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Volumn 4, Issue 12, 1996, Pages 1401-1412

The UmuD' protein filament and its potential role in damage induced mutagenesis

Author keywords

filament structure; mutagenesis; self cleavage reaction; SOS response; X ray crystallography

Indexed keywords

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0030589718     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(96)00148-7     Document Type: Article
Times cited : (37)

References (56)
  • 1
    • 0027482444 scopus 로고
    • Base selection, proof reading, and mismatch repair during DNA replication in Escherichia coli
    • Schaaper, R.M. (1993). Base selection, proof reading, and mismatch repair during DNA replication in Escherichia coli. J. Biol. Chem. 268, 23762-23765.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23762-23765
    • Schaaper, R.M.1
  • 3
    • 0026640077 scopus 로고
    • Mutagenesis induced by bacterial UmuDC proteins and their plasmid homologs
    • Woodgate, R., & Sedgwick, S.G. (1992). Mutagenesis induced by bacterial UmuDC proteins and their plasmid homologs. Mol. Microbiol. 6, 2213-2218.
    • (1992) Mol. Microbiol. , vol.6 , pp. 2213-2218
    • Woodgate, R.1    Sedgwick, S.G.2
  • 4
    • 0021879770 scopus 로고
    • Mutagenic repair in Escherichia coli: Products of the recA gene and of the umuD and umuC genes act at different steps in UV-mutagenesis
    • Bridges, B.A. & Woodgate, R. (1985). Mutagenic repair in Escherichia coli: products of the recA gene and of the umuD and umuC genes act at different steps in UV-mutagenesis. Proc. Natl. Acad. Sci. USA 82, 4193-4197.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 4193-4197
    • Bridges, B.A.1    Woodgate, R.2
  • 5
    • 0026443726 scopus 로고
    • Activity of the purified mutagenesis proteins UmuC, UmuD·, and RecA in replicative bypass of an abasic DNA lesion by DNA polymerase III
    • Rajagopalan, M., Lu, C., Woodgate, R., O'Donnell, M., Goodman, M.F. & Echols, H. (1992). Activity of the purified mutagenesis proteins UmuC, UmuD·, and RecA in replicative bypass of an abasic DNA lesion by DNA polymerase III. Proc. Natl. Acad. Sci. USA 89, 10777-10781.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10777-10781
    • Rajagopalan, M.1    Lu, C.2    Woodgate, R.3    O'Donnell, M.4    Goodman, M.F.5    Echols, H.6
  • 6
    • 0023189017 scopus 로고
    • DNA polymerase III of Escherichia coli is required for UV and ethyl methanesulfonate mutagenesis
    • Hagensee, M.E., Timme, T., Bryan, S.K. & Moses, R.E. (1987). DNA polymerase III of Escherichia coli is required for UV and ethyl methanesulfonate mutagenesis. Proc. Natl. Acad. Sci. USA 84, 4195-4199.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 4195-4199
    • Hagensee, M.E.1    Timme, T.2    Bryan, S.K.3    Moses, R.E.4
  • 7
    • 0024121565 scopus 로고
    • UmuD mutagenesis protein of Escherichia coli: Overproduction, purification, and cleavage by RecA
    • Burckhardt, S.E., Woodgate, R., Scheuermann, R.H. & Echols, H. (1988). UmuD mutagenesis protein of Escherichia coli: overproduction, purification, and cleavage by RecA. Proc. Natl. Acad. Sci. USA 85, 1811-1815.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 1811-1815
    • Burckhardt, S.E.1    Woodgate, R.2    Scheuermann, R.H.3    Echols, H.4
  • 8
    • 0024121518 scopus 로고
