메뉴 건너뛰기




Volumn 44, Issue 4, 2007, Pages 541-557

Mapping and molecular characterization of novel monoclonal antibodies to conformational epitopes on NH2 and COOH termini of mammalian tryptophanyl-tRNA synthetase reveal link of the epitopes to aggregation and Alzheimer's disease

Author keywords

Aggregation disaggregation; Alzheimer's disease; Aminoacyl tRNA synthetases; Epitope mapping; Monoclonal antibodies; Neuroblastoma; Pancreatic, cervical and kidney cancer cells

Indexed keywords

6C10 ANTIBODY; 9D7 ANTIBODY; AMIDE; ASPARTIC ACID; CARBOXYLIC ACID; EPITOPE; IMMUNOGLOBULIN G1 ANTIBODY; METHIONINE; MONOCLONAL ANTIBODY; MONOMER; OLIGOMER; RECOMBINANT ENZYME; SERINE; TRYPTOPHAN TRANSFER RNA LIGASE; TYROSINE; UNCLASSIFIED DRUG;

EID: 33748632378     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molimm.2006.02.006     Document Type: Article
Times cited : (25)

References (61)
  • 2
    • 0024459804 scopus 로고
    • Molecular and cellular studies of tryptophanyl-tRNA synthetase using monoclonal antibodies. Evaluation of a common antigenic determinant in eukaryotic, prokaryotic and archaebacterial enzymes which maps outside the catalytic domain
    • Beresten S.F., Zargarova T.A., Favorova O.O., Rubikaite B.I., Ryazanov A.G., and Kisselev L.L. Molecular and cellular studies of tryptophanyl-tRNA synthetase using monoclonal antibodies. Evaluation of a common antigenic determinant in eukaryotic, prokaryotic and archaebacterial enzymes which maps outside the catalytic domain. Eur. J. Biochem. 184 (1989) 575-581
    • (1989) Eur. J. Biochem. , vol.184 , pp. 575-581
    • Beresten, S.F.1    Zargarova, T.A.2    Favorova, O.O.3    Rubikaite, B.I.4    Ryazanov, A.G.5    Kisselev, L.L.6
  • 3
    • 0015817744 scopus 로고
    • Morphology and growth, tumorigenicity, and cytogenetics of human neuroblastoma cells in continuous culture
    • Biedler J., Helson L., and Spengler B.A. Morphology and growth, tumorigenicity, and cytogenetics of human neuroblastoma cells in continuous culture. Cancer Res. 33 (1973) 2643-2652
    • (1973) Cancer Res. , vol.33 , pp. 2643-2652
    • Biedler, J.1    Helson, L.2    Spengler, B.A.3
  • 4
    • 0032112043 scopus 로고    scopus 로고
    • Autoantibodies to tryptophanyl-tRNA-synthetase in systemic autoimmune diseases
    • Bolgarin R.N., Rodnin N.V., and Sidorik L.L. Autoantibodies to tryptophanyl-tRNA-synthetase in systemic autoimmune diseases. Mol. Biol. (Mosk.) 32 (1998) 745-749
    • (1998) Mol. Biol. (Mosk.) , vol.32 , pp. 745-749
    • Bolgarin, R.N.1    Rodnin, N.V.2    Sidorik, L.L.3
  • 5
    • 0034653970 scopus 로고    scopus 로고
    • 117 → Val mutation
    • 117 → Val mutation. Biochem. J. 346 (2000) 785-791
    • (2000) Biochem. J. , vol.346 , pp. 785-791
    • Brown, D.R.1
  • 6
    • 0035139831 scopus 로고    scopus 로고
    • Purification and properties of a GTPase-activating protein for yeast Rab GTPases
    • Du L.L., and Novick P. Purification and properties of a GTPase-activating protein for yeast Rab GTPases. Methods Enzymol. 329 (2001) 91-99
    • (2001) Methods Enzymol. , vol.329 , pp. 91-99
    • Du, L.L.1    Novick, P.2
  • 7
    • 0035874389 scopus 로고    scopus 로고
    • The rational design of a 'type 88' genetically stable peptide display vector in the filamentous bacteriophage fd
    • Enshell-Seijffers D., Smelyanski L., and Gershoni J.M. The rational design of a 'type 88' genetically stable peptide display vector in the filamentous bacteriophage fd. Nucl. Acids Res. 29 (2001) E50-0
    • (2001) Nucl. Acids Res. , vol.29
