메뉴 건너뛰기




Volumn 17, Issue 5, 2004, Pages 390-396

Bacteriophage ∅29 protein p6: An architectural protein involved in genome organization, replication and control of transcription

Author keywords

B. subtilis phage; DNA replication; DNA supercoiling; DNA protein interaction; Nucleoid associated protein; Protein protein interaction; Transcription control

Indexed keywords

BACILLUS SUBTILIS;

EID: 4544297319     PISSN: 09523499     EISSN: None     Source Type: Journal    
DOI: 10.1002/jmr.701     Document Type: Conference Paper
Times cited : (9)

References (55)
  • 1
    • 0030612613 scopus 로고    scopus 로고
    • Phage ∅29 protein p6 is in a monomer-dimer equilibrium that shifts to higher association states at the millimolar concentrations found in vivo
    • Abril AM, Salas M, Andreu JM, Hermoso JM, Rivas G. 1997. Phage ∅29 protein p6 is in a monomer-dimer equilibrium that shifts to higher association states at the millimolar concentrations found in vivo. Biochemistry 36: 11901-11908.
    • (1997) Biochemistry , vol.36 , pp. 11901-11908
    • Abril, A.M.1    Salas, M.2    Andreu, J.M.3    Hermoso, J.M.4    Rivas, G.5
  • 3
    • 0034714243 scopus 로고    scopus 로고
    • Identification of residues within two regions involved in self-association of viral histone-like protein p6 from phage ∅29
    • Abril AM, Salas M, Hermoso JM. 2000. Identification of residues within two regions involved in self-association of viral histone-like protein p6 from phage ∅29. J. Biol. Chem. 275: 26404-26410.
    • (2000) J. Biol. Chem. , vol.275 , pp. 26404-26410
    • Abril, A.M.1    Salas, M.2    Hermoso, J.M.3
  • 4
    • 0037151778 scopus 로고    scopus 로고
    • The in vivo function of phage ∅29 nucleoid-associated protein p6 requires formation of dimers
    • Abril AM, Salas M, Hermoso JM. 2002. The in vivo function of phage ∅29 nucleoid-associated protein p6 requires formation of dimers. Gene 296: 187-194.
    • (2002) Gene , vol.296 , pp. 187-194
    • Abril, A.M.1    Salas, M.2    Hermoso, J.M.3
  • 5
    • 0024314474 scopus 로고
    • Characterization of a new prokaryotic transcriptional activator and its DNA recognition site
    • Barthelemy I, Salas M. 1989. Characterization of a new prokaryotic transcriptional activator and its DNA recognition site. J. Mol. Biol. 208: 225-232.
    • (1989) J. Mol. Biol. , vol.208 , pp. 225-232
    • Barthelemy, I.1    Salas, M.2
  • 6
    • 0024579407 scopus 로고
    • In vitro transcription of bacteriophage ∅29 DNA: Inhibition of early promoters by the viral replication protein p6
    • Barthelemy I, Mellado RP, Salas M. 1989. In vitro transcription of bacteriophage ∅29 DNA: inhibition of early promoters by the viral replication protein p6. J. Virol. 63: 460-462.
    • (1989) J. Virol. , vol.63 , pp. 460-462
    • Barthelemy, I.1    Mellado, R.P.2    Salas, M.3
  • 7
    • 0023056801 scopus 로고
    • Replication of phage ∅29 DNA in vitro: Role of the viral protein p6 in initiation and elongation
    • Blanco L, Gutiérrez J, Lázaro JM, Bernad A, Salas M. 1986. Replication of phage ∅29 DNA in vitro: role of the viral protein p6 in initiation and elongation. Nucl. Acids Res. 14: 4923-4937.
    • (1986) Nucl. Acids Res. , vol.14 , pp. 4923-4937
    • Blanco, L.1    Gutiérrez, J.2    Lázaro, J.M.3    Bernad, A.4    Salas, M.5
  • 8
    • 0024110408 scopus 로고
    • Transition from initiation to elongation in protein-primed ∅29 DNA replication: Salt-dependent stimulation by the viral protein p6
    • Blanco L, Bernad A, Salas M. 1988. Transition from initiation to elongation in protein-primed ∅29 DNA replication: salt-dependent stimulation by the viral protein p6. J. Virol. 62: 4167-4172.