    • RecAmediated cleavage activates UmuD for mutagenesis: Mechanistic relationship between transcriptional derepression and posttranslational activation
    • Nohmi, T., Battista, J.R., Dodson, L.A. & Walker, G.C. (1988). RecAmediated cleavage activates UmuD for mutagenesis: mechanistic relationship between transcriptional derepression and posttranslational activation. Proc. Natl. Acad. Sci. USA 85, 1816-1820.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 1816-1820
    • Nohmi, T.1    Battista, J.R.2    Dodson, L.A.3    Walker, G.C.4
  • 9
    • 0024121627 scopus 로고
    • RecA protein-dependent cleavage of UmuD protein and SOS mutagenesis
    • Shinagawa, H., Iwasaki, H., Kato, T. & Nakata, A. (1988). RecA protein-dependent cleavage of UmuD protein and SOS mutagenesis. Proc. Natl. Acad. Sci. USA 85, 1806-1810.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 1806-1810
    • Shinagawa, H.1    Iwasaki, H.2    Kato, T.3    Nakata, A.4
  • 10
    • 0025043337 scopus 로고
    • Dominant negative umuD mutations decreasing RecA-mediated cleavage suggest roles for intact UmuD in modulation of SOS mutagenesis
    • Battista, J.R., Ohta, T., Nohmi, T., Sun, W. & Walker, G.C. (1990). Dominant negative umuD mutations decreasing RecA-mediated cleavage suggest roles for intact UmuD in modulation of SOS mutagenesis. Proc. Natl. Acad. Sci. USA 87, 7190-7194.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 7190-7194
    • Battista, J.R.1    Ohta, T.2    Nohmi, T.3    Sun, W.4    Walker, G.C.5
  • 11
    • 0343188817 scopus 로고
    • Autodigestion of LexA and phage λ repressors
    • Little, J.W. (1984). Autodigestion of LexA and phage λ repressors. Proc. Natl. Acad. Sci. USA 81, 1375-1379.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 1375-1379
    • Little, J.W.1
  • 12
    • 0023042845 scopus 로고
    • λ repressor inactivation: Properties of purified ind-proteins in the autodigestion and RecA-mediated cleavage reactions
    • Gimble, F.S. & Sauer, R.T. (1986). λ repressor inactivation: properties of purified ind-proteins in the autodigestion and RecA-mediated cleavage reactions. J. Mol. Biol. 192, 39-47.
    • (1986) J. Mol. Biol. , vol.192 , pp. 39-47
    • Gimble, F.S.1    Sauer, R.T.2
  • 13
    • 0023821287 scopus 로고
    • Cleavage of bacteriophage φ80 cl repressor by RecA protein
    • Eguchi, Y., Ogawa, T. & Ogawa, H. (1988). Cleavage of bacteriophage φ80 cl repressor by RecA protein. J. Mol. Biol. 202, 565-573.
    • (1988) J. Mol. Biol. , vol.202 , pp. 565-573
    • Eguchi, Y.1    Ogawa, T.2    Ogawa, H.3
  • 14
    • 0026699297 scopus 로고
    • The enhanced mutagenic potential of the MucAB proteins correlates with the highly efficient processing of the MucA protein
    • Hauser, J., Levine, A.S., Ennis, D.G., Chumakov, K.M. & Woodgate, R. (1992). The enhanced mutagenic potential of the MucAB proteins correlates with the highly efficient processing of the MucA protein. J. Bacteriol. 174, 6844-6851.
    • (1992) J. Bacteriol. , vol.174 , pp. 6844-6851
    • Hauser, J.1    Levine, A.S.2    Ennis, D.G.3    Chumakov, K.M.4    Woodgate, R.5
  • 15
    • 0027195935 scopus 로고
    • LexA and λ cl repressors as enzymes: Specific cleavage in an intermolecular reaction
    • Kim, B. & Little, J.W. (1993). LexA and λ cl repressors as enzymes: specific cleavage in an intermolecular reaction. Cell 73, 1165-1173.