    • Enshell-Seijffers, D.1    Smelyanski, L.2    Gershoni, J.M.3
  • 8
    • 85060773995 scopus 로고    scopus 로고
    • Phage-display selection and analysis of Ab-binding epitopes
    • Coligan A.M.K., Margulies D.H., and Strober W. (Eds), John Wiley & Sons, New York
    • Enshell-Siejffers D., and Gershoni J.M. Phage-display selection and analysis of Ab-binding epitopes. In: Coligan A.M.K., Margulies D.H., and Strober W. (Eds). Current Protocols in Immunology (2002), John Wiley & Sons, New York
    • (2002) Current Protocols in Immunology
    • Enshell-Siejffers, D.1    Gershoni, J.M.2
  • 10
    • 0024437165 scopus 로고
    • Molecular and cellular studies of tryptophanyl-tRNA synthetases using monoclonal antibodies. Remarkable variations in the content of tryptophanyl-tRNA synthetase in the pancreas of different mammals
    • Favorova O.O., Zargarova T.A., Rukosuyev V.S., Beresten S.F., and Kisselev L.L. Molecular and cellular studies of tryptophanyl-tRNA synthetases using monoclonal antibodies. Remarkable variations in the content of tryptophanyl-tRNA synthetase in the pancreas of different mammals. Eur. J. Biochem. 184 (1989) 583-588
    • (1989) Eur. J. Biochem. , vol.184 , pp. 583-588
    • Favorova, O.O.1    Zargarova, T.A.2    Rukosuyev, V.S.3    Beresten, S.F.4    Kisselev, L.L.5
  • 11
  • 12
    • 0026286195 scopus 로고
    • Monoclonal antibodies to the components of the high-molecular-mass aminoacyl-tRNA synthetase complex
    • Filonenko V.V., Wolfson A.D., Wartanyan O.A., and Beresten S.F. Monoclonal antibodies to the components of the high-molecular-mass aminoacyl-tRNA synthetase complex. Biomed. Sci. 2 (1991) 289-292
    • (1991) Biomed. Sci. , vol.2 , pp. 289-292
    • Filonenko, V.V.1    Wolfson, A.D.2    Wartanyan, O.A.3    Beresten, S.F.4
  • 13
    • 0028264012 scopus 로고
    • Evidence for similar structural organization of the multienzyme aminoacyl-tRNA synthetase complex in vivo and in vitro
    • Filonenko V.V., and Deutscher M.P. Evidence for similar structural organization of the multienzyme aminoacyl-tRNA synthetase complex in vivo and in vitro. J. Biol. Chem. 269 (1994) 17375-17378
    • (1994) J. Biol. Chem. , vol.269 , pp. 17375-17378
    • Filonenko, V.V.1    Deutscher, M.P.2
  • 16
    • 0026351552 scopus 로고
    • Cloning and nucleotide sequence of the structural gene encoding for human tryptophanyl-tRNA synthetase
    • Frolova L.Yu., Sudomoina M.A., Grigorieva A.Yu., Zinovieva O.L., and Kisselev L.L. Cloning and nucleotide sequence of the structural gene encoding for human tryptophanyl-tRNA synthetase. Gene 109 (1991) 291-296
    • (1991) Gene , vol.109 , pp. 291-296
    • Frolova, L.Yu.1    Sudomoina, M.A.2    Grigorieva, A.Yu.3    Zinovieva, O.L.4    Kisselev, L.L.5
  • 17
    • 0019739585 scopus 로고
    • Preparation of monoclonal antibodies: strategies and procedures
    • Galfre G., and Milstein C. Preparation of monoclonal antibodies: strategies and procedures. Methods Enzymol. 73 Pt B (1981) 3-46
    • (1981) Methods Enzymol. , vol.73 , Issue.PART B , pp. 3-46
    • Galfre, G.1    Milstein, C.2
  • 19
    • 1342279255 scopus 로고    scopus 로고
    • Protein profiling of the human epidermis from the elderly reveals up-regulation of a signature of interferon-{gamma}-induced polypeptides that includes manganese-superoxide dismutase and the p85{beta} subunit of phosphatidylinositol 3-kinase