    • (1988) J. Virol. , vol.62 , pp. 4167-4172
    • Blanco, L.1    Bernad, A.2    Salas, M.3
  • 9
    • 0028000275 scopus 로고
    • A genetic approach to the identification of functional amino acids in protein p6 of Bacillus subtilis phage ∅29
    • Bravo A, Hermoso JM, Salas M. 1994. A genetic approach to the identification of functional amino acids in protein p6 of Bacillus subtilis phage ∅29. Mol. Gen. Genet. 245: 529-536.
    • (1994) Mol. Gen. Genet. , vol.245 , pp. 529-536
    • Bravo, A.1    Hermoso, J.M.2    Salas, M.3
  • 10
    • 0037112903 scopus 로고    scopus 로고
    • The ∅29 transcriptional regulator contacts the nucleoid protein p6 to organize a repression complex
    • Calles B, Salas M, Rojo F. 2002. The ∅29 transcriptional regulator contacts the nucleoid protein p6 to organize a repression complex. EMBO J. 21: 6185-6194.
    • (2002) EMBO J. , vol.21 , pp. 6185-6194
    • Calles, B.1    Salas, M.2    Rojo, F.3
  • 11
    • 0034459548 scopus 로고    scopus 로고
    • Pleiotropic effect of protein p6 on the viral cycle of bacteriophage ∅29
    • Camacho A, Salas M. 2000. Pleiotropic effect of protein p6 on the viral cycle of bacteriophage ∅29. J. Bacteriol. 182: 6927-6932.
    • (2000) J. Bacteriol. , vol.182 , pp. 6927-6932
    • Camacho, A.1    Salas, M.2
  • 12
    • 0035503311 scopus 로고    scopus 로고
    • Mechanism for the switch of ∅29 DNA early to late transcription by regulatory protein p4 and histone-like protein p6
    • Camacho A, Salas M. 2001a. Mechanism for the switch of ∅29 DNA early to late transcription by regulatory protein p4 and histone-like protein p6. EMBO J. 20: 6060-6070.
    • (2001) EMBO J. , vol.20 , pp. 6060-6070
    • Camacho, A.1    Salas, M.2
  • 13
    • 0035800876 scopus 로고    scopus 로고
    • Repression of bacteriophage ∅29 early promoter C2 by viral protein p6 is due to impairment of closed complex
    • Camacho A, Salas M. 2001b. Repression of bacteriophage ∅29 early promoter C2 by viral protein p6 is due to impairment of closed complex. J. Biol. Chem. 276: 28927-28932.
    • (2001) J. Biol. Chem. , vol.276 , pp. 28927-28932
    • Camacho, A.1    Salas, M.2
  • 15
    • 0039554345 scopus 로고    scopus 로고
    • Functional interactions between a phage histone-like protein and a transcriptional factor in regulation of ∅29 early-late transcriptional switch
    • Elías-Arnanz M, Salas M. 1999. Functional interactions between a phage histone-like protein and a transcriptional factor in regulation of ∅29 early-late transcriptional switch. Genes Dev. 13: 2502-2513.
    • (1999) Genes Dev. , vol.13 , pp. 2502-2513
    • Elías-Arnanz, M.1    Salas, M.2
  • 16
    • 0035478585 scopus 로고    scopus 로고
    • Macromolecular crowding: Obvious but under-appreciated
    • Ellis RJ. 2001. Macromolecular crowding: obvious but under-appreciated. Trends Biochem. Sci. 26: 597-604.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 597-604
    • Ellis, R.J.1
  • 17
    • 0024477476 scopus 로고
    • Replication of recombinant ∅29 DNA molecules in Bacillus subtilis protoplasts
    • Escarmís C, Guirao D, Salas M. 1989. Replication of recombinant ∅29 DNA molecules in Bacillus subtilis protoplasts. Virology 169: 152-160.
    • (1989) Virology , vol.169 , pp. 152-160
    • Escarmís, C.1    Guirao, D.2    Salas, M.3
  • 18
    • 0027933891 scopus 로고
    • A new protein domain for binding to DNA through the minor groove
    • Freire R, Salas M, Hermoso JM. 1994. A new protein domain for binding to DNA through the minor groove. EMBO J. 13: 4353-4360.
