메뉴 건너뛰기




Volumn 52, Issue 8, 2009, Pages 2420-2428

Binding epitopes and interaction structure of the neuroprotective protease inhibitor cystatin C with β-amyloid revealed by proteolytic excision mass spectrometry and molecular docking simulation

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[17-28]; CYSTATIN C; EPITOPE; NEUROPROTECTIVE AGENT; PROTEINASE INHIBITOR; UNCLASSIFIED DRUG;

EID: 65249086686     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm801115e     Document Type: Article
Times cited : (48)

References (43)
  • 1
    • 0021207461 scopus 로고
    • Alzheimer's disease and Down's syndrome: Sharing of a unique cerebrovascular amyloid fibril protein
    • Glenner, G. G.; Wong, C. W. Alzheimer's disease and Down's syndrome: sharing of a unique cerebrovascular amyloid fibril protein. Biochem. Biophys. Res. Commun. 1984, 122 , 1131-1135.
    • (1984) Biochem. Biophys. Res. Commun , vol.122 , pp. 1131-1135
    • Glenner, G.G.1    Wong, C.W.2
  • 2
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy, J.; Selkoe, D. J. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 2002, 297, 353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 3
    • 0023105114 scopus 로고
    • The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
    • Kang, J.; Lemaire, H. G.; Unterbeck, A.; Salbaum, J. M.; Masters, C. L. The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor. Nature 1987, 325, 733-736.
    • (1987) Nature , vol.325 , pp. 733-736
    • Kang, J.1    Lemaire, H.G.2    Unterbeck, A.3    Salbaum, J.M.4    Masters, C.L.5
  • 4
    • 0023109592 scopus 로고
    • Amyloid beta protein gene: CDNA, mRNA distribution, and genetic linkage near the Alzheimer locus
    • Tanzi, R. E.; Gusella, J. F.; Watkins, P. C.; Brans, G. A.; St George- Hyslop, P. Amyloid beta protein gene: cDNA, mRNA distribution, and genetic linkage near the Alzheimer locus. Science 1987, 235, 880- 884.
    • (1987) Science , vol.235 , pp. 880-884
    • Tanzi, R.E.1    Gusella, J.F.2    Watkins, P.C.3    Brans, G.A.4    St George- Hyslop, P.5
  • 6
    • 0345760069 scopus 로고    scopus 로고
    • Characterization of beta amyloid assemblies in drusen: The deposits associated with aging and age-related macular degeneration
    • Anderson, D. H.; Talaga, K. C.; Rivest, A. J.; Barron, E.; Hageman, G. S. Characterization of beta amyloid assemblies in drusen: the deposits associated with aging and age-related macular degeneration. Exp. Eye Res. 2004, 78 , 243-256.
    • (2004) Exp. Eye Res , vol.78 , pp. 243-256
    • Anderson, D.H.1    Talaga, K.C.2    Rivest, A.J.3    Barron, E.4    Hageman, G.S.5
  • 7
    • 0033835996 scopus 로고    scopus 로고
    • Peripherally administered antibodies against amyloid beta-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease
    • Bard, F.; Cannon, C.; Barbour, R.; Burke, R. L.; Games, D. Peripherally administered antibodies against amyloid beta-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease. Nat. Med. 2000, 6 , 916-919.
    • (2000) Nat. Med , vol.6 , pp. 916-919
    • Bard, F.1    Cannon, C.2    Barbour, R.3    Burke, R.L.4    Games, D.5
  • 8
    • 0033536163 scopus 로고    scopus 로고
    • Immunization with amyloid-beta attenuates Alzheimer-disease-like pathology in the PDAPP mouse
    • Schenk, D.; Barbour, R.; Dunn, W.; Gordon, G.; Grajeda, H. Immunization with amyloid-beta attenuates Alzheimer-disease-like pathology in the PDAPP mouse. Nature 1999, 400, 173-177.