    • Gromov P., Skovgaard G.L., Palsdottir H., Gromova I., Ostergaard M., and Celis J.E. Protein profiling of the human epidermis from the elderly reveals up-regulation of a signature of interferon-{gamma}-induced polypeptides that includes manganese-superoxide dismutase and the p85{beta} subunit of phosphatidylinositol 3-kinase. Mol. Cell. Proteomics 2 (2003) 70-84
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 70-84
    • Gromov, P.1    Skovgaard, G.L.2    Palsdottir, H.3    Gromova, I.4    Ostergaard, M.5    Celis, J.E.6
  • 20
    • 0015500971 scopus 로고
    • The subunit structure of tryptophanyl transfer ribonucleic acid synthetase from beef pancreas
    • Gros C., Le Maire G., Van Rapenbusch R., and Labouesse B. The subunit structure of tryptophanyl transfer ribonucleic acid synthetase from beef pancreas. J. Biol. Chem. 247 (1972) 2931-2943
    • (1972) J. Biol. Chem. , vol.247 , pp. 2931-2943
    • Gros, C.1    Le Maire, G.2    Van Rapenbusch, R.3    Labouesse, B.4
  • 21
    • 0020329044 scopus 로고
    • The nucleotide sequence of the structural gene for Escherichia coli tryptophanyl-tRNA synthetase
    • Hall C.V., vanCleemput M., Muench K.H., and Yanofsky C. The nucleotide sequence of the structural gene for Escherichia coli tryptophanyl-tRNA synthetase. J. Biol. Chem. 257 (1982) 6132-6136
    • (1982) J. Biol. Chem. , vol.257 , pp. 6132-6136
    • Hall, C.V.1    vanCleemput, M.2    Muench, K.H.3    Yanofsky, C.4
  • 22
    • 0000358981 scopus 로고
    • Storing and purifying antibodies
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Harlow E., and Lane D. Storing and purifying antibodies. Antibodies: A Laboratory Manual (1988), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY 283-319
    • (1988) Antibodies: A Laboratory Manual , pp. 283-319
    • Harlow, E.1    Lane, D.2
  • 24
    • 84873781652 scopus 로고
    • Development and characteristics of the rabbit kidney cell strain, LLC-RK1
    • Hull R.N., Dwyer A.C., Cherry W.R., and Tritch O.J. Development and characteristics of the rabbit kidney cell strain, LLC-RK1. Proc. Soc. Exp. Biol. Med. 118 (1965) 1054-1059
    • (1965) Proc. Soc. Exp. Biol. Med. , vol.118 , pp. 1054-1059
    • Hull, R.N.1    Dwyer, A.C.2    Cherry, W.R.3    Tritch, O.J.4
  • 25
    • 0016834992 scopus 로고
    • Structure-activity relationships in tryptophanyl transfer ribonucleic acid synthetase from beef pancreas. Influence of alkylation of the sulfhydryl groups on the dimer-monomer equilibrium
    • Iborra F., Labouesse B., and Labouesse J. Structure-activity relationships in tryptophanyl transfer ribonucleic acid synthetase from beef pancreas. Influence of alkylation of the sulfhydryl groups on the dimer-monomer equilibrium. J. Biol. Chem. 250 (1975) 6659-6665
    • (1975) J. Biol. Chem. , vol.250 , pp. 6659-6665
    • Iborra, F.1    Labouesse, B.2    Labouesse, J.3
  • 26
    • 12744278411 scopus 로고    scopus 로고
    • Cytokine-like activities of some aminoacyl-tRNA synthetases and auxiliary p43 cofactor of aminoacylation reaction and their role in oncogenesis
    • Ivakhno S.S., and Kornelyuk A.I. Cytokine-like activities of some aminoacyl-tRNA synthetases and auxiliary p43 cofactor of aminoacylation reaction and their role in oncogenesis. Exp. Oncol. 26 (2004) 250-255
    • (2004) Exp. Oncol. , vol.26 , pp. 250-255
    • Ivakhno, S.S.1    Kornelyuk, A.I.2
  • 27
    • 0027601316 scopus 로고
    • Comparative study of localization of tryptophanyl-tRNA-synthetase and components of high molecular weight aminoacyl-tRNA-synthetase complex in animal cells
