메뉴 건너뛰기




Volumn 6, Issue 6, 1997, Pages 1179-1189

MultiCoil: A program for predicting two- and three-stranded coiled coils

Author keywords

Coiled coil; Protein folding; Statistical prediction

Indexed keywords

DNA BINDING PROTEIN; LEUCINE ZIPPER PROTEIN; PROTEIN;

EID: 0030987407     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560060606     Document Type: Article
Times cited : (657)

References (70)
  • 2
    • 0027231255 scopus 로고
    • Ionic interactions in the coiled-coil domain of laminin determine the specificity of chain assembly
    • Beck K, Dixon T, Engel J, Parry D. 1993. Ionic interactions in the coiled-coil domain of laminin determine the specificity of chain assembly. J Mol Biol 231:311-323.
    • (1993) J Mol Biol , vol.231 , pp. 311-323
    • Beck, K.1    Dixon, T.2    Engel, J.3    Parry, D.4
  • 3
    • 0029258846 scopus 로고
    • Algorithms for protein structural motif recognition
    • Berger B. 1995. Algorithms for protein structural motif recognition. J Comput Biol 2:125-138.
    • (1995) J Comput Biol , vol.2 , pp. 125-138
    • Berger, B.1
  • 6
    • 0028864614 scopus 로고
    • A trimeric subdomain of the simian immunodeficiency virus envelope glycoprotein
    • Blacklow S, Lu M, Kim PS. 1995. A trimeric subdomain of the simian immunodeficiency virus envelope glycoprotein. Biochemistry 34:14955.
    • (1995) Biochemistry , vol.34 , pp. 14955
    • Blacklow, S.1    Lu, M.2    Kim, P.S.3
  • 7
    • 0025234646 scopus 로고
    • Construction of validated, non-redundant composite protein sequence databases
    • Bleasby AJ, Wootton J. 1990. Construction of validated, non-redundant composite protein sequence databases. Protein Eng 3:153-159.
    • (1990) Protein Eng , vol.3 , pp. 153-159
    • Bleasby, A.J.1    Wootton, J.2
  • 8
    • 0023054737 scopus 로고
    • Complementary DNA sequence of lamprey fibrinogen beta chain
    • Bohonus V, Doolittle R, Pontes M, Strong D. 1986. Complementary DNA sequence of lamprey fibrinogen beta chain. Biochemistry 25:6512-6516.
    • (1986) Biochemistry , vol.25 , pp. 6512-6516
    • Bohonus, V.1    Doolittle, R.2    Pontes, M.3    Strong, D.4
  • 9
    • 0029957901 scopus 로고    scopus 로고
    • Heptad breaks in α-helical coiled coils: Stutters and stammers
    • Brown JH, Cohen C, Parry DAD. 1996. Heptad breaks in α-helical coiled coils: Stutters and stammers. Proteins Struct Funct Genet 26:134-145.
    • (1996) Proteins Struct Funct Genet , vol.26 , pp. 134-145
    • Brown, J.H.1    Cohen, C.2    Parry, D.A.D.3
  • 10
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • Bullough PA, Hughson FM, Skehel JJ, Wiley DC. 1994. Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 371:37-43.
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 11
    • 0027253445 scopus 로고
    • A spring-loaded mechanism for the conformational change of influenza hemagglutinin
    • Carr CM, Kim PS. 1993. A spring-loaded mechanism for the conformational change of influenza hemagglutinin. Cell 73:823-832.
    • (1993) Cell , vol.73 , pp. 823-832
    • Carr, C.M.1    Kim, P.S.2
  • 12
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan DC, Fass D, Berger JM, Kim PS. 1997. Core structure of gp41 from the HIV envelope glycoprotein. Cell 89:263-267.
    • (1997) Cell , vol.89 , pp. 263-267
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 13
    • 0021109426 scopus 로고
    • Characterization of complementary deoxyribonucleic acid coding for the gamma chain of human fibrinogen
    • Chung DW, Chan WY, Davie E. 1983a. Characterization of complementary deoxyribonucleic acid coding for the gamma chain of human fibrinogen. Biochemistry 22:3250-3256.
