메뉴 건너뛰기




Volumn 73, Issue 9, 1999, Pages 7357-7367

Identification of amino acid residues of influenza virus nucleoprotein essential for RNA binding

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ARGININE; PHENYLALANINE; RNA POLYMERASE; TRYPTOPHAN; VIRUS NUCLEOPROTEIN; VIRUS RNA;

EID: 0032854172     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.73.9.7357-7367.1999     Document Type: Article
Times cited : (98)

References (50)
  • 1
    • 0029069869 scopus 로고
    • Identification of an RNA binding region within the N-terminal third of the influenza A virus nucleoprotein
    • Albo, C., A. Valencia, and A. Portela. 1995. Identification of an RNA binding region within the N-terminal third of the influenza A virus nucleoprotein. J. Virol. 69:3799-3806.
    • (1995) J. Virol. , vol.69 , pp. 3799-3806
    • Albo, C.1    Valencia, A.2    Portela, A.3
  • 2
    • 0024655246 scopus 로고
    • RNA-binding proteins as developmental regulators
    • Bandziulis, R. J., M. S. Swanson, and G. Dreyfuss. 1989. RNA-binding proteins as developmental regulators. Genes Dev. 3:431-442.
    • (1989) Genes Dev. , vol.3 , pp. 431-442
    • Bandziulis, R.J.1    Swanson, M.S.2    Dreyfuss, G.3
  • 3
    • 0028275669 scopus 로고
    • Structure of influenza RNP. I. Influenza virus nucleoprotein melts secondary structure in panhandle RNA and exposes the bases to solvent
    • Baudin, F., C. Bach, S. Cusak, and R. W. H. Ruigrok. 1994. Structure of influenza RNP. I. Influenza virus nucleoprotein melts secondary structure in panhandle RNA and exposes the bases to solvent. EMBO J. 13:3158-3165.
    • (1994) EM , vol.13 , pp. 3158-3165
    • Baudin, F.1    Bach, C.2    Cusak, S.3    Ruigrok, R.W.H.4    B5    O J6
  • 4
    • 2142778976 scopus 로고
    • Transcription antitermination during influenza viral template RNA synthesis requires the nucleocapsid proteins and the absence of a 5′ capped end
    • Beaton, A. R., and R. M. Krug. 1986. Transcription antitermination during influenza viral template RNA synthesis requires the nucleocapsid proteins and the absence of a 5′ capped end. Proc. Natl. Acad. Sci. USA 83:6282-6286.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 6282-6286
    • Beaton, A.R.1    Krug, R.M.2
  • 5
    • 0031778876 scopus 로고    scopus 로고
    • Influenza virus nucleoprotein interacts with influenza virus polymerase proteins
    • Biswas, S. K., P. L. Boutz, and D. P. Nayak. 1998. Influenza virus nucleoprotein interacts with influenza virus polymerase proteins. J. Virol. 72:5493-5501.
    • (1998) J. Virol. , vol.72 , pp. 5493-5501
    • Biswas, S.K.1    Boutz, P.L.2    Nayak, D.P.3
  • 6
    • 0029968771 scopus 로고    scopus 로고
    • Inhibition of the influenza virus RNA-dependent RNA polymerase by antisera directed against the carboxy-terminal region of the PB2 subunit
    • Blok, V., C. Cianci, K. W. Tibbles, S. C. Inglis, M. Krystal, and P. Digard. 1996. Inhibition of the influenza virus RNA-dependent RNA polymerase by antisera directed against the carboxy-terminal region of the PB2 subunit. J. Gen. Virol. 77:1025-1033.
    • (1996) J. Gen. Virol. , vol.77 , pp. 1025-1033
    • Blok, V.1    Cianci, C.2    Tibbles, K.W.3    Inglis, S.C.4    Krystal, M.5    Digard, P.6
  • 7
    • 0031030449 scopus 로고    scopus 로고
    • Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA
    • Bochkarev, A., R. A. Pfuetzner, A. M. Edwards and L. Frappier. 1997. Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA. Nature 385:176-181.