    • (1993) Cell , vol.73 , pp. 1165-1173
    • Kim, B.1    Little, J.W.2
  • 17
    • 0025314791 scopus 로고
    • RecA protein of Escherichia coli has a third essential role in SOS mutator activity
    • Sweasy, J.B., Witkin, E.M., Sinha, N. & Roegner-Maniscalco, V. (1990). RecA protein of Escherichia coli has a third essential role in SOS mutator activity. J. Bacteriol. 172, 3030-3036.
    • (1990) J. Bacteriol. , vol.172 , pp. 3030-3036
    • Sweasy, J.B.1    Witkin, E.M.2    Sinha, N.3    Roegner-Maniscalco, V.4
  • 18
    • 0025909497 scopus 로고
    • A RecA protein mutant deficient in its interaction with the UmuDC complex
    • Bailone, A., Sommer, S., Knezevic, J., Dutreix, M. & Devoret, R. (1991). A RecA protein mutant deficient in its interaction with the UmuDC complex. Biochimie 73, 479-484.
    • (1991) Biochimie , vol.73 , pp. 479-484
    • Bailone, A.1    Sommer, S.2    Knezevic, J.3    Dutreix, M.4    Devoret, R.5
  • 19
    • 0027166335 scopus 로고
    • Targeting of the UmuD, UmuD· and MucA· mutagenesis proteins to DNA by RecA protein
    • Frank, E.G., Hauser, A.S., Levine, A.S. & Woodgate, R. (1993). Targeting of the UmuD, UmuD· and MucA· mutagenesis proteins to DNA by RecA protein. Proc. Natl. Acad. Sci. USA 90, 8169-8173.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8169-8173
    • Frank, E.G.1    Hauser, A.S.2    Levine, A.S.3    Woodgate, R.4
  • 20
    • 2542472534 scopus 로고
    • UmuC mutagenesis protein of Escherichia coli: Purification and interaction with UmuD and UmuD·
    • Woodgate, R., Rajagopalan, M., Lu, C. & Echols, H. (1989). UmuC mutagenesis protein of Escherichia coli: purification and interaction with UmuD and UmuD·. Proc. Natl. Acad. Sci. USA 86, 7301-7305.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 7301-7305
    • Woodgate, R.1    Rajagopalan, M.2    Lu, C.3    Echols, H.4
  • 21
  • 22
    • 0024549529 scopus 로고
    • λ repressor mutants that are better substrates for RecA-mediated cleavage
    • Gimble, F.S. & Sauer, R.T. (1989). λ repressor mutants that are better substrates for RecA-mediated cleavage. J. Mol. Biol. 206, 29-39.
    • (1989) J. Mol. Biol. , vol.206 , pp. 29-39
    • Gimble, F.S.1    Sauer, R.T.2
  • 23
    • 0025815515 scopus 로고
    • Levels of chromosomally encoded Umu proteins and requirements for in vivo UmuD cleavage
    • Woodgate, R. & Ennis, D.G. (1991). Levels of chromosomally encoded Umu proteins and requirements for in vivo UmuD cleavage. Mol. Gen. Genet. 229, 10-16.
    • (1991) Mol. Gen. Genet. , vol.229 , pp. 10-16
    • Woodgate, R.1    Ennis, D.G.2
  • 25
    • 17544368037 scopus 로고    scopus 로고
    • Purification of a soluble UmuD·C complex from Escherichia coli
    • Bruck, I., Woodgate, R., McEntee, K. & Goodman, M.F. (1996). Purification of a soluble UmuD·C complex from Escherichia coli. J. Biol. Chem. 271, 10767-10774.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10767-10774
    • Bruck, I.1    Woodgate, R.2    McEntee, K.3    Goodman, M.F.4
  • 26
    • 0025361131 scopus 로고
    • Nature of the SOS-inducing signal in Escherichia coli
    • Sassanfar, M. & Roberts, J.W. (1990). Nature of the SOS-inducing signal in Escherichia coli. J. Mol. Biol. 212, 79-96.