    • (1983) Biochemistry , vol.22 , pp. 3250-3256
    • Chung, D.W.1    Chan, W.Y.2    Davie, E.3
  • 14
    • 0021109413 scopus 로고
    • Characterization of complementary deoxyribonucleic acid and genomic deoxyribonucleic acid for the beta chain of human fibrinogen
    • Chung DW, Que B, Rixon MW, Mace M Jr, Davie E. 1983b. Characterization of complementary deoxyribonucleic acid and genomic deoxyribonucleic acid for the beta chain of human fibrinogen. Biochemistry 22:3244-3250.
    • (1983) Biochemistry , vol.22 , pp. 3244-3250
    • Chung, D.W.1    Que, B.2    Rixon, M.W.3    Mace Jr., M.4    Davie, E.5
  • 15
    • 0019430043 scopus 로고
    • Characterization of a cDNA clone coding for the beta chain of bovine fibrinogen
    • Chung DW, Rixon M, MacGillivvray R, Daie E. 1981. Characterization of a cDNA clone coding for the beta chain of bovine fibrinogen. Proc Natl Acad Sci USA 78:1466-1470.
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 1466-1470
    • Chung, D.W.1    Rixon, M.2    MacGillivvray, R.3    Daie, E.4
  • 16
    • 0025272940 scopus 로고
    • α-Helical coiled coils and bundles: How to design an α-helical protein
    • Cohen C, Parry DAD. 1990. α-Helical coiled coils and bundles: How to design an α-helical protein. Proteins Struct Fund Genet 7:1-15.
    • (1990) Proteins Struct Fund Genet , vol.7 , pp. 1-15
    • Cohen, C.1    Parry, D.A.D.2
  • 17
    • 33749357063 scopus 로고
    • Intermediate filament structure: 3. Analysis of sequence homologies
    • Conway JF, Parry DAD. 1988. Intermediate filament structure: 3. Analysis of sequence homologies. Int J Biol Macromol 10:79-98.
    • (1988) Int J Biol Macromol , vol.10 , pp. 79-98
    • Conway, J.F.1    Parry, D.A.D.2
  • 18
    • 0026028894 scopus 로고
    • Three-stranded α-fibrous proteins: The heptad repeat and its implications for structure
    • Conway JF, Parry DA. 1991. Three-stranded α-fibrous proteins: The heptad repeat and its implications for structure. Int J Biol Macromol 13:14-16.
    • (1991) Int J Biol Macromol , vol.13 , pp. 14-16
    • Conway, J.F.1    Parry, D.A.2
  • 20
    • 0020426116 scopus 로고
    • Organization of the rat gamma-fibrinogen gene
    • Crabtree GR, Kant JA. 1982. Organization of the rat gamma-fibrinogen gene. Cell 31:159-166.
    • (1982) Cell , vol.31 , pp. 159-166
    • Crabtree, G.R.1    Kant, J.A.2
  • 22
    • 0026442649 scopus 로고
    • Laminins and other strange proteins
    • Engel J. 1992. Laminins and other strange proteins. Biochemistry 37:10645-10651.
    • (1992) Biochemistry , vol.37 , pp. 10645-10651
    • Engel, J.1
  • 23
    • 0029914299 scopus 로고    scopus 로고
    • Retrovirus envelope domain at 1.7 Å resolution
    • Fass D, Harrison SC, Kim PS. 1996. Retrovirus envelope domain at 1.7 Å resolution. Nature Struct Biol 3:465-469.
    • (1996) Nature Struct Biol , vol.3 , pp. 465-469
    • Fass, D.1    Harrison, S.C.2    Kim, P.S.3
  • 24
    • 0027491528 scopus 로고
    • Refined crystal structure of the seryl-tma synthetase from Thermus thermophitus at 2.5 Å
    • Funjinaga M, Berthet-Colominas C, Yaremchuk AD, Tukalo MA, Cusack S. 1993. Refined crystal structure of the seryl-tma synthetase from Thermus thermophitus at 2.5 Å. J Mol Biol 204:222-233.