    • (1997) Nature , vol.385 , pp. 176-181
    • Bochkarev, A.1    Pfuetzner, R.A.2    Edwards, A.M.3    Frappier, L.4
  • 8
    • 0016663420 scopus 로고
    • Interactions of aromatic residues of proteins with nucleic acids. Fluorescence studies of the binding of oligopeptides containing tryptophan and tyrosine residues to polynucleotides
    • Brun, F., J.-J. Toulme, and C. Helene. 1975. Interactions of aromatic residues of proteins with nucleic acids. Fluorescence studies of the binding of oligopeptides containing tryptophan and tyrosine residues to polynucleotides. Biochemistry 14:558-563.
    • (1975) Biochemistry , vol.14 , pp. 558-563
    • Brun, F.1    Toulme, J.-J.2    Helene, C.3
  • 9
    • 0028129989 scopus 로고
    • Conserved structures and diversity of functions of RNA-binding proteins
    • Burd, C. G., and G. Dreyfuss. 1994. Conserved structures and diversity of functions of RNA-binding proteins. Science 265:615-621.
    • (1994) Science , vol.265 , pp. 615-621
    • Burd, C.G.1    Dreyfuss, G.2
  • 11
    • 0242565884 scopus 로고
    • The structure of influenza virus
    • E. D. Kilbourne (ed.), Academic Press, Inc., New York, N.Y.
    • Choppin, P. W., and H. W. Compans. 1975. The structure of influenza virus, p. 15-51. In E. D. Kilbourne (ed.), The influenza viruses and influenza. Academic Press, Inc., New York, N.Y.
    • (1975) The Influenza Viruses and Influenza , pp. 15-51
    • Choppin, P.W.1    Compans, H.W.2
  • 12
    • 0024395266 scopus 로고
    • Complex formation between influenza virus polymerase proteins expressed in Xenopus oocytes
    • Digard, P., V. C. Blok, and S. C. Inglis. 1989. Complex formation between influenza virus polymerase proteins expressed in Xenopus oocytes. Virology 171:162-169.
    • (1989) Virology , vol.171 , pp. 162-169
    • Digard, P.1    Blok, V.C.2    Inglis, S.C.3
  • 13
    • 0032981158 scopus 로고    scopus 로고
    • Modulation of nuclear localization of influenza virus nucleoprotein through interaction with actin filaments
    • Digard, P., D. Elton, K. Bishop, E. Medcalf, A. Weeds, and B. Pope. 1999. Modulation of nuclear localization of influenza virus nucleoprotein through interaction with actin filaments. J. Virol. 73:2222-2231.
    • (1999) J. Virol. , vol.73 , pp. 2222-2231
    • Digard, P.1    Elton, D.2    Bishop, K.3    Medcalf, E.4    Weeds, A.5    Pope, B.6
  • 14
    • 0014693884 scopus 로고
    • Distinct subunits of the ribonucleoprotein of influenza virus
    • Duesberg, P. 1969. Distinct subunits of the ribonucleoprotein of influenza virus. J. Mol. Biol. 42:485-499.
    • (1969) J. Mol. Biol. , vol.42 , pp. 485-499
    • Duesberg, P.1
  • 15
    • 0021252896 scopus 로고
    • Sequences of the male gene and its product, the maltose-binding protein of Escherichia coli K12
    • Duplay, P., H. Bedouelle, A. Fowler, I. Zabin, W. Saurin, and M. Hofnung. 1984. Sequences of the malE gene and its product, the maltose-binding protein of Escherichia coli K12. J. Biol. Chem. 259:10606-10613.
    • (1984) J. Biol. Chem. , vol.259 , pp. 10606-10613
    • Duplay, P.1    Bedouelle, H.2    Fowler, A.3    Zabin, I.4    Saurin, W.5    Hofnung, M.6
  • 16
    • 0033587599 scopus 로고    scopus 로고
    • Oligomerisation of influenza A virus nucleoprotein: Identification of positive and negative sequence elements
    • in press
    • Elton, D., E. Medcalf, K. Bishop, and P. Digard. Oligomerisation of influenza A virus nucleoprotein: identification of positive and negative sequence elements. Virology, in press.
