메뉴 건너뛰기




Volumn 15, Issue 2, 2009, Pages 58-66

The persisting challenge of selective and specific proteasome inhibition

Author keywords

Crystallographic analysis; Inhibitors; Polyvalency; Proteasome; Synthetic and natural products

Indexed keywords

ALDEHYDE DERIVATIVE; AMINO ACID DERIVATIVE; ARGYRIN A; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; BETA LACTONE DERIVATIVE; BIA 1A; BIA 2A; BORTEZOMIB; CALPASTATIN; EPOXOMICIN; FELLUTAMIDE B; GLIDOBACTIN A; HEPTAKIS [6 (SUCCINYLPHENYLALANINEAMIDE)AMIDO 6 DEOXY]BETA CYCLODEXTRIN; HOMOBELACTOSIN C; LACTACYSTIN BETA LACTONE; NATURAL PRODUCT; OCTAPEPTIDE; PR 171; PROTEASOME; PROTEASOME INHIBITOR; SALINOSPORAMIDE A; SYRBACTIN DERIVATIVE; SYRINGOLIN A; TMC 95; TMC 95A; TRIPEPTIDE DERIVATIVE; UNCLASSIFIED DRUG; VINYL SULFONE DERIVATIVE; BORONIC ACID DERIVATIVE; PROTEINASE INHIBITOR; PYRAZINE DERIVATIVE;

EID: 61449206184     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.1107     Document Type: Review
Times cited : (62)

References (65)
  • 2
    • 0346220392 scopus 로고    scopus 로고
    • Molecular shredders: How proteasomes fulfill their role
    • Groll M, Clausen T. Molecular shredders: how proteasomes fulfill their role. Curr. Opin. Struct. Biol. 2003; 13: 665-673.
    • (2003) Curr. Opin. Struct. Biol , vol.13 , pp. 665-673
    • Groll, M.1    Clausen, T.2
  • 4
    • 2342667387 scopus 로고    scopus 로고
    • The development of proteasome inhibitors as anticancer drugs
    • Adams J. The development of proteasome inhibitors as anticancer drugs. Cancer Cell 2004; 5: 417-421.
    • (2004) Cancer Cell , vol.5 , pp. 417-421
    • Adams, J.1
  • 5
    • 2342613652 scopus 로고    scopus 로고
    • The proteasome: A suitable antineoplastic target
    • Adams J. The proteasome: a suitable antineoplastic target. Nature Rev. Cancer 2004; 4: 349-360.
    • (2004) Nature Rev. Cancer , vol.4 , pp. 349-360
    • Adams, J.1
  • 7
    • 33847066706 scopus 로고    scopus 로고
    • Functions of the proteasome: From protein degradation and immune surveillance to cancer therapy
    • Goldberg AL. Functions of the proteasome: from protein degradation and immune surveillance to cancer therapy. Biochem. Soc. Trans. 2007; 35: 12-17.
    • (2007) Biochem. Soc. Trans , vol.35 , pp. 12-17
    • Goldberg, A.L.1
  • 9
    • 41549133200 scopus 로고    scopus 로고
    • Proteasome inhibitors in cancer therapy: Lessons from the first decade
    • Orlowski RZ, Kuhn DJ. Proteasome inhibitors in cancer therapy: lessons from the first decade. Clin. Cancer Res. 2008; 14: 1649-1657.
    • (2008) Clin. Cancer Res , vol.14 , pp. 1649-1657
    • Orlowski, R.Z.1    Kuhn, D.J.2
  • 10
    • 52649114697 scopus 로고    scopus 로고
    • Bortezomib-induced peripheral neuropathy in multiple myeloma: A comprehensive review of the literature
    • Argyriou AA, Iconomou G, Kalofonos HP. Bortezomib-induced peripheral neuropathy in multiple myeloma: a comprehensive review of the literature. Blood 2008; 112: 1593-1599.
    • (2008) Blood , vol.112 , pp. 1593-1599
    • Argyriou, A.A.1    Iconomou, G.2    Kalofonos, H.P.3
  • 11
    • 0025829436 scopus 로고
    • The 3-dimensional structure of proteasomes from Thermoplasma-Acidophilum as determined by electron-microscopy using random conical tilting
    • Hegerl R, Pfeifer G, Puhler G, Dahlmann B, Baumeister W. The 3-dimensional structure of proteasomes from Thermoplasma-Acidophilum as determined by electron-microscopy using random conical tilting. FEBS Lett. 1991; 283: 117-121.