    • (1993) J Mol Biol , vol.204 , pp. 222-233
    • Funjinaga, M.1    Berthet-Colominas, C.2    Yaremchuk, A.D.3    Tukalo, M.A.4    Cusack, S.5
  • 25
    • 0342891805 scopus 로고
    • Genetics Computer Group, 575 Science Drive, Madison, Wisconsin 53711, USA
    • Genetics Computer Group. 1994. PILEUP: Program Manual for the Wisconsin Package, August 1994. Genetics Computer Group, 575 Science Drive, Madison, Wisconsin 53711, USA.
    • (1994) PILEUP: Program Manual for the Wisconsin Package, August 1994
  • 26
    • 0028310422 scopus 로고
    • The complete primary structure for a novel laminin chain, the laminin b1k chain
    • Gerecke DR, Wagman DW, Champliaud M, Burgeson R. 1994. The complete primary structure for a novel laminin chain, the laminin b1k chain. J Biol Chem 269:11073-11080.
    • (1994) J Biol Chem , vol.269 , pp. 11073-11080
    • Gerecke, D.R.1    Wagman, D.W.2    Champliaud, M.3    Burgeson, R.4
  • 27
    • 0027934571 scopus 로고
    • Crystal structure of an isoleucine-zipper trimer
    • Harhury PB, Kim PS, Alber T. 1994. Crystal structure of an isoleucine-zipper trimer. Nature 371:80-83.
    • (1994) Nature , vol.371 , pp. 80-83
    • Harhury, P.B.1    Kim, P.S.2    Alber, T.3
  • 28
    • 0029091449 scopus 로고
    • Repacking protein cores with backbone freedom: Structure prediction for coiled coils
    • Harbury PB, Tidor B, Kim PS. 1995. Repacking protein cores with backbone freedom: Structure prediction for coiled coils. Biochemistry 92:8408-8412.
    • (1995) Biochemistry , vol.92 , pp. 8408-8412
    • Harbury, P.B.1    Tidor, B.2    Kim, P.S.3
  • 29
    • 0027756896 scopus 로고
    • A switch between two-, three-, and four-stranded coiled coils in gcn4 leucine zipper mutants
    • Harbury PB, Zhang T, Kim PS, Alber T. 1993. A switch between two-, three-, and four-stranded coiled coils in gcn4 leucine zipper mutants. Science 262:1401-1406.
    • (1993) Science , vol.262 , pp. 1401-1406
    • Harbury, P.B.1    Zhang, T.2    Kim, P.S.3    Alber, T.4
  • 30
  • 31
    • 0024535958 scopus 로고
    • A laminin-like adhesive protein concentrated in the synaptic cleft of the neuromuscular junction
    • Hunter DD, Shah V, Merlie J, Sanes J. 1989. A laminin-like adhesive protein concentrated in the synaptic cleft of the neuromuscular junction. Nature 335:229-234.
    • (1989) Nature , vol.335 , pp. 229-234
    • Hunter, D.D.1    Shah, V.2    Merlie, J.3    Sanes, J.4
  • 32
    • 0026779450 scopus 로고
    • Laminin chain assembly by triple and double stranded coiled-coil structures
    • Hunter I, Schulthess T, Engel J. 1992. Laminin chain assembly by triple and double stranded coiled-coil structures. J Biol Chem 267:6006-6011.
    • (1992) J Biol Chem , vol.267 , pp. 6006-6011
    • Hunter, I.1    Schulthess, T.2    Engel, J.3
  • 33
    • 0028678794 scopus 로고
    • Bzip proteins
    • Hurst HC. 1994. bzip proteins. Protein Profile 1:123-168.
    • (1994) Protein Profile , vol.1 , pp. 123-168
    • Hurst, H.C.1
  • 36
    • 0343326827 scopus 로고
    • Structure of a cytotoxic t-lymphocyte-specific gene shows a strong homology to fibrinogen beta and gamma chains
    • Koyama T, Hall L, Haser W, Tonegawa S, Saito H. 1987. Structure of a cytotoxic t-lymphocyte-specific gene shows a strong homology to fibrinogen beta and gamma chains. Proc Natl Acad Sci USA 85:1609-1613.