    • Virology
    • Elton, D.1    Medcalf, E.2    Bishop, K.3    Digard, P.4
  • 17
    • 77957004481 scopus 로고
    • The rapid determination of amino groups with TNBS
    • Fields, R. 1972. The rapid determination of amino groups with TNBS. Methods Enzymol. 25:464-468.
    • (1972) Methods Enzymol. , vol.25 , pp. 464-468
    • Fields, R.1
  • 18
    • 0023373687 scopus 로고
    • Use of a hybrid vaccinia virus-T7 RNA polymerase system for expression of target genes
    • Fuerst, T. R., P. L. Earl, and B. Moss. 1987. Use of a hybrid vaccinia virus-T7 RNA polymerase system for expression of target genes. Mol. Cell. Biol. 7: 2538-2544.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2538-2544
    • Fuerst, T.R.1    Earl, P.L.2    Moss, B.3
  • 19
    • 0014800618 scopus 로고
    • The effect of polyvinylsulphate on the ribonucleoprotein of influenza virus
    • Goldstein, E. A., and M. W. Pons. 1970. The effect of polyvinylsulphate on the ribonucleoprotein of influenza virus. Virology 41:382-384.
    • (1970) Virology , vol.41 , pp. 382-384
    • Goldstein, E.A.1    Pons, M.W.2
  • 20
    • 0026757694 scopus 로고
    • Interaction of the RNA-binding domain of the hnRNP c proteins with RNA
    • Gorlach, M., M. Wittekind, R. A. Beckman, L. Mueller, and G. Dreyfuss. 1992. Interaction of the RNA-binding domain of the hnRNP C proteins with RNA. EMBO J. 11:3289-3295.
    • (1992) EMBO J. , vol.11 , pp. 3289-3295
    • Gorlach, M.1    Wittekind, M.2    Beckman, R.A.3    Mueller, L.4    Dreyfuss, G.5
  • 21
    • 0023680201 scopus 로고
    • Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose-binding protein
    • Guan, C., P. Li, P. D. Riggs, and H. Inouye. 1987. Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose-binding protein. Gene 67:21-30.
    • (1987) Gene , vol.67 , pp. 21-30
    • Guan, C.1    Li, P.2    Riggs, P.D.3    Inouye, H.4
  • 22
    • 0013889689 scopus 로고
    • Determination of free amino groups in proteins by trinitrobenzenesulfonic acid
    • Habeeb, A. F. S. A. 1966. Determination of free amino groups in proteins by trinitrobenzenesulfonic acid. Anal. Biochem. 14:328-336.
    • (1966) Anal. Biochem. , vol.14 , pp. 328-336
    • Habeeb, A.F.S.A.1
  • 23
    • 0024263928 scopus 로고
    • RNA polymerase of influenza virus: Role of NP on RNA chain elongation
    • Honda, A., K. Ueda, K. Nagata, and A. Ishihama. 1988. RNA polymerase of influenza virus: role of NP on RNA chain elongation. J. Biochem. 104: 1021-1026.
    • (1988) J. Biochem. , vol.104 , pp. 1021-1026
    • Honda, A.1    Ueda, K.2    Nagata, K.3    Ishihama, A.4
  • 24
    • 0024990401 scopus 로고
    • Determination of influenza virus proteins required for genome replication
    • Huang, T.-S., P. Palese, and M. Krystal. 1990. Determination of influenza virus proteins required for genome replication. J. Virol. 64:5669-5673.
    • (1990) J. Virol. , vol.64 , pp. 5669-5673
    • Huang, T.-S.1    Palese, P.2    Krystal, M.3
  • 25
    • 0020826340 scopus 로고
    • Does the higher order structure of the influenza virus ribonucleoprotein guide the sequence rearrangements in influenza viral RNA?
    • Jennings, P. A., J. T. Finch, G. Winter, and J. S. Robertson. 1983. Does the higher order structure of the influenza virus ribonucleoprotein guide the sequence rearrangements in influenza viral RNA? Cell 34:619-627.