    • (1999) Nature , vol.400 , pp. 173-177
    • Schenk, D.1    Barbour, R.2    Dunn, W.3    Gordon, G.4    Grajeda, H.5
  • 9
    • 0035902619 scopus 로고    scopus 로고
    • Peripheral anti-A beta antibody alters CNS and plasma A beta clearance and decreases brain A beta burden in a mouse model of Alzheimer's disease
    • DeMattos, R. B.; Bales, K. R.; Cummins, D. J.; Dodart, J. C.; Paul, S. M. Peripheral anti-A beta antibody alters CNS and plasma A beta clearance and decreases brain A beta burden in a mouse model of Alzheimer's disease. Proc. Natl. Acad. Sci. U. S. A. 2001, 98 , 8850- 8855.
    • (2001) Proc. Natl. Acad. Sci. U. S. A , vol.98 , pp. 8850-8855
    • DeMattos, R.B.1    Bales, K.R.2    Cummins, D.J.3    Dodart, J.C.4    Paul, S.M.5
  • 10
    • 0034700471 scopus 로고    scopus 로고
    • Janus, C.; Pearson, J.; McLaurin, J.; Mathews, P. M; Jiang, Y. A beta peptide immunization reduces behavioural impairment and plaques in a model of Alzheimer's disease. Nature 2000, 408, 979-982.
    • Janus, C.; Pearson, J.; McLaurin, J.; Mathews, P. M; Jiang, Y. A beta peptide immunization reduces behavioural impairment and plaques in a model of Alzheimer's disease. Nature 2000, 408, 979-982.
  • 11
    • 0038100154 scopus 로고    scopus 로고
    • Antibodies against beta-amyloid slow cognitive decline in Alzheimer's disease
    • Hock, C.; Konietzko, U.; Streffer, J. R.; Tracy, J.; Signorell, A. Antibodies against beta-amyloid slow cognitive decline in Alzheimer's disease. Neuron 2003, 38, 547-554.
    • (2003) Neuron , vol.38 , pp. 547-554
    • Hock, C.1    Konietzko, U.2    Streffer, J.R.3    Tracy, J.4    Signorell, A.5
  • 12
    • 0036852750 scopus 로고    scopus 로고
    • Therapeutically effective antibodies against amyloid-beta peptide target amyloid-beta residues 4-10 and inhibit cytotoxicity and fibriHogenesis
    • McLaurin, J.; Cecal, R.; Kierstead, M. E.; Tian, X.; Phinney, A. L. Therapeutically effective antibodies against amyloid-beta peptide target amyloid-beta residues 4-10 and inhibit cytotoxicity and fibriHogenesis. Nat. Med. 2002, 8 , 1263-1269.
    • (2002) Nat. Med , vol.8 , pp. 1263-1269
    • McLaurin, J.1    Cecal, R.2    Kierstead, M.E.3    Tian, X.4    Phinney, A.L.5
  • 13
    • 29144508651 scopus 로고    scopus 로고
    • Identification and structural characterisation of carboxy-terminal polypeptides and antibody epitopes of Alzheimer's amyloid precursor protein using high-resolution mass spectrometry
    • Tian, X.; Cecal, R.; McLaurin, J.; Manea, M.; Stefanescu, R. Identification and structural characterisation of carboxy-terminal polypeptides and antibody epitopes of Alzheimer's amyloid precursor protein using high-resolution mass spectrometry. Eur. J. Mass Spectrom. (Chichester. Engl.) 2005, 11 , 547-556.
    • (2005) Eur. J. Mass Spectrom. (Chichester. Engl.) , vol.11 , pp. 547-556
    • Tian, X.1    Cecal, R.2    McLaurin, J.3    Manea, M.4    Stefanescu, R.5
  • 14
    • 0035845614 scopus 로고    scopus 로고
    • Reduced levels of amyloid beta-peptide antibody in Alzheimer disease
    • Du, Y.; Dodel, R.; Hampel, H.; Buerger, K.; Lin, S. Reduced levels of amyloid beta-peptide antibody in Alzheimer disease. Neurology 2001, 57 , 801-805.
