메뉴 건너뛰기




Volumn 89, Issue 3, 2005, Pages 1941-1956

Theory of electrostatically regulated binding of T4 gene 32 protein to single- and double-stranded DNA

Author keywords

[No Author keywords available]

Indexed keywords

DNA BINDING PROTEIN; NUCLEIC ACID; SINGLE STRANDED DNA; T4 GENE 32 PROTEIN; UNCLASSIFIED DRUG;

EID: 24144463904     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.105.063776     Document Type: Article
Times cited : (31)

References (49)
  • 1
    • 18844364649 scopus 로고    scopus 로고
    • Salt dependent binding of T4 gene 32 protein to single- and double-stranded DNA: Single molecule force spectroscopy measurements
    • Pant, K., R. L. Karpel, I. Rouzina, and M. C. Williams. 2005. Salt dependent binding of T4 gene 32 protein to single- and double-stranded DNA: single molecule force spectroscopy measurements. J. Mol. Biol. 349:317-330.
    • (2005) J. Mol. Biol. , vol.349 , pp. 317-330
    • Pant, K.1    Karpel, R.L.2    Rouzina, I.3    Williams, M.C.4
  • 2
    • 0344406718 scopus 로고    scopus 로고
    • Kinetic regulation of single DNA molecule denaturation by T4 gene 32 protein structural domains
    • Pant, K., R. L. Karpel, and M. C. Williams. 2003. Kinetic regulation of single DNA molecule denaturation by T4 gene 32 protein structural domains. J. Mol. Biol. 327:571-578.
    • (2003) J. Mol. Biol. , vol.327 , pp. 571-578
    • Pant, K.1    Karpel, R.L.2    Williams, M.C.3
  • 3
    • 1042298812 scopus 로고    scopus 로고
    • Mechanical measurement of single-molecule binding rates: Kinetics of DNA helix-destabilization by T4 gene 32 protein
    • Pant, K., R. L. Karpel, I. Rouzina, and M. C. Williams. 2004. Mechanical measurement of single-molecule binding rates: kinetics of DNA helix-destabilization by T4 gene 32 protein. J. Mol. Biol. 336:851-870.
    • (2004) J. Mol. Biol. , vol.336 , pp. 851-870
    • Pant, K.1    Karpel, R.L.2    Rouzina, I.3    Williams, M.C.4
  • 4
    • 0036600949 scopus 로고    scopus 로고
    • Force spectroscopy of single DNA and RNA molecules
    • Williams, M. C., and I. Rouzina. 2002. Force spectroscopy of single DNA and RNA molecules. Curr. Opin. Struct. Biol. 12:330-336.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 330-336
    • Williams, M.C.1    Rouzina, I.2
  • 5
    • 0036009140 scopus 로고    scopus 로고
    • Thermodynamics of DNA interactions from single molecule stretching experiments
    • Williams, M. C., I. Rouzina, and V. A. Bloomfield. 2002. Thermodynamics of DNA interactions from single molecule stretching experiments. Acct. Chem. Res. 35:159-166.
    • (2002) Acct. Chem. Res. , vol.35 , pp. 159-166
    • Williams, M.C.1    Rouzina, I.2    Bloomfield, V.A.3
  • 6
    • 0019350732 scopus 로고
    • Interactions of bacteriophage T4-coded gene 32 protein with nucleic acids. III. Binding properties of two specific proteolytic digestion products of the protein (G32P*I and G32*III)
    • Lonberg, N., S. C. Kowalczykowski, L. S. Paul, and P. H. von Hippel. 1981. Interactions of bacteriophage T4-coded gene 32 protein with nucleic acids. III. Binding properties of two specific proteolytic digestion products of the protein (G32P*I and G32*III). J. Mol. Biol. 145:123-138.
    • (1981) J. Mol. Biol. , vol.145 , pp. 123-138
    • Lonberg, N.1    Kowalczykowski, S.C.2    Paul, L.S.3    Von Hippel, P.H.4
  • 7
    • 0019349524 scopus 로고
    • Interactions of bacteriophage T4-coded gene 32 protein with nucleic acids. II. Specificity of binding to DNA and RNA
    • Newport, J. W., N. Lonberg, S. C. Kowalczykowski, and P. H. von Hippel. 1981. Interactions of bacteriophage T4-coded gene 32 protein with nucleic acids. II. Specificity of binding to DNA and RNA. J. Mol. Biol. 145:105-121.