    • (1991) FEBS Lett , vol.283 , pp. 117-121
    • Hegerl, R.1    Pfeifer, G.2    Puhler, G.3    Dahlmann, B.4    Baumeister, W.5
  • 12
    • 0029042511 scopus 로고    scopus 로고
    • L öwe J, Stock D, Jap R, Zwickl P, Baumeister W, Huber R. Crystal structure of the 20S proteasome from the archaeon T-Acidophilum at 3.4 Å resolution. Science 1995; 268: 533-539.
    • L öwe J, Stock D, Jap R, Zwickl P, Baumeister W, Huber R. Crystal structure of the 20S proteasome from the archaeon T-Acidophilum at 3.4 Å resolution. Science 1995; 268: 533-539.
  • 14
    • 33947659939 scopus 로고    scopus 로고
    • 20S proteasome and its inhibitors: Crystallographic knowledge for drug development
    • Borissenko L, Groll M. 20S proteasome and its inhibitors: crystallographic knowledge for drug development. Chem. Rev. 2007; 107: 687-717.
    • (2007) Chem. Rev , vol.107 , pp. 687-717
    • Borissenko, L.1    Groll, M.2
  • 16
    • 0033117370 scopus 로고    scopus 로고
    • Bifunctional inhibitors of the trypsin-like activity of eukaryotic proteasomes
    • Loidl G, Groll M, Musiol H-J, Ditzel L, Huber R, Moroder L. Bifunctional inhibitors of the trypsin-like activity of eukaryotic proteasomes. Chem. Biol. 1999; 6: 197-204.
    • (1999) Chem. Biol , vol.6 , pp. 197-204
    • Loidl, G.1    Groll, M.2    Musiol, H.-J.3    Ditzel, L.4    Huber, R.5    Moroder, L.6
  • 17
    • 0037436376 scopus 로고    scopus 로고
    • Investigations on the maturation and regulation of archaebacterial proteasomes
    • Groll M, Brandstetter H, Bartunik H, Bourenkow G, Huber R. Investigations on the maturation and regulation of archaebacterial proteasomes. J. Mol. Biol. 2003; 327: 75-83.
    • (2003) J. Mol. Biol , vol.327 , pp. 75-83
    • Groll, M.1    Brandstetter, H.2    Bartunik, H.3    Bourenkow, G.4    Huber, R.5
  • 19
    • 0040008534 scopus 로고    scopus 로고
    • Proteasome β-type subunits: Unequal roles of propeptides in core particle maturation and a hierarchy of active site function
    • Jager S, Groll M, Huber R, Wolf DH, Heinemeyer W. Proteasome β-type subunits: unequal roles of propeptides in core particle maturation and a hierarchy of active site function. J. Mol. Biol. 1999; 291: 997-1013.
    • (1999) J. Mol. Biol , vol.291 , pp. 997-1013
    • Jager, S.1    Groll, M.2    Huber, R.3    Wolf, D.H.4    Heinemeyer, W.5
  • 20
    • 0033613196 scopus 로고    scopus 로고
    • The catalytic sites of 20S proteasomes and their role in subunit maturation: A mutational and crystallographic study
    • Groll M, Heinemeyer W, Jager S, Ullrich T, Bochtler M, Wolf DH, Huber R. The catalytic sites of 20S proteasomes and their role in subunit maturation: a mutational and crystallographic study. Proc. Natl. Acad. Sci. U.S.A. 1999; 96: 10976-10983.
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 10976-10983
    • Groll, M.1    Heinemeyer, W.2    Jager, S.3    Ullrich, T.4    Bochtler, M.5    Wolf, D.H.6    Huber, R.7
  • 21
    • 0026786503 scopus 로고
    • Inhibition of the chymotrypsin-like activity of the pituitary multicatalytic proteinase complex
    • Vinitsky A, Michaud C, Powers JC, Orlowski M. Inhibition of the chymotrypsin-like activity of the pituitary multicatalytic proteinase complex. Biochemistry 1992; 31: 9421-9428.
    • (1992) Biochemistry , vol.31 , pp. 9421-9428
    • Vinitsky, A.1    Michaud, C.2    Powers, J.C.3    Orlowski, M.4
  • 22
    • 0025033039 scopus 로고
    • Cysteinyl proteinases and their selective inactivation
    • Shaw E. Cysteinyl proteinases and their selective inactivation. Adv. Enzymol. Relat. Areas Mol. Biol. 1990; 63: 271-347.
