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Volumn 15, Issue 2, 1999, Pages 213-220

Expression in Escherichia coli, refolding, and purification of human procathepsin K, an osteoclast-specific protease

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME PURIFICATION; GEL PERMEATION CHROMATOGRAPHY; PROCATHEPSIN K; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEINASE;

EID: 0033102214     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.1998.1013     Document Type: Article
Times cited : (31)

References (20)
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    • Crystal structure of human cathepsin K complexed with a potent inhibitor
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    • Smith, S.1    Gottesman, M.2
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    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
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  • 14
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    • Pedigrees of some mutant strains ofEscherichia coli
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    • The proregion of cathepsin L is required for proper folding, stability and ER exit
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    • (1994) Arch. Biochem. Biophys. , vol.311 , pp. 19-27
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  • 19
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    • Potency and selectivity of the cathepsin L propeptide as an inhibitor of cysteine proteases
    • Carmona E., Dufour E., Plouffe C., Takebe S., Mason P., Mort J., Menard R. Potency and selectivity of the cathepsin L propeptide as an inhibitor of cysteine proteases. Biochemistry. 35:1996;8149-8157.
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  • 20
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    • Proregion structure of members of the papain superfamily. Mode of inhibition of enzymatic activity
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.