    • (1981) J. Mol. Biol. , vol.145 , pp. 105-121
    • Newport, J.W.1    Lonberg, N.2    Kowalczykowski, S.C.3    Von Hippel, P.H.4
  • 9
    • 0019774929 scopus 로고
    • Kinetics and mechanism of the association of the bacteriophage T4 gene 32 (helix destabilizing) protein with single-stranded nucleic acids. Evidence for protein translocation
    • Lohman, T. M., and S. C. Kowalczykowski. 1981. Kinetics and mechanism of the association of the bacteriophage T4 gene 32 (helix destabilizing) protein with single-stranded nucleic acids. Evidence for protein translocation. J. Mol. Biol. 152:67-109.
    • (1981) J. Mol. Biol. , vol.152 , pp. 67-109
    • Lohman, T.M.1    Kowalczykowski, S.C.2
  • 10
    • 0029052511 scopus 로고
    • Crystal structure of a replication fork single-stranded DNA binding protein (T4 gp32) complexed to DNA
    • Shamoo, Y., A. M. Friedman, M. R. Parsons, W. H. Konigsberg, and T. A. Steitz. 1995. Crystal structure of a replication fork single-stranded DNA binding protein (T4 gp32) complexed to DNA. Nature. 376:362-366.
    • (1995) Nature , vol.376 , pp. 362-366
    • Shamoo, Y.1    Friedman, A.M.2    Parsons, M.R.3    Konigsberg, W.H.4    Steitz, T.A.5
  • 11
    • 0017813456 scopus 로고
    • Structural changes in the T4 gene 32 protein induced by DNA polynucleotides
    • Williams, K. R., and W. Konigsberg. 1978. Structural changes in the T4 gene 32 protein induced by DNA polynucleotides. J. Biol. Chem. 253:2463-2470.
    • (1978) J. Biol. Chem. , vol.253 , pp. 2463-2470
    • Williams, K.R.1    Konigsberg, W.2
  • 12
    • 0018289487 scopus 로고
    • T4 gene 32 protein trypsin-generated fragments. Fluorescence measurement of DNA-binding parameters
    • Spicer, E. K., K. R. Williams, and W. H. Konigsberg. 1979. T4 gene 32 protein trypsin-generated fragments. Fluorescence measurement of DNA-binding parameters. J. Biol. Chem. 254:6433-6436.
    • (1979) J. Biol. Chem. , vol.254 , pp. 6433-6436
    • Spicer, E.K.1    Williams, K.R.2    Konigsberg, W.H.3
  • 13
    • 0018118521 scopus 로고
    • Purification and physicochemical properties of limited proteolysis products of T4 helix destabilizing protein (gene 32 protein)
    • Hosoda, J., and H. Moise. 1978. Purification and physicochemical properties of limited proteolysis products of T4 helix destabilizing protein (gene 32 protein). J. Biol. Chem. 253:7547-7558.
    • (1978) J. Biol. Chem. , vol.253 , pp. 7547-7558
    • Hosoda, J.1    Moise, H.2
  • 14
    • 0020580529 scopus 로고
    • Limited proteolysis studies on the Escherichia coli single-stranded DNA binding protein. Evidence for a functionally homologous domain in both the Escherichia coli and T4 DNA binding proteins
    • Williams, K. R., E. K. Spicer, M. B. LoPresti, R. A. Guggenheimer, and J. W. Chase. 1983. Limited proteolysis studies on the Escherichia coli single-stranded DNA binding protein. Evidence for a functionally homologous domain in both the Escherichia coli and T4 DNA binding proteins. J. Biol. Chem. 258:3346-3355.
    • (1983) J. Biol. Chem. , vol.258 , pp. 3346-3355
    • Williams, K.R.1    Spicer, E.K.2    LoPresti, M.B.3    Guggenheimer, R.A.4    Chase, J.W.5
  • 15
    • 0017895903 scopus 로고
    • The molecular theory of polyelectrolyte solutions with applications to the electrostatic properties of polynucleotides
    • Manning, G. S. 1978. The molecular theory of polyelectrolyte solutions with applications to the electrostatic properties of polynucleotides. Q. Rev. Biophys. 11:179-246.