    • (1987) Proc Natl Acad Sci USA , vol.85 , pp. 1609-1613
    • Koyama, T.1    Hall, L.2    Haser, W.3    Tonegawa, S.4    Saito, H.5
  • 37
    • 0024518919 scopus 로고
    • Leucine repeats and an adjacent DNA binding domain mediate the formation of functional cfos-cjun heterodimers
    • Landshulz W, Johnson P, McKnight S. 1989. Leucine repeats and an adjacent DNA binding domain mediate the formation of functional cfos-cjun heterodimers. Science 243:1681-1688.
    • (1989) Science , vol.243 , pp. 1681-1688
    • Landshulz, W.1    Johnson, P.2    McKnight, S.3
  • 38
    • 0021719074 scopus 로고
    • Synthesis of a model protein of defined secondary and quaternary structure. Effect of chain length on the stabilization and formation of two-stranded alpha-helical coiled-coils
    • Lau SYM, Taneja AK, Hodges RS. 1984. Synthesis of a model protein of defined secondary and quaternary structure. Effect of chain length on the stabilization and formation of two-stranded alpha-helical coiled-coils. J Biol Chem 259:13253-13261.
    • (1984) J Biol Chem , vol.259 , pp. 13253-13261
    • Lau, S.Y.M.1    Taneja, A.K.2    Hodges, R.S.3
  • 39
    • 0028834461 scopus 로고
    • A trimeric structural domain of the HIV-1 transmembrane glycoprotein
    • Lu M, Blacklow S, Kim PS. 1995. A trimeric structural domain of the HIV-1 transmembrane glycoprotein. Nature Struct Biol 2:1075-1082.
    • (1995) Nature Struct Biol , vol.2 , pp. 1075-1082
    • Lu, M.1    Blacklow, S.2    Kim, P.S.3
  • 40
    • 0028306360 scopus 로고
    • Subdomain folding of the coiled coil leucine zipper from the bzip transcriptional activator gcn4
    • Lumb KJ, Carr CM, Kim PS. 1994. Subdomain folding of the coiled coil leucine zipper from the bzip transcriptional activator gcn4. Biochemistry 33:7361-7367.
    • (1994) Biochemistry , vol.33 , pp. 7361-7367
    • Lumb, K.J.1    Carr, C.M.2    Kim, P.S.3
  • 41
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas A, van Dyke M, Stock J. 1991. Predicting coiled coils from protein sequences. Science 252:1162-1164.
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 42
    • 0029911261 scopus 로고    scopus 로고
    • The crystal structure of a five-stranded coiled coil in COMP: A prototype ion channel?
    • Malashkevich VN, Kammerer RA, Efimov VP, Schulthess T, Engel J. 1996. The crystal structure of a five-stranded coiled coil in COMP: A prototype ion channel? Science 274:761-764.
    • (1996) Science , vol.274 , pp. 761-764
    • Malashkevich, V.N.1    Kammerer, R.A.2    Efimov, V.P.3    Schulthess, T.4    Engel, J.5
  • 43
    • 0024279859 scopus 로고
    • Drosophila substrate adhesion molecule: Sequence of laminin b1 chain
    • Montell DJ, Goodman CS. 1988. Drosophila substrate adhesion molecule: Sequence of laminin b1 chain. Cell 53:463-473.
    • (1988) Cell , vol.53 , pp. 463-473
    • Montell, D.J.1    Goodman, C.S.2
  • 44
    • 0024432466 scopus 로고
    • Drosophila laminin: Sequence of b2 subunit
    • Montell DJ, Goodman CS. 1989. Drosophila laminin: Sequence of b2 subunit. J Cell Biol 109:2441-2453.
    • (1989) J Cell Biol , vol.109 , pp. 2441-2453
    • Montell, D.J.1    Goodman, C.S.2
  • 45
    • 0028608066 scopus 로고
    • Redesigning the hydrohobic core of a four-helix-bundle protein
    • Munson M, O'Brien R, Sturtevant JM, Regan L. 1994. Redesigning the hydrohobic core of a four-helix-bundle protein. Protein Sci 3:2015-2022.
