메뉴 건너뛰기




Volumn 14, Issue 3, 2010, Pages 421-427

Acylating drugs: redesigning natural covalent inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

3 HYDROXY 3 METHYLGLUTARYL COENZYME A; BETA LACTAM ANTIBIOTIC; BETA LACTAM DERIVATIVE; BETA LACTAMASE; BETA LACTAMASE INHIBITOR; BLI 489; CEFTAZIDIME; CLAVULANIC ACID; EZETIMIBE; FATTY ACID SYNTHASE; LACTACYSTIN; LACTACYSTIN BETA LACTONE; LACTIVICIN; NXL 104; PENICILLIN BINDING PROTEIN; PENICILLIN BINDING PROTEIN 2A; POLYKETIDE; SALINOSPORAMIDE A; SULBACTAM; TAZOBACTAM; TETRAHYDROLIPSTATIN; TRIACYLGLYCEROL LIPASE; UNCLASSIFIED DRUG;

EID: 77952542136     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpa.2010.03.035     Document Type: Review
Times cited : (53)

References (50)
  • 1
    • 17244362388 scopus 로고    scopus 로고
    • Mechanistic basis of enzyme-targeted drugs
    • Robertson J.G. Mechanistic basis of enzyme-targeted drugs. Biochemistry 44 (2005) 5561-5571
    • (2005) Biochemistry , vol.44 , pp. 5561-5571
    • Robertson, J.G.1
  • 2
    • 64349093749 scopus 로고    scopus 로고
    • Covalent modifiers: an orthogonal approach to drug design
    • A comprehensive Perspective article that details the mechanisms employed by drugs that covalently modify their targets. This article makes the important point that covalently modifying drugs can be both safe and effective.
    • Potashman M.H., and Duggan M.E. Covalent modifiers: an orthogonal approach to drug design. J Med Chem 52 (2009) 1231-1246. A comprehensive Perspective article that details the mechanisms employed by drugs that covalently modify their targets. This article makes the important point that covalently modifying drugs can be both safe and effective.
    • (2009) J Med Chem , vol.52 , pp. 1231-1246
    • Potashman, M.H.1    Duggan, M.E.2
  • 4
    • 0031736387 scopus 로고    scopus 로고
    • Multimodular penicillin-binding proteins: an enigmatic family of orthologs and paralogs
    • Goffin C., and Ghusyen J.-M. Multimodular penicillin-binding proteins: an enigmatic family of orthologs and paralogs. Microbiol Mol Biol Rev 62 (1998) 1079-1093
    • (1998) Microbiol Mol Biol Rev , vol.62 , pp. 1079-1093
    • Goffin, C.1    Ghusyen, J.-M.2
  • 5
    • 33845894155 scopus 로고    scopus 로고
    • Multi-targeting by monotherapeutic antibacterials
    • An analysis of how antibacterial efficacy, spectrum, potency, and low potential for resistance are crucially linked to covalently modifying multiple PBPs.
    • Silver L. Multi-targeting by monotherapeutic antibacterials. Nat Rev Drug Discov 6 (2007) 41-55. An analysis of how antibacterial efficacy, spectrum, potency, and low potential for resistance are crucially linked to covalently modifying multiple PBPs.