    • (1994) EMBO J. , vol.13 , pp. 4353-4360
    • Freire, R.1    Salas, M.2    Hermoso, J.M.3
  • 19
    • 0029852327 scopus 로고    scopus 로고
    • Activation of replication origins in ∅29-related phages requires the recognition of initiation proteins to specific nucleoprotein complexes
    • Freire R, Serrano M, Salas M, Hermoso JM. 1996. Activation of replication origins in ∅29-related phages requires the recognition of initiation proteins to specific nucleoprotein complexes. J. Biol. Chem. 271: 31000-31007.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31000-31007
    • Freire, R.1    Serrano, M.2    Salas, M.3    Hermoso, J.M.4
  • 20
    • 4544361798 scopus 로고    scopus 로고
    • Ph.D. Thesis. Reconocimiento del origen de replicación del DNA del bacteriofago ∅29. Universidad Autónoma de Madrid
    • González- Huici V. 2001. Ph.D. Thesis. Reconocimiento del origen de replicación del DNA del bacteriofago ∅29. Universidad Autónoma de Madrid.
    • (2001)
    • González- Huici, V.1
  • 21
    • 4344592253 scopus 로고    scopus 로고
    • Binding of phage ∅29 architectural protein p6 to the viral genome: Evidence for topological restriction of the phage linear DNA
    • González-Huici V, Alcorlo M, Salas M, Hermoso JM. 2004a. Binding of phage ∅29 architectural protein p6 to the viral genome: evidence for topological restriction of the phage linear DNA. Nucleic Acids Res. 32: 3493-3502.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 3493-3502
    • González-Huici, V.1    Alcorlo, M.2    Salas, M.3    Hermoso, J.M.4
  • 22
    • 2342574263 scopus 로고    scopus 로고
    • Genome wide, supercoiling-dependent in vivo binding of a viral protein involved in DNA replication and transcriptional control
    • González-Huici V, Salas M, Hermoso JM. 2004b. Genome wide, supercoiling-dependent in vivo binding of a viral protein involved in DNA replication and transcriptional control. Nucleic Acids Res. 32: 2306-2314.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 2306-2314
    • González-Huici, V.1    Salas, M.2    Hermoso, J.M.3
  • 23
    • 1942501103 scopus 로고    scopus 로고
    • The push-pull mechanism of bacteriophage ∅29 DNA injection
    • González-Huici V, Salas M, Hermoso JM. 2004c. The push-pull mechanism of bacteriophage ∅29 DNA injection. Mol. Microbiol. 52: 529-540.
    • (2004) Mol. Microbiol. , vol.52 , pp. 529-540
    • González-Huici, V.1    Salas, M.2    Hermoso, J.M.3
  • 24
    • 0028175764 scopus 로고
    • Assembly of phage ∅29 genome with viral protein p6 into a compact complex
    • Gutiérrez C, Freire R, Salas M, Hermoso JM. 1994. Assembly of phage ∅29 genome with viral protein p6 into a compact complex. EMBO J. 13: 269-276.
    • (1994) EMBO J. , vol.13 , pp. 269-276
    • Gutiérrez, C.1    Freire, R.2    Salas, M.3    Hermoso, J.M.4
  • 25
    • 0033064319 scopus 로고    scopus 로고
    • Mapping DNA interaction sites of chromosomal proteins using immunoprecipitation and polymerase chain reaction
    • Hecht A, Grunstein M. 1999. Mapping DNA interaction sites of chromosomal proteins using immunoprecipitation and polymerase chain reaction. Meth. Enzymol. 304: 399-414.
