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Activation of human prolegumain by cleavage at a C-terminal asparagine residueDesign of potent and selective human cathepsin K inhibitors that span the active siteCollagen degradation in the abdominal aneurysm: a conspiracy of matrix metalloproteinase and cysteine collagenasesCysteine Proteases: Modes of Activation and Future Prospects as Pharmacological TargetsCrystal structure of wild-type human procathepsin KThe structure of a thermostable mutant of pro-papain reveals its activation mechanismAutocatalytic processing of recombinant human procathepsin L. Contribution of both intermolecular and unimolecular events in the processing of procathepsin L in vitroMatriptase autoactivation is tightly regulated by the cellular chemical environmentsLocalization of rat cathepsin K in osteoclasts and resorption pits: inhibition of bone resorption and cathepsin K-activity by peptidyl vinyl sulfonesAutocatalytic activation of human legumain at aspartic acid residuesProteomic identification of Drosophila melanogaster male accessory gland proteins, including a pro-cathepsin and a soluble gamma-glutamyl transpeptidase.Cathepsin K analysis in a pycnodysostosis cohort: demographic, genotypic and phenotypic features.The Lys-Asp-Tyr Triad within the Mite Allergen Der p 1 Propeptide Is a Critical Structural Element for the pH-Dependent Initiation of the Protease Maturation.Characterization of novel cathepsin K mutations in the pro and mature polypeptide regions causing pycnodysostosis.Expression of cathepsin K is regulated by shear stress in cultured endothelial cells and is increased in endothelium in human atherosclerosis.Cathepsin K is present in invasive oral tongue squamous cell carcinoma in vivo and in vitroClinical and animal research findings in pycnodysostosis and gene mutations of cathepsin K from 1996 to 2011Cathepsin k is a critical protease in synovial fibroblast-mediated collagen degradation.Excessive activity of cathepsin K is associated with cartilage defects in a zebrafish model of mucolipidosis II.Autocatalytic processing of procathepsin B is triggered by proenzyme activityProteolytic-antiproteolytic balance and its regulation in carcinogenesis.Cathepsins L and S are not required for activation of dipeptidyl peptidase I (cathepsin C) in miceEnzymatic and Structural Characterization of the Major Endopeptidase in the Venus Flytrap Digestion Fluid.Endothelial cells and cathepsins: Biochemical and biomechanical regulation.Therapeutic inhibition of cathepsin K-reducing bone resorption while maintaining bone formation.Glycosaminoglycans facilitate procathepsin B activation through disruption of propeptide-mature enzyme interactions.Approaches for the generation of active papain-like cysteine proteases from inclusion bodies of Escherichia coli.Cathepsin K expression and activity in canine osteosarcoma.Characterization of native and recombinant falcipain-2, a principal trophozoite cysteine protease and essential hemoglobinase of Plasmodium falciparum.Chondroitin sulfate promotes activation of cathepsin K.Actin-binding protein coronin 1A controls osteoclastic bone resorption by regulating lysosomal secretion of cathepsin K.Dipeptidyl peptidase I is essential for activation of mast cell chymases, but not tryptases, in mice.Activation of Arabidopsis vacuolar processing enzyme by self-catalytic removal of an auto-inhibitory domain of the C-terminal propeptide.Acidic cysteine endoproteinase cathepsin K in the degeneration of the superficial articular hyaline cartilage in osteoarthritis.Maturation processing and characterization of streptopain.Procongopain from Trypanosoma congolense is processed at basic pH: an unusual feature among cathepsin L-like cysteine proteases.Cathepsin L1, the major protease involved in liver fluke (Fasciola hepatica) virulence: propetide cleavage sites and autoactivation of the zymogen secreted from gastrodermal cells.Recombinant human procathepsin S is capable of autocatalytic processing at neutral pH in the presence of glycosaminoglycans.Mechanism of the maturation process of SARS-CoV 3CL protease.Autocatalytic processing of recombinant human procathepsin B is a bimolecular process.
P2860
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P2860
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
Autocatalytic activation of human cathepsin K.
@en
type
label
Autocatalytic activation of human cathepsin K.
@en
prefLabel
Autocatalytic activation of human cathepsin K.
@en
P2093
P2860
P356
P1476
Autocatalytic activation of human cathepsin K.
@en
P2093
Amegadzie BY
D'Alessio K
Hanning CR
McLaughlin MM
McQueney MS
P2860
P304
13955-13960
P356
10.1074/JBC.272.21.13955
P407
P577
1997-05-01T00:00:00Z