    • (2007) Nat Rev Drug Discov , vol.6 , pp. 41-55
    • Silver, L.1
  • 6
    • 0028287583 scopus 로고
    • Interactive design and synthesis of a novel antibacterial agent
    • Wolfe S., Jin H., Yang K., Kim C.-K., and McEachern E. Interactive design and synthesis of a novel antibacterial agent. Can J Chem 72 (1994) 1051-1065
    • (1994) Can J Chem , vol.72 , pp. 1051-1065
    • Wolfe, S.1    Jin, H.2    Yang, K.3    Kim, C.-K.4    McEachern, E.5
  • 7
    • 0024306878 scopus 로고
    • Reactivation of peptidoglycan synthesis in ether-permeabilized Escherichia coli after inhibition by β-lactam antibiotics
    • Talbot M.K., Schaefer F., Brocks V., and Christenson J.G. Reactivation of peptidoglycan synthesis in ether-permeabilized Escherichia coli after inhibition by β-lactam antibiotics. Antimicrob Agents Chemother 33 (1989) 2101-2108
    • (1989) Antimicrob Agents Chemother , vol.33 , pp. 2101-2108
    • Talbot, M.K.1    Schaefer, F.2    Brocks, V.3    Christenson, J.G.4
  • 8
    • 0028305362 scopus 로고
    • Kinetics of penicillin binding to penicillin-binding proteins of Staphylococcus aureus
    • Chambers H.F., Sachdeva M.J., and Hackbarth C.J. Kinetics of penicillin binding to penicillin-binding proteins of Staphylococcus aureus. Biochem J 301 (1994) 139-144
    • (1994) Biochem J , vol.301 , pp. 139-144
    • Chambers, H.F.1    Sachdeva, M.J.2    Hackbarth, C.J.3
  • 9
    • 0035943720 scopus 로고    scopus 로고
    • Kinetics of β-lactam interactions with penicillin-susceptible and -resistant penicillin-binding protein 2x proteins from Streptococcus pneumonia
    • Lu Y.-P., Kincade E., Sun Y., and Bauer M.D. Kinetics of β-lactam interactions with penicillin-susceptible and -resistant penicillin-binding protein 2x proteins from Streptococcus pneumonia. J Biol Chem 276 (2001) 31494-31501
    • (2001) J Biol Chem , vol.276 , pp. 31494-31501
    • Lu, Y.-P.1    Kincade, E.2    Sun, Y.3    Bauer, M.D.4
  • 10
    • 9644281538 scopus 로고    scopus 로고
    • Crystal structures of complexes between the R61 DD-peptidase and peptidoglycan-mimetic beta-lactams: a non-covalent complex with a "perfect penicillin"
    • Silvaggi N.R., Josephine H.R., Kuzin A.P., Nagarajan R., Pratt R.F., and Kelly J.A. Crystal structures of complexes between the R61 DD-peptidase and peptidoglycan-mimetic beta-lactams: a non-covalent complex with a "perfect penicillin". J Mol Biol 345 (2005) 521-533
    • (2005) J Mol Biol , vol.345 , pp. 521-533
    • Silvaggi, N.R.1    Josephine, H.R.2    Kuzin, A.P.3    Nagarajan, R.4    Pratt, R.F.5    Kelly, J.A.6
  • 11
    • 35648930904 scopus 로고    scopus 로고
    • Reactions of peptidoglycan-mimetic beta-lactams with penicillin-binding proteins in vivo and in membranes
    • Shows that β-lactams with peptidoglycan-mimetic side chains are not more reactive than 'drug-like' analogs and makes the important point that substrate recognition involves an extended structure.
    • Kumar I., Josephine H.R., and Pratt R.F. Reactions of peptidoglycan-mimetic beta-lactams with penicillin-binding proteins in vivo and in membranes. ACS Chem Biol 2 (2007) 620-624. Shows that β-lactams with peptidoglycan-mimetic side chains are not more reactive than 'drug-like' analogs and makes the important point that substrate recognition involves an extended structure.
