about
sameAs
Cysteine Proteases: Modes of Activation and Future Prospects as Pharmacological TargetsCrystal structure of the zymogen form of the group A Streptococcus virulence factor SpeB: An integrin-binding cysteine proteaseA New Autocatalytic Activation Mechanism for Cysteine Proteases Revealed by Prevotella intermedia Interpain APorphyromonas gingivalis Virulence Factor Gingipain RgpB Shows a Unique Zymogenic Mechanism for Cysteine PeptidasesThe crystal structure of the cysteine protease Xylellain from Xylella fastidiosa reveals an intriguing activation mechanismThe structure of the cysteine protease and lectin-like domains of Cwp84, a surface layer-associated protein fromClostridium difficileResidue-specific annotation of disorder-to-order transition and cathepsin inhibition of a propeptide-like crammer from D. melanogaster.Inhibition of cathepsin L-like proteases by cathepsin V propeptide.Clinical and animal research findings in pycnodysostosis and gene mutations of cathepsin K from 1996 to 2011Proteases involved in cartilage matrix degradation in osteoarthritis.Structural and Functional Characterization of the Major Allergen Amb a 11 from Short Ragweed PollenThe alpha1/2 helical backbone of the prodomains defines the intrinsic inhibitory specificity in the cathepsin L-like cysteine protease subfamily.Dental Abnormalities Caused by Novel Compound Heterozygous CTSK Mutations.The crystal structure of a Cys25 -> Ala mutant of human procathepsin S elucidates enzyme-prosequence interactions.Cysteine cathepsin activity regulation by glycosaminoglycans.Overexpression of the riboflavin biosynthetic pathway in Pichia pastoris.Folding incompetence of cathepsin L-like cysteine proteases may be compensated by the highly conserved, domain-building N-terminal extension of the proregion.Role of the prosegment of Fasciola hepatica cathepsin L1 in folding of the catalytic domain.Comprehensive search for cysteine cathepsins in the human genome.Autocatalytic processing of recombinant human procathepsin B is a bimolecular process.
P2860
Q26747530-3D2BFFBE-1EE9-4969-ABCC-330B4C967B1AQ27621469-C250AE58-9793-425D-8588-F91E89A86AA7Q27648990-37121811-6F59-4632-8320-15DED2B14067Q27677225-CF8A0288-FFA3-4EA6-9E60-62B510C1C66FQ27683786-34D053BB-644F-48F4-9108-FC695D3DF17DQ27684602-DA5351F0-F83E-43D7-8C06-10FC42153823Q34562722-75091487-9C1F-411F-8418-3013A1B129F3Q34630480-B93BD5CB-AD46-4836-B2F7-58B3BBC47166Q35040136-77300C00-BAFD-4E03-9E78-FE381EA63462Q35560686-57624E5B-B031-464B-9E8A-8FABEFCDF840Q37065874-380B0004-DC0D-4BEA-BD28-566A143FC8E0Q40894384-37F1E191-59E0-426F-A1D4-FC72311FA1B6Q41455648-4AC765AE-ED4A-499D-8DDD-A005B12152A9Q41767615-F57A4414-1F33-43A7-B02B-CF9904D49A25Q41852264-FBE51ADE-6CC6-4C84-8DAF-350641C9B6E6Q42130077-9490B362-855C-45BD-A448-FB2EDC27C641Q43716345-BDC5FE1B-107F-499E-A60C-04EC6E7ADDB5Q44219908-E1366551-FC11-4013-BDE3-353F7A64F428Q44935351-58DD09A3-DD78-4559-9D44-7E06CFEE715DQ47851086-A79C574E-0D71-430E-83C7-06C47597CEFB
P2860
description
1999 nî lūn-bûn
@nan
1999 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Crystal structure of wild-type human procathepsin K
@ast
Crystal structure of wild-type human procathepsin K
@en
Crystal structure of wild-type human procathepsin K
@nl
type
label
Crystal structure of wild-type human procathepsin K
@ast
Crystal structure of wild-type human procathepsin K
@en
Crystal structure of wild-type human procathepsin K
@nl
prefLabel
Crystal structure of wild-type human procathepsin K
@ast
Crystal structure of wild-type human procathepsin K
@en
Crystal structure of wild-type human procathepsin K
@nl
P2093
P2860
P3181
P356
P1433
P1476
Crystal structure of wild-type human procathepsin K
@en
P2093
J Sivaraman
M Lalumière
P2860
P304
P3181
P356
10.1110/PS.8.2.283
P577
1999-02-01T00:00:00Z