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Volumn 45, Issue 30, 2006, Pages 9059-9067

Exploring the S4 and S1 prime subsite specificities in caspase-3 with aza-peptide epoxide inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; CATALYSIS; CATALYSTS; CRYSTAL STRUCTURE; HYDROGEN BONDS; POLYPEPTIDES;

EID: 33746646754     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi060364p     Document Type: Article
Times cited : (26)

References (46)
  • 1
    • 0034522342 scopus 로고    scopus 로고
    • Caspases: Key players in programmed cell death
    • Grütter, M. G. (2000) Caspases: key players in programmed cell death, Curr. Opin. Struct. Biol. 10, 649-655.
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 649-655
    • Grütter, M.G.1
  • 2
    • 0032785021 scopus 로고    scopus 로고
    • Caspase structure, proteolytic substrates, and function during apoptotic cell death
    • Nicholson, D. W. (1999) Caspase structure, proteolytic substrates, and function during apoptotic cell death, Cell Death Differ. 6, 1028-1042.
    • (1999) Cell Death Differ. , vol.6 , pp. 1028-1042
    • Nicholson, D.W.1
  • 3
    • 0033617402 scopus 로고    scopus 로고
    • Involvement of caspases in proteolytic cleavage of Alzheimer's amyloid-β precursor protein and amyloidogenic A-β peptide formation
    • Gervais, F. G., Xu, D., Robertson, G. S., Vaillancourt, J. P., Zhu, Y., Huang, J., LeBlanc, A., Smith, D., Rigby, M., and Shearman, M. S. (1999) Involvement of caspases in proteolytic cleavage of Alzheimer's amyloid-β precursor protein and amyloidogenic A-β peptide formation, Cell 97, 395.
    • (1999) Cell , vol.97 , pp. 395
    • Gervais, F.G.1    Xu, D.2    Robertson, G.S.3    Vaillancourt, J.P.4    Zhu, Y.5    Huang, J.6    Leblanc, A.7    Smith, D.8    Rigby, M.9    Shearman, M.S.10
  • 6
    • 0742303572 scopus 로고    scopus 로고
    • Non-apoptotic functions of caspase-3 in nervous tissue
    • Gulyaeva, N. V. (2003) Non-apoptotic functions of caspase-3 in nervous tissue, Biochemistry (Moscow) 68, 1171-1180.
    • (2003) Biochemistry (Moscow) , vol.68 , pp. 1171-1180
    • Gulyaeva, N.V.1
  • 8
    • 0642314384 scopus 로고    scopus 로고
    • Non-apoptotic functions of caspases in cellular proliferation and differentiation
    • Schwerk, C., and Schulze-Osthoff, K. (2003) Non-apoptotic functions of caspases in cellular proliferation and differentiation, Biochem. Pharmacol. 66, 1453-1458.
    • (2003) Biochem. Pharmacol. , vol.66 , pp. 1453-1458
    • Schwerk, C.1    Schulze-Osthoff, K.2
  • 9
    • 3042850072 scopus 로고    scopus 로고
    • Prospects for caspase inhibitors
    • O'Brien, T. (2004) Prospects for caspase inhibitors. Mini Rev. Med. Chem. 4, 153-165.
    • (2004) Mini Rev. Med. Chem. , vol.4 , pp. 153-165
    • O'Brien, T.1
  • 10
    • 0035831473 scopus 로고    scopus 로고
    • Executioner caspase-3, -6, and -7 perform distinct, non-redundant roles during the demolition phase of apoptosis
    • Slee, E. A., Adrain, C., and Martin, J. S. (2001) Executioner caspase-3, -6, and -7 perform distinct, non-redundant roles during the demolition phase of apoptosis, J. Biol. Chem. 276, 7320-7326.
    • (2001) J. Biol. Chem. , vol.276 , pp. 7320-7326
    • Slee, E.A.1    Adrain, C.2    Martin, J.S.3
  • 12
    • 10644282148 scopus 로고    scopus 로고
    • The protein structures that shape caspase activity, specificity, activation and inhibition
    • Fuentes-Prior, P., and Salvesen, G. S. (2004) The protein structures that shape caspase activity, specificity, activation and inhibition, Biochem. J. 384, 201-232.