    • (2001) Neurology , vol.57 , pp. 801-805
    • Du, Y.1    Dodel, R.2    Hampel, H.3    Buerger, K.4    Lin, S.5
  • 15
    • 0041320819 scopus 로고    scopus 로고
    • Human antibeta-amyloid antibodies block beta-amyloid fibril formation and prevent beta-amyloid-induced neurotoxicity
    • Du, Y.; Wei, X.; Dodel, R.; Sommer, N.; Hampel, H. Human antibeta-amyloid antibodies block beta-amyloid fibril formation and prevent beta-amyloid-induced neurotoxicity. Brain 2003, 126, 1935- 1939.
    • (2003) Brain , vol.126 , pp. 1935-1939
    • Du, Y.1    Wei, X.2    Dodel, R.3    Sommer, N.4    Hampel, H.5
  • 16
    • 4644275963 scopus 로고    scopus 로고
    • Intravenous immunoglobulins containing antibodies against betaamyloid for the treatment of Alzheimer's disease
    • Dodel, R. C.; Du, Y.; Depboylu, C.; Hampel, H.; Frolich, L. Intravenous immunoglobulins containing antibodies against betaamyloid for the treatment of Alzheimer's disease. J. Neurol. Neurosurg. Psychiatry 2004, 75 , 1472-1474.
    • (2004) J. Neurol. Neurosurg. Psychiatry , vol.75 , pp. 1472-1474
    • Dodel, R.C.1    Du, Y.2    Depboylu, C.3    Hampel, H.4    Frolich, L.5
  • 17
  • 18
    • 65249090123 scopus 로고    scopus 로고
    • Przybylski, M, Stefanescu, R, Manea, M, Bacher, M, Dodel, R. Diagnosis and Treatment of Alzheimer's and Other Neurodementing Diseases. PCT Patent Appl. WO 2008/084402A2, July 17, 2008; University of Konstanz, University of Marburg
    • Przybylski, M.; Stefanescu, R.; Manea, M., ; Bacher, M.; Dodel, R. Diagnosis and Treatment of Alzheimer's and Other Neurodementing Diseases. PCT Patent Appl. WO 2008/084402A2, July 17, 2008; University of Konstanz, University of Marburg.
  • 19
    • 0035140013 scopus 로고    scopus 로고
    • Codeposition of cystatin C with amyloid-beta protein in the brain of Alzheimer disease patients
    • Levy, E.; Sastre, M.; Kumar, A.; Gallo, G.; Piccardo, P. Codeposition of cystatin C with amyloid-beta protein in the brain of Alzheimer disease patients. J. Neuropathol Exp. Neurol. 2001, 60 , 94-104.
    • (2001) J. Neuropathol Exp. Neurol , vol.60 , pp. 94-104
    • Levy, E.1    Sastre, M.2    Kumar, A.3    Gallo, G.4    Piccardo, P.5
  • 20
    • 33645003090 scopus 로고    scopus 로고
    • Checking the conformational stability of cystatin C and its L68Q variant by molecular dynamics studies: Why is the L68Q variant amyloidogenic?
    • Rodziewicz-Motowidlo, S.; Wahlbom, M.; Wang, X.; Lagiewka, J.; Janowski, R. Checking the conformational stability of cystatin C and its L68Q variant by molecular dynamics studies: why is the L68Q variant amyloidogenic? J. Struct. Biol. 2006, 154 , 68-78.
    • (2006) J. Struct. Biol , vol.154 , pp. 68-78
    • Rodziewicz-Motowidlo, S.1    Wahlbom, M.2    Wang, X.3    Lagiewka, J.4    Janowski, R.5
  • 21
    • 0035047801 scopus 로고    scopus 로고
    • Distinct properties of wild-type and the amyloidogenic human cystatin C variant of hereditary cerebral hemorrhage with amyloidosis, Icelandic type
    • Calero, M.; Pawlik, M.; Soto, C.; Castano, E. M.; Sigurdsson, E. M. Distinct properties of wild-type and the amyloidogenic human cystatin C variant of hereditary cerebral hemorrhage with amyloidosis, Icelandic type. J. Neurochem. 2001, 77 , 628-637.
    • (2001) J. Neurochem , vol.77 , pp. 628-637
    • Calero, M.1    Pawlik, M.2    Soto, C.3    Castano, E.M.4    Sigurdsson, E.M.5
  • 22
    • 33646576172 scopus 로고    scopus 로고
    • The role of cystatin C in cerebral amyloid angiopathy and stroke: Cell biology and animal models
    • Levy, E.; Jaskolski, M.; Grabb, A. The role of cystatin C in cerebral amyloid angiopathy and stroke: cell biology and animal models. Brain Pathol. 2006, 16 , 60-70.
