메뉴 건너뛰기




Volumn 28, Issue 8, 2000, Pages 1665-1675

The morph server: A standardized system for analyzing and visualizing macromolecular motions in a database framework

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOL DEHYDROGENASE; DIPHTHERIA TOXIN; DNA POLYMERASE; RECOVERIN;

EID: 0034655949     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (209)

References (64)
  • 2
    • 0000709475 scopus 로고
    • Acceleration of reactions by enzymes
    • Lipscomb, W.N. (1982) Acceleration of reactions by enzymes. Accounts Chem. Res., 15, 232.
    • (1982) Accounts Chem. Res. , vol.15 , pp. 232
    • Lipscomb, W.N.1
  • 3
    • 0029644728 scopus 로고
    • Movie of the structural changes during a catalytic cycle of nucleoside monophosphate kinases
    • Vonrhein, C., Schlauderer, G.J. and Schulz, G.E. (1995) Movie of the structural changes during a catalytic cycle of nucleoside monophosphate kinases. Structure, 3, 483-490.
    • (1995) Structure , vol.3 , pp. 483-490
    • Vonrhein, C.1    Schlauderer, G.J.2    Schulz, G.E.3
  • 4
    • 0345515997 scopus 로고    scopus 로고
    • The structure of a trimeric archaeal adenylate kinase
    • Vonrhein, C., Bonisch, H., Schafer, G. and Schulz, G.E. (1998) The structure of a trimeric archaeal adenylate kinase. J. Mol. Biol., 282, 167-179.
    • (1998) J. Mol. Biol. , vol.282 , pp. 167-179
    • Vonrhein, C.1    Bonisch, H.2    Schafer, G.3    Schulz, G.E.4
  • 5
    • 0030930760 scopus 로고    scopus 로고
    • Crystal structures of human DNA polymerase beta completed with gapped and nicked DNA: Evidence for an induced fit mechanism
    • Sawaya, M.R., Prasad, R., Wilson, S.H., Kraut, J. and Pelletier, H. (1997) Crystal structures of human DNA polymerase beta completed with gapped and nicked DNA: evidence for an induced fit mechanism. Biochemistry, 36, 11205-11215.
    • (1997) Biochemistry , vol.36 , pp. 11205-11215
    • Sawaya, M.R.1    Prasad, R.2    Wilson, S.H.3    Kraut, J.4    Pelletier, H.5
  • 6
    • 0028179616 scopus 로고
    • Open "back door" in a molecular dynamics simulation of acetylcholinesterase
    • Gilson, M.K., et al. (1994) Open "Back Door" in a Molecular Dynamics Simulation of Acetylcholinesterase. Science, 263, 1276-1278.
    • (1994) Science , vol.263 , pp. 1276-1278
    • Gilson, M.K.1
  • 7
    • 0029911582 scopus 로고    scopus 로고
    • Site-directed mutants designed to test back-door hypotheses of acetylcholinesterase function
    • Faerman, C., et al. (1996) Site-directed mutants designed to test back-door hypotheses of acetylcholinesterase function. FEBS Lett., 386, 65-71.
    • (1996) FEBS Lett. , vol.386 , pp. 65-71
    • Faerman, C.1
  • 8
    • 0027265211 scopus 로고
    • An electrostatic mechanism for substrate guidance down the aromatic gorge of acetylcholinesterase
    • Ripoll, D.R., Faerman, C.H., Axelsen, P.H., Silman, I. and Sussman, J.L. (1993) An electrostatic mechanism for substrate guidance down the aromatic gorge of acetylcholinesterase. Proc. Natl Acad. Sci. USA, 90, 5128-5132.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 5128-5132
    • Ripoll, D.R.1    Faerman, C.H.2    Axelsen, P.H.3    Silman, I.4    Sussman, J.L.5
  • 9
    • 0033529908 scopus 로고    scopus 로고
    • Molecular dynamics simulations of unfolding and refolding of a beta-hairpin fragment of protein G
    • Pande, V.S. and Rokhsar, D.S. (1999) Molecular dynamics simulations of unfolding and refolding of a beta-hairpin fragment of protein G [In Process Citation]. Proc. Natl Acad. Sci. USA, 96, 9062-9067.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 9062-9067
    • Pande, V.S.1    Rokhsar, D.S.2
  • 10
    • 0033574069 scopus 로고    scopus 로고
    • Folding pathway of a lattice model for proteins
    • Pande, V.S. and Rokhsar, D.S. (1999) Folding pathway of a lattice model for proteins. Proc. Natl Acad. Sci. USA, 96, 1273-1278.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 1273-1278
    • Pande, V.S.1    Rokhsar, D.S.2
  • 11
    • 0030870719 scopus 로고    scopus 로고
    • The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
    • Xu, Z., Horwich, A.L. and Sigler, P.B. (1997) The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature, 388, 741-750.