    • (1983) Cell , vol.34 , pp. 619-627
    • Jennings, P.A.1    Finch, J.T.2    Winter, G.3    Robertson, J.S.4
  • 26
    • 0025938601 scopus 로고
    • Identification of molecular contacts between the U1 A small nuclear ribonucleoprotein and U1 RNA
    • Jessen, T. H., C. Oubridge, C. H. Teo, C. Pritchard, and K. Nagai. 1991. Identification of molecular contacts between the U1 A small nuclear ribonucleoprotein and U1 RNA. EMBO J. 10:3447-3456.
    • (1991) EMBO J. , vol.10 , pp. 3447-3456
    • Jessen, T.H.1    Oubridge, C.2    Teo, C.H.3    Pritchard, C.4    Nagai, K.5
  • 27
    • 0023095557 scopus 로고
    • Assembly of influenza ribonucleoprotein in vitro using recombinant nucleoprotein
    • Kingsbury, D. W., I. M. Jones, and K. G. Murti. 1987. Assembly of influenza ribonucleoprotein in vitro using recombinant nucleoprotein. Virology 156: 396-403.
    • (1987) Virology , vol.156 , pp. 396-403
    • Kingsbury, D.W.1    Jones, I.M.2    Murti, K.G.3
  • 28
    • 0031003878 scopus 로고    scopus 로고
    • Roles of the influenza virus polymerase and nucleoprotein in forming a functional RNP structure
    • Klump, K., R. W. H. Ruigrok, and F. Baudin. 1997. Roles of the influenza virus polymerase and nucleoprotein in forming a functional RNP structure. EMBO J. 16:1248-1257.
    • (1997) EMBO J. , vol.16 , pp. 1248-1257
    • Klump, K.1    Ruigrok, R.W.H.2    Baudin, F.3
  • 29
    • 0028131905 scopus 로고
    • Molecular dissection of influenza virus nucleoprotein: Deletion mapping of the RNA binding domain
    • Kobayashi, M., T. Toyoda, D. M. Adyshev, Y. Azuma, and A. Ishihama. 1994. Molecular dissection of influenza virus nucleoprotein: deletion mapping of the RNA binding domain. J. Virol. 68:8433-8436.
    • (1994) J. Virol. , vol.68 , pp. 8433-8436
    • Kobayashi, M.1    Toyoda, T.2    Adyshev, D.M.3    Azuma, Y.4    Ishihama, A.5
  • 30
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. A. 1985. Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl. Acad. Sci. USA 82:488-492.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 31
    • 0001178028 scopus 로고    scopus 로고
    • Orthomyxoviridae: The viruses and their replication
    • B. N. Fields, D. M. Knipe, P. M. Howley, et al. (ed.), Lippincott-Raven, Philadelphia, Pa
    • Lamb, R. A., and R. M. Krug. 1996. Orthomyxoviridae: the viruses and their replication, p. 1353-1396. In B. N. Fields, D. M. Knipe, P. M. Howley, et al. (ed.), Fields virology, 3rd ed. Lippincott-Raven, Philadelphia, Pa.
    • (1996) Fields Virology, 3rd Ed. , pp. 1353-1396
    • Lamb, R.A.1    Krug, R.M.2
  • 32
    • 0017637023 scopus 로고
    • Cleavage at aspartyl-prolyl bonds
    • Landon, M. 1977. Cleavage at aspartyl-prolyl bonds. Methods Enzymol. 47: 145-149.
    • (1977) Methods Enzymol. , vol.47 , pp. 145-149
    • Landon, M.1
  • 33
    • 0024549976 scopus 로고
    • Complementation and analysis of an NP mutant of influenza virus
    • Li, R., P. Palese, and M. Krystal. 1989. Complementation and analysis of an NP mutant of influenza virus. Virus Res. 12:97-112.
    • (1989) Virus Res. , vol.12 , pp. 97-112
    • Li, R.1    Palese, P.2    Krystal, M.3
  • 34
    • 0024593153 scopus 로고
    • Localisation of the temperature-sensitive defect in the nucleoprotein of an influenza A/FPV/Rostock/34 virus
    • Mandler, J., and C. Scholtissek. 1989. Localisation of the temperature-sensitive defect in the nucleoprotein of an influenza A/FPV/Rostock/34 virus. Virus Res. 12:113.
