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Volumn 83, Issue 4, 2004, Pages 552-573

Proteomics in the chicken: Tools for understanding immune responses to avian diseases

Author keywords

Mass spectrometry; Polyacrylamide gel electrophoresis; Proteome; Proteomic; Two dimensional

Indexed keywords

ANIMALIA; AVES; GALLIFORMES; GALLUS GALLUS;

EID: 4043083306     PISSN: 00325791     EISSN: None     Source Type: Journal    
DOI: 10.1093/ps/83.4.552     Document Type: Conference Paper
Times cited : (25)

References (126)
  • 1
    • 0031709082 scopus 로고    scopus 로고
    • Preclinical development and current status of the fluorinated 2-nitroimidazole hypoxia probe N-(2-hydroxy-3,3,3-trifluoropropyl)-2-(2-nitro-1- imidazolyl) acetamide (SR 4554, CRC 94/17): A non-invasive diagnostic probe for the measurement of tumor hypoxia by magnetic resonance spectroscopy and imaging, and by positron emission tomography
    • Aboagye, E. O., A. B. Kelson, M. Tracy, and P. Workman. 1998. Preclinical development and current status of the fluorinated 2-nitroimidazole hypoxia probe N-(2-hydroxy-3,3,3-trifluoropropyl)-2-(2-nitro-1-imidazolyl) acetamide (SR 4554, CRC 94/17): A non-invasive diagnostic probe for the measurement of tumor hypoxia by magnetic resonance spectroscopy and imaging, and by positron emission tomography. Anticancer Drug Des. 13:703-730.
    • (1998) Anticancer Drug Des. , vol.13 , pp. 703-730
    • Aboagye, E.O.1    Kelson, A.B.2    Tracy, M.3    Workman, P.4
  • 3
    • 1242296295 scopus 로고    scopus 로고
    • Antimicrobial peptides and protease inhibitors in the skin secretions of the crawfish frog, Rana areolata
    • Ali, M. F., K. R. Lips, F. C. Knoop, B. Fritzsch, C. Miller, and J. M. Conlon. 2002. Antimicrobial peptides and protease inhibitors in the skin secretions of the crawfish frog, Rana areolata. Biochim. Biophys. Acta 1601:55-63.
    • (2002) Biochim. Biophys. Acta , vol.1601 , pp. 55-63
    • Ali, M.F.1    Lips, K.R.2    Knoop, F.C.3    Fritzsch, B.4    Miller, C.5    Conlon, J.M.6
  • 4
    • 0031848226 scopus 로고    scopus 로고
    • Proteome and proteomics: New technologies, new concepts, and new words
    • Anderson, N. L., and N. G. Anderson. 1998. Proteome and proteomics: new technologies, new concepts, and new words. Electrophoresis 19:1853-1861.
    • (1998) Electrophoresis , vol.19 , pp. 1853-1861
    • Anderson, N.L.1    Anderson, N.G.2
  • 5
    • 0036463388 scopus 로고    scopus 로고
    • Selective detection of membrane proteins without antibodies: A mass spectrometric version of the Western blot
    • Arnott, D., A. Kishiyama, E. A. Luis, S. G. Ludlum, J. C Marsters, Jr., and J. T. Stults. 2002. Selective detection of membrane proteins without antibodies: a mass spectrometric version of the Western blot. Mol. Cell Proteomics 1:148-156.
    • (2002) Mol. Cell Proteomics , vol.1 , pp. 148-156
    • Arnott, D.1    Kishiyama, A.2    Luis, E.A.3    Ludlum, S.G.4    Marsters Jr., J.C.5    Stults, J.T.6
  • 6
    • 0031008715 scopus 로고    scopus 로고
    • The SWISS-PROT protein sequence database: Its relevance to human molecular medical research
    • Bairoch, A., and R. Apweiler. 1997. The SWISS-PROT protein sequence database: its relevance to human molecular medical research. J. Mol. Med. 75:312-316.