    • (1978) Q. Rev. Biophys. , vol.11 , pp. 179-246
    • Manning, G.S.1
  • 16
    • 0017820499 scopus 로고
    • Thermodynamic analysis of ion effects on the binding and conformational equilibria of proteins and nucleic acids: The roles of ion association or release, screening, and ion effects on water activity
    • Record, M. T., Jr., C. F. Anderson, and T. M. Lohman. 1978. Thermodynamic analysis of ion effects on the binding and conformational equilibria of proteins and nucleic acids: the roles of ion association or release, screening, and ion effects on water activity. Q. Rev. Biophys. 11:103-178.
    • (1978) Q. Rev. Biophys. , vol.11 , pp. 103-178
    • Record Jr., M.T.1    Anderson, C.F.2    Lohman, T.M.3
  • 17
    • 0031447208 scopus 로고    scopus 로고
    • DNA condensation by multivalent cations
    • Bloomfield, V. A. 1997. DNA condensation by multivalent cations. Biopolymers. 44:269-282.
    • (1997) Biopolymers. , vol.44 , pp. 269-282
    • Bloomfield, V.A.1
  • 18
    • 0030932899 scopus 로고    scopus 로고
    • Competitive electrostatic binding of charged ligands to polyelectrolytes-practical approach using the non-linear Poisson-Boltzmann equation
    • Rouzina, I., and V. A. Bloomfield. 1997. Competitive electrostatic binding of charged ligands to polyelectrolytes-practical approach using the non-linear Poisson-Boltzmann equation. Biophys. Chem. 64:139-155.
    • (1997) Biophys. Chem. , vol.64 , pp. 139-155
    • Rouzina, I.1    Bloomfield, V.A.2
  • 19
    • 0028297873 scopus 로고
    • Linkage of pH, anion and cation effects in protein-nucleic acid equilibria. Escherichia coli SSB protein-single stranded nucleic acid interactions
    • Overman, L. B., and T. M. Lohman. 1994. Linkage of pH, anion and cation effects in protein-nucleic acid equilibria. Escherichia coli SSB protein-single stranded nucleic acid interactions. J. Mol. Biol. 236:165-178.
    • (1994) J. Mol. Biol. , vol.236 , pp. 165-178
    • Overman, L.B.1    Lohman, T.M.2
  • 20
    • 0027133566 scopus 로고
    • Ion-exchange reactions of proteins during DNA binding
    • Fried, M. G., and D. F. Stickle. 1993. Ion-exchange reactions of proteins during DNA binding. Eur. J. Biochem. 218:469-475.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 469-475
    • Fried, M.G.1    Stickle, D.F.2
  • 22
    • 0031776135 scopus 로고    scopus 로고
    • Analysis of effects of salts and uncharged solutes on protein and nucleic acid equilibria and processes: A practical guide to recognizing and interpreting polyelectrolyte effects, Höfmeister effects, and osmotic effects of salts
    • Record, M. T. J., W. Zhang, and C. F. Anderson. 1998. Analysis of effects of salts and uncharged solutes on protein and nucleic acid equilibria and processes: a practical guide to recognizing and interpreting polyelectrolyte effects, Höfmeister effects, and osmotic effects of salts. Adv. Protein Chem. 51:281-353.
    • (1998) Adv. Protein Chem. , vol.51 , pp. 281-353
    • Record, M.T.J.1    Zhang, W.2    Anderson, C.F.3
  • 23
    • 0024962352 scopus 로고
    • Site-specific mutagenesis of T4 gene 32: The role of tyrosine residues in protein-nucleic acid interactions
    • Shamoo, Y., L. R. Ghosaini, K. M. Keating, K. R. Williams, J. M. Sturtevant, and W. H. Konigsberg. 1989. Site-specific mutagenesis of T4 gene 32: the role of tyrosine residues in protein-nucleic acid interactions. Biochemistry. 28:7409-7417.