    • (1997) Nature , vol.388 , pp. 741-750
    • Xu, Z.1    Horwich, A.L.2    Sigler, P.B.3
  • 12
    • 0030804446 scopus 로고    scopus 로고
    • Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL
    • Rye, H., et al. (1997) Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL. Nature, 388, 792-798.
    • (1997) Nature , vol.388 , pp. 792-798
    • Rye, H.1
  • 13
    • 0032464019 scopus 로고    scopus 로고
    • GroEL/GroES: Structure and function of a two-stroke folding machine
    • Xu, Z. and Sigler, P.B. (1998) GroEL/GroES: structure and function of a two-stroke folding machine. J. Struct. Biol., 124, 129-141.
    • (1998) J. Struct. Biol. , vol.124 , pp. 129-141
    • Xu, Z.1    Sigler, P.B.2
  • 14
    • 0031684079 scopus 로고    scopus 로고
    • Structure and function in GroEL-mediated protein folding
    • Sigler, P.B., et al. (1998) Structure and function in GroEL-mediated protein folding. Annu. Rev. Biochem., 67, 581-608.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 581-608
    • Sigler, P.B.1
  • 15
    • 0032513152 scopus 로고    scopus 로고
    • Analysis of three human interleukin 5 structures suggests a possible receptor binding mechanism
    • Verschelde, J.L., et al. (1998) Analysis of three human interleukin 5 structures suggests a possible receptor binding mechanism. FEBS Lett., 424, 121-126.
    • (1998) FEBS Lett. , vol.424 , pp. 121-126
    • Verschelde, J.L.1
  • 16
    • 0033621166 scopus 로고    scopus 로고
    • Pathways for proton release during ubihydroquinone oxidation by the bc(l) complex
    • Crofts, A.R., et al. (1999) Pathways for proton release during ubihydroquinone oxidation by the bc(l) complex. Proc. Natl Acad. Sci. USA, 96, 10021-10026.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 10021-10026
    • Crofts, A.R.1
  • 17
    • 0032143551 scopus 로고    scopus 로고
    • Structure and function of the cytochrome bcl complex of mitochondria and photosynthetic bacteria
    • Crofts, A.R. and Berry, E.A. (1998) Structure and function of the cytochrome bcl complex of mitochondria and photosynthetic bacteria. Curr. Opin. Struct. Biol., 8, 501-509.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 501-509
    • Crofts, A.R.1    Berry, E.A.2
  • 18
    • 0033596853 scopus 로고    scopus 로고
    • Crystal structures of Escherichia coli glycerol kinase variant S58→W in complex with nonhydrolyzable ATP analogues reveal a putative active conformation of the enzyme as a result of domain motion
    • Bystrom, C.E., Pettigrew, D.W., Branchaud, B.P., O'Brien, P. and Remington, S.J. (1999) Crystal structures of Escherichia coli glycerol kinase variant S58→W in complex with nonhydrolyzable ATP analogues reveal a putative active conformation of the enzyme as a result of domain motion. Biochemistry, 38, 3508-3518.
    • (1999) Biochemistry , vol.38 , pp. 3508-3518
    • Bystrom, C.E.1    Pettigrew, D.W.2    Branchaud, B.P.3    O'Brien, P.4    Remington, S.J.5
  • 19
    • 0032533833 scopus 로고    scopus 로고
    • Glycerol kinase from Escherichia coli and an Ala65→Thr mutant: The crystal structures reveal conformational changes with implications for allosteric regulation
    • Feese, M.D., Faber, H.R., Bystrom, C.E., Pettigrew, D.W. and Remington, S.J. (1998) Glycerol kinase from Escherichia coli and an Ala65→Thr mutant: the crystal structures reveal conformational changes with implications for allosteric regulation. Structure, 6, 1407-1418.