    • (1997) J. Mol. Med. , vol.75 , pp. 312-316
    • Bairoch, A.1    Apweiler, R.2
  • 7
    • 0036244045 scopus 로고    scopus 로고
    • Proteomic analysis of cytokine induced proteins in human intestinal epithelial cells: Implications for inflammatory bowel diseases
    • Barcelo-Batllori, S., M. Andre, C. Servis, N. Levy, O. Takikawa, P. Michetti, M. Reymond, and E. Felley-Bosco. 2002. Proteomic analysis of cytokine induced proteins in human intestinal epithelial cells: Implications for inflammatory bowel diseases. Proteomics 2:551-560.
    • (2002) Proteomics , vol.2 , pp. 551-560
    • Barcelo-Batllori, S.1    Andre, M.2    Servis, C.3    Levy, N.4    Takikawa, O.5    Michetti, P.6    Reymond, M.7    Felley-Bosco, E.8
  • 8
    • 0344721480 scopus 로고    scopus 로고
    • Complete sequence, and gene map of a human major histocompatibility complex
    • The MHC sequencing consortium
    • Beck, S., D. Geraghty, H. Inoko, L. Rowen, et al. 1999. Complete sequence, and gene map of a human major histocompatibility complex. The MHC sequencing consortium. Nature 401:921-923.
    • (1999) Nature , vol.401 , pp. 921-923
    • Beck, S.1    Geraghty, D.2    Inoko, H.3    Rowen, L.4
  • 9
    • 0037182761 scopus 로고    scopus 로고
    • Identification of novel candidates for replicative senescence by functional proteomics
    • Benvenuti, S., R. Cramer, J. Bruce, M. D. Waterfield, and P. S. Jat. 2002. Identification of novel candidates for replicative senescence by functional proteomics. Oncogene 21:4403-4413.
    • (2002) Oncogene , vol.21 , pp. 4403-4413
    • Benvenuti, S.1    Cramer, R.2    Bruce, J.3    Waterfield, M.D.4    Jat, P.S.5
  • 10
    • 0036968792 scopus 로고    scopus 로고
    • Identification of sesame seed allergens by 2-dimensional proteomics and Edman sequencing: Seed storage proteins as common food allergens
    • Beyer, K., L. Bardina, G. Grishina, and H. A. Sampson. 2002. Identification of sesame seed allergens by 2-dimensional proteomics and Edman sequencing: seed storage proteins as common food allergens. J. Allergy Clin. Immunol. 110:154-159.
    • (2002) J. Allergy Clin. Immunol. , vol.110 , pp. 154-159
    • Beyer, K.1    Bardina, L.2    Grishina, G.3    Sampson, H.A.4
  • 11
    • 0037215734 scopus 로고    scopus 로고
    • The importance of thermodynamic equilibrium for high throughput gene expression arrays
    • Bhanot, G., Y. Louzoun, J. Zhu, and C. DeLisi. 2003. The importance of thermodynamic equilibrium for high throughput gene expression arrays. Biophys. J. 84:124-135.
    • (2003) Biophys. J. , vol.84 , pp. 124-135
    • Bhanot, G.1    Louzoun, Y.2    Zhu, J.3    DeLisi, C.4
  • 13
    • 0037722862 scopus 로고    scopus 로고
    • Immune infertility: Towards a better understanding of sperm (auto)-immunity: The value of proteomic analysis
    • Bohring, C., and W. Krause. 2003. Immune infertility: towards a better understanding of sperm (auto)-immunity: The value of proteomic analysis. Hum. Reprod. 18:915-924.
    • (2003) Hum. Reprod. , vol.18 , pp. 915-924
    • Bohring, C.1    Krause, W.2
  • 14
    • 18344396568 scopus 로고    scopus 로고
    • Minimum information about a microarray experiment (MIAME)-toward standards for microarray data
    • Brazma, A., P. Hingamp, J. Quackenbush, G. Sherlock, et al. 2001. Minimum information about a microarray experiment (MIAME)-toward standards for microarray data. Nat. Genet. 29:365-371.
    • (2001) Nat. Genet. , vol.29 , pp. 365-371
    • Brazma, A.1    Hingamp, P.2    Quackenbush, J.3    Sherlock, G.4
  • 15
    • 0035503380 scopus 로고    scopus 로고
    • Proteomics-based identification of protein gene product 9.5 as a tumor antigen that induces a humoral immune response in lung cancer
    • Brichory, F., D. Beer, F. Le Naour, T. Giordano, and S. Hanash. 2001. Proteomics-based identification of protein gene product 9.5 as a tumor antigen that induces a humoral immune response in lung cancer. Cancer Res. 61:7908-7912.