    • (2004) Biochem. J. , vol.384 , pp. 201-232
    • Fuentes-Prior, P.1    Salvesen, G.S.2
  • 13
    • 2342531089 scopus 로고    scopus 로고
    • Reducing the peptidyl features of caspase-3 inhibitors: A structural analysis
    • Becker, J. W. (2004) Reducing the peptidyl features of caspase-3 inhibitors: a structural analysis, J. Med. Chem. 47, 2466-74.
    • (2004) J. Med. Chem. , vol.47 , pp. 2466-2474
    • Becker, J.W.1
  • 14
    • 23944461510 scopus 로고    scopus 로고
    • Using peptidic inhibitors to systematically probe the S1′ site of caspase-3 and caspase-7
    • Goode, D. R., Sharma, A. K., and Hergenrother, P. J. (2005) Using peptidic inhibitors to systematically probe the S1′ site of caspase-3 and caspase-7, Org. Lett. 7, 3529-3532.
    • (2005) Org. Lett. , vol.7 , pp. 3529-3532
    • Goode, D.R.1    Sharma, A.K.2    Hergenrother, P.J.3
  • 16
    • 0034283578 scopus 로고    scopus 로고
    • Internally quenched fluorescent peptide substrates disclose the subsite preferences of human caspases 1, 3, 6, 7 and 8
    • Stennicke, H. R., Renatas, M., Meldal, M., and Salvesen, G. S. (2000) Internally quenched fluorescent peptide substrates disclose the subsite preferences of human caspases 1, 3, 6, 7 and 8, Biochem. J. 350, 563-568.
    • (2000) Biochem. J. , vol.350 , pp. 563-568
    • Stennicke, H.R.1    Renatas, M.2    Meldal, M.3    Salvesen, G.S.4
  • 17
    • 0035980006 scopus 로고    scopus 로고
    • Evidence that inhibition of cathepsin-B contributes to the neuroprotective properties of caspase inhibitor Tyr-Val-Ala-Asp-chloromethyl ketone
    • Gray, J., Haran, M. M., Schneider, K., Vesce, S., Ray, A. M., Owen, D., White, I. R., Cutler, P., and Davis, J. B. (2001) Evidence that inhibition of cathepsin-B contributes to the neuroprotective properties of caspase inhibitor Tyr-Val-Ala-Asp-chloromethyl ketone, J. Biol. Chem. 276, 32750-32755.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32750-32755
    • Gray, J.1    Haran, M.M.2    Schneider, K.3    Vesce, S.4    Ray, A.M.5    Owen, D.6    White, I.R.7    Cutler, P.8    Davis, J.B.9
  • 23
    • 1542328053 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of aza-peptide epoxides as selective and potent inhibitors of caspases-1, -3, -6, and -8
    • James, K. E., Asgian, J. L., Li, Z. Z., Ekici, O. D., Rubin, J. R., Mikolajczyk, J., Salvesen, G. S., and Powers, J. C. (2004) Design, synthesis, and evaluation of aza-peptide epoxides as selective and potent inhibitors of caspases-1, -3, -6, and -8, J. Med. Chem. 47, 1553-1574.
    • (2004) J. Med. Chem. , vol.47 , pp. 1553-1574
    • James, K.E.1    Asgian, J.L.2    Li, Z.Z.3    Ekici, O.D.4    Rubin, J.R.5    Mikolajczyk, J.6    Salvesen, G.S.7    Powers, J.C.8
  • 26
    • 85027632383 scopus 로고
    • Automatic indexing of rotation diffraction patterns
    • Kabsch, W. (1988) Automatic indexing of rotation diffraction patterns, J. Appl. Crystallogr. 21, 67-72.
    • (1988) J. Appl. Crystallogr. , vol.21 , pp. 67-72
    • Kabsch, W.1
  • 28
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J. Y., Cowan, S. W., and Kjeldgaard. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models, Acta Crystallogr., Sect. A 47, 110-119.
    • (1991) Acta Crystallogr., Sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard4
  • 29
    • 0036882396 scopus 로고    scopus 로고
    • Irreversible inhibitors of serine, cysteine, and threonine proteases
    • Powers, J. C., Asgian, J. L., Ekici, O. D., and James, K. E. (2002) Irreversible inhibitors of serine, cysteine, and threonine proteases, Chem. Rev. 102, 4639-4750.