    • (2007) ACS Chem Biol , vol.2 , pp. 620-624
    • Kumar, I.1    Josephine, H.R.2    Pratt, R.F.3
  • 12
    • 35848970949 scopus 로고    scopus 로고
    • Crystal structure of cefditoren complexed with Streptococcus pneumoniae penicillin-binding protein 2X: structural basis for its high antimicrobial activity
    • Yamada M., Watanabe T., Miyara T., Baba N., Saito J., Takeuchi Y., and Ohsawa F. Crystal structure of cefditoren complexed with Streptococcus pneumoniae penicillin-binding protein 2X: structural basis for its high antimicrobial activity. Antimicrob Agents Chemother 51 (2007) 3902-3907
    • (2007) Antimicrob Agents Chemother , vol.51 , pp. 3902-3907
    • Yamada, M.1    Watanabe, T.2    Miyara, T.3    Baba, N.4    Saito, J.5    Takeuchi, Y.6    Ohsawa, F.7
  • 13
    • 0029147002 scopus 로고
    • Binding of cephalothin and cefotaxime to D-Ala-D-Ala-peptidase reveals a functional basis of a natural mutation in a low-affinity penicillin-binding protein and in extended-spectrum beta-lactamases
    • Kuzin A.P., Liu H., Kelly J.A., and Knox J.R. Binding of cephalothin and cefotaxime to D-Ala-D-Ala-peptidase reveals a functional basis of a natural mutation in a low-affinity penicillin-binding protein and in extended-spectrum beta-lactamases. Biochemistry 34 (1995) 9532-9540
    • (1995) Biochemistry , vol.34 , pp. 9532-9540
    • Kuzin, A.P.1    Liu, H.2    Kelly, J.A.3    Knox, J.R.4
  • 15
    • 0347362788 scopus 로고    scopus 로고
    • Crystal structure of wild-type penicillin-binding protein 5 from Escherichia coli: implications for deacylation of the acyl-enzyme complex
    • Nicholas R.A., Krings S., Tomberg J., Nicola G., and Davies C. Crystal structure of wild-type penicillin-binding protein 5 from Escherichia coli: implications for deacylation of the acyl-enzyme complex. J Biol Chem 278 (2003) 52826-52833
    • (2003) J Biol Chem , vol.278 , pp. 52826-52833
    • Nicholas, R.A.1    Krings, S.2    Tomberg, J.3    Nicola, G.4    Davies, C.5
  • 16
    • 33744504974 scopus 로고    scopus 로고
    • Mechanistic basis for the action of new cephalosporin antibiotics effective against methicillin- and vancomycin-resistant Staphylococcus aureus
    • Fuda C., Hesek D., Lee M., Heilmayer W., Novak R., Vakulenko S.B., and Mobashery S. Mechanistic basis for the action of new cephalosporin antibiotics effective against methicillin- and vancomycin-resistant Staphylococcus aureus. J Biol Chem 281 (2006) 10035-10041
    • (2006) J Biol Chem , vol.281 , pp. 10035-10041
    • Fuda, C.1    Hesek, D.2    Lee, M.3    Heilmayer, W.4    Novak, R.5    Vakulenko, S.B.6    Mobashery, S.7
  • 18
    • 0032803407 scopus 로고    scopus 로고
    • Class C, β-lactamases operate at the diffusion limit for turnover of their preferred cephalosporin substrates
    • Bulychev A., and Mobashery S. Class C, β-lactamases operate at the diffusion limit for turnover of their preferred cephalosporin substrates. Antimicrob Agents Chemother 43 (1999) 1743-1746
    • (1999) Antimicrob Agents Chemother , vol.43 , pp. 1743-1746
    • Bulychev, A.1    Mobashery, S.2
  • 19
    • 53049108025 scopus 로고    scopus 로고
    • Recent developments in β-lactamases and inhibitors
    • A survey of general principles and recent lead structures.
    • Mansour T.S., Bradford P.A., and Venkatesan A.M. Recent developments in β-lactamases and inhibitors. Ann Rep Med Chem 43 (2008) 247-267. A survey of general principles and recent lead structures.
    • (2008) Ann Rep Med Chem , vol.43 , pp. 247-267
    • Mansour, T.S.1    Bradford, P.A.2    Venkatesan, A.M.3
  • 20
    • 52449111304 scopus 로고    scopus 로고
    • Inhibition of class A beta-lactamases by carbapenems: crystallographic observation of two conformations of meropenem in SHV-1
    • A case study for the use of structural biology to understand the principles of β-lactamase inhibition.