    • (2006) Brain Pathol , vol.16 , pp. 60-70
    • Levy, E.1    Jaskolski, M.2    Grabb, A.3
  • 23
    • 33947133671 scopus 로고    scopus 로고
    • Selenica, M. L.; Wang, X.; Ostergaard-Pedersen, L.; Westlind- Danielsson, A.; Grabb, A. Cystatin C reduces the in vitro formation of soluble Abet al.-42 oligomers and protofibrils. Scand. J. Clin. Lab. Invest. 2007, 67 , 179-190.
    • Selenica, M. L.; Wang, X.; Ostergaard-Pedersen, L.; Westlind- Danielsson, A.; Grabb, A. Cystatin C reduces the in vitro formation of soluble Abet al.-42 oligomers and protofibrils. Scand. J. Clin. Lab. Invest. 2007, 67 , 179-190.
  • 24
    • 0038472441 scopus 로고    scopus 로고
    • Cystatin C colocalizes with amyloid-beta and coimmunoprecipitates with amyloidbeta precursor protein in sporadic inclusion-body myositis muscles
    • Vattemi, G.; Engel, W. K.; McFerrin, J.; Askanas, V. Cystatin C colocalizes with amyloid-beta and coimmunoprecipitates with amyloidbeta precursor protein in sporadic inclusion-body myositis muscles. J. Neurochem. 2003, 85 , 1539-1546.
    • (2003) J. Neurochem , vol.85 , pp. 1539-1546
    • Vattemi, G.1    Engel, W.K.2    McFerrin, J.3    Askanas, V.4
  • 25
    • 2942737051 scopus 로고    scopus 로고
    • Binding of cystatin C to Alzheimer's amyloid beta inhibits in vitro amyloid fibril formation
    • Sastre, M.; Calero, M.; Pawlik, M.; Mathews, P. M.; Kumar, A. Binding of cystatin C to Alzheimer's amyloid beta inhibits in vitro amyloid fibril formation. Neurobiol. Aging 2004, 25, 1033-1043.
    • (2004) Neurobiol. Aging , vol.25 , pp. 1033-1043
    • Sastre, M.1    Calero, M.2    Pawlik, M.3    Mathews, P.M.4    Kumar, A.5
  • 26
    • 0041358773 scopus 로고    scopus 로고
    • A panel of cerebrospinal fluid potential biomarkers for the diagnosis of Alzheimer's disease
    • Carrette, O.; Demalte, I.; Scherl, A.; Yalkinoglu, O.; Corthals, G. A panel of cerebrospinal fluid potential biomarkers for the diagnosis of Alzheimer's disease. Proteomic 2003, 3, 1486-1494.
    • (2003) Proteomic , vol.3 , pp. 1486-1494
    • Carrette, O.1    Demalte, I.2    Scherl, A.3    Yalkinoglu, O.4    Corthals, G.5
  • 27
    • 0035069135 scopus 로고    scopus 로고
    • Human cystatin C, an amyloidogenic protein, dimerizes through threedimensional domain swapping
    • Janowski, R.; Kozak, M.; Jankowska, E.; Grzonka, Z.; Grabb, A. Human cystatin C, an amyloidogenic protein, dimerizes through threedimensional domain swapping. Nat. Struct. Biol. 2001, 8 , 316-320.
    • (2001) Nat. Struct. Biol , vol.8 , pp. 316-320
    • Janowski, R.1    Kozak, M.2    Jankowska, E.3    Grzonka, Z.4    Grabb, A.5
  • 28
    • 16844381477 scopus 로고    scopus 로고
    • Mares, J.; Stejskal, D.; Vavrouskova, J.; Urbanek, K.; Herzig, R. Use of cystatin C determination in clinical diagnostics. Biomed. Pap. Med. Fac. Univ. Palacky Olomouc Czech. Repub. 2003, 147 , 177-180.