    • (1989) Biochemistry , vol.28 , pp. 7409-7417
    • Shamoo, Y.1    Ghosaini, L.R.2    Keating, K.M.3    Williams, K.R.4    Sturtevant, J.M.5    Konigsberg, W.H.6
  • 24
    • 0017145254 scopus 로고
    • DNA "melting" proteins. II. Effects of bacteriophage T4 gene 32-protein binding on the conformation and stability of nucleic acid structures
    • Jensen, D. E., R. C. Kelly, and P. H. von Hippel. 1976. DNA "melting" proteins. II. Effects of bacteriophage T4 gene 32-protein binding on the conformation and stability of nucleic acid structures. J. Biol. Chem. 251:7215-7228.
    • (1976) J. Biol. Chem. , vol.251 , pp. 7215-7228
    • Jensen, D.E.1    Kelly, R.C.2    Von Hippel, P.H.3
  • 25
    • 0021770892 scopus 로고
    • Kinetics and mechanism of dissociation of cooperatively bound T4 gene 32 protein-single-stranded nucleic acid complexes. I. Irreversible dissociation induced by sodium chloride concentration jumps
    • Lohman, T. M. 1984. Kinetics and mechanism of dissociation of cooperatively bound T4 gene 32 protein-single-stranded nucleic acid complexes. I. Irreversible dissociation induced by sodium chloride concentration jumps. Biochemistry. 23:4656-4665.
    • (1984) Biochemistry , vol.23 , pp. 4656-4665
    • Lohman, T.M.1
  • 27
    • 0019887628 scopus 로고
    • Diffusion-driven mechanisms of protein translocation on nucleic acids. I. Models and theory
    • Berg, O. G., R. B. Winter, and P. H. von Hippel. 1981. Diffusion-driven mechanisms of protein translocation on nucleic acids. I. Models and theory. Biochemistry. 20:6929-6948.
    • (1981) Biochemistry , vol.20 , pp. 6929-6948
    • Berg, O.G.1    Winter, R.B.2    Von Hippel, P.H.3
  • 28
    • 0021770897 scopus 로고
    • Kinetics and mechanism of dissociation of cooperatively bound T4 gene 32 protein-single-stranded nucleic acid complexes. II. Changes in mechanism as a function of sodium chloride concentration and other solution variables
    • Lohman, T. M. 1984. Kinetics and mechanism of dissociation of cooperatively bound T4 gene 32 protein-single-stranded nucleic acid complexes. II. Changes in mechanism as a function of sodium chloride concentration and other solution variables. Biochemistry. 23:4665-4675.
    • (1984) Biochemistry , vol.23 , pp. 4665-4675
    • Lohman, T.M.1
  • 29
    • 0007425498 scopus 로고    scopus 로고
    • Competitive electrostatic binding of charged ligands to polyelectrolytes, planar and cylindrical geometries
    • Rouzina, I., and V. A. Bloomfield. 1996. Competitive electrostatic binding of charged ligands to polyelectrolytes, planar and cylindrical geometries. J. Phys. Chem. 100:4292-4304.
    • (1996) J. Phys. Chem. , vol.100 , pp. 4292-4304
    • Rouzina, I.1    Bloomfield, V.A.2
  • 31
    • 77953603315 scopus 로고
    • Interaction between parallel rodlike macroions
    • Oosawa, F. 1968. Interaction between parallel rodlike macroions. Biopolymers. 6:1633-1647.
    • (1968) Biopolymers , vol.6 , pp. 1633-1647
    • Oosawa, F.1
  • 32
    • 0017146579 scopus 로고
    • Ion effects on ligand-nuclei acid interactions
    • Record, M. T., T. M. Lohman, and P. L. deHaseth. 1976. Ion effects on ligand-nuclei acid interactions. J. Mol. Biol. 107:145-158.
    • (1976) J. Mol. Biol. , vol.107 , pp. 145-158
    • Record, M.T.1    Lohman, T.M.2    Dehaseth, P.L.3
  • 34
    • 35949014974 scopus 로고
    • Stability and phase behavior of mixed surfactant vesicles
    • Safran, S. A., P. A. Pincus, D. Andelman, and F. C. MacKintosh. 1991. Stability and phase behavior of mixed surfactant vesicles. Phys. Rev. A. 43:1071-1078.