    • (1990) Adv. Enzymol. Relat. Areas Mol. Biol , vol.63 , pp. 271-347
    • Shaw, E.1
  • 23
    • 43149103265 scopus 로고    scopus 로고
    • Proteasome inhibition by fellutamide B induces nerve growth factor synthesis
    • Hines J, Groll M, Fahnestock M, Crews CM. Proteasome inhibition by fellutamide B induces nerve growth factor synthesis. Chem. Biol. 2008; 15: 501-512.
    • (2008) Chem. Biol , vol.15 , pp. 501-512
    • Hines, J.1    Groll, M.2    Fahnestock, M.3    Crews, C.M.4
  • 24
    • 0027980321 scopus 로고
    • The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-κB
    • Palombella VJ, Rando OJ, Goldberg AL, Maniatis T. The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-κB. Cell 1994; 78:773-785.
    • (1994) Cell , vol.78 , pp. 773-785
    • Palombella, V.J.1    Rando, O.J.2    Goldberg, A.L.3    Maniatis, T.4
  • 25
    • 0032103006 scopus 로고    scopus 로고
    • Substrate binding and sequence preference of the proteasome revealed by active-site directed affinity probes
    • Bogyo M, Shin S, McMaster JS, Ploegh HL. Substrate binding and sequence preference of the proteasome revealed by active-site directed affinity probes. Chem. Biol. 1998; 5: 307-320.
    • (1998) Chem. Biol , vol.5 , pp. 307-320
    • Bogyo, M.1    Shin, S.2    McMaster, J.S.3    Ploegh, H.L.4
  • 26
    • 0036015847 scopus 로고    scopus 로고
    • Probing structural determinants distal to the site of hydrolysis that control substrate specificity of the 20S proteasome
    • Groll M, Nazif T, Huber R, Bogyo M. Probing structural determinants distal to the site of hydrolysis that control substrate specificity of the 20S proteasome. Chem. Biol. 2002; 9: 655-662.
    • (2002) Chem. Biol , vol.9 , pp. 655-662
    • Groll, M.1    Nazif, T.2    Huber, R.3    Bogyo, M.4
  • 27
    • 0035853116 scopus 로고    scopus 로고
    • Global analysis of proteasomal substrate specificity using positional-scanning libraries of covalent inhibitors
    • Nazif T, Bogyo M. Global analysis of proteasomal substrate specificity using positional-scanning libraries of covalent inhibitors. Proc. Natl. Acad. Sci. U.S.A. 2001; 98: 2967-2972.
    • (2001) Proc. Natl. Acad. Sci. U.S.A , vol.98 , pp. 2967-2972
    • Nazif, T.1    Bogyo, M.2
  • 29
    • 33644845743 scopus 로고    scopus 로고
    • Crystal structure of the boronic acid-based proteasome inhibitor bortezomib in complex with the yeast 20S proteasome
    • Groll M, Berkers CR, Ploegh HL, Ovaa H. Crystal structure of the boronic acid-based proteasome inhibitor bortezomib in complex with the yeast 20S proteasome. Structure 2006; 14: 451-456.
    • (2006) Structure , vol.14 , pp. 451-456
    • Groll, M.1    Berkers, C.R.2    Ploegh, H.L.3    Ovaa, H.4
  • 30
    • 0029033981 scopus 로고
    • Inhibition of proteasome activities and subunit-specific aminoterminal threonine modification by lactacystin
    • Fenteany G, Standaert RF, Lane WS, Choi S, Corey EJ, Schreiber SL. Inhibition of proteasome activities and subunit-specific aminoterminal threonine modification by lactacystin. Science 1995; 268: 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
  • 31
    • 33646137808 scopus 로고    scopus 로고
    • Crystal structures of salinosporamide A (NPI-0052) and B (NPI-0047) in complex with the 20S proteasome reveal important consequences of β-lactone ring opening and a mechanism for irreversible binding
    • Groll M, Huber R, Potts BC. Crystal structures of salinosporamide A (NPI-0052) and B (NPI-0047) in complex with the 20S proteasome reveal important consequences of β-lactone ring opening and a mechanism for irreversible binding. J. Am. Chem. Soc. 2006; 128: 5136-5141.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 5136-5141
    • Groll, M.1    Huber, R.2    Potts, B.C.3
  • 32
    • 33645237455 scopus 로고    scopus 로고
    • Inhibitor-binding mode of homobelactosin C to proteasomes: New insights into class I MHC ligand generation
    • Groll M, Larionov OV, Huber R, de Meijere A. Inhibitor-binding mode of homobelactosin C to proteasomes: new insights into class I MHC ligand generation. Proc. Natl. Acad. Sci. U.S.A. 2006; 103: 4576-4579.