    • Nukaga M., Bethel C.R., Thompson J.M., Hujer A.M., Anderson V.E., Knox J.R., and Bonomo R.A. Inhibition of class A beta-lactamases by carbapenems: crystallographic observation of two conformations of meropenem in SHV-1. J Am Chem Soc 130 (2008) 12656-12662. A case study for the use of structural biology to understand the principles of β-lactamase inhibition.
    • (2008) J Am Chem Soc , vol.130 , pp. 12656-12662
    • Nukaga, M.1    Bethel, C.R.2    Thompson, J.M.3    Hujer, A.M.4    Anderson, V.E.5    Knox, J.R.6    Bonomo, R.A.7
  • 21
    • 0030883194 scopus 로고    scopus 로고
    • Nuances of mechanisms and their implications for evolution of the versatile β-lactamase activity: from biosynthetic enzymes to drug resistance factors
    • Bulychev A., Massova I., Miyashita K., and Mobashery S. Nuances of mechanisms and their implications for evolution of the versatile β-lactamase activity: from biosynthetic enzymes to drug resistance factors. J Am Chem Soc 119 (1997) 7619-7625
    • (1997) J Am Chem Soc , vol.119 , pp. 7619-7625
    • Bulychev, A.1    Massova, I.2    Miyashita, K.3    Mobashery, S.4
  • 22
    • 0036263032 scopus 로고    scopus 로고
    • Resistance to β-lactam antibiotics: structure and mechanism based design of β-lactamase inhibitors
    • Sandanayaka V., and Prashad A.S. Resistance to β-lactam antibiotics: structure and mechanism based design of β-lactamase inhibitors. Curr Med Chem 9 (2002) 1145-1165
    • (2002) Curr Med Chem , vol.9 , pp. 1145-1165
    • Sandanayaka, V.1    Prashad, A.S.2
  • 23
    • 0242569199 scopus 로고    scopus 로고
    • Inhibition of Class A and Class C β-lactamases by penems: crystallographic structures of a NOVEL 1,4-thiazepine intermediate
    • Nukaga M., Abe T., Venkatesan A.M., Mansour T.S., Bonomo R.A., and Knox J.R. Inhibition of Class A and Class C β-lactamases by penems: crystallographic structures of a NOVEL 1,4-thiazepine intermediate. Biochemistry 42 (2003) 13152-13159
    • (2003) Biochemistry , vol.42 , pp. 13152-13159
    • Nukaga, M.1    Abe, T.2    Venkatesan, A.M.3    Mansour, T.S.4    Bonomo, R.A.5    Knox, J.R.6
  • 24
    • 67650718178 scopus 로고    scopus 로고
    • In vitro activity of the β-lactamase inhibitor NXL104 against KPC-2 carbapenemase and Enterobacteriaceae expressing KPC carbapenamases
    • In late 2009 AstraZeneca announced a deal to acquire Novexel, the originator of NXL104, and to develop this β-lactamase inhibitor in two drug combinations for treating drug-resistant infections.
    • Stachyra T., Levasseur P., Pechereau M.-C., Girard A.-M., Claudon M., Miossec C., and Black M.T. In vitro activity of the β-lactamase inhibitor NXL104 against KPC-2 carbapenemase and Enterobacteriaceae expressing KPC carbapenamases. J Antimicrob Chemother 64 (2009) 326-329. In late 2009 AstraZeneca announced a deal to acquire Novexel, the originator of NXL104, and to develop this β-lactamase inhibitor in two drug combinations for treating drug-resistant infections.