    • Ivanova Iu.L., Cherni N.E., Popenko V.I., Filonenko V.V., and Vartanian O.G. Comparative study of localization of tryptophanyl-tRNA-synthetase and components of high molecular weight aminoacyl-tRNA-synthetase complex in animal cells. Mol. Biol. (Mosk.) 27 (1993) 666-684
    • (1993) Mol. Biol. (Mosk.) , vol.27 , pp. 666-684
    • Ivanova, Iu.L.1    Cherni, N.E.2    Popenko, V.I.3    Filonenko, V.V.4    Vartanian, O.G.5
  • 28
    • 0034595624 scopus 로고    scopus 로고
    • Identification and characterization of human mitochondrial tryptophanyl-tRNA synthetase
    • Jorgensen R., Sogaard T.M., Rossing A.B., Martensen P.M., and Justesen J. Identification and characterization of human mitochondrial tryptophanyl-tRNA synthetase. J. Biol. Chem. 275 (2000) 16820-16826
    • (2000) J. Biol. Chem. , vol.275 , pp. 16820-16826
    • Jorgensen, R.1    Sogaard, T.M.2    Rossing, A.B.3    Martensen, P.M.4    Justesen, J.5
  • 30
    • 0027423060 scopus 로고
    • Cloning and analysis of a cDNA encoding mammalian arginyl-tRNA synthetase, a component of the multisynthetase complex with a hydrophobic N-terminal extension
    • Lazard M., and Mirande M. Cloning and analysis of a cDNA encoding mammalian arginyl-tRNA synthetase, a component of the multisynthetase complex with a hydrophobic N-terminal extension. Gene 132 (1993) 237-245
    • (1993) Gene , vol.132 , pp. 237-245
    • Lazard, M.1    Mirande, M.2
  • 31
    • 1942435278 scopus 로고    scopus 로고
    • Study of protein aggregation using two-dimensional correlation infrared spectroscopy and spectral simulations
    • Lefevre T., Arseneault K., and Pezolet M. Study of protein aggregation using two-dimensional correlation infrared spectroscopy and spectral simulations. Biopolymers 73 (2004) 705-715
    • (2004) Biopolymers , vol.73 , pp. 705-715
    • Lefevre, T.1    Arseneault, K.2    Pezolet, M.3
  • 33
    • 0016793022 scopus 로고
    • Establishment of a continuous tumor-cell line (panc-1) from a human carcinoma of the exocrine pancreas
    • Lieber M., Mazzetta J., Nelson-Rees W., Kaplan M., and Todaro G. Establishment of a continuous tumor-cell line (panc-1) from a human carcinoma of the exocrine pancreas. Int. J. Cancer 15 (1975) 741-747
    • (1975) Int. J. Cancer , vol.15 , pp. 741-747
    • Lieber, M.1    Mazzetta, J.2    Nelson-Rees, W.3    Kaplan, M.4    Todaro, G.5
  • 34
    • 0017098572 scopus 로고
    • Human tryptophanyl transfer ribonucleic acid synthetase. Composition, function of thiol groups, and structure of thiol peptides
    • Lipscomb M.S., Lee M.-L., and Muench K.H. Human tryptophanyl transfer ribonucleic acid synthetase. Composition, function of thiol groups, and structure of thiol peptides. J. Biol. Chem. 251 (1976) 3261-3268
    • (1976) J. Biol. Chem. , vol.251 , pp. 3261-3268
    • Lipscomb, M.S.1    Lee, M.-L.2    Muench, K.H.3
  • 35
    • 0036454809 scopus 로고    scopus 로고
    • Analysis of gene expression during maturation of immature dendritic cells derived from peripheral blood monocytes
    • Matsunaga T., Ishida T., Takekawa M., Nishimura S., Adachi M., and Imai K. Analysis of gene expression during maturation of immature dendritic cells derived from peripheral blood monocytes. Scand. J. Immunol. 56 (2002) 593-601
    • (2002) Scand. J. Immunol. , vol.56 , pp. 593-601
    • Matsunaga, T.1    Ishida, T.2    Takekawa, M.3    Nishimura, S.4    Adachi, M.5    Imai, K.6
  • 36
    • 0025641623 scopus 로고
    • The role of an autoantigen, histidyl-tRNA synthetase, in the induction and maintenance of autoimmunity