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 4576-4579
    • Groll, M.1    Larionov, O.V.2    Huber, R.3    de Meijere, A.4
  • 33
    • 0033621047 scopus 로고    scopus 로고
    • Meng LH, Mohan R, Kwok BHB, Elofsson M, Sin N, Crews CM. Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity. Proc. Natl. Acad. Sci. U.S.A. 1999; 96: 10403-10408.
    • Meng LH, Mohan R, Kwok BHB, Elofsson M, Sin N, Crews CM. Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity. Proc. Natl. Acad. Sci. U.S.A. 1999; 96: 10403-10408.
  • 34
    • 0343262654 scopus 로고    scopus 로고
    • Crystal structure of epoxomicin:20S proteasome reveals a molecular basis for selectivity of α′, β′-epoxyketone proteasome inhibitors
    • Groll M, Kim KB, Kairies N, Huber R, Crews CM. Crystal structure of epoxomicin:20S proteasome reveals a molecular basis for selectivity of α′, β′-epoxyketone proteasome inhibitors. J. Am. Chem. Soc. 2000; 122: 1237-1238.
    • (2000) J. Am. Chem. Soc , vol.122 , pp. 1237-1238
    • Groll, M.1    Kim, K.B.2    Kairies, N.3    Huber, R.4    Crews, C.M.5
  • 36
    • 9644262422 scopus 로고    scopus 로고
    • Inhibitors of the eukaryotic 20S proteasome core particle: A structural approach
    • Groll M, Huber R. Inhibitors of the eukaryotic 20S proteasome core particle: a structural approach. Biochim. Biophys. Acta 2004; 1695: 33-44.
    • (2004) Biochim. Biophys. Acta , vol.1695 , pp. 33-44
    • Groll, M.1    Huber, R.2
  • 37
    • 34547858920 scopus 로고    scopus 로고
    • Diversity of proteasomal missions: Fine tuning of the immune response
    • Borissenko L, Groll M. Diversity of proteasomal missions: fine tuning of the immune response. Biol. Chem. 2007; 388: 947-955.
    • (2007) Biol. Chem , vol.388 , pp. 947-955
    • Borissenko, L.1    Groll, M.2
  • 39
    • 0037455147 scopus 로고    scopus 로고
    • Feling RH, Buchanan GO, Mincer TJ, Kauffman CA, Jensen PR, Fenical W. Salinosporamide A: a highly cytotoxic proteasome inhibitor from a novel microbial source, a marine bacterium of the new genus Salinospora. Angew. Chem., Int. Ed. Engl. 2003; 42: 355-357.
    • Feling RH, Buchanan GO, Mincer TJ, Kauffman CA, Jensen PR, Fenical W. Salinosporamide A: a highly cytotoxic proteasome inhibitor from a novel microbial source, a marine bacterium of the new genus Salinospora. Angew. Chem., Int. Ed. Engl. 2003; 42: 355-357.
  • 40
    • 34948881265 scopus 로고    scopus 로고
    • Salinosporamide A (NPI-0052) potentiates apoptosis, suppresses osteoclastogenesis, and inhibits invasion through down-modulation of NF-κB-regulated gene products
    • Ahn KS, Sethi G, Chao TH, Neuteboom STC, Chaturvedi MM, Palladino MA, Younes A, Aggarwal BB. Salinosporamide A (NPI-0052) potentiates apoptosis, suppresses osteoclastogenesis, and inhibits invasion through down-modulation of NF-κB-regulated gene products. Blood 2007; 110: 2286-2295.
    • (2007) Blood , vol.110 , pp. 2286-2295
    • Ahn, K.S.1    Sethi, G.2    Chao, T.H.3    Neuteboom, S.T.C.4    Chaturvedi, M.M.5    Palladino, M.A.6    Younes, A.7    Aggarwal, B.B.8
  • 41
    • 34347375499 scopus 로고    scopus 로고
    • NPI-0052, a novel proteasome inhibitor, induces caspase-8 and ROS-dependent apoptosis alone and in combination with HDAC inhibitors in leukemia cells
    • Miller CP, Ban K, Dujka ME, McConkey DJ, Munsell M, Palladino M, Chandra J. NPI-0052, a novel proteasome inhibitor, induces caspase-8 and ROS-dependent apoptosis alone and in combination with HDAC inhibitors in leukemia cells. Blood 2007; 110: 267-277.