    • (1998) Structure , vol.6 , pp. 1407-1418
    • Feese, M.D.1    Faber, H.R.2    Bystrom, C.E.3    Pettigrew, D.W.4    Remington, S.J.5
  • 20
    • 0026683015 scopus 로고
    • Aerosolized beclomethasone in chronic bronchitis. Improved pulmonary function and diminished airway inflammation
    • Thompson, A.B., et al. (1992) Aerosolized beclomethasone in chronic bronchitis. Improved pulmonary function and diminished airway inflammation. Am. Rev. Respir. Dis., 146, 389-395.
    • (1992) Am. Rev. Respir. Dis. , vol.146 , pp. 389-395
    • Thompson, A.B.1
  • 21
    • 0019946741 scopus 로고
    • Plasma lactoferrin levels in pregnancy and cystic fibrosis
    • Sykes, J.A., Thomas, M.J., Goldie, D.J. and Turner, G.M. (1982) Plasma lactoferrin levels in pregnancy and cystic fibrosis. Clin. Chim. Acta, 122, 385-393.
    • (1982) Clin. Chim. Acta , vol.122 , pp. 385-393
    • Sykes, J.A.1    Thomas, M.J.2    Goldie, D.J.3    Turner, G.M.4
  • 23
    • 0032190489 scopus 로고    scopus 로고
    • Screening a peptidyl database for potential ligands to proteins with side-chain flexibility
    • Schnecke, V., Swanson, C.A., Getzoff, E.D., Tainer, J.A. and Kuhn, L.A. (1998) Screening a peptidyl database for potential ligands to proteins with side-chain flexibility. Proteins, 33, 74-87.
    • (1998) Proteins , vol.33 , pp. 74-87
    • Schnecke, V.1    Swanson, C.A.2    Getzoff, E.D.3    Tainer, J.A.4    Kuhn, L.A.5
  • 24
    • 0032530836 scopus 로고    scopus 로고
    • A database of macromolecular movements
    • Gerstein, M. and Krebs, W. (1998) A Database of Macromolecular Movements. Nucleic Acids Res., 26, 4280.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 4280
    • Gerstein, M.1    Krebs, W.2
  • 25
    • 0000987560 scopus 로고    scopus 로고
    • Studying macromolecular motions in a database framework: From structure to sequence
    • Thorpe, M.F. and Duxbury, P.M. (eds), Kluwer Academic/Plenum Press, Norwell, MA, USA
    • Gerstein, M.B., Jansen, R., Johnson, T., Park, B. and Krebs, W. (1999) Studying Macromolecular Motions in a Database Framework: From Structure to Sequence. In Thorpe, M.F. and Duxbury, P.M. (eds), Rigidity Theory and Applications. Kluwer Academic/Plenum Press, Norwell, MA, USA. pp. 401-442.
    • (1999) Rigidity Theory and Applications , pp. 401-442
    • Gerstein, M.B.1    Jansen, R.2    Johnson, T.3    Park, B.4    Krebs, W.5
  • 26
    • 0031565915 scopus 로고
    • A structural census of genomes: Comparing bacterial, eukaryotic, and archaeal genomes in terms of protein structure
    • Gerstein, M. (1991) A Structural Census of Genomes: Comparing Bacterial, Eukaryotic, and Archaeal Genomes in terms of Protein Structure. J. Mol. Biol., 274, 562-576.
    • (1991) J. Mol. Biol. , vol.274 , pp. 562-576
    • Gerstein, M.1
  • 27
    • 0034677669 scopus 로고    scopus 로고
    • Assessing annotation transfer for genomics: Quantifying the relations between protein sequence, structure, and function through traditional and probabilistic scores
    • Wilson, C.A., Kreychman, J. and Gerstein, M. (2000) Assessing Annotation Transfer for Genomics: Quantifying the relations between protein sequence, structure, and function through traditional and probabilistic scores. J. Mol. Biol., 297, 233-249.