    • (1990) J. Mol. Biol. , vol.212 , pp. 79-96
    • Sassanfar, M.1    Roberts, J.W.2
  • 27
    • 0027729063 scopus 로고
    • The appearance of the UmuD·C protein complex in Escherichia coli switches repair from homologous recombination to SOS mutagenesis
    • Sommer, S., Bailone, A. & Devoret, R. (1993). The appearance of the UmuD·C protein complex in Escherichia coli switches repair from homologous recombination to SOS mutagenesis. Mol. Microbiol. 10, 963-971.
    • (1993) Mol. Microbiol. , vol.10 , pp. 963-971
    • Sommer, S.1    Bailone, A.2    Devoret, R.3
  • 28
    • 0026500416 scopus 로고
    • The structure of the E. coli recA protein monomer and polymer
    • Story, R.M., Weber, I.T. & Steitz, T.A. (1992). The structure of the E. coli recA protein monomer and polymer. Nature 355, 318-325.
    • (1992) Nature , vol.355 , pp. 318-325
    • Story, R.M.1    Weber, I.T.2    Steitz, T.A.3
  • 29
    • 0023008741 scopus 로고
    • Structure of helical RecA-DNA complexes
    • Egelman, E.H. & Stasiak, A. (1986). Structure of helical RecA-DNA complexes. J. Mol. Biol. 191, 677-697.
    • (1986) J. Mol. Biol. , vol.191 , pp. 677-697
    • Egelman, E.H.1    Stasiak, A.2
  • 30
    • 0030584124 scopus 로고    scopus 로고
    • The structure of simian virus 40 refined at 3.1 Å resolution
    • Stehle, T., Gamblin, S.J., Yan, Y. & Harrison, S.C. (1996). The structure of simian virus 40 refined at 3.1 Å resolution. Structure 4, 165-182.
    • (1996) Structure , vol.4 , pp. 165-182
    • Stehle, T.1    Gamblin, S.J.2    Yan, Y.3    Harrison, S.C.4
  • 31
    • 0015244426 scopus 로고
    • The structural analysis of muscle contraction
    • Huxley, H.E. (1971 ). The structural analysis of muscle contraction. Proc. R. Soc. Lond. Ser. B 178, 131-149.
    • (1971) Proc. R. Soc. Lond. Ser. B , vol.178 , pp. 131-149
    • Huxley, H.E.1
  • 32
    • 0028142571 scopus 로고
    • A monocysteine approach for probing the structure and interactions of the UmuD protein
    • Lee, M.H., Ohta, T. & Walker, G.C. (1994). A monocysteine approach for probing the structure and interactions of the UmuD protein. J. Bacteriol. 176, 4825-4837.
    • (1994) J. Bacteriol. , vol.176 , pp. 4825-4837
    • Lee, M.H.1    Ohta, T.2    Walker, G.C.3
  • 33
    • 0024670196 scopus 로고
    • Genetic separation of Escherichia coli recA functions for SOS mutagenesis and repressor cleavage
    • Ennis, D.G., Ossanna, N. & Mount, D.W. (1989). Genetic separation of Escherichia coli recA functions for SOS mutagenesis and repressor cleavage. J. Bacteriol. 171, 2533-2541.
    • (1989) J. Bacteriol. , vol.171 , pp. 2533-2541
    • Ennis, D.G.1    Ossanna, N.2    Mount, D.W.3
  • 34
    • 0024583633 scopus 로고
    • New recA mutations that dissociate the various RecA protein activities in Escherichia coli provide evidence for an additional role for RecA protein in UV mutagenesis
    • Dutreix, M., et al., & Devoret, R. (1989). New recA mutations that dissociate the various RecA protein activities in Escherichia coli provide evidence for an additional role for RecA protein in UV mutagenesis. J. Bacteriol. 171, 2415-2423.
    • (1989) J. Bacteriol. , vol.171 , pp. 2415-2423
    • Dutreix, M.1    Devoret, R.2
  • 35
    • 0028888642 scopus 로고
    • Analysis of recA mutants with altered SOS functions
    • Ennis, D.G., Levine, A.S., Koch, W.H. & Woodgate, R. (1995). Analysis of recA mutants with altered SOS functions. Mutat. Res. 336, 39-48.