    • (1989) Virus Res. , vol.12 , pp. 113
    • Mandler, J.1    Scholtissek, C.2
  • 35
    • 0032837329 scopus 로고    scopus 로고
    • Temperature-sensitive lesions in two influenza A viruses defective for replicative transcription disrupt RNA binding by the nucleoprotein
    • Medcalf, L., E. Poole, D. Elton, and P. Digard. 1999. Temperature-sensitive lesions in two influenza A viruses defective for replicative transcription disrupt RNA binding by the nucleoprotein. J. Virol. 73:7349-7356.
    • (1999) J. Virol. , vol.73 , pp. 7349-7356
    • Medcalf, L.1    Poole, E.2    Elton, D.3    Digard, P.4
  • 36
    • 0028979910 scopus 로고
    • NPI-1, the human homologue of SRP-1, interacts with influenza virus nucleoprotein
    • O'Neill, R. E., and P. Palese. 1995. NPI-1, the human homologue of SRP-1, interacts with influenza virus nucleoprotein. Virology 206:116-125.
    • (1995) Virology , vol.206 , pp. 116-125
    • O'Neill, R.E.1    Palese, P.2
  • 37
    • 0029130751 scopus 로고
    • Nuclear import of influenza virus RNA can be mediated by viral nucleoprotein and transport factors required for protein import
    • O'Neill, R. E., R. Jaskunas, G. Blobel, P. Palese, and J. Moroianu. 1995. Nuclear import of influenza virus RNA can be mediated by viral nucleoprotein and transport factors required for protein import. J. Biol. Chem. 270: 22701-22704.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22701-22704
    • O'Neill, R.E.1    Jaskunas, R.2    Blobel, G.3    Palese, P.4    Moroianu, J.5
  • 38
    • 0028004607 scopus 로고
    • Crystal structure at 1.92 Å resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin
    • Oubridge, C., N. Ito, P. R. Evans, C.-H. Teo, and K. Nagai. 1994. Crystal structure at 1.92 Å resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin. Nature 372:432-438.
    • (1994) Nature , vol.372 , pp. 432-438
    • Oubridge, C.1    Ito, N.2    Evans, P.R.3    Teo, C.-H.4    Nagai, K.5
  • 39
    • 0014591650 scopus 로고
    • Isolation and characterization of the ribonucleoprotein of influenza virus
    • Pons, M. W., I. T. Schulze, G. K. Hirst, and R. Hauser. 1969. Isolation and characterization of the ribonucleoprotein of influenza virus. Virology 39: 250-259.
    • (1969) Virology , vol.39 , pp. 250-259
    • Pons, M.W.1    Schulze, I.T.2    Hirst, G.K.3    Hauser, R.4
  • 40
    • 0028873824 scopus 로고
    • Dissecting RNA-protein interactions: RNA-RNA recognition by Rop
    • Predki, P. F., L. M. Nayak, M. B. C. Gottlieb, and L. Regan. 1995. Dissecting RNA-protein interactions: RNA-RNA recognition by Rop. Cell 80:41-50.
    • (1995) Cell , vol.80 , pp. 41-50
    • Predki, P.F.1    Nayak, L.M.2    Gottlieb, M.B.C.3    Regan, L.4
  • 41
    • 0028916010 scopus 로고
    • Structure of influenza virus ribonucleoprotein particles. II. Purified RNA-free influenza virus ribonucleoprotein forms structures that are indistinguishable from the intact influenza virus ribonucleoprotein particles
    • Ruigrok, R. W. H., and F. Baudin. 1995. Structure of influenza virus ribonucleoprotein particles. II. Purified RNA-free influenza virus ribonucleoprotein forms structures that are indistinguishable from the intact influenza virus ribonucleoprotein particles. J. Gen. Virol. 76:1009-1014.