    • (2002) Chem. Rev. , vol.102 , pp. 4639-4750
    • Powers, J.C.1    Asgian, J.L.2    Ekici, O.D.3    James, K.E.4
  • 30
    • 0033041936 scopus 로고    scopus 로고
    • Peptidyl beta-homo-aspartals (3-amino-4-carboxybutyraldehydes): New specific inhibitors of caspases
    • Bajusz, S., Fauszt, I., Nemeth, K., Barabas, E., Juhasz, A., Patthy, M., and Bauer, P. I. (1999) Peptidyl beta-homo-aspartals (3-amino-4- carboxybutyraldehydes): new specific inhibitors of caspases, Biopolymers 51, 109-118.
    • (1999) Biopolymers , vol.51 , pp. 109-118
    • Bajusz, S.1    Fauszt, I.2    Nemeth, K.3    Barabas, E.4    Juhasz, A.5    Patthy, M.6    Bauer, P.I.7
  • 31
    • 0142142211 scopus 로고    scopus 로고
    • Cysteine protease inhibitors containing small rings
    • Schirmeister, T., and Klockow, A. (2003) Cysteine protease inhibitors containing small rings, Mini Rev. Med. Chem. 3, 589.
    • (2003) Mini Rev. Med. Chem. , vol.3 , pp. 589
    • Schirmeister, T.1    Klockow, A.2
  • 32
    • 0021186126 scopus 로고
    • Reaction of azapeptides with chymotrypsin-like enzymes. New inhibitors and active site titrants for chymotrypsin A alpha, subtilisin BPN', subtilisin Carlsberg, and human leukocyte cathepsin G
    • Gupton, B. F., Carroll, D. L., Tuhy, P. M., Kam, C. M., and Powers, J. C. (1984) Reaction of azapeptides with chymotrypsin-like enzymes. New inhibitors and active site titrants for chymotrypsin A alpha, subtilisin BPN', subtilisin Carlsberg, and human leukocyte cathepsin G, J. Biol. Chem. 259, 4279-4287.
    • (1984) J. Biol. Chem. , vol.259 , pp. 4279-4287
    • Gupton, B.F.1    Carroll, D.L.2    Tuhy, P.M.3    Kam, C.M.4    Powers, J.C.5
  • 33
    • 0343433408 scopus 로고    scopus 로고
    • Cysteine proteases and their inhibitors
    • Otto, H. H., and Schirmeister, T. (1997) Cysteine proteases and their inhibitors, Chem. Rev. 97, 133-172.
    • (1997) Chem. Rev. , vol.97 , pp. 133-172
    • Otto, H.H.1    Schirmeister, T.2
  • 38
    • 85082699866 scopus 로고
    • Azapeptides
    • Gante, J. (1989) Azapeptides, Synthesis, 405-413.
    • (1989) Synthesis , pp. 405-413
    • Gante, J.1
  • 40
    • 0012771519 scopus 로고
    • Hydrazinverbindungen als heterobestandteile in peptiden. XV. Synthese von eledoisin-octapeptiden mit den carbazylresten azaglycin und α-azaasparagin statt glycin und asparagin
    • Hartmut Niedlich, and Christa Oehme. (1972) Hydrazinverbindungen als heterobestandteile in peptiden. XV. Synthese von eledoisin-octapeptiden mit den carbazylresten azaglycin und α-azaasparagin statt glycin und asparagin, J. Prakt. Chem. 314, 759-768.
    • (1972) J. Prakt. Chem. , vol.314 , pp. 759-768
    • Niedlich, H.1    Oehme, C.2
  • 43
    • 33745260957 scopus 로고    scopus 로고
    • Extended substrate recognition in caspase-3 revealed by high-resolution X-ray structure analysis
    • Ganesan, R., Mittl, P. R., Jelakovic, S., and Grutter, M. G. (2006) Extended substrate recognition in caspase-3 revealed by high-resolution X-ray structure analysis, J. Mol. Biol. 359(5), 1378-1388.
    • (2006) J. Mol. Biol. , vol.359 , Issue.5 , pp. 1378-1388
    • Ganesan, R.1    Mittl, P.R.2    Jelakovic, S.3    Grutter, M.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.