    • (1995) Mutat. Res. , vol.336 , pp. 39-48
    • Ennis, D.G.1    Levine, A.S.2    Koch, W.H.3    Woodgate, R.4
  • 36
    • 0026511367 scopus 로고
    • A partially deficient mutant, recA1730, that fails to form normal nucleoprotein filaments
    • Dutreix, M., Burnett, B., Bailone, A., Radding, C.M. & Devoret, R. (1992). A partially deficient mutant, recA1730, that fails to form normal nucleoprotein filaments. Mol. Gen. Genet. 232, 489-497.
    • (1992) Mol. Gen. Genet. , vol.232 , pp. 489-497
    • Dutreix, M.1    Burnett, B.2    Bailone, A.3    Radding, C.M.4    Devoret, R.5
  • 37
    • 0030005608 scopus 로고    scopus 로고
    • In vivo stability of the umu mutagenesis proteins: A major role for RecA
    • Frank, E.G., Gonzalez, M., Ennis, D.G., Levine, A.S. & Woodgate, R. (1996). In vivo stability of the umu mutagenesis proteins: a major role for RecA. J. Bacteriol. 178, 3550-3556.
    • (1996) J. Bacteriol. , vol.178 , pp. 3550-3556
    • Frank, E.G.1    Gonzalez, M.2    Ennis, D.G.3    Levine, A.S.4    Woodgate, R.5
  • 38
    • 0028986780 scopus 로고
    • Structural basis of cell-cell adhesion by cadherins
    • Shapiro, L., et al., & Hendrickson, W.A. (1995). Structural basis of cell-cell adhesion by cadherins. Nature 374, 327-337.
    • (1995) Nature , vol.374 , pp. 327-337
    • Shapiro, L.1    Hendrickson, W.A.2
  • 39
    • 0028225239 scopus 로고
    • Crystal structure of the adenovirus DNA binding protein reveals a hook-on model for cooperative binding
    • Tucker, P.A., Tsernoglou, D., Tucker, A.D., Coenjaerts, F.E.J., Leenders, H. & van der Vliet, P.C. (1994). Crystal structure of the adenovirus DNA binding protein reveals a hook-on model for cooperative binding. EMBO J. 13, 2994-3002.
    • (1994) EMBO J. , vol.13 , pp. 2994-3002
    • Tucker, P.A.1    Tsernoglou, D.2    Tucker, A.D.3    Coenjaerts, F.E.J.4    Leenders, H.5    Van Der Vliet, P.C.6
  • 40
    • 0028204771 scopus 로고
    • Domain swapping: Entangling alliances between proteins
    • Bennett, M.J., Choe, S. & Eisenberg, D. (1994). Domain swapping: entangling alliances between proteins. Proc. Natl. Acad. Sci. USA 91, 3127-3131.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3127-3131
    • Bennett, M.J.1    Choe, S.2    Eisenberg, D.3
  • 41
    • 0029950688 scopus 로고    scopus 로고
    • Arrested DNA replication in Xenopus and release by E. coli mutagenesis proteins
    • Oda, N., et al., & Ackerman, E.J. (1996). Arrested DNA replication in Xenopus and release by E. coli mutagenesis proteins. Science 272, 1644-1646.
    • (1996) Science , vol.272 , pp. 1644-1646
    • Oda, N.1    Ackerman, E.J.2
  • 42
    • 0029798273 scopus 로고    scopus 로고
    • Production and crystallization of a selenomethionyl variant of UmuD·, an Escherichia coli SOS response protein
    • Peat, T.S., Frank, E.G., Woodgate, R. & Hendrickson, W.A. (1996). Production and crystallization of a selenomethionyl variant of UmuD·, an Escherichia coli SOS response protein. Proteins 25, 506-509.