    • Miller F.W., Waite K.A., Biswas T., and Plotz P.H. The role of an autoantigen, histidyl-tRNA synthetase, in the induction and maintenance of autoimmunity. Proc. Natl. Acad. Sci. U.S.A. 87 (1990) 9933-9937
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 9933-9937
    • Miller, F.W.1    Waite, K.A.2    Biswas, T.3    Plotz, P.H.4
  • 37
    • 0036281211 scopus 로고    scopus 로고
    • Processing of gene expression data generated by quantitative real-time RT-PCR
    • Muller P.Y., Janovjak H., Miserez A.R., and Dobbie Z. Processing of gene expression data generated by quantitative real-time RT-PCR. Biotechniques 32 (2002) 1372-1379
    • (2002) Biotechniques , vol.32 , pp. 1372-1379
    • Muller, P.Y.1    Janovjak, H.2    Miserez, A.R.3    Dobbie, Z.4
  • 38
    • 0024419067 scopus 로고
    • Isolation and electron microscopic characterization of the high molecular mass aminoacyl-tRNA synthetase complex from murine erthroleukemia cells
    • Norcum M.T. Isolation and electron microscopic characterization of the high molecular mass aminoacyl-tRNA synthetase complex from murine erthroleukemia cells. J. Biol. Chem. 284 (1989) 15043-15061
    • (1989) J. Biol. Chem. , vol.284 , pp. 15043-15061
    • Norcum, M.T.1
  • 39
    • 1242293857 scopus 로고    scopus 로고
    • Gene expression in the elicitation phase of guinea pig DTH and CHS reactions
    • Ohtani M., Kobayashi Y., and Watanabe N. Gene expression in the elicitation phase of guinea pig DTH and CHS reactions. Cytokine 25 (2004) 246-253
    • (2004) Cytokine , vol.25 , pp. 246-253
    • Ohtani, M.1    Kobayashi, Y.2    Watanabe, N.3
  • 40
    • 0028075594 scopus 로고
    • An alternative splicing modifies the C-terminal end of tryptophanyl-tRNA synthetase in murine embryonic stem cells
    • Pajot B., Sarger C., Bonnet J., and Garret M. An alternative splicing modifies the C-terminal end of tryptophanyl-tRNA synthetase in murine embryonic stem cells. J. Mol. Biol. 242 (1994) 599-603
    • (1994) J. Mol. Biol. , vol.242 , pp. 599-603
    • Pajot, B.1    Sarger, C.2    Bonnet, J.3    Garret, M.4
  • 41
    • 0025896135 scopus 로고
    • Tryptophanyl-tRNA synthetase in cell lines resistant to tryptophan analogs
    • Paley E.L., Baranov V.N., Alexandrova N.M., and Kisselev L.L. Tryptophanyl-tRNA synthetase in cell lines resistant to tryptophan analogs. Exp. Cell Res. 195 (1991) 66-78
    • (1991) Exp. Cell Res. , vol.195 , pp. 66-78
    • Paley, E.L.1    Baranov, V.N.2    Alexandrova, N.M.3    Kisselev, L.L.4
  • 42
    • 0029597925 scopus 로고
    • Tryptophanyl-tRNA synthetase as a human antigen
    • Paley E.L., Alexandrova N., and Smelansky L. Tryptophanyl-tRNA synthetase as a human antigen. Immunol. Lett. 48 (1995) 201-207
    • (1995) Immunol. Lett. , vol.48 , pp. 201-207
    • Paley, E.L.1    Alexandrova, N.2    Smelansky, L.3
  • 43
    • 0030997080 scopus 로고    scopus 로고
    • A mammalian tryptophanyl-tRNA synthetase is associated with protein kinase activity
    • Paley E.L. A mammalian tryptophanyl-tRNA synthetase is associated with protein kinase activity. Eur. J. Biochem. 244 (1997) 780-788
    • (1997) Eur. J. Biochem. , vol.244 , pp. 780-788
    • Paley, E.L.1
  • 44
    • 0032901623 scopus 로고    scopus 로고
    • Tryptamine-mediated stabilization of tryptophanyl-tRNA synthetase in human cervical carcinoma cell line
    • Paley E.L. Tryptamine-mediated stabilization of tryptophanyl-tRNA synthetase in human cervical carcinoma cell line. Cancer Lett. 137 (1999) 1-7
    • (1999) Cancer Lett. , vol.137 , pp. 1-7
    • Paley, E.L.1
  • 45
    • 0015976679 scopus 로고