    • (2007) Blood , vol.110 , pp. 267-277
    • Miller, C.P.1    Ban, K.2    Dujka, M.E.3    McConkey, D.J.4    Munsell, M.5    Palladino, M.6    Chandra, J.7
  • 42
    • 0029564960 scopus 로고    scopus 로고
    • Imajoh-Ohmi S, Kawaguchi T, Sugiyama S, Tanaka K, Omura S, Kikuchi H. Lactacystin, a specific inhibitor of the proteasome, induces apoptosis in human monoblast U937 cells. Biochem. Biophys. Res. Commun. 1995; 217: 1070-1077.
    • Imajoh-Ohmi S, Kawaguchi T, Sugiyama S, Tanaka K, Omura S, Kikuchi H. Lactacystin, a specific inhibitor of the proteasome, induces apoptosis in human monoblast U937 cells. Biochem. Biophys. Res. Commun. 1995; 217: 1070-1077.
  • 44
    • 0035300479 scopus 로고    scopus 로고
    • The proteasome inhibitor PS-341 inhibits growth, induces apoptosis, and overcomes drug resistance in human multiple myeloma cells
    • Hideshima T, Richardson P, Chauhan D, Palombella VJ, Elliott PJ, Adams J, Anderson KC. The proteasome inhibitor PS-341 inhibits growth, induces apoptosis, and overcomes drug resistance in human multiple myeloma cells. Cancer Res. 2001; 61: 3071-3076.
    • (2001) Cancer Res , vol.61 , pp. 3071-3076
    • Hideshima, T.1    Richardson, P.2    Chauhan, D.3    Palombella, V.J.4    Elliott, P.J.5    Adams, J.6    Anderson, K.C.7
  • 45
    • 0034105791 scopus 로고    scopus 로고
    • TMC-95A, B, C, and D, novel proteasome inhibitors produced by Apiospora montagnei Sacc. TC 1093 - Taxonomy, production, isolation, and biological activities
    • Koguchi Y, Kohno J, Nishio M, Takahashi K, Okuda T, Ohnuki T, Komatsubara S. TMC-95A, B, C, and D, novel proteasome inhibitors produced by Apiospora montagnei Sacc. TC 1093 - Taxonomy, production, isolation, and biological activities. J. Antibiot. 2000; 53: 105-109.
    • (2000) J. Antibiot , vol.53 , pp. 105-109
    • Koguchi, Y.1    Kohno, J.2    Nishio, M.3    Takahashi, K.4    Okuda, T.5    Ohnuki, T.6    Komatsubara, S.7
  • 47
    • 0035902778 scopus 로고    scopus 로고
    • Crystal structure of the 20S proteasome/TMC-95A complex: A non-covalent proteasome inhibitor
    • Groll M, Koguchi Y, Huber R, Kohno J. Crystal structure of the 20S proteasome/TMC-95A complex: a non-covalent proteasome inhibitor. J. Mol. Biol. 2001; 311: 543-548.
    • (2001) J. Mol. Biol , vol.311 , pp. 543-548
    • Groll, M.1    Koguchi, Y.2    Huber, R.3    Kohno, J.4
  • 48
    • 33745187107 scopus 로고    scopus 로고
    • TMC-95-based inhibitor design provides evidence for the catalytic versatility of the proteasome
    • Groll M, Götz M, Kaiser M, Weyher E, Moroder L. TMC-95-based inhibitor design provides evidence for the catalytic versatility of the proteasome. Chem. Biol. 2006; 13: 607-614.
    • (2006) Chem. Biol , vol.13 , pp. 607-614
    • Groll, M.1    Götz, M.2    Kaiser, M.3    Weyher, E.4    Moroder, L.5
  • 49
    • 0036494798 scopus 로고    scopus 로고
    • The core structure of TMC-95A is a promising lead for reversible proteasome inhibition
    • Kaiser M, Groll M, Renner C, Huber R, Moroder L. The core structure of TMC-95A is a promising lead for reversible proteasome inhibition. Angew. Chem., Int. Ed. Engl. 2002; 41: 780-783.