    • (2001) Cancer Res. , vol.61 , pp. 7908-7912
    • Brichory, F.1    Beer, D.2    Le Naour, F.3    Giordano, T.4    Hanash, S.5
  • 16
    • 0035859922 scopus 로고    scopus 로고
    • An immune response manifested by the common occurrence of annexins I and II autoantibodies and high circulating levels of IL-6 in lung cancer
    • Brichory, F. M., D. E. Misek, A. M. Yim, M. C. Krause, T. J. Giordano, D. G. Beer, and S. M. Hanash. 2001. An immune response manifested by the common occurrence of annexins I and II autoantibodies and high circulating levels of IL-6 in lung cancer. Proc. Natl. Acad. Sci. USA 98:9824-9829.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 9824-9829
    • Brichory, F.M.1    Misek, D.E.2    Yim, A.M.3    Krause, M.C.4    Giordano, T.J.5    Beer, D.G.6    Hanash, S.M.7
  • 17
    • 0036729950 scopus 로고    scopus 로고
    • The Reed-Steinberg cell: Molecular characterization by proteomic analysis with therapeutic implications
    • Brown, R. E., and R. K. Nazmi. 2002. The Reed-Steinberg cell: molecular characterization by proteomic analysis with therapeutic implications. Ann. Clin. Lab. Sci. 32:339-351.
    • (2002) Ann. Clin. Lab. Sci. , vol.32 , pp. 339-351
    • Brown, R.E.1    Nazmi, R.K.2
  • 18
    • 0035892602 scopus 로고    scopus 로고
    • Detection of epitope-tagged proteins in flow cytometry: Fluorescence resonance energy transfer-based assays on beads with femtomole resolution
    • Buranda, T., G. P. Lopez, P. Simons, A. Pastuszyn, and L. A. Sklar. 2001. Detection of epitope-tagged proteins in flow cytometry: fluorescence resonance energy transfer-based assays on beads with femtomole resolution. Anal. Biochem. 298:151-162.
    • (2001) Anal. Biochem. , vol.298 , pp. 151-162
    • Buranda, T.1    Lopez, G.P.2    Simons, P.3    Pastuszyn, A.4    Sklar, L.A.5
  • 19
    • 0037930609 scopus 로고    scopus 로고
    • Genetics. Chicken genome - Science nuggets to come soon
    • Burt, D., and O. Pourquie. 2003. Genetics. Chicken genome - Science nuggets to come soon. Science 300:1669.
    • (2003) Science , vol.300 , pp. 1669
    • Burt, D.1    Pourquie, O.2
  • 20
    • 85039499498 scopus 로고    scopus 로고
    • Final Report. Cambridge, Hinxton Genome Campus
    • Burt, D., and O. Pourquie. 2003. International Chicken Genome Workshop. Final Report. Cambridge, Hinxton Genome Campus.http://www.chicken-genome.org/ events/icgwr2003. html. Accessed July 2003.
    • (2003) International Chicken Genome Workshop
    • Burt, D.1    Pourquie, O.2
  • 24
    • 0036747311 scopus 로고    scopus 로고
    • Direct profiling and imaging of peptides and proteins from mammalian cells and tissue sections by mass spectrometry
    • Chaurand, P., and R. M. Caprioli. 2002. Direct profiling and imaging of peptides and proteins from mammalian cells and tissue sections by mass spectrometry. Electrophoresis 23:3125-3135.
    • (2002) Electrophoresis , vol.23 , pp. 3125-3135
    • Chaurand, P.1    Caprioli, R.M.2
  • 25
    • 0035319968 scopus 로고    scopus 로고
    • The application of proteomics in defining the T cell antigens of Mycobacterium tuberculosis
    • Covert, B. A., J. S. Spencer, I. M. Orme, and J. T. Belisle. 2001. The application of proteomics in defining the T cell antigens of Mycobacterium tuberculosis. Proteomics 1:574-586.