    • (2000) J. Mol. Biol. , vol.297 , pp. 233-249
    • Wilson, C.A.1    Kreychman, J.2    Gerstein, M.3
  • 28
    • 0031938039 scopus 로고    scopus 로고
    • Comprehensive assessment of automatic structural alignment against a manual standard, the scop classification of proteins
    • Gerstein., M. and Levitt, M. (1998) Comprehensive Assessment of Automatic Structural Alignment against a Manual Standard, the Scop Classification of Proteins. Protein Sci., 7, 445-456.
    • (1998) Protein Sci. , vol.7 , pp. 445-456
    • Gerstein, M.1    Levitt, M.2
  • 29
    • 0032568649 scopus 로고    scopus 로고
    • A unified statistical framework for sequence comparison and structure comparison
    • Levitt, M. and Gerstein, M. (1998) A Unified Statistical Framework for Sequence Comparison and Structure Comparison. (1998) Proc. Natl Acad. Sci. USA, 95, 5913-5920.
    • (1998) (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 5913-5920
    • Levitt, M.1    Gerstein, M.2
  • 30
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins for the investigation of sequences and structures
    • Murzin, A., Brenner, S.E., Hubbard, T. and Chothia, C. (1995) SCOP: A Structural Classification of Proteins for the Investigation of Sequences and Structures. J. Mol. Biol., 247, 536-540.
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 32
    • 0023518540 scopus 로고
    • A strategy for the rapid multiple alignment of protein sequences: Confidence levels from tertiary structure comparisons
    • Barton, G.J. and Sternberg, M.J.E. (1987) A strategy for the rapid multiple alignment of protein sequences: Confidence levels from tertiary structure comparisons. J. Mol. Biol., 198, 327-338.
    • (1987) J. Mol. Biol. , vol.198 , pp. 327-338
    • Barton, G.J.1    Sternberg, M.J.E.2
  • 33
    • 0025275917 scopus 로고
    • Flexible protein sequence patterns: A sensitive method to detect weak structural similarities
    • Barton, G.J. and Sternberg, M.J.E. (1990) Flexible protein sequence patterns: A sensitive method to detect weak structural similarities. J. Mol. Biol., 212, 389-402.
    • (1990) J. Mol. Biol. , vol.212 , pp. 389-402
    • Barton, G.J.1    Sternberg, M.J.E.2
  • 36
    • 0025777309 scopus 로고
    • Analysis of protein loop closure: Two types of hinges produce one motion in lactate dehydrogenase
    • Gerstein, M. and Chothia, C.H. (1991) Analysis of Protein Loop Closure: Two Types of Hinges Produce One Motion in Lactate Dehydrogenase. J. Mol. Biol., 220, 133-149.
    • (1991) J. Mol. Biol. , vol.220 , pp. 133-149
    • Gerstein, M.1    Chothia, C.H.2
  • 37
    • 0029091249 scopus 로고
    • Average core structures and variability measures for protein families: Application to the immunoglobulins
    • Gerstein, M. and Altman, R. (1995) Average core structures and variability measures for protein families: Application to the immunoglobulins. J. Mol. Biol., 251, 161-175.
    • (1995) J. Mol. Biol. , vol.251 , pp. 161-175
    • Gerstein, M.1    Altman, R.2
  • 38
    • 0021604916 scopus 로고
    • Mechanisms of domain closure in proteins
    • Lesk, A.M. and Chothia, C. (1984) Mechanisms of Domain Closure in Proteins. J. Mol. Biol., 174, 175-191.
    • (1984) J. Mol. Biol. , vol.174 , pp. 175-191
    • Lesk, A.M.1    Chothia, C.2
  • 39
    • 0028335096 scopus 로고
    • Structural mechanisms for protein motions
    • Gerstein, M. Lesk, A. and Chothia, C. (1994) Structural Mechanisms for Protein Motions. Biochemistry, 33, 6739-6749
    • (1994) Biochemistry , vol.33 , pp. 6739-6749
    • Gerstein, M.1    Lesk, A.2    Chothia, C.3
  • 40
    • 0030883755 scopus 로고    scopus 로고
    • Protein domain movements: Detection of rigid domains and visualization of hinges in comparisons of atomic coordinates
    • Wriggers, W. and Schulten, K. (1997) Protein domain movements: detection of rigid domains and visualization of hinges in comparisons of atomic coordinates. Proteins, 29, 1-14.