    • Mares, J.; Stejskal, D.; Vavrouskova, J.; Urbanek, K.; Herzig, R. Use of cystatin C determination in clinical diagnostics. Biomed. Pap. Med. Fac. Univ. Palacky Olomouc Czech. Repub. 2003, 147 , 177-180.
  • 29
    • 0035757051 scopus 로고    scopus 로고
    • 3D domain swapping, protein oligomerization, and amyloid formation
    • Jaskolski, M. 3D domain swapping, protein oligomerization, and amyloid formation. Acta Biochim. Pol. 2001, 48 , 807-827.
    • (2001) Acta Biochim. Pol , vol.48 , pp. 807-827
    • Jaskolski, M.1
  • 30
    • 0033790878 scopus 로고    scopus 로고
    • Molecular structure of a fibrillar Alzheimer's A beta fragment
    • Serpell, L. C.; Blake, C. C.; Fraser, P. E. Molecular structure of a fibrillar Alzheimer's A beta fragment. Biochemistry 2000, 39, 13269- 13275.
    • (2000) Biochemistry , vol.39 , pp. 13269-13275
    • Serpell, L.C.1    Blake, C.C.2    Fraser, P.E.3
  • 31
    • 0037465708 scopus 로고    scopus 로고
    • Insights into the amyloid folding problem from solid-state NMR
    • Tycko, R. Insights into the amyloid folding problem from solid-state NMR. Biochemistry 2003, 42, 3151-3159.
    • (2003) Biochemistry , vol.42 , pp. 3151-3159
    • Tycko, R.1
  • 32
    • 0037168655 scopus 로고    scopus 로고
    • A structural model for Alzheimer's beta-amyloid fibrils based on experimental constraints from solid state NMR
    • Petkova, A. T.; Ishii, Y.; Balbach, J. J.; Antzutkin, O. N.; Leapman, R. D. A structural model for Alzheimer's beta-amyloid fibrils based on experimental constraints from solid state NMR. Proc. Natl. Acad. Sci. U. S. A. 2002, 99 , 16742-16747.
    • (2002) Proc. Natl. Acad. Sci. U. S. A , vol.99 , pp. 16742-16747
    • Petkova, A.T.1    Ishii, Y.2    Balbach, J.J.3    Antzutkin, O.N.4    Leapman, R.D.5
  • 33
    • 0028981219 scopus 로고
    • Structure-activity analyses of beta-amyloid peptides: Contributions of the beta 25-35 region to aggregation and neurotoxicity
    • Pike, C. J.; Walencewicz-Wasserman, A. J.; Kosmoski, J.; Cribbs, D. H.; Glabe, C. G. Structure-activity analyses of beta-amyloid peptides: contributions of the beta 25-35 region to aggregation and neurotoxicity. J. Neurochem. 1995, 64 , 253-265.
    • (1995) J. Neurochem , vol.64 , pp. 253-265
    • Pike, C.J.1    Walencewicz-Wasserman, A.J.2    Kosmoski, J.3    Cribbs, D.H.4    Glabe, C.G.5
  • 34
    • 0034282630 scopus 로고    scopus 로고
    • Substitutions at codon 22 of Alzheimer's abeta peptide induce diverse conformational changes and apoptotic effects in human cerebral endothelial cells
    • Miravalle, L.; Tokuda, T.; Chiarle, R.; Giaccone, G.; Bugiani, O. Substitutions at codon 22 of Alzheimer's abeta peptide induce diverse conformational changes and apoptotic effects in human cerebral endothelial cells. J. Biol. Chem. 2000, 275 , 27110-27116.
    • (2000) J. Biol. Chem , vol.275 , pp. 27110-27116
    • Miravalle, L.1    Tokuda, T.2    Chiarle, R.3    Giaccone, G.4    Bugiani, O.5
  • 35
    • 0037038813 scopus 로고    scopus 로고
    • Amyloidosis and Alzheimer's disease
    • Ghiso, J.; Frangione, B. Amyloidosis and Alzheimer's disease. Adv. Drus Delivery Rev. 2002, 54 , 1539-1551.