    • (2001) Proteomics , vol.1 , pp. 574-586
    • Covert, B.A.1    Spencer, J.S.2    Orme, I.M.3    Belisle, J.T.4
  • 26
    • 0242417007 scopus 로고    scopus 로고
    • LipL21 is a novel surface-exposed lipoprotein of pathogenic Leptospira species
    • Cullen, P. A., D. A. Haake, D. M. Bulach, R. L. Zuerner, and B. Adler. 2003. LipL21 is a novel surface-exposed lipoprotein of pathogenic Leptospira species. Infect. Immun. 71:2414-2421.
    • (2003) Infect. Immun. , vol.71 , pp. 2414-2421
    • Cullen, P.A.1    Haake, D.A.2    Bulach, D.M.3    Zuerner, R.L.4    Adler, B.5
  • 27
    • 0038482160 scopus 로고    scopus 로고
    • The immunologists' debt to the chicken
    • Davison, T. F. 2003. The immunologists' debt to the chicken. Br. Poult Sci. 44:6-21.
    • (2003) Br. Poult Sci. , vol.44 , pp. 6-21
    • Davison, T.F.1
  • 29
    • 0033553440 scopus 로고    scopus 로고
    • A coat protein on phagosomes involved in the intracellular survival of mycobacteria
    • Ferrari, G., H. Langen, M. Naito, and J. Pieters. 1999. A coat protein on phagosomes involved in the intracellular survival of mycobacteria. Cell 97:435-447.
    • (1999) Cell , vol.97 , pp. 435-447
    • Ferrari, G.1    Langen, H.2    Naito, M.3    Pieters, J.4
  • 30
    • 0038116819 scopus 로고    scopus 로고
    • Proteomics in 2002: A year of technical development and wide-ranging applications
    • Figeys, D. 2003. Proteomics in 2002: A year of technical development and wide-ranging applications. Anal. Chem. 75:2891-2905.
    • (2003) Anal. Chem. , vol.75 , pp. 2891-2905
    • Figeys, D.1
  • 31
    • 18344390036 scopus 로고    scopus 로고
    • Identification by redox proteomics of glutathionylated proteins in oxidatively stressed human T lymphocytes
    • Fratelli, M., H. Demol, M. Puype, S. Casagrande, et al. 2002. Identification by redox proteomics of glutathionylated proteins in oxidatively stressed human T lymphocytes. Proc. Natl. Acad. Sci. USA 99:3505-3510.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 3505-3510
    • Fratelli, M.1    Demol, H.2    Puype, M.3    Casagrande, S.4
  • 33
    • 0033672240 scopus 로고    scopus 로고
    • Proteome analysis of activated murine B-lymphocytes
    • Frey, J. R., M. Fountoulakis, and I. Lefkovits. 2000. Proteome analysis of activated murine B-lymphocytes. Electrophoresis 21:3730-3739.
    • (2000) Electrophoresis , vol.21 , pp. 3730-3739
    • Frey, J.R.1    Fountoulakis, M.2    Lefkovits, I.3
  • 34
    • 0037050026 scopus 로고    scopus 로고
    • Functional organization of the yeast proteome by systematic analysis of protein complexes
    • Gavin, A. C., M. Bosche, R. Krause, P. Grandi, et al. 2002. Functional organization of the yeast proteome by systematic analysis of protein complexes. Nature 415:141-147.
    • (2002) Nature , vol.415 , pp. 141-147
    • Gavin, A.C.1    Bosche, M.2    Krause, R.3    Grandi, P.4
  • 35
    • 0345012430 scopus 로고    scopus 로고
    • The T-dependent immune system
    • T. F. Davison, T. R. Morris and L. N. Payne, ed. Carfax Publishing, Abingdon, UK
    • Gobel, T. W. F. 1996. The T-dependent immune system. Pages 31-46 in Poultry Science Symposium Series. T. F. Davison, T. R. Morris and L. N. Payne, ed. Carfax Publishing, Abingdon, UK.