    • (1999) Meth. Enzymol. , vol.304 , pp. 399-414
    • Hecht, A.1    Grunstein, M.2
  • 28
    • 0030003385 scopus 로고    scopus 로고
    • Transcription activation by phage ∅29 protein p4 is mediated by interaction with the α subunit of Bacillus subtilis RNA polymerase
    • Mencía M, Monsalve M, Rojo F, Salas M. 1996a. Transcription activation by phage ∅29 protein p4 is mediated by interaction with the α subunit of Bacillus subtilis RNA polymerase. Proc. Natl Acad. Sci. USA 93: 6616-6620.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6616-6620
    • Mencía, M.1    Monsalve, M.2    Rojo, F.3    Salas, M.4
  • 29
    • 0029925824 scopus 로고    scopus 로고
    • Transcriptional activator of phage ∅29 late promoter: Mapping of residues involved in interaction with RNA polymerase and in DNA bending
    • Mencía M, Monsalve M, Salas M, Rojo F. 1996b. Transcriptional activator of phage ∅29 late promoter: mapping of residues involved in interaction with RNA polymerase and in DNA bending. Mol. Microbiol. 20: 273-282.
    • (1996) Mol. Microbiol. , vol.20 , pp. 273-282
    • Mencía, M.1    Monsalve, M.2    Salas, M.3    Rojo, F.4
  • 30
    • 0033969150 scopus 로고    scopus 로고
    • Implications of macromolecular crowding for protein assembly
    • Minton AP. 2000. Implications of macromolecular crowding for protein assembly. Curr. Opin. Struct. Biol. 10: 34-39.
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 34-39
    • Minton, A.P.1
  • 31
    • 0035815743 scopus 로고    scopus 로고
    • The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media
    • Minton AP. 2001. The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media. J. Biol. Chem. 276: 10577-10580.
    • (2001) J. Biol. Chem. , vol.276 , pp. 10577-10580
    • Minton, A.P.1
  • 32
    • 0026453399 scopus 로고
    • Phage ∅29 regulatory protein p4 stabilizes the binding of the RNA polymerase to the late promoter in a process involving direct protein-protein contacts
    • Nuez B, Rojo F, Salas M. 1992. Phage ∅29 regulatory protein p4 stabilizes the binding of the RNA polymerase to the late promoter in a process involving direct protein-protein contacts. Proc. Natl Acad. Sci. USA 89: 11401-11405.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11401-11405
    • Nuez, B.1    Rojo, F.2    Salas, M.3
  • 33
    • 0031080378 scopus 로고    scopus 로고
    • Analysis of chromatin structure by in vivo formaldehyde cross-linking
    • Orlando V, Strutt H, Paro R. 1997. Analysis of chromatin structure by in vivo formaldehyde cross-linking. Meth. Compan. Meth. Enzymol. 11: 205-214.
    • (1997) Meth. Compan. Meth. Enzymol. , vol.11 , pp. 205-214
    • Orlando, V.1    Strutt, H.2    Paro, R.3
  • 34
    • 0024370945 scopus 로고
    • Regions at the carboxyl end of bacteriophage ∅29 protein p6 required for DNA binding and activity in ∅29 DNA replication
    • Otero MJ, Salas M. 1989. Regions at the carboxyl end of bacteriophage ∅29 protein p6 required for DNA binding and activity in ∅29 DNA replication. Nucl. Acids Res. 17: 4567-4577.
    • (1989) Nucl. Acids Res. , vol.17 , pp. 4567-4577
    • Otero, M.J.1    Salas, M.2
  • 35
    • 0025223741 scopus 로고
    • Deletions at the N-terminus of bacteriophage ∅29 protein p6: DNA binding and activity in ∅29 DNA replication
    • Otero MJ, Lȧzaro JM, Salas M. 1990. Deletions at the N-terminus of bacteriophage ∅29 protein p6: DNA binding and activity in ∅29 DNA replication. Gene 95: 25-30.
    • (1990) Gene , vol.95 , pp. 25-30
    • Otero, M.J.1    Lazaro, J.M.2    Salas, M.3
  • 36
    • 0022422712 scopus 로고
    • Overproduction and purification of protein p6 of Bacillus subtilis phage ∅29: Role in the initiation of DNA replication
    • Pastrana R, Lȧzaro JM, Blanco L, García JA, Méndez E, Salas M. 1985. Overproduction and purification of protein p6 of Bacillus subtilis phage ∅29: role in the initiation of DNA replication. Nucl. Acids Res. 13: 3083-3100.
