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The peptides acetyl-(Gly-3(S)Hyp-4(R)Hyp)10-NH2 and acetyl-(Gly-Pro-3(S)Hyp)10-NH2 do not form a collagen triple helix.Hydroxylation-induced stabilization of the collagen triple helix. Acetyl-(glycyl-4(R)-hydroxyprolyl-4(R)-hydroxyprolyl)(10)-NH(2) forms a highly stable triple helix.Intercellular accumulation of type V collagen fibrils in accordance with cell aggregation.The effect of deuterium oxide on the stability of the collagen model peptides H-(Pro-Pro-Gly)(10)-OH, H-(Gly-Pro-4(R)Hyp)(9)-OH, and Type I collagen.Kinetic analysis of the metal binding mechanism of Escherichia coli manganese superoxide dismutase.Posttranslational modifications in type I collagen from different tissues extracted from wild type and prolyl 3-hydroxylase 1 null mice.Kinetic hysteresis in collagen folding.Conformational change from rigid rod to star: a triple-helical peptide with a linker domain at the C-terminal end.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 foldingCalorimetric studies on the tight binding metal interactions of Escherichia coli manganese superoxide dismutase.Effect of the -Gly-3(S)-hydroxyprolyl-4(R)-hydroxyprolyl- tripeptide unit on the stability of collagen model peptides.The crystal structure of the collagen-like polypeptide (glycyl-4(R)-hydroxyprolyl-4(R)-hydroxyprolyl)9 at 1.55 A resolution shows up-puckering of the proline ring in the Xaa position.Ziploc-ing the structure 2.0: Endoplasmic reticulum-resident peptidyl prolyl isomerases show different activities toward hydroxyproline.Type I collagen induces mesenchymal cell differentiation into myofibroblasts through YAP-induced TGF-β1 activation.Reactive oxygen species are responsible for the cell aggregation and production of pro-inflammatory mediators in phorbol ester (PMA)-treated U937 cells on gelatin-coated dishes through upregulation of autophagySeparation of the subtypes of type V collagen molecules, [alpha 1(V)]2 alpha 2(V) and alpha 1(V) alpha 2(V) alpha 3(V), by chain composition-dependent affinity for heparin: single alpha 1(V) chain shows intermediate heparin affinity between those ofPeculiar effect of urea on the interaction of type I collagen with heparin on chromatographyCollagen triple helix formation can be nucleated at either endThe crystal structure of a collagen-like polypeptide with 3(S)-hydroxyproline residues in the Xaa position forms a standard 7/2 collagen triple helixFragility of reconstituted type V collagen fibrils with the chain composition of α1(V)α2(V)α3(V) respective of the D-periodic banding patternEvaluation of Keratinocyte Proliferation on Two- and Three-dimensional Type I Collagen SubstratesSilibinin-induced apoptosis of breast cancer cells involves mitochondrial impairmentSilibinin's regulation of proliferation and collagen gene expressions of rat pancreatic β-cells cultured on types I and V collagen involves β-catenin nuclear translocationImproved in Vivo Tracking of Orally Administered Collagen Hydrolysate Using Stable Isotope Labeling and LC-MS TechniquesType I collagen inhibits adipogenic differentiation via YAP activation in vitro
P50
Q30882774-FCAB7CDA-3499-43CC-BC3A-50D7CB8438CCQ30940504-55594571-60E1-4AE5-AE9D-34FB39105767Q33367491-B6389C48-28E3-48FE-BBD1-58CB956286E8Q33505366-0FA89C35-B219-4D32-BE41-040FBAA1A776Q34353021-0A7C82BC-3883-491B-9407-CC3301A5E7E3Q37112713-461190BB-1147-4952-A1D8-5AB1A3D994C2Q41006604-D495044C-510B-4128-B5FC-2781DFA6C6F4Q41429412-A3CE58EB-865C-4D08-A05E-131EFAAA58C5Q42033519-6067DC23-D4D7-4AA4-A3A0-B2F66B3C1CACQ43015446-B9DCD06D-4A24-44CD-AF7D-15DD488E0AFCQ46236307-94262358-8776-4C7A-9B92-CA442340622CQ46398264-0438A308-90C1-46D8-89CA-3FA13F291CBAQ51068389-8E776388-E52A-48FA-8931-CCDABD39349EQ54978751-81A53E9E-416B-48D1-AC52-DB3EA718F340Q57045306-F214A0EC-D38E-478A-AD9D-170D7E526552Q71943309-29BCA6DA-B313-4D30-984B-5C691D99280FQ72132024-D966304E-9D18-47D4-ACEB-68560DD206BEQ78830503-796A4EC2-6CA2-46D5-A477-8FE4ADFD6F36Q79785484-418B9B88-EAC5-4E33-919B-B8D195C59477Q85256190-1277E256-0EFC-4BD0-B1E7-20696E3D157DQ91784362-755AFD9C-772E-4E45-B475-92222C02F724Q91992573-E9CF7EE5-E26E-4C9A-A325-6171FBBE077BQ92363854-4915A92F-BE29-4497-B6B9-73121ECD294AQ92723620-0C68ED51-7BBD-486D-8179-5CF15B1C7C1FQ92740473-02940810-9CF2-477B-BFCF-60A9218ACE79
P50
description
researcher, ORCID id # 0000-0003-3354-6264
@en
wetenschapper
@nl
name
Kazunori Mizuno
@ast
Kazunori Mizuno
@en
Kazunori Mizuno
@es
Kazunori Mizuno
@nl
type
label
Kazunori Mizuno
@ast
Kazunori Mizuno
@en
Kazunori Mizuno
@es
Kazunori Mizuno
@nl
prefLabel
Kazunori Mizuno
@ast
Kazunori Mizuno
@en
Kazunori Mizuno
@es
Kazunori Mizuno
@nl
P106
P31
P496
0000-0003-3354-6264