    • (2009) J Antimicrob Chemother , vol.64 , pp. 326-329
    • Stachyra, T.1    Levasseur, P.2    Pechereau, M.-C.3    Girard, A.-M.4    Claudon, M.5    Miossec, C.6    Black, M.T.7
  • 25
    • 0942290637 scopus 로고    scopus 로고
    • Tazobactam forms a stoichiometric trans-enamine intermediate in the E166A variant of SHV-1 beta-lactamase: 1.63 Å crystal structure
    • Padayatti P.S., Helfand M.S., Totir M.A., Carey M.P., Hujer A.M., Carey P.R., Bonomo R.A., and van den Akker F. Tazobactam forms a stoichiometric trans-enamine intermediate in the E166A variant of SHV-1 beta-lactamase: 1.63 Å crystal structure. Biochemistry 43 (2004) 843-8488
    • (2004) Biochemistry , vol.43 , pp. 843-8488
    • Padayatti, P.S.1    Helfand, M.S.2    Totir, M.A.3    Carey, M.P.4    Hujer, A.M.5    Carey, P.R.6    Bonomo, R.A.7    van den Akker, F.8
  • 26
    • 8344289224 scopus 로고    scopus 로고
    • Inhibitor-resistant class A beta-lactamases: consequences of the Ser130-to-Gly mutation seen in Apo and tazobactam structures of the SHV-1 variant
    • Sun T., Bethel C.R., Bonomo R.A., and Knox J.R. Inhibitor-resistant class A beta-lactamases: consequences of the Ser130-to-Gly mutation seen in Apo and tazobactam structures of the SHV-1 variant. Biochemistry 43 (2004) 14111-14117
    • (2004) Biochemistry , vol.43 , pp. 14111-14117
    • Sun, T.1    Bethel, C.R.2    Bonomo, R.A.3    Knox, J.R.4
  • 27
    • 0035852794 scopus 로고    scopus 로고
    • Inhibition of the SHV-1 beta-lactamase by sulfones: crystallographic observation of two reaction intermediates with tazobactam
    • Kuzin A.P., Nukaga Y., Hujer A., Bonomo R.A., and Knox J.R. Inhibition of the SHV-1 beta-lactamase by sulfones: crystallographic observation of two reaction intermediates with tazobactam. Biochemistry 40 (2001) 1861-1866
    • (2001) Biochemistry , vol.40 , pp. 1861-1866
    • Kuzin, A.P.1    Nukaga, Y.2    Hujer, A.3    Bonomo, R.A.4    Knox, J.R.5
  • 28
    • 0345254956 scopus 로고    scopus 로고
    • Following the reactions of mechanism-based inhibitors with β-lactamase by Raman crystallography
    • Helfand M.S., Totir M.A., Carey M.P., Hujer A.M., Bonomo R.A., and Carey P.R. Following the reactions of mechanism-based inhibitors with β-lactamase by Raman crystallography. Biochemistry 42 (2003) 13386-13392
    • (2003) Biochemistry , vol.42 , pp. 13386-13392
    • Helfand, M.S.1    Totir, M.A.2    Carey, M.P.3    Hujer, A.M.4    Bonomo, R.A.5    Carey, P.R.6
  • 29
    • 0042423395 scopus 로고    scopus 로고
    • Design of β-lactams with mechanism-based non-antibacterial activities
    • Veinberg G., Vorona M., Shestakova I., Kanepe I., and Lukevics E. Design of β-lactams with mechanism-based non-antibacterial activities. Curr Med Chem 10 (2003) 1741-1757
    • (2003) Curr Med Chem , vol.10 , pp. 1741-1757
    • Veinberg, G.1    Vorona, M.2    Shestakova, I.3    Kanepe, I.4    Lukevics, E.5
  • 30
    • 3042621839 scopus 로고    scopus 로고
    • β-Lactam cholesterol absorption inhibitors
    • Burnett D.A. β-Lactam cholesterol absorption inhibitors. Curr Med Chem 11 (2004) 1873-1887
    • (2004) Curr Med Chem , vol.11 , pp. 1873-1887
    • Burnett, D.A.1
  • 32
    • 77955455980 scopus 로고
    • Naturally occurring β-lactones: occurrence, syntheses and properties. A review