    • (1985) Nucl. Acids Res. , vol.13 , pp. 3083-3100
    • Pastrana, R.1    Lazaro, J.M.2    Blanco, L.3    García, J.A.4    Méndez, E.5    Salas, M.6
  • 38
    • 0026040582 scopus 로고
    • A DNA curvature can substitute phage ∅29 regulatory protein p4 when acting as a transcriptional repressor
    • Rojo F, Salas M. 1991. A DNA curvature can substitute phage ∅29 regulatory protein p4 when acting as a transcriptional repressor. EMBO J. 10: 3429-3438.
    • (1991) EMBO J. , vol.10 , pp. 3429-3438
    • Rojo, F.1    Salas, M.2
  • 39
    • 0025323444 scopus 로고
    • Bend induced by the phage ∅29 transcriptional activator in the viral late promoter is required for activation
    • Rojo F, Zaballos A, Salas M. 1990. Bend induced by the phage ∅29 transcriptional activator in the viral late promoter is required for activation. J. Mol. Biol. 211: 713-725.
    • (1990) J. Mol. Biol. , vol.211 , pp. 713-725
    • Rojo, F.1    Zaballos, A.2    Salas, M.3
  • 40
    • 0023001414 scopus 로고
    • Sequence periodicities in chicken nucleosome core DNA
    • Satchwell SC, Drew HR, Travers AA. 1986. Sequence periodicities in chicken nucleosome core DNA. J. Mol. Biol. 191: 659-675.
    • (1986) J. Mol. Biol. , vol.191 , pp. 659-675
    • Satchwell, S.C.1    Drew, H.R.2    Travers, A.A.3
  • 41
    • 0015535384 scopus 로고
    • Selective replication of bacteriophage ∅29 deoxyribonucleic acid in 6-(p-hydroxyphenylazo)-uracil-treated Bacillus subtilis
    • Schachtele CF, Reilly BE, De Sain CV, Whittington MO, Anderson DL. 1973. Selective replication of bacteriophage ∅29 deoxyribonucleic acid in 6-(p-hydroxyphenylazo)-uracil-treated Bacillus subtilis. J. Virol. 11: 153-155.
    • (1973) J. Virol. , vol.11 , pp. 153-155
    • Schachtele, C.F.1    Reilly, B.E.2    De Sain, C.V.3    Whittington, M.O.4    Anderson, D.L.5
  • 42
    • 0024454856 scopus 로고
    • Signals at the bacteriophage ∅29 DNA replication origins required for protein p6 binding and activity
    • Serrano M, Gutiérrez J, Prieto I, Hermoso JM, Salas M. 1989. Signals at the bacteriophage ∅29 DNA replication origins required for protein p6 binding and activity. EMBO J. 8: 1879-1885.
    • (1989) EMBO J. , vol.8 , pp. 1879-1885
    • Serrano, M.1    Gutiérrez, J.2    Prieto, I.3    Hermoso, J.M.4    Salas, M.5
  • 43
    • 0025279627 scopus 로고
    • A novel nucleoprotein complex at a replication origin
    • Serrano M, Salas M, Hermoso JM. 1990. A novel nucleoprotein complex at a replication origin. Science 248: 1012-1016.
    • (1990) Science , vol.248 , pp. 1012-1016
    • Serrano, M.1    Salas, M.2    Hermoso, J.M.3
  • 44
    • 0027530897 scopus 로고
    • Super-helical path of the DNA in the nucleoprotein complex that activates the initiation of phage ∅29 DNA replication
    • Serrano M, Gutiérrez C, Salas M, Hermoso JM. 1993a. Super-helical path of the DNA in the nucleoprotein complex that activates the initiation of phage ∅29 DNA replication. J. Mol. Biol. 230: 248-259.
    • (1993) J. Mol. Biol. , vol.230 , pp. 248-259
    • Serrano, M.1    Gutiérrez, C.2    Salas, M.3    Hermoso, J.M.4
  • 45
    • 0027155567 scopus 로고
    • Multimeric complexes formed by DNA-binding proteins of low sequence-specificity
    • Serrano M, Salas M, Hermoso JM. 1993b. Multimeric complexes formed by DNA-binding proteins of low sequence-specificity. Trends Biochem. Sci. 18: 202-206.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 202-206
    • Serrano, M.1    Salas, M.2    Hermoso, J.M.3
  • 47
    • 0024455692 scopus 로고
    • Electron microscopy of chromatin
    • Sogo JM, Thoma F. 1989. Electron microscopy of chromatin. Meth. Enzymol. 170: 142-165.