    • (1991) Phys. Rev. A , vol.43 , pp. 1071-1078
    • Safran, S.A.1    Pincus, P.A.2    Andelman, D.3    MacKintosh, F.C.4
  • 35
    • 0019641904 scopus 로고
    • Polyelectrolyte theory of charged-ligand binding to nucleic acids
    • Gueron, M., and G. Weisbuch. 1981. Polyelectrolyte theory of charged-ligand binding to nucleic acids. Biochimie. 63:821-825.
    • (1981) Biochimie. , vol.63 , pp. 821-825
    • Gueron, M.1    Weisbuch, G.2
  • 36
    • 0036280384 scopus 로고    scopus 로고
    • LAST motifs and SMART domains in gene 32 protein: An unfolding story of autoregulation?
    • Karpel, R. L. 2002. LAST motifs and SMART domains in gene 32 protein: an unfolding story of autoregulation? IUBMB Life. 53:161-166.
    • (2002) IUBMB Life , vol.53 , pp. 161-166
    • Karpel, R.L.1
  • 37
    • 0017125322 scopus 로고
    • DNA "melting" proteins. III. Fluorescence "mapping" of the nucleic acid binding site of bacteriophage T4 gene 32-protein
    • Kelly, R. C., and P. H. von Hippel. 1976. DNA "melting" proteins. III. Fluorescence "mapping" of the nucleic acid binding site of bacteriophage T4 gene 32-protein. J. Biol. Chem. 251:7229-7239.
    • (1976) J. Biol. Chem. , vol.251 , pp. 7229-7239
    • Kelly, R.C.1    Von Hippel, P.H.2
  • 38
    • 0019351776 scopus 로고
    • Interactions of bacteriophage T4-coded gene 32 protein with nucleic acids. I. Characterization of the binding interactions
    • Kowalczykowski, S. C., N. Lonberg, J. W. Newport, and P. H. von Hippel. 1981. Interactions of bacteriophage T4-coded gene 32 protein with nucleic acids. I. Characterization of the binding interactions. J. Mol. Biol. 145:75-104.
    • (1981) J. Mol. Biol. , vol.145 , pp. 75-104
    • Kowalczykowski, S.C.1    Lonberg, N.2    Newport, J.W.3    Von Hippel, P.H.4
  • 39
    • 0025286323 scopus 로고
    • Overexpression, purification and characterization of recombinant T4 gene 32 protein22-301(g32P-B)
    • Giedroc, D. P., R. Khan, and K. Barnhart. 1990. Overexpression, purification and characterization of recombinant T4 gene 32 protein22-301(g32P- B). J. Biol. Chem. 265:11444-11455.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11444-11455
    • Giedroc, D.P.1    Khan, R.2    Barnhart, K.3
  • 40
    • 3042626449 scopus 로고    scopus 로고
    • Interactions of the KWK6 cationic peptide with short nucleic acid oligomers: Demonstration of large Coulombic end effects on binding at 0.1-0.2 M salt
    • Ballin, J. D., I. A. Shkel, and M. T. J. Record. 2004. Interactions of the KWK6 cationic peptide with short nucleic acid oligomers: demonstration of large Coulombic end effects on binding at 0.1-0.2 M salt. Nucleic Acids Res. 32:3271-3281.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 3271-3281
    • Ballin, J.D.1    Shkel, I.A.2    Record, M.T.J.3
  • 41
    • 0017077538 scopus 로고
    • DNA "melting" proteins. IV. Fluorescence measurements of binding parameters for bacteriophage T4 gene 32-protein to mono-, oligo-, and polynucleotides
    • Kelly, R. C., D. E. Jensen, and P. H. von Hippel. 1976. DNA "melting" proteins. IV. Fluorescence measurements of binding parameters for bacteriophage T4 gene 32-protein to mono-, oligo-, and polynucleotides. J. Biol. Chem. 251:7240-7250.
    • (1976) J. Biol. Chem. , vol.251 , pp. 7240-7250
    • Kelly, R.C.1    Jensen, D.E.2    Von Hippel, P.H.3
  • 42
    • 0017293312 scopus 로고
    • T4 gene 32 protein model for control of activity at replication fork
    • Moise, H., and J. Hosoda. 1976. T4 gene 32 protein model for control of activity at replication fork. Nature. 259:455-458.