    • (2002) Angew. Chem., Int. Ed. Engl , vol.41 , pp. 780-783
    • Kaiser, M.1    Groll, M.2    Renner, C.3    Huber, R.4    Moroder, L.5
  • 51
    • 0031055496 scopus 로고    scopus 로고
    • Novel cyclic biphenyl ether peptide β-strand mimetics and HIV-protease inhibitors
    • Janetka JW, Raman P, Satyshur K, Flentke GR, Rich DH. Novel cyclic biphenyl ether peptide β-strand mimetics and HIV-protease inhibitors. J. Am. Chem. Soc. 1997; 119: 441-442.
    • (1997) J. Am. Chem. Soc , vol.119 , pp. 441-442
    • Janetka, J.W.1    Raman, P.2    Satyshur, K.3    Flentke, G.R.4    Rich, D.H.5
  • 52
    • 0031627194 scopus 로고    scopus 로고
    • Protein secondary structure templates derived from bioactive natural products - Combinatorial chemistry meets structure-based design
    • Müller G, Giera H. Protein secondary structure templates derived from bioactive natural products - Combinatorial chemistry meets structure-based design. J. Comput.-Aided Mol. Des. 1998; 12: 1-6.
    • (1998) J. Comput.-Aided Mol. Des , vol.12 , pp. 1-6
    • Müller, G.1    Giera, H.2
  • 58
    • 0028985861 scopus 로고
    • Conformational constraints in protein degradation by the 20S proteasome
    • Wenzel T, Baumeister W. Conformational constraints in protein degradation by the 20S proteasome. Nat. Struct. Biol. 1995; 2: 199-204.
    • (1995) Nat. Struct. Biol , vol.2 , pp. 199-204
    • Wenzel, T.1    Baumeister, W.2
  • 59
    • 0032476812 scopus 로고    scopus 로고
    • Polyvalent interactions in biological systems: Implications for design and use of multivalent ligands and inhibitors
    • Mammen M, Choi SK, Whitesides GM. Polyvalent interactions in biological systems: implications for design and use of multivalent ligands and inhibitors. Angew. Chem., Int. Ed. Engl. 1998; 37: 2755-2794.
    • (1998) Angew. Chem., Int. Ed. Engl , vol.37 , pp. 2755-2794
    • Mammen, M.1    Choi, S.K.2    Whitesides, G.M.3
  • 60
    • 84860339139 scopus 로고    scopus 로고
    • Application of the principle of polyvalency to protease inhibition
    • Knäblein J ed, Wiley-VCH: Weinheim
    • Moroder L. Application of the principle of polyvalency to protease inhibition. In Modern Biopharmaceuticals - Design, Development and Optimization, Vol. 2, Knäblein J (ed.). Wiley-VCH: Weinheim, 2005; 395-417.
    • (2005) Modern Biopharmaceuticals - Design, Development and Optimization , vol.2 , pp. 395-417
    • Moroder, L.1
  • 62
    • 0000913277 scopus 로고    scopus 로고
    • Estimating the entropic cost of self-assembly of multiparticle hydrogen-bonded aggregates based on the cyanuric acid-melamine lattice
    • Mammen M, Shakhnovich EI, Deutch JM, Whitesides GM. Estimating the entropic cost of self-assembly of multiparticle hydrogen-bonded aggregates based on the cyanuric acid-melamine lattice. J. Org. Chem. 1998; 63: 3821-3830.
    • (1998) J. Org. Chem , vol.63 , pp. 3821-3830
    • Mammen, M.1    Shakhnovich, E.I.2    Deutch, J.M.3    Whitesides, G.M.4
  • 63
    • 0000598486 scopus 로고    scopus 로고
    • Using a convenient, quantitative model for torsional entropy to establish qualitative trends formolecular processes that restrict conformational freedom
    • Mammen M, Shakhnovich EI, Whitesides GM. Using a convenient, quantitative model for torsional entropy to establish qualitative trends formolecular processes that restrict conformational freedom. J. Org. Chem. 1998; 63: 3168-3175.
    • (1998) J. Org. Chem , vol.63 , pp. 3168-3175
    • Mammen, M.1    Shakhnovich, E.I.2    Whitesides, G.M.3
  • 64
    • 26944452043 scopus 로고    scopus 로고
    • PEGylation, successful approach for drug delivery
    • Veronese FM, Pasut G. PEGylation, successful approach for drug delivery. Drug Discov. Today 2005; 10: 1451-1458.
    • (2005) Drug Discov. Today , vol.10 , pp. 1451-1458
    • Veronese, F.M.1    Pasut, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.