    • Lowe C.V., and John C. Naturally occurring β-lactones: occurrence, syntheses and properties. A review. Org Prep Proced Int 27 (1995) 305-346
    • (1995) Org Prep Proced Int , vol.27 , pp. 305-346
    • Lowe, C.V.1    John, C.2
  • 33
    • 0025911832 scopus 로고
    • The lipase inhibitor tetrahydrolipstatin binds covalently to the putative active site serine of pancreatic lipase
    • Hadvary P., Sidler W., Meister W., Vetter W., and Wolfer H. The lipase inhibitor tetrahydrolipstatin binds covalently to the putative active site serine of pancreatic lipase. J Biol Chem 266 (1991) 2021-2027
    • (1991) J Biol Chem , vol.266 , pp. 2021-2027
    • Hadvary, P.1    Sidler, W.2    Meister, W.3    Vetter, W.4    Wolfer, H.5
  • 34
    • 33845690506 scopus 로고    scopus 로고
    • Mass spectrometric evidence of covalently-bound tetrahydrolipstatin at the catalytic serine of Streptomyces rimosus lipase
    • [General Subjects]
    • Asler I.L., Zehl M., Kovacic F., Mueller R., Abramic M., Allmaier G., and Kojic-Prodic B. Mass spectrometric evidence of covalently-bound tetrahydrolipstatin at the catalytic serine of Streptomyces rimosus lipase. Biochim Biophys Acta 1770 (2007) 163-170 [General Subjects]
    • (2007) Biochim Biophys Acta , vol.1770 , pp. 163-170
    • Asler, I.L.1    Zehl, M.2    Kovacic, F.3    Mueller, R.4    Abramic, M.5    Allmaier, G.6    Kojic-Prodic, B.7
  • 35
    • 33845909566 scopus 로고    scopus 로고
    • Pharmacological inhibitors of fatty acid synthase (FASN)-catalyzed endogenous fatty acid biogenesis: a new family of anti-cancer agents?
    • Lupu R., and Menendez J.A. Pharmacological inhibitors of fatty acid synthase (FASN)-catalyzed endogenous fatty acid biogenesis: a new family of anti-cancer agents?. Curr Pharm Biotech 7 (2006) 483-494
    • (2006) Curr Pharm Biotech , vol.7 , pp. 483-494
    • Lupu, R.1    Menendez, J.A.2
  • 36
    • 1542720382 scopus 로고    scopus 로고
    • Orlistat is a novel inhibitor of fatty acid synthase with antitumor activity
    • Kridel S.J., Axelrod F., Rozenkrantz N., and Smith J.W. Orlistat is a novel inhibitor of fatty acid synthase with antitumor activity. Cancer Res 64 (2004) 2070-2075
    • (2004) Cancer Res , vol.64 , pp. 2070-2075
    • Kridel, S.J.1    Axelrod, F.2    Rozenkrantz, N.3    Smith, J.W.4
  • 37
    • 67349217677 scopus 로고    scopus 로고
    • Inhibition of fatty acid synthase by orlistat accelerates gastric tumor cell apoptosis in culture and increases survival rates in gastric tumor bearing mice in vivo
    • Dowling S., Cox J., and Cenedella R.J. Inhibition of fatty acid synthase by orlistat accelerates gastric tumor cell apoptosis in culture and increases survival rates in gastric tumor bearing mice in vivo. Lipids 44 (2009) 489-498
    • (2009) Lipids , vol.44 , pp. 489-498
    • Dowling, S.1    Cox, J.2    Cenedella, R.J.3
  • 38
    • 34547672758 scopus 로고    scopus 로고
    • Crystal structure of the thioesterase domain of human fatty acid synthase inhibited by Orlistat
    • Pemble IV C.W., Johnson L.C., Kridel S.J., and Lowther W.T. Crystal structure of the thioesterase domain of human fatty acid synthase inhibited by Orlistat. Nat Struct Mol Biol 14 (2007) 704-709
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 704-709
    • Pemble IV, C.W.1    Johnson, L.C.2    Kridel, S.J.3    Lowther, W.T.4
  • 40