    • (1995) J. Gen. Virol. , vol.76 , pp. 1009-1014
    • Ruigrok, R.W.H.1    Baudin, F.2
  • 42
    • 0000722070 scopus 로고
    • Spectral methods of characterising protein conformation and conformational changes
    • T. E. Creighton (ed.), IRL Press, Oxford, United Kingdom
    • Schmid, F. X. 1989. Spectral methods of characterising protein conformation and conformational changes, p 251-285. In T. E. Creighton (ed.), Protein structure. A practical approach. IRL Press, Oxford, United Kingdom.
    • (1989) Protein Structure. A Practical Approach , pp. 251-285
    • Schmid, F.X.1
  • 43
    • 0014977403 scopus 로고
    • Binding of ribonucleic acids to the RNP-antigen protein of influenza viruses
    • Scholtissek, C., and H. Becht. 1971. Binding of ribonucleic acids to the RNP-antigen protein of influenza viruses. J. Gen. Virol. 10:11-16.
    • (1971) J. Gen. Virol. , vol.10 , pp. 11-16
    • Scholtissek, C.1    Becht, H.2
  • 44
    • 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
  • 45
    • 0023948949 scopus 로고
    • Influenza virus RNA replication in vitro: Synthesis of viral template RNAs and virion RNAs in the absence of an added primer
    • Shapiro, G. I., and R. M. Krug. 1988. Influenza virus RNA replication in vitro: synthesis of viral template RNAs and virion RNAs in the absence of an added primer. J. Virol. 62:2285-2290.
    • (1988) J. Virol. , vol.62 , pp. 2285-2290
    • Shapiro, G.I.1    Krug, R.M.2
  • 46
    • 0023433327 scopus 로고
    • Synthesis and cellular location of the ten influenza polypeptides individually expressed by recombinant vaccinia viruses
    • Smith, G. L., J. Z. Levin, P. Palese, and B. Moss. 1987. Synthesis and cellular location of the ten influenza polypeptides individually expressed by recombinant vaccinia viruses. Virology 160:336-345.
    • (1987) Virology , vol.160 , pp. 336-345
    • Smith, G.L.1    Levin, J.Z.2    Palese, P.3    Moss, B.4
  • 47
    • 0031058042 scopus 로고    scopus 로고
    • The NPI-1/NPI-3 (karyopherin α) binding site on the influenza A virus nucleoprotein NP is a nonconventional nuclear localization signal
    • Wang, P., P. Palese, and R. E. O'Neil. 1997. The NPI-1/NPI-3 (karyopherin α) binding site on the influenza A virus nucleoprotein NP is a nonconventional nuclear localization signal. J. Virol. 71:1850-1856.
    • (1997) J. Virol. , vol.71 , pp. 1850-1856
    • Wang, P.1    Palese, P.2    O'Neil, R.E.3
  • 48
    • 0019416519 scopus 로고
    • The structure of the gene encoding the nucleoprotein of human influenza virus A/PR/8/34
    • Winter, G., and S. Fields. 1981. The structure of the gene encoding the nucleoprotein of human influenza virus A/PR/8/34. Virology 114:423-428.
    • (1981) Virology , vol.114 , pp. 423-428
    • Winter, G.1    Fields, S.2
  • 49
    • 0025299610 scopus 로고
    • Reconstitution of influenza virus RNA-nucleoprotein complexes structurally resembling native viral ribonucleoprotein cores
    • Yamanaka, K., A. Ishihama, and K. Nagata. 1990. Reconstitution of influenza virus RNA-nucleoprotein complexes structurally resembling native viral ribonucleoprotein cores. J. Biol. Chem. 265:11151-11155.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11151-11155
    • Yamanaka, K.1    Ishihama, A.2    Nagata, K.3
  • 50
    • 0019276655 scopus 로고
    • Modification of available arginine residues in proteins by p-hydroxyphenylglyoxal
    • Yamasaki, R. B., A. Vega, and R. E. Feeney. 1980. Modification of available arginine residues in proteins by p-hydroxyphenylglyoxal. Anal. Biochem. 109: 32-40.
    • (1980) Anal. Biochem. , vol.109 , pp. 32-40
    • Yamasaki, R.B.1    Vega, A.2    Feeney, R.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.