    • (1996) Proteins , vol.25 , pp. 506-509
    • Peat, T.S.1    Frank, E.G.2    Woodgate, R.3    Hendrickson, W.A.4
  • 43
    • 0026095584 scopus 로고
    • Determination of macromolecular structures from anomalous diffraction of synchrotron radiation
    • Hendrickson, W.A. (1991). Determination of macromolecular structures from anomalous diffraction of synchrotron radiation. Science 254, 51-58.
    • (1991) Science , vol.254 , pp. 51-58
    • Hendrickson, W.A.1
  • 44
    • 0025262173 scopus 로고
    • Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): A vehicle for direct determination of three-dimensional structure
    • Hendrickson, W.A., Horton, J.R. & LeMaster, D.M. (1990). Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): a vehicle for direct determination of three-dimensional structure. EMBO J. 9, 1665-1672.
    • (1990) EMBO J. , vol.9 , pp. 1665-1672
    • Hendrickson, W.A.1    Horton, J.R.2    LeMaster, D.M.3
  • 48
    • 0027194501 scopus 로고
    • A rapid method for cloning mutagenic DNA repair genes: Isolation of umucomplementing genes from multidrug resistance plasmids R391, R446b, and R471a
    • Ho, C., Kulaeva, O.I., Levine, A.S. & Woodgate, R. (1993). A rapid method for cloning mutagenic DNA repair genes: isolation of umucomplementing genes from multidrug resistance plasmids R391, R446b, and R471a. J. Bacteriol. 175, 5411-5419.
    • (1993) J. Bacteriol. , vol.175 , pp. 5411-5419
    • Ho, C.1    Kulaeva, O.I.2    Levine, A.S.3    Woodgate, R.4
  • 49
    • 0017743308 scopus 로고
    • Isolation and characterization of mutants of Escherichia coli deficient in induction of mutations by ultraviolet light
    • Kato, T. & Shinoura, Y. (1977). Isolation and characterization of mutants of Escherichia coli deficient in induction of mutations by ultraviolet light. Mol. Gen. Genet. 156, 121-131.
    • (1977) Mol. Gen. Genet. , vol.156 , pp. 121-131
    • Kato, T.1    Shinoura, Y.2
  • 50
    • 0015458045 scopus 로고
    • Survival, mutation and capacity to repair single strand DNA breaks after gamma irradiation in different exr-strains of Escherichia coli
    • Sedgwick, S.G. & Bridges, B.A. (1972). Survival, mutation and capacity to repair single strand DNA breaks after gamma irradiation in different exr-strains of Escherichia coli. Mol. Gen. Genet. 119, 93-102.
    • (1972) Mol. Gen. Genet. , vol.119 , pp. 93-102
    • Sedgwick, S.G.1    Bridges, B.A.2
  • 51
    • 0002452464 scopus 로고
    • Oscillation Data Reduction Program
    • Sawyer, L., Isaacs, N. & Bailey, S., eds, SERC Daresbury Laboratory, Warrington, UK
    • Otwinowski, Z. (1993). Oscillation Data Reduction Program. In Proceeding of the CCP4 Study Weekend: Data Collection and Processing. (Sawyer, L., Isaacs, N. & Bailey, S., eds), pp. 56-62, SERC Daresbury Laboratory, Warrington, UK.
    • (1993) Proceeding of the CCP4 Study Weekend: Data Collection and Processing , pp. 56-62
    • Otwinowski, Z.1
  • 52
    • 0028103275 scopus 로고
    • The CCP4 Suite: Programs for protein crystallography
    • Collaborative Computational Project No.4. (1994). The CCP4 Suite: programs for protein crystallography. Acta Cryst. D 50, 760-763.
    • (1994) Acta Cryst. D , vol.50 , pp. 760-763
  • 53
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.-Y., Cowan, S.W. & Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst. A 47, 110-119.
    • (1991) Acta Cryst. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 55
    • 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. Cryst. 24, 946-950.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 56
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K.A. & Honig, B. (1991). Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3


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