    • Human placental transfer ribonucleic acid synthetase. Purification and subunit structure
    • Penneyes N.S., and Muench K.H. Human placental transfer ribonucleic acid synthetase. Purification and subunit structure. Biochemistry 13 (1974) 560-565
    • (1974) Biochemistry , vol.13 , pp. 560-565
    • Penneyes, N.S.1    Muench, K.H.2
  • 47
    • 0027983773 scopus 로고
    • A motif in human histidyl-tRNA synthetase which is shared among several aminoacyl-tRNA synthetases is a coiled-coil that is essential for enzymatic activity and contains the major autoantigenic epitope
    • Raben N., Nichols R., Dohlman J., McPhien P., Sridharll V., Hydell C., Richard Leff R., and Plotz P. A motif in human histidyl-tRNA synthetase which is shared among several aminoacyl-tRNA synthetases is a coiled-coil that is essential for enzymatic activity and contains the major autoantigenic epitope. J. Biol. Chem. 269 (1994) 24277-24283
    • (1994) J. Biol. Chem. , vol.269 , pp. 24277-24283
    • Raben, N.1    Nichols, R.2    Dohlman, J.3    McPhien, P.4    Sridharll, V.5    Hydell, C.6    Richard Leff, R.7    Plotz, P.8
  • 48
    • 0024404419 scopus 로고
    • Epitope mapping of the cloned human autoantigen, histidyl-tRNA synthetase. Analysis of the myositis-associated anti-Jo-1 autoimmune response
    • Ramsden D.A., Chen J., Miller F.W., Misener V., Bernstein R.M., Siminovitch K.A., and Tsui F.W. Epitope mapping of the cloned human autoantigen, histidyl-tRNA synthetase. Analysis of the myositis-associated anti-Jo-1 autoimmune response. J. Immunol. 143 (1989) 2267-2272
    • (1989) J. Immunol. , vol.143 , pp. 2267-2272
    • Ramsden, D.A.1    Chen, J.2    Miller, F.W.3    Misener, V.4    Bernstein, R.M.5    Siminovitch, K.A.6    Tsui, F.W.7
  • 49
    • 0026343599 scopus 로고
    • Interferon induces tryptophanyl-tRNA synthetase expression in human fibroblasts
    • Rubin B.Y., Anderson S.L., Xing L., Powell R., and Tate W.P. Interferon induces tryptophanyl-tRNA synthetase expression in human fibroblasts. J. Biol. Chem. 266 (1991) 24245-24248
    • (1991) J. Biol. Chem. , vol.266 , pp. 24245-24248
    • Rubin, B.Y.1    Anderson, S.L.2    Xing, L.3    Powell, R.4    Tate, W.P.5
  • 50
    • 3042737393 scopus 로고    scopus 로고
    • Evidence for the involvement of SDF-1 and CXCR4 in the disruption of endothelial cell-branching morphogenesis and angiogenesis by TNF-alpha and IFN-gamma
    • Salvucci O., Basik M., Yao L., Bianchi R., and Tosato G. Evidence for the involvement of SDF-1 and CXCR4 in the disruption of endothelial cell-branching morphogenesis and angiogenesis by TNF-alpha and IFN-gamma. J. Leukoc. Biol. 76 (2004) 217-226
    • (2004) J. Leukoc. Biol. , vol.76 , pp. 217-226
    • Salvucci, O.1    Basik, M.2    Yao, L.3    Bianchi, R.4    Tosato, G.5
  • 51
    • 0018420119 scopus 로고
    • Immunochemical studies of beef pancreas tryptophanyl-tRNA synthetase and its fragments. Determination of the number of antigenic determinants and a comparison with tryptophanyl-tRNA synthetases from other sources and with reverse transcriptase from avian myeloblastosis virus
    • Scheinker V.S., Beresten S.F., Mazo A.M., Ambartsumyan N.S., Rokhlin O.V., Favorova O.O., and Kisselev L.L. Immunochemical studies of beef pancreas tryptophanyl-tRNA synthetase and its fragments. Determination of the number of antigenic determinants and a comparison with tryptophanyl-tRNA synthetases from other sources and with reverse transcriptase from avian myeloblastosis virus. Eur. J. Biochem. 97 (1979) 529-540