    • 33746835442 scopus 로고    scopus 로고
    • Structural basis for the design of potent and species-specific inhibitors of 3-hydroxy-3-methylglutaryl CoA synthases
    • Pojer F., Ferrer J.-L., Richard S.B., Nagegowda D.A., Chye M.-L., Bach T.J., and Noel J.P. Structural basis for the design of potent and species-specific inhibitors of 3-hydroxy-3-methylglutaryl CoA synthases. Proc Natl Acad Sci U S A 103 (2006) 11491-11496
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 11491-11496
    • Pojer, F.1    Ferrer, J.-L.2    Richard, S.B.3    Nagegowda, D.A.4    Chye, M.-L.5    Bach, T.J.6    Noel, J.P.7
  • 42
    • 0028180516 scopus 로고
    • A β-Lactone related to lactacystin induces neurite outgrowth in a neuroblastoma cell line and inhibits cell cycle progression in an osteosarcoma cell line
    • Fenteany G., Standaert R.F., Reichard G.A., Corey E.J., and Schreiber S.L. A β-Lactone related to lactacystin induces neurite outgrowth in a neuroblastoma cell line and inhibits cell cycle progression in an osteosarcoma cell line. Proc Natl Acad Sci U S A 91 (1994) 3358-3362
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 3358-3362
    • Fenteany, G.1    Standaert, R.F.2    Reichard, G.A.3    Corey, E.J.4    Schreiber, S.L.5
  • 44
    • 0029033981 scopus 로고
    • Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin
    • Fenteany G., Standaert R.F., Lane W.S., Choi S., Corey E.J., and Schreiber S.L. Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science 268 (1995) 726-731
    • (1995) Science , vol.268 , pp. 726-731
    • Fenteany, G.1    Standaert, R.F.2    Lane, W.S.3    Choi, S.4    Corey, E.J.5    Schreiber, S.L.6
  • 45
    • 0029937677 scopus 로고    scopus 로고
    • Mechanistic studies on the inactivation of the proteasome by lactacystin. A central role for clasto-lactacystin β-lactone
    • Dick L.R., Cruikshank A.A., Grenier L., Melandri F.D., Nunes S.L., and Stein R.L. Mechanistic studies on the inactivation of the proteasome by lactacystin. A central role for clasto-lactacystin β-lactone. J Biol Chem 271 (1996) 7273-7276
    • (1996) J Biol Chem , vol.271 , pp. 7273-7276
    • Dick, L.R.1    Cruikshank, A.A.2    Grenier, L.3    Melandri, F.D.4    Nunes, S.L.5    Stein, R.L.6
  • 47
    • 0036379624 scopus 로고    scopus 로고
    • Early clinical experience with the novel proteasome inhibitor PS-519
    • Shah I.M., Lees K.R., Pien C.P., and Elliott P.J. Early clinical experience with the novel proteasome inhibitor PS-519. Br J Clin Pharmacol 54 (2002) 269-276
    • (2002) Br J Clin Pharmacol , vol.54 , pp. 269-276
    • Shah, I.M.1    Lees, K.R.2    Pien, C.P.3    Elliott, P.J.4
  • 49
    • 33646137808 scopus 로고    scopus 로고
    • Crystal structure of Salinosporamide A (NPI-0052) and B (NPI-0047) in complex with the 20S proteasome reveal important consequences of a β-lactone ring opening and a mechanism for irreversible binding
    • Groll M., Huber R., and Potts B.C.M. Crystal structure of Salinosporamide A (NPI-0052) and B (NPI-0047) in complex with the 20S proteasome reveal important consequences of a β-lactone ring opening and a mechanism for irreversible binding. J Am Chem Soc 128 (2006) 5136-5141
    • (2006) J Am Chem Soc , vol.128 , pp. 5136-5141
    • Groll, M.1    Huber, R.2    Potts, B.C.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.