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Volumn 384, Issue 6, 2003, Pages 833-836

Vito Turk - 30 years of research on cysteine proteases and their inhibitors

(2)  Turk, Boris a   Fritz, Hans a  

a NONE

Author keywords

[No Author keywords available]

Indexed keywords

ANTIMALARIAL AGENT; ASPARTIC PROTEINASE; CATHEPSIN B; CATHEPSIN D; CATHEPSIN H; CATHEPSIN L; CATHEPSIN S; CYSTATIN; CYSTEINE PROTEINASE; KININOGEN; PAPAIN; PLASMA PROTEIN; PROTEINASE INHIBITOR; RECOMBINANT DNA; STEFIN B; SULFONE DERIVATIVE;

EID: 0038148113     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.2003.093     Document Type: Editorial
Times cited : (3)

References (29)
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  • 3
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  • 5
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    • Cloning a synthetic gene for human stefin B and its expression in E. coli
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    • (1988) FEBS Lett. , vol.239 , pp. 41-44
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  • 7
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    • Folding and activation of human procathepsin S from inclusion bodies produced in Escherichia coli
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    • (1996) Eur. J. Biochem. , vol.236 , pp. 558-562
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  • 9
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  • 10
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    • Thyroglobulin type-1 domains in equistatin inhibit both papain-like cysteine proteinases and cathepsin D
    • Lenarčič, B. and Turk, V. (1999). Thyroglobulin type-1 domains in equistatin inhibit both papain-like cysteine proteinases and cathepsin D. J. Biol. Chem. 274, 563-566.
    • (1999) J. Biol. Chem. , vol.274 , pp. 563-566
    • Lenarčič, B.1    Turk, V.2
  • 11
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    • Equistatin, a new protein inhibitor of cysteine proteinases from Actinia equina is structurally related to thyroglobulin type-1 domain
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    • Machleidt, W.1    Borchart, U.2    Fritz, H.3    Brzin, J.4    Ritonja, A.5    Turk, V.6
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    • Purification of the complex of cathepsin L and the MHC class II-associated invariant chain fragment from human kidney
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    • (1993) FEBS Lett. , vol.336 , pp. 555-559
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  • 25
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    • Crystal structures of human procathepsin B at 3.2 and 3.3 Å resolution reveal an interaction motif between a papain-like cysteine protease and its propeptide
    • Turk, D., Podobnik, M., Kuhelj, R., Dolinar, M. and Turk, V. (1996). Crystal structures of human procathepsin B at 3.2 and 3.3 Å resolution reveal an interaction motif between a papain-like cysteine protease and its propeptide. FEBS Lett. 384, 211-214.
    • (1996) FEBS Lett. , vol.384 , pp. 211-214
    • Turk, D.1    Podobnik, M.2    Kuhelj, R.3    Dolinar, M.4    Turk, V.5
  • 26
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    • Structure of human dipeptidyl peptidase I (cathepsin C): Exclusion domain added to an endopeptidase framework creates the machine for activation of granular serine proteases
    • Turk, D., Janjić, V., Štern, I., Podobnik, M., Lamba, D., Dahl, S.W., Lauritzen, C., Pedersen, J., Turk, V. and Turk, B. (2001). Structure of human dipeptidyl peptidase I (cathepsin C): exclusion domain added to an endopeptidase framework creates the machine for activation of granular serine proteases. EMBO J. 20, 6570-6582.
    • (2001) EMBO J. , vol.20 , pp. 6570-6582
    • Turk, D.1    Janjić, V.2    Štern, I.3    Podobnik, M.4    Lamba, D.5    Dahl, S.W.6    Lauritzen, C.7    Pedersen, J.8    Turk, V.9    Turk, B.10
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    • Acid sulphydryl protease from calf lymph nodes
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  • 29
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    • A thiol dependent acid protease
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    • Turnšek, T., Kregar, I., Lebez, D. and Turk, V. (1977). A thiol dependent acid protease. In: Intracellular Protein Catabolism II, V. Turk and N. Marks, eds. (New York, USA: Plenum Press), pp. 290-298.
    • (1977) Intracellular Protein Catabolism II , pp. 290-298
    • Turnšek, T.1    Kregar, I.2    Lebez, D.3    Turk, V.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.