chick-embryo tendon and cartilage cells.Underhydroxylated minor cartilage collagen precursors cannot form stable triple helices.Collagen proline hydroxylase activity and 35S sulphate uptake in human liver biopsies.Retention of nonhelical procollagen containing cis-hydroxyproline in rough endoplasmic reticulum.Morphological influence of ascorbic acid deficiency on endochondral ossification in osteogenic disorder Shionogi rat.Ascorbate can act as an inducer of the collagen pathway because most steps are tightly coupled.Prolyl hydroxylase in platelets.Ziploc-ing the structure 2.0: Endoplasmic reticulum-resident peptidyl prolyl isomerases show different activities toward hydroxyproline.Effects of ascorbic acid concentration on the tissue engineering of the temporomandibular joint disc.Procollagen is more stable in cellulo than in vitro.Type V collagen regulates the assembly of collagen fibrils in cultures of bovine vascular smooth muscle cells.Collagen Hydroxylases and the Protein Disulfide Isomerase Subunit of Prolyl 4-HydroxylasesExtruded Collagen Fibres for Tissue-Engineering Applications: Influence of Collagen Concentration and NaCl Amount
P2860
Q28305907-52DC96FF-0805-466F-8710-11640E10C8F3Q28340214-B01352F2-CEBC-41F4-AA4E-71682F4BF85DQ33822216-BB73E9FF-BE3F-49B9-AB21-999CD64A9FCCQ34305223-9A67938D-1644-4481-9DBB-18670B4416EEQ34371713-1D1F6973-85B0-48A0-A29F-CB7125525D59Q35360129-70FF9A52-D48E-40AF-B5A6-BA2FFE0835F0Q36376038-51B109F7-417A-45A1-B6FA-124148C0DA65Q36615661-434BCC1A-8A9F-4D37-A7D5-96F354985029Q36859407-569B66AD-D865-4309-B578-DA32A6309BDDQ36872408-F6C987E3-1CA3-4B01-AFA9-828BE6807475Q36936482-6537D029-8263-4FB4-8B27-3020006BFE7FQ36957512-5E422663-5F7B-47B3-8938-78CB9AE2654CQ36993250-42C6B55A-0D24-46AE-A4B9-7780DCE0DE67Q39106303-FF4C808F-7114-441E-A858-63355D394578Q39927760-4E3ABC8A-7546-4A44-8C4C-71BD14BE4B64Q40978647-0061C69D-A1D7-47F6-88A3-F743A072FC00Q41038016-D9A3920E-75F6-4FC1-BF89-6EC77BCCE92AQ41841265-5DEA63BF-5719-4E0C-9774-9D0535AD68DDQ41849924-2C819B7D-5919-4B39-857A-1C4D4567561DQ41879498-0F834125-824A-4CE3-A6B7-ABFA146F8C50Q42022377-749AEF55-4FB2-424C-A724-A2B015700F16Q42548878-83296769-DE1F-4A31-9C1D-48EB42037AD0Q42857722-14F3DB3C-9DA0-4C2B-99EF-4391B414B664Q43250433-6A3833B7-FFD2-46CE-A2A0-46D05D1502C0Q43634377-0F00C2EB-AC0D-4F43-BF04-06C6F9E335ACQ44131671-7575051E-4557-443F-B63C-68DB40D2EFDCQ44253656-6863BEFF-545D-4A25-91B1-070D191ECA4EQ47958525-454B559C-B2FC-45FA-A7C8-6B8A2C926CC7Q51068389-DFF7C36D-3EC4-4780-9B85-36E6FC8DB9B5Q51170975-7D8C8829-7D67-446B-A784-86D10B86CBB8Q51233629-8D554E08-8990-499B-B54C-87C916B75A91Q54033716-2C0C96C2-4A51-4F8B-BCB1-1B3F0DE9574CQ56038109-7468D2DA-5518-4F97-A828-DBDC220C9B5BQ57971842-68C1D895-F4A2-4970-A436-D225A844E717
P2860
Hydroxyproline stabilizes the triple helix of chick tendon collagen.
description
1973 nî lūn-bûn
@nan
1973年の論文
@ja
1973年学术文章
@wuu
1973年学术文章
@zh
1973年学术文章
@zh-cn
1973年学术文章
@zh-hans
1973年学术文章
@zh-my
1973年学术文章
@zh-sg
1973年學術文章
@yue
1973年學術文章
@zh-hant
name
Hydroxyproline stabilizes the triple helix of chick tendon collagen.
@en
Hydroxyproline stabilizes the triple helix of chick tendon collagen.
@nl
type
label
Hydroxyproline stabilizes the triple helix of chick tendon collagen.
@en
Hydroxyproline stabilizes the triple helix of chick tendon collagen.
@nl
prefLabel
Hydroxyproline stabilizes the triple helix of chick tendon collagen.
@en
Hydroxyproline stabilizes the triple helix of chick tendon collagen.
@nl
P2093
P1476
Hydroxyproline stabilizes the triple helix of chick tendon collagen.
@en
P2093
P304
P356
10.1016/0006-291X(73)90960-1
P407
P577
1973-05-01T00:00:00Z