    • (1989) Meth. Enzymol. , vol.170 , pp. 142-165
    • Sogo, J.M.1    Thoma, F.2
  • 48
    • 0030976054 scopus 로고    scopus 로고
    • The oligomeric, structure of nucleoid protein H-NS is necessary for recognition of intrinsically curved DNA and for DNA bending
    • Spurio R, Falconi M, Brandi A, Pon CL, Gualerzi CO. 1997. The oligomeric, structure of nucleoid protein H-NS is necessary for recognition of intrinsically curved DNA and for DNA bending. EMBO J. 16: 1795-1805.
    • (1997) EMBO J. , vol.16 , pp. 1795-1805
    • Spurio, R.1    Falconi, M.2    Brandi, A.3    Pon, C.L.4    Gualerzi, C.O.5
  • 49
    • 0023818825 scopus 로고
    • Structure refinement to 2 A of a nicked DNA oligonucleotide complex with DNase I
    • Suck D, Lahm A, Oefner C. 1988. Structure refinement to 2 A of a nicked DNA oligonucleotide complex with DNase I. Nature 332: 464-468.
    • (1988) Nature , vol.332 , pp. 464-468
    • Suck, D.1    Lahm, A.2    Oefner, C.3
  • 50
    • 0001268975 scopus 로고
    • Hydroxyl radical "footprinting": High resolution information about DNA-protein contacts and application to λ repressor and Cro protein
    • Tullius TD, Dombroski BA. 1986. Hydroxyl radical "footprinting" : high resolution information about DNA-protein contacts and application to λ repressor and Cro protein. Proc. Natl. Acad. Sci. USA 83: 5469-5473.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 5469-5473
    • Tullius, T.D.1    Dombroski, B.A.2
  • 51
    • 0022916928 scopus 로고
    • Nucleotide sequence of the late region of Bacillus phage ∅29 completes the 19285-bp sequence of ∅29 genome. Comparison with the homologous sequence of phage PZA
    • Vlček C, Pačes V. 1986. Nucleotide sequence of the late region of Bacillus phage ∅29 completes the 19285-bp sequence of ∅29 genome. Comparison with the homologous sequence of phage PZA. Gene 46: 215-225.
    • (1986) Gene , vol.46 , pp. 215-225
    • Vlček, C.1    Pačes, V.2
  • 52
    • 0023811057 scopus 로고
    • Helical repeat and linking number of surface-wrapped DNA
    • White JH, Cozzarelli NR, Bauer WR. 1988. Helical repeat and linking number of surface-wrapped DNA. Science 241: 323-327.
    • (1988) Science , vol.241 , pp. 323-327
    • White, J.H.1    Cozzarelli, N.R.2    Bauer, W.R.3
  • 53
    • 0026527508 scopus 로고
    • Closed circular DNA as a probe for protein-induced structural changes
    • White JH, Gallo RM, Bauer WR. 1992. Closed circular DNA as a probe for protein-induced structural changes. Trends Biochem. Sci. 17: 7-12.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 7-12
    • White, J.H.1    Gallo, R.M.2    Bauer, W.R.3
  • 54
    • 0022861016 scopus 로고
    • Modulation of in vivo and in vitro transcription of bacteriophage ∅29 early genes
    • Whiteley HR, Ramey WD, Spiegelman GB, Holder RD. 1986. Modulation of in vivo and in vitro transcription of bacteriophage ∅29 early genes. Virology 155: 392-401.
    • (1986) Virology , vol.155 , pp. 392-401
    • Whiteley, H.R.1    Ramey, W.D.2    Spiegelman, G.B.3    Holder, R.D.4
  • 55
    • 0027318513 scopus 로고
    • Macromolecular crowding: Biochemical, biophysical, and physiological consequences
    • Zimmerman SB, Minton AP. 1993. Macromolecular crowding: biochemical, biophysical, and physiological consequences. An. Rev. Biophys. Biomol. Struct., 22: 27-65.
    • (1993) An. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 27-65
    • Zimmerman, S.B.1    Minton, A.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.