    • (1976) Nature , vol.259 , pp. 455-458
    • Moise, H.1    Hosoda, J.2
  • 43
    • 0017838992 scopus 로고
    • Circular dichroism studies of the interaction of a limited hydrolysate of T4 gene 32 protein with T4 DNA and poly[d(A-T)]
    • Greve, J., M. F. Maestre, H. Moise, and J. Hosoda. 1978. Circular dichroism studies of the interaction of a limited hydrolysate of T4 gene 32 protein with T4 DNA and poly[d(A-T)]. Biochemistry. 17:893-898.
    • (1978) Biochemistry , vol.17 , pp. 893-898
    • Greve, J.1    Maestre, M.F.2    Moise, H.3    Hosoda, J.4
  • 44
    • 0035951425 scopus 로고    scopus 로고
    • A general model for nucleic acid helicases and their "coupling" within macromolecular machines
    • von Hippel, P. H., and E. Delagoutte. 2001. A general model for nucleic acid helicases and their "coupling" within macromolecular machines. Cell. 104:177-190.
    • (2001) Cell. , vol.104 , pp. 177-190
    • Von Hippel, P.H.1    Delagoutte, E.2
  • 45
    • 0033579935 scopus 로고    scopus 로고
    • Biochemical interactions within a ternary complex of the bacteriophage T4 recombination proteins uvsY and gp32 bound to single-stranded DNA
    • Sweezy, M. A., and S. W. Morrical. 1999. Biochemical interactions within a ternary complex of the bacteriophage T4 recombination proteins uvsY and gp32 bound to single-stranded DNA. Biochemistry. 38:936-944.
    • (1999) Biochemistry , vol.38 , pp. 936-944
    • Sweezy, M.A.1    Morrical, S.W.2
  • 46
    • 0035902508 scopus 로고    scopus 로고
    • Mediator proteins orchestrate enzyme-ssDNA assembly during T4 recombination-dependent DNA replication and repair
    • Bleuit, J. S., H. Xu, Y. Ma, T. Wang, J. Liu, and S. W. Morrical. 2001. Mediator proteins orchestrate enzyme-ssDNA assembly during T4 recombination-dependent DNA replication and repair. Proc. Natl. Acad. Sci. USA. 98:8298-8305.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 8298-8305
    • Bleuit, J.S.1    Xu, H.2    Ma, Y.3    Wang, T.4    Liu, J.5    Morrical, S.W.6
  • 47
    • 0025884453 scopus 로고
    • Protein-protein interactions with the acidic COOH terminus of the single-stranded DNA-binding protein of the bacteriophage T4
    • Krassa, K. B., L. S. Green, and L. Gold. 1991. Protein-protein interactions with the acidic COOH terminus of the single-stranded DNA-binding protein of the bacteriophage T4. Proc. Natl. Acad. Sci. USA. 88:4010-4014.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 4010-4014
    • Krassa, K.B.1    Green, L.S.2    Gold, L.3
  • 48
    • 0027457508 scopus 로고
    • Assembly of the bacteriophage T4 replication machine requires the acidic carboxy terminus of gene 32 protein
    • Hurley, J. M., S. A. Chervitz, T. C. Jarvis, B. S. Singer, and L. Gold. 1993. Assembly of the bacteriophage T4 replication machine requires the acidic carboxy terminus of gene 32 protein. J. Mol. Biol. 229:398-418.
    • (1993) J. Mol. Biol. , vol.229 , pp. 398-418
    • Hurley, J.M.1    Chervitz, S.A.2    Jarvis, T.C.3    Singer, B.S.4    Gold, L.5
  • 49
    • 0041529868 scopus 로고    scopus 로고
    • The carboxyl-terminal domain of bacteriophage T7 single-stranded DNA-binding protein modulates DNA binding and interaction with T7 DNA polymerase
    • He, Z. G., L. F. Rezende, S. Willcox, J. D. Griffith, and C. C. Richardson. 2003. The carboxyl-terminal domain of bacteriophage T7 single-stranded DNA-binding protein modulates DNA binding and interaction with T7 DNA polymerase. J. Biol. Chem. 278:29538-29545.
    • (2003) J. Biol. Chem. , vol.278 , pp. 29538-29545
    • He, Z.G.1    Rezende, L.F.2    Willcox, S.3    Griffith, J.D.4    Richardson, C.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.