    • (1996) Poultry Science Symposium Series , pp. 31-46
    • Gobel, T.W.F.1
  • 36
  • 37
    • 0002599337 scopus 로고    scopus 로고
    • Post-translational modifications
    • Principles and Practice. M. R. Wilkins, K. L. Williams, R. D. Appel, and D. F. Hochstrasser, ed.. Springer, New York
    • Gooley, A., and N. Packer. 1997. Post-translational modifications. Pages 65-91 in Proteome Research: New Frontiers in Functional Genomics. Principles and Practice. M. R. Wilkins, K. L. Williams, R. D. Appel, and D. F. Hochstrasser, ed.. Springer, New York.
    • (1997) Proteome Research: New Frontiers in Functional Genomics , pp. 65-91
    • Gooley, A.1    Packer, N.2
  • 38
    • 0035676769 scopus 로고    scopus 로고
    • Computational aspects of protein identification by mass spectrometry
    • Gras, R., and M. Muller. 2001. Computational aspects of protein identification by mass spectrometry. Curr. Opin. Mol. Ther. 3:526-532.
    • (2001) Curr. Opin. Mol. Ther. , vol.3 , pp. 526-532
    • Gras, R.1    Muller, M.2
  • 39
    • 1342279255 scopus 로고    scopus 로고
    • Protein profiling of the human epidermis from the elderly reveals up-regulation of a signature of interferon-γ-induced polypeptides that includes manganese-superoxide dismutase and the p85 β-subunit of phosphatidylinositol 3-kinase
    • Gromov, P., G. L. Skovgaard, H. Palsdottir, I. Gromova, M. Ostergaard, and J. E. Celis. 2003. Protein profiling of the human epidermis from the elderly reveals up-regulation of a signature of interferon-γ-induced polypeptides that includes manganese-superoxide dismutase and the p85 β-subunit of phosphatidylinositol 3-kinase. Mol. Cell Proteomics 2:70-84.
    • (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
  • 40
    • 0037418318 scopus 로고    scopus 로고
    • Quantitative proteomic analysis indicates increased synthesis of a quinolone by Pseudomonas aeruginosa isolates from cystic fibrosis airways
    • Guina, T., S. O. Purvine, E. C. Yi, J. Eng, D. R. Goodlett, R. Aebersold, and S. I. Miller. 2003. Quantitative proteomic analysis indicates increased synthesis of a quinolone by Pseudomonas aeruginosa isolates from cystic fibrosis airways. Proc. Natl. Acad. Sci. USA 100:2771-2776.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 2771-2776
    • Guina, T.1    Purvine, S.O.2    Yi, E.C.3    Eng, J.4    Goodlett, D.R.5    Aebersold, R.6    Miller, S.I.7
  • 42
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
    • Gygi, S. P., B. Rist, S. A. Gerber, F. Turecek, M. H. Gelb, and R. Aebersold. 1999. Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat. Biotechnol. 17:994-999.
    • (1999) Nat. Biotechnol. , vol.17 , pp. 994-999
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3    Turecek, F.4    Gelb, M.H.5    Aebersold, R.6
  • 43
    • 0036615478 scopus 로고    scopus 로고
    • The human proteome organization: A mission to advance proteome knowledge
    • Hanash, S., and J. E. Celis. 2002. The human proteome organization: a mission to advance proteome knowledge. Mol. Cell Proteomics 1:413-414.
    • (2002) Mol. Cell Proteomics , vol.1 , pp. 413-414
    • Hanash, S.1    Celis, J.E.2
  • 46
    • 0037050004 scopus 로고    scopus 로고
    • Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry
    • Ho, Y., A. Gruhler, A. Heilbut, G. D. Bader, et al. 2002. Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry. Nature 415:180-183.
    • (2002) Nature , vol.415 , pp. 180-183
    • Ho, Y.1    Gruhler, A.2    Heilbut, A.3    Bader, G.D.4
  • 47
    • 0036132831 scopus 로고    scopus 로고
    • Two antigenic peptides from genes m123 and m164 of murine cytomegalovirus quantitatively dominate CD8 T-cell memory in the H-2d haplotype
    • Holtappels, R., D. Thomas, J. Podlech, and M. J. Reddehase. 2002. Two antigenic peptides from genes m123 and m164 of murine cytomegalovirus quantitatively dominate CD8 T-cell memory in the H-2d haplotype. J. Virol. 76:151-164.