    • (1997) Proteins , vol.29 , pp. 1-14
    • Wriggers, W.1    Schulten, K.2
  • 41
    • 0030939896 scopus 로고    scopus 로고
    • A new method for modeling large-scale rearrangements of protein domains
    • Maiorov, V. and Abagyan, R. (1997) A new method for modeling large-scale rearrangements of protein domains. Proteins, 27, 410-424.
    • (1997) Proteins , vol.27 , pp. 410-424
    • Maiorov, V.1    Abagyan, R.2
  • 43
    • 0030014616 scopus 로고    scopus 로고
    • A dynamic look at structures: WWW-Entrez and the molecular modeling database
    • Hogue, C.W., Ohkawa, H. and Bryant, S.H. (1996) A dynamic look at structures: WWW-Entrez and the Molecular Modeling Database. Trends Biochem. Sci., 21, 226-229.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 226-229
    • Hogue, C.W.1    Ohkawa, H.2    Bryant, S.H.3
  • 44
    • 0029198903 scopus 로고
    • MMDB: An ASN.1 specification for macromolecular structure
    • Ohkawa, H., Ostell, J. and Bryant, S. (1995) MMDB: an ASN.1 specification for macromolecular structure. ISMB, 3, 259-267.
    • (1995) ISMB , vol.3 , pp. 259-267
    • Ohkawa, H.1    Ostell, J.2    Bryant, S.3
  • 45
    • 0029644940 scopus 로고
    • Where freedom is given, liberties are taken
    • Kleywegt, G.J. and Jones, T.A. (1995) Where freedom is given, liberties are taken. Structure, 3, 535-540.
    • (1995) Structure , vol.3 , pp. 535-540
    • Kleywegt, G.J.1    Jones, T.A.2
  • 46
    • 0030589514 scopus 로고    scopus 로고
    • Philpsi-chology: Ramachandran revisited
    • Kleywegt, G.J. and Jones, T.A. (1996) Philpsi-chology: Ramachandran revisited. Structure, 4, 1395-1400.
    • (1996) Structure , vol.4 , pp. 1395-1400
    • Kleywegt, G.J.1    Jones, T.A.2
  • 48
    • 0024528771 scopus 로고
    • Time-resolved macromolecular crystallography
    • Moffat, K. (1989) Time-resolved macromolecular crystallography. Annu. Rev. Biophys. Biophys. Chem., 18, 309-332.
    • (1989) Annu. Rev. Biophys. Biophys. Chem. , vol.18 , pp. 309-332
    • Moffat, K.1
  • 49
    • 0031039399 scopus 로고    scopus 로고
    • Structure of a protein photocycle intermediate by millisecond time-resolved crystallography
    • Genick, U.K., et al. (1997) Structure of a protein photocycle intermediate by millisecond time-resolved crystallography. Science, 275, 1471-1475.
    • (1997) Science , vol.275 , pp. 1471-1475
    • Genick, U.K.1
  • 50
    • 0342873608 scopus 로고    scopus 로고
    • Silicon-Graphics (1996) VRML 2 Specification. URL: http:// webspace.sgi.com/moving-worlds/Design.html
    • (1996) VRML 2 Specification
  • 51
    • 0343308702 scopus 로고
    • New Riders Indianapolis, IN
    • Pesce, M. (1995) VRML. New Riders Indianapolis, IN.
    • (1995) VRML
    • Pesce, M.1
  • 52
    • 0343744242 scopus 로고    scopus 로고
    • Introduction to acrobat reader
    • Adobe Corporation
    • Introduction to Acrobat Reader, in Description of Portable Document Format, Adobe Corporation: URL: http://www.adobe.com/ supportservice/custsupport/SOLUTIONS/ac76.htm
    • Description of Portable Document Format
  • 53
    • 0026244229 scopus 로고
    • MOLSCRIPT - A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991) MOLSCRIPT - A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr., 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 55
    • 84986512474 scopus 로고
    • CHARMM: A program for macromolecular energy, minimization, and dynamics calculations
    • Brooks, B.R., et al. (1983) CHARMM: A Program for Macromolecular Energy, Minimization, and Dynamics Calculations. J. Conip. Chem., 4. 187-217.