    • (1994) Protein Sci , vol.3 , pp. 2015-2022
    • Munson, M.1    O'Brien, R.2    Sturtevant, J.M.3    Regan, L.4
  • 47
    • 0031028937 scopus 로고    scopus 로고
    • Protein dissection of the antiparallel coiled coil from E. coli seryl tRNA synthetase
    • Forthcoming
    • Oakley MG, Kim PS. 1997. Protein dissection of the antiparallel coiled coil from E. coli seryl tRNA synthetase. Biochemistry. Forthcoming.
    • (1997) Biochemistry
    • Oakley, M.G.1    Kim, P.S.2
  • 48
    • 0026331267 scopus 로고
    • X-ray structure of the gcn4 leucine zipper, a two-stranded, parallel coiled coil
    • O'Shea EK, Klemm JD, Kim PS, Alber T. 1991. X-ray structure of the gcn4 leucine zipper, a two-stranded, parallel coiled coil. Science 254:539-544.
    • (1991) Science , vol.254 , pp. 539-544
    • O'Shea, E.K.1    Klemm, J.D.2    Kim, P.S.3    Alber, T.4
  • 49
    • 0024534241 scopus 로고
    • Evidence that the leucine zipper is a coiled coil
    • O'Shea EK, Rutkowski R, Kim PS. 1989. Evidence that the leucine zipper is a coiled coil. Science 243:538-542.
    • (1989) Science , vol.243 , pp. 538-542
    • O'Shea, E.K.1    Rutkowski, R.2    Kim, P.S.3
  • 50
    • 0026507982 scopus 로고
    • cDNA sequence for a second fibrinogen alpha chain in lamprey
    • Pan Y, Dooliltle RF. 1992. cDNA sequence for a second fibrinogen alpha chain in lamprey. Proc Natl Acad Sci USA 89:2066-2070.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 2066-2070
    • Pan, Y.1    Dooliltle, R.F.2
  • 51
    • 0020446736 scopus 로고
    • Coiled-coils in alpha-helix-containing proteins: Analysis of the residue types within the heptad repeat and the use of these data in the prediction of coiled-coils in other proteins
    • Parry D. 1982. Coiled-coils in alpha-helix-containing proteins: Analysis of the residue types within the heptad repeat and the use of these data in the prediction of coiled-coils in other proteins. Biosci Rep (England) 2:1017-1024.
    • (1982) Biosci Rep (England) , vol.2 , pp. 1017-1024
    • Parry, D.1
  • 52
    • 0029863942 scopus 로고    scopus 로고
    • The spectrin repeat folds into a three-helix bundle in solution
    • Pascual J, Pfuhl M, Rivas G, Pastore A, Saraste M. 1996. The spectrin repeat folds into a three-helix bundle in solution. FEBS Lett 353:201-207.
    • (1996) FEBS Lett , vol.353 , pp. 201-207
    • Pascual, J.1    Pfuhl, M.2    Rivas, G.3    Pastore, A.4    Saraste, M.5
  • 53
    • 0025344229 scopus 로고
    • Estrogen regulation of Xenopus laevis gamma-fibrinogen gene expression
    • Pastori RL, Moskaitis J, Smith LH Jr, Shoenberg D. 1990. Estrogen regulation of Xenopus laevis gamma-fibrinogen gene expression. Biochemistry 29:2599-2605.
    • (1990) Biochemistry , vol.29 , pp. 2599-2605
    • Pastori, R.L.1    Moskaitis, J.2    Smith Jr., L.H.3    Shoenberg, D.4
  • 54
    • 0026621935 scopus 로고
    • Trimerization of the heat shock transcription factor by a triple-stranded alpha-helical coiled-coil
    • Peteranderl R, Nelson HCM. 1992. Trimerization of the heat shock transcription factor by a triple-stranded alpha-helical coiled-coil. Biochemistry 31:12272-12276.
    • (1992) Biochemistry , vol.31 , pp. 12272-12276
    • Peteranderl, R.1    Nelson, H.C.M.2
  • 57
    • 0027221561 scopus 로고
    • S-laminin: Mapping to mouse chromosome 9 and expression in the linked mutants tippy and ducky
    • Porter BE, Justice M, Copeland N, Jenkins N, Hunter D, Merlie J, Sanes J. 1993. S-laminin: Mapping to mouse chromosome 9 and expression in the linked mutants tippy and ducky. Genomics 16:278-281.