    • (2002) J. Virol. , vol.76 , pp. 151-164
    • Holtappels, R.1    Thomas, D.2    Podlech, J.3    Reddehase, M.J.4
  • 48
    • 0037224581 scopus 로고    scopus 로고
    • Is proteomics heading in the wrong direction?
    • Huber, L. A. 2003. Is proteomics heading in the wrong direction? Nat. Rev. Mol. Cell Biol. 4:74-80.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 74-80
    • Huber, L.A.1
  • 52
    • 0037879089 scopus 로고    scopus 로고
    • Identification of metastasis-associated proteins by proteomic analysis and functional exploration of interleukin-18 in metastasis
    • Jiang, D., W. Ying, Y. Lu, J. Wan, Y. Zhai, W. Liu, Y. Zhu, Z. Qiu, X. Qian, and F. He. 2003. Identification of metastasis-associated proteins by proteomic analysis and functional exploration of interleukin-18 in metastasis. Proteomics 3:724-737.
    • (2003) Proteomics , vol.3 , pp. 724-737
    • Jiang, D.1    Ying, W.2    Lu, Y.3    Wan, J.4    Zhai, Y.5    Liu, W.6    Zhu, Y.7    Qiu, Z.8    Qian, X.9    He, F.10
  • 54
    • 0034807582 scopus 로고    scopus 로고
    • Proteome analysis of bacterial pathogens
    • Jungblut, P. R. 2001. Proteome analysis of bacterial pathogens. Microbes Infect. 3:831-840.
    • (2001) Microbes Infect. , vol.3 , pp. 831-840
    • Jungblut, P.R.1
  • 55
    • 0037012884 scopus 로고    scopus 로고
    • Proteomics. Public-private group maps out initiatives
    • Kaiser, J. 2002. Proteomics. Public-private group maps out initiatives. Science 296:827.
    • (2002) Science , vol.296 , pp. 827
    • Kaiser, J.1
  • 56
    • 0041845320 scopus 로고    scopus 로고
    • Proteome analysis reveals caspase activation in hyporesponsive CD4 T lymphocytes induced in vivo by the oral administration of antigen
    • Kaji, T., S. Hachimura, W. Ise, and S. Kaminogawa. 2003. Proteome analysis reveals caspase activation in hyporesponsive CD4 T lymphocytes induced in vivo by the oral administration of antigen. J. Biol. Chem.
    • (2003) J. Biol. Chem.
    • Kaji, T.1    Hachimura, S.2    Ise, W.3    Kaminogawa, S.4
  • 60
    • 2042437650 scopus 로고    scopus 로고
    • Initial sequencing and analysis of the human genome
    • Lander, E. S., L. M. Linton, B. Birren, C. Nusbaum, et al. 2001. Initial sequencing and analysis of the human genome. Nature 409:860-921.
    • (2001) Nature , vol.409 , pp. 860-921
    • Lander, E.S.1    Linton, L.M.2    Birren, B.3    Nusbaum, C.4
  • 62
    • 0035320134 scopus 로고    scopus 로고
    • Proteomic analysis of rare molecular species of translated polypeptides from a mouse fetal thymus cDNA library
    • Lefkovits, I., J. R. Kettman, and J. R. Frey. 2001. Proteomic analysis of rare molecular species of translated polypeptides from a mouse fetal thymus cDNA library. Proteomics 1:560-573.
    • (2001) Proteomics , vol.1 , pp. 560-573
    • Lefkovits, I.1    Kettman, J.R.2    Frey, J.R.3
  • 64
    • 0035947669 scopus 로고    scopus 로고
    • Profiling changes in gene expression during differentiation and maturation of monocyte-derived dendritic cells using both oligonucleotide microarrays and proteomics
    • Le Naour, F., L. Hohenkirk, A. Grolleau, D. E. Misek, P. Lescure, J. D. Geiger, S. Hanash, and L. Beretta. 2001. Profiling changes in gene expression during differentiation and maturation of monocyte-derived dendritic cells using both oligonucleotide microarrays and proteomics. J. Biol. Chem. 276:17920-17931.