    • (1979) Eur. J. Biochem. , vol.97 , pp. 529-540
    • Scheinker, V.S.1    Beresten, S.F.2    Mazo, A.M.3    Ambartsumyan, N.S.4    Rokhlin, O.V.5    Favorova, O.O.6    Kisselev, L.L.7
  • 52
    • 0032896655 scopus 로고    scopus 로고
    • D.J. WRS-85D: a tryptophanyl-tRNA synthetase expressed to high levels in the developing Drosophila salivary gland
    • Seshaiah P., and Andrew. D.J. WRS-85D: a tryptophanyl-tRNA synthetase expressed to high levels in the developing Drosophila salivary gland. Mol. Biol. Cell 10 (1999) 1595-1608
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1595-1608
    • Seshaiah, P.1    Andrew2
  • 54
    • 0036777060 scopus 로고    scopus 로고
    • Idiopathic inflammatory myopathy: autoantibody update
    • Targoff I.N. Idiopathic inflammatory myopathy: autoantibody update. Curr. Rheumatol. Rep. 5 (2002) 434-441
    • (2002) Curr. Rheumatol. Rep. , vol.5 , pp. 434-441
    • Targoff, I.N.1
  • 57
    • 0025768572 scopus 로고
    • Detection of autoantibodies against phenylalanyl-, tyrosyl-, and tryptophanyl-tRNA-synthetase and anti-idiotypic antibodies to it in serum from patients with autoimmune diseases
    • Vartanian O.A. Detection of autoantibodies against phenylalanyl-, tyrosyl-, and tryptophanyl-tRNA-synthetase and anti-idiotypic antibodies to it in serum from patients with autoimmune diseases. Mol. Biol. (Mosk.) 25 (1991) 1033-1039
    • (1991) Mol. Biol. (Mosk.) , vol.25 , pp. 1033-1039
    • Vartanian, O.A.1
  • 58
    • 0346103681 scopus 로고    scopus 로고
    • Crystal structures that suggest late development of genetic code components for differentiating aromatic side chains
    • Yang X.-L., Otero F.J., Skene R.J., McRee D.E., Schimmel P., and Ribas de Pouplana L. Crystal structures that suggest late development of genetic code components for differentiating aromatic side chains. Proc. Natl. Acad. Sci. 100 (2003) 15376-15380
    • (2003) Proc. Natl. Acad. Sci. , vol.100 , pp. 15376-15380
    • Yang, X.-L.1    Otero, F.J.2    Skene, R.J.3    McRee, D.E.4    Schimmel, P.5    Ribas de Pouplana, L.6
  • 59
    • 0017331005 scopus 로고
    • Human pancreatic carcinoma (MIA PaCa-2) in continuous culture: sensitivity to asparaginase
    • Yunis A.A., Arimura G.K., and Russin D.J. Human pancreatic carcinoma (MIA PaCa-2) in continuous culture: sensitivity to asparaginase. Int. J. Cancer 19 (1977) 218-235
    • (1977) Int. J. Cancer , vol.19 , pp. 218-235
    • Yunis, A.A.1    Arimura, G.K.2    Russin, D.J.3
  • 60
    • 0025481232 scopus 로고
    • A peptide, containing the universal antigenic determinant of tryptophanyl-tRNA-synthetase
    • Zargarova T.A., Zargarov A.A., Bolotina I.A., Beresten' S.F., and Favorova O.O. A peptide, containing the universal antigenic determinant of tryptophanyl-tRNA-synthetase. Bioorg. Khim. 16 (1990) 1259-1267
    • (1990) Bioorg. Khim. , vol.16 , pp. 1259-1267
    • Zargarova, T.A.1    Zargarov, A.A.2    Bolotina, I.A.3    Beresten', S.F.4    Favorova, O.O.5
  • 61
    • 0037017399 scopus 로고    scopus 로고
    • Selective cytotoxicity of intracellular amyloid peptide 1-42 through p53 and Bax in cultured primary human neurons
    • Zhang Y., McLaughlin R., Goodyer C., and LeBlanc A. Selective cytotoxicity of intracellular amyloid peptide 1-42 through p53 and Bax in cultured primary human neurons. J. Cell Biol. 156 (2002) 519-529
    • (2002) J. Cell Biol. , vol.156 , pp. 519-529
    • Zhang, Y.1    McLaughlin, R.2    Goodyer, C.3    LeBlanc, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.