    • (2002) Adv. Drus Delivery Rev , vol.54 , pp. 1539-1551
    • Ghiso, J.1    Frangione, B.2
  • 36
    • 0029854533 scopus 로고    scopus 로고
    • Point substitution in the central hydrophobic cluster of a human betaamyloid congener disrupts peptide folding and abolishes plaque competence
    • Esler, W. P.; Stimson, E. R.; Ghilardi, J. R.; Lu, Y. A.; Felix, A. M. Point substitution in the central hydrophobic cluster of a human betaamyloid congener disrupts peptide folding and abolishes plaque competence. Biochemistry 1996, 35, 13914-13921.
    • (1996) Biochemistry , vol.35 , pp. 13914-13921
    • Esler, W.P.1    Stimson, E.R.2    Ghilardi, J.R.3    Lu, Y.A.4    Felix, A.M.5
  • 37
    • 34547111066 scopus 로고    scopus 로고
    • Fibrillogenic oligomers of human cystatin C are formed by propagated domain swapping
    • Wahlbom, M.; Wang, X.; Lindstrom, V.; Carlemalm, E.; Jaskolski, M. Fibrillogenic oligomers of human cystatin C are formed by propagated domain swapping. J. Biol. Chem. 2007, 282 , 18318- 18326.
    • (2007) J. Biol. Chem , vol.282 , pp. 18318-18326
    • Wahlbom, M.1    Wang, X.2    Lindstrom, V.3    Carlemalm, E.4    Jaskolski, M.5
  • 38
    • 43249100084 scopus 로고    scopus 로고
    • Alzheimer's treatment
    • a potential target for
    • Levy, E. Cystatin C: a potential target for Alzheimer's treatment. Expert Rev. Neurother. 2008, 8 , 687-689.
    • (2008) Expert Rev. Neurother , vol.8 , pp. 687-689
    • Levy, E.1    Cystatin, C.2
  • 39
    • 0024407065 scopus 로고
    • High-level expression of active human cystatin C in Escherichia coli
    • Dalboge, H.; Jensen, E. B.; Tottrup, H.; Grubb, A.; Abrahamson, M. High-level expression of active human cystatin C in Escherichia coli. Gene 1989, 79 , 325-332.
    • (1989) Gene , vol.79 , pp. 325-332
    • Dalboge, H.1    Jensen, E.B.2    Tottrup, H.3    Grubb, A.4    Abrahamson, M.5
  • 40
    • 0041859598 scopus 로고    scopus 로고
    • High resolution proteome analysis of cryoglobulins using Fourier transform-ion cyclotron resonance mass spectrometry
    • Damoc, E.; Youhnovski, N.; Crettaz, D.; Tissot, J. D.; Przybylski, M. High resolution proteome analysis of cryoglobulins using Fourier transform-ion cyclotron resonance mass spectrometry. Proteomics 2003, 3 , 1425-1433.
    • (2003) Proteomics , vol.3 , pp. 1425-1433
    • Damoc, E.1    Youhnovski, N.2    Crettaz, D.3    Tissot, J.D.4    Przybylski, M.5
  • 41
    • 3242877815 scopus 로고    scopus 로고
    • Comeau, S. R.; Gatchell, D. W.; Vajda, S.; Camacho, C. J. ClusPro: a fully automated algorithm for protein-protein docking. Nucleic Acids Res. 2004, 32 , W96-W99.
    • Comeau, S. R.; Gatchell, D. W.; Vajda, S.; Camacho, C. J. ClusPro: a fully automated algorithm for protein-protein docking. Nucleic Acids Res. 2004, 32 , W96-W99.
  • 42
    • 33747840389 scopus 로고    scopus 로고
    • GRAMM-X public Web server for protein-protein docking
    • Tovchigrechko, A.; Vakser, I. A. GRAMM-X public Web server for protein-protein docking. Nucleic Acids Res. 2006, 34 , W310-W314.
    • (2006) Nucleic Acids Res , vol.34
    • Tovchigrechko, A.1    Vakser, I.A.2
  • 43
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R.; Billeter, M.; Wuthrich, K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graphics 1996, 14 , 51-55, 29-32.
    • (1996) J. Mol. Graphics , vol.14 , Issue.51-55 , pp. 29-32
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.