    • (2001) J. Biol. Chem. , vol.276 , pp. 17920-17931
    • Le Naour, F.1    Hohenkirk, L.2    Grolleau, A.3    Misek, D.E.4    Lescure, P.5    Geiger, J.D.6    Hanash, S.7    Beretta, L.8
  • 67
    • 0015968532 scopus 로고
    • The heterogeneity of mouse-chromatin nonhistone proteins as evidenced by two-dimensional polyacrylamide-gel electrophoresis and ion-exchange chromatography
    • MacGillivray, A. J., and D. Rickwood. 1974. The heterogeneity of mouse-chromatin nonhistone proteins as evidenced by two-dimensional polyacrylamide-gel electrophoresis and ion-exchange chromatography. Eur. J. Biochem. 41:181-190.
    • (1974) Eur. J. Biochem. , vol.41 , pp. 181-190
    • MacGillivray, A.J.1    Rickwood, D.2
  • 68
    • 0034721074 scopus 로고    scopus 로고
    • Increased protein synthesis after T cell activation in presence of cyclosporin A
    • Mascarell, L., J. R. Frey, F. Michel, I. Lefkovits, and P. Truffa-Bachi. 2000. Increased protein synthesis after T cell activation in presence of cyclosporin A. Transplantation 70:340-348.
    • (2000) Transplantation , vol.70 , pp. 340-348
    • Mascarell, L.1    Frey, J.R.2    Michel, F.3    Lefkovits, I.4    Truffa-Bachi, P.5
  • 69
    • 0037051685 scopus 로고    scopus 로고
    • Monoclonal and polyclonal humoral immune response to EC HER-2/NEU peptides with low similarity to the host's proteome
    • Mittelman, A., A. Lucchese, A. A. Sinha, and D. Kanduc. 2002. Monoclonal and polyclonal humoral immune response to EC HER-2/NEU peptides with low similarity to the host's proteome. Int. J. Cancer 98:741-747.
    • (2002) Int. J. Cancer , vol.98 , pp. 741-747
    • Mittelman, A.1    Lucchese, A.2    Sinha, A.A.3    Kanduc, D.4
  • 72
    • 0037044851 scopus 로고    scopus 로고
    • Proteomic analysis of a detergent-resistant membrane skeleton from neutrophil plasma membranes
    • Nebl, T., K. N. Pestonjamasp, J. D. Leszyk, J. L. Crowley, S. W. Oh, and E. J. Luna. 2002. Proteomic analysis of a detergent-resistant membrane skeleton from neutrophil plasma membranes. J. Biol. Chem. 277:43399-43409.
    • (2002) J. Biol. Chem. , vol.277 , pp. 43399-43409
    • Nebl, T.1    Pestonjamasp, K.N.2    Leszyk, J.D.3    Crowley, J.L.4    Oh, S.W.5    Luna, E.J.6
  • 73
    • 0036046826 scopus 로고    scopus 로고
    • Bacterial proteomics and vaccine development
    • Nilsson, C. L. 2002. Bacterial proteomics and vaccine development. Am. J. Pharmacogenomics 2:59-65.
    • (2002) Am. J. Pharmacogenomics , vol.2 , pp. 59-65
    • Nilsson, C.L.1
  • 74
    • 0033946833 scopus 로고    scopus 로고
    • Proteome analysis reveals ubiquitin-conjugating enzymes to be a new family of interferon- A-regulated genes
    • Nyman, T. A., S. Matikainen, T. Sareneva, I. Julkunen, and N. Kalkkinen. 2000. Proteome analysis reveals ubiquitin-conjugating enzymes to be a new family of interferon- a-regulated genes. Eur. J. Biochem. 267:4011-4019.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 4011-4019
    • Nyman, T.A.1    Matikainen, S.2    Sareneva, T.3    Julkunen, I.4    Kalkkinen, N.5
  • 78
    • 0041355325 scopus 로고    scopus 로고
    • Proteomics identification of Acyl-acceptor and Acyl-donor substrates for transglutaminase in a human intestinal epithelial cell line: Implications for coeliac disease
    • Orru, S., I. Caputo, A. D'Amato, M. Ruoppolo, and C. Esposito. 2003. Proteomics identification of Acyl-acceptor and Acyl-donor substrates for transglutaminase in a human intestinal epithelial cell line: implications for coeliac disease. J. Biol. Chem.