    • (1983) J. Conip. Chem. , vol.4 , pp. 187-217
    • Brooks, B.R.1
  • 56
    • 0023035967 scopus 로고
    • Interdomain motion in liver alcohol dehydrogenase: Structural and energetic analysis of the hinge bending mode
    • Colonna-Cesari, F., et al. (1986) Interdomain motion in liver alcohol dehydrogenase: structural and energetic analysis of the hinge bending mode. J. Biol. Chem., 261, 15273-15280.
    • (1986) J. Biol. Chem. , vol.261 , pp. 15273-15280
    • Colonna-Cesari, F.1
  • 57
    • 0019880506 scopus 로고
    • Structure of a triclinic ternary complex of horse liver alcohol dehydrogenase at 2.9 A resolution
    • Eklund, H., et al. (1981) Structure of a triclinic ternary complex of horse liver alcohol dehydrogenase at 2.9 A resolution. J. Mol. Biol., 146, 561-587.
    • (1981) J. Mol. Biol. , vol.146 , pp. 561-587
    • Eklund, H.1
  • 58
    • 0030848464 scopus 로고    scopus 로고
    • Molecular mechanics of calcium-myristoyl switches
    • Ames, J.B., et al. (1997) Molecular mechanics of calcium-myristoyl switches. Nature. 389, 198-202.
    • (1997) Nature. , vol.389 , pp. 198-202
    • Ames, J.B.1
  • 59
    • 0029135419 scopus 로고
    • Sequestration of the membrane-targeting myristoyl group of recoverin in the calcium-free state
    • Tanaka, T., Ames, J.B., Harvey, T.S., Stryer, L. and Ikura, M. (1995) Sequestration of the membrane-targeting myristoyl group of recoverin in the calcium-free state. Nature, 376, 444-447.
    • (1995) Nature , vol.376 , pp. 444-447
    • Tanaka, T.1    Ames, J.B.2    Harvey, T.S.3    Stryer, L.4    Ikura, M.5
  • 61
    • 0028136070 scopus 로고
    • Crystal structure of rat DNA polymerase beta: Evidence for a common polymerase mechanism
    • Sawaya, M.R., Pelletier, H., Kumar, A., Wilson, S.H. and Kraut, J. (1994) Crystal structure of rat DNA polymerase beta: evidence for a common polymerase mechanism. Science. 264, 1930-1935.
    • (1994) Science , vol.264 , pp. 1930-1935
    • Sawaya, M.R.1    Pelletier, H.2    Kumar, A.3    Wilson, S.H.4    Kraut, J.5
  • 62
    • 0021677578 scopus 로고
    • Large-amplitude bending motions in phenylalaine transfer RNA
    • Tung, C.S., Harvey, S.C. and McCammon, J.A. (1984) Large-amplitude bending motions in phenylalaine transfer RNA. Biopolymers, 23, 2173.
    • (1984) Biopolymers , vol.23 , pp. 2173
    • Tung, C.S.1    Harvey, S.C.2    McCammon, J.A.3
  • 63
    • 0028865843 scopus 로고
    • 3D domain swapping: A mechanism for oligomer assembly
    • Bennett, M.J., Schlunegger, M.P. and Eisenberg, D. (1995) 3D domain swapping: a mechanism for oligomer assembly. Protein Sci., 4, 2455-2468.
    • (1995) Protein Sci. , vol.4 , pp. 2455-2468
    • Bennett, M.J.1    Schlunegger, M.P.2    Eisenberg, D.3
  • 64
    • 0028204771 scopus 로고
    • Domain swapping: Entangling alliances between proteins
    • Bennett, M.J., Choe, S. and Eisenberg, D. (1994) Domain swapping: entangling alliances between proteins. Proc. NatlAcad. Sci. USA, 91, 3127-3131.
    • (1994) Proc. NatlAcad. Sci. USA , vol.91 , pp. 3127-3131
    • Bennett, M.J.1    Choe, S.2    Eisenberg, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.