    • (1993) Genomics , vol.16 , pp. 278-281
    • Porter, B.E.1    Justice, M.2    Copeland, N.3    Jenkins, N.4    Hunter, D.5    Merlie, J.6    Sanes, J.7
  • 58
    • 0027452754 scopus 로고
    • Regulation of heat shock factor trimer formation: Role of a conserved leucine zipper
    • Rabindran SK, Haroun RI, Clos J, Wisniewski J, Wu C. 1993. Regulation of heat shock factor trimer formation: Role of a conserved leucine zipper. Science 259:230-234.
    • (1993) Science , vol.259 , pp. 230-234
    • Rabindran, S.K.1    Haroun, R.I.2    Clos, J.3    Wisniewski, J.4    Wu, C.5
  • 59
    • 0021109431 scopus 로고
    • Characterization of complementary deoxyribonucleic acid coding for the alpha chain of human fibrinogen
    • Rixon MW, Chan WY, Davie E, Chung DW. 1983. Characterization of complementary deoxyribonucleic acid coding for the alpha chain of human fibrinogen. Biochemistry 22:3237-3244.
    • (1983) Biochemistry , vol.22 , pp. 3237-3244
    • Rixon, M.W.1    Chan, W.Y.2    Davie, E.3    Chung, D.W.4
  • 60
    • 0042383817 scopus 로고
    • Sequence of the cDNA encoding the laminin b1 chain reveals a multidomain protein containing cysteine-rich repeats
    • Sasaki M, Kato S, Kohno K, Martin G, Yamada Y. 1987. Sequence of the cDNA encoding the laminin b1 chain reveals a multidomain protein containing cysteine-rich repeats. Proc Natl Acad Sci USA 54:935-939.
    • (1987) Proc Natl Acad Sci USA , vol.54 , pp. 935-939
    • Sasaki, M.1    Kato, S.2    Kohno, K.3    Martin, G.4    Yamada, Y.5
  • 62
    • 0023657117 scopus 로고
    • The laminin b2 chain has a multidomain structure homologous to the b1 chain
    • Sasaki M, Yamada Y. 1987. The laminin b2 chain has a multidomain structure homologous to the b1 chain. J Biol Chem 262:17111-17117.
    • (1987) J Biol Chem , vol.262 , pp. 17111-17117
    • Sasaki, M.1    Yamada, Y.2
  • 63
    • 0024852809 scopus 로고
    • Trimerization of a yeast transcriptional activator via a coiled coil motif
    • Sorger PK, Nelson HCM. 1989. Trimerization of a yeast transcriptional activator via a coiled coil motif. Cell 59:807-813.
    • (1989) Cell , vol.59 , pp. 807-813
    • Sorger, P.K.1    Nelson, H.C.M.2
  • 67
    • 0025280399 scopus 로고
    • Bipartite mrna for chicken alpha-fibrinogen potentially encodes an amino acid sequence homologous to beta- and gama-fibrinogens
    • Weissbach L, Grieninger G. 1990. Bipartite mrna for chicken alpha-fibrinogen potentially encodes an amino acid sequence homologous to beta- and gama-fibrinogens. Proc Natl Acad Sci USA 87:5192-5202.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 5192-5202
    • Weissbach, L.1    Grieninger, G.2
  • 69
    • 0025860481 scopus 로고
    • Three-dimensional structure of the Id1 receptor-binding domain of human apolipoprotein e
    • Wilson C, Wardell MR, Weisgraber KH, Mahley RW, Agard DA. 1991. Three-dimensional structure of the Id1 receptor-binding domain of human apolipoprotein e. Science 252:1817-1822.
    • (1991) Science , vol.252 , pp. 1817-1822
    • Wilson, C.1    Wardell, M.R.2    Weisgraber, K.H.3    Mahley, R.W.4    Agard, D.A.5
  • 70
    • 0029083811 scopus 로고
    • Predicting oligomerization states of coiled coils
    • Woolfson DN, Alber T. 1995. Predicting oligomerization states of coiled coils. Protein Sci 4:1596-1607.
    • (1995) Protein Sci , vol.4 , pp. 1596-1607
    • Woolfson, D.N.1    Alber, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.