    • (2003) J. Biol. Chem.
    • Orru, S.1    Caputo, I.2    D'Amato, A.3    Ruoppolo, M.4    Esposito, C.5
  • 79
    • 0034792051 scopus 로고    scopus 로고
    • Identification of a serine protease inhibitor homologue in Bird's Nest by an integrated proteomics approach
    • Ou, K., T. K. Seow, R. C. Liang, B. W. Lee, D. L. Goh, K. Y. Chua, and M. C. Chung. 2001. Identification of a serine protease inhibitor homologue in Bird's Nest by an integrated proteomics approach. Electrophoresis 22:3589-3595.
    • (2001) Electrophoresis , vol.22 , pp. 3589-3595
    • Ou, K.1    Seow, T.K.2    Liang, R.C.3    Lee, B.W.4    Goh, D.L.5    Chua, K.Y.6    Chung, M.C.7
  • 81
    • 0037370373 scopus 로고    scopus 로고
    • Proteomics: The first decade and beyond
    • Patterson, S. D., and R. H. Aebersold. 2003. Proteomics: the first decade and beyond. Nat. Genet. 33(Suppl.):311-323.
    • (2003) Nat. Genet. , vol.33 , Issue.SUPPL. , pp. 311-323
    • Patterson, S.D.1    Aebersold, R.H.2
  • 82
    • 0034969901 scopus 로고    scopus 로고
    • New technologies for biomarker analysis of prostate cancer progression: Laser capture microdissection and tissue proteomics
    • Paweletz, C. P., L. A. Liotta, and E. F. Petricoin, 3rd. 2001. New technologies for biomarker analysis of prostate cancer progression: Laser capture microdissection and tissue proteomics. Urology 57:160-163.
    • (2001) Urology , vol.57 , pp. 160-163
    • Paweletz, C.P.1    Liotta, L.A.2    Petricoin III, E.F.3
  • 83
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D. N., D. J. Pappin, D. M. Creasy, and J. S. Cottrell. 1999. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20:3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 87
    • 0029742635 scopus 로고    scopus 로고
    • Proteome of Salmonella typhimurium SL1344: Identification of novel abundant cell envelope proteins and assignment to a two-dimensional reference map
    • Qi, S. Y., A. Moir, and C. D. O'Connor. 1996. Proteome of Salmonella typhimurium SL1344: identification of novel abundant cell envelope proteins and assignment to a two-dimensional reference map. J. Bacteriol. 178:5032-5038.
    • (1996) J. Bacteriol. , vol.178 , pp. 5032-5038
    • Qi, S.Y.1    Moir, A.2    O'Connor, C.D.3
  • 88
    • 0036208433 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis in proteomics: Old, old fashioned, but it still climbs up the mountains
    • Rabilloud, T. 2002. Two-dimensional gel electrophoresis in proteomics: old, old fashioned, but it still climbs up the mountains. Proteomics 2:3-10.
    • (2002) Proteomics , vol.2 , pp. 3-10
    • Rabilloud, T.1
  • 90
    • 0027787526 scopus 로고
    • Primary sequence, evolution, and repetitive elements of the Gallus gallus (chicken) β-globin cluster
    • Reitman, M., J. A. Grasso, R. Blumenthal, and P. Lewit. 1993. Primary sequence, evolution, and repetitive elements of the Gallus gallus (chicken) β-globin cluster. Genomics 18:616-626.
    • (1993) Genomics , vol.18 , pp. 616-626
    • Reitman, M.1    Grasso, J.A.2    Blumenthal, R.3    Lewit, P.4
  • 91
    • 0034097576 scopus 로고    scopus 로고
    • Compositional bias and mimicry toward the nonself proteome in immunodominant T cell epitopes of self and nonself antigens
    • Ristori, G., M. Salvetti, G. Pesole, M. Attimonelli, C. Buttinelli, R. Martin, and P. Riccio. 2000. Compositional bias and mimicry toward the nonself proteome in immunodominant T cell epitopes of self and nonself antigens. FASEB J. 14:431-438.
    • (2000) FASEB J. , vol.14 , pp. 431-438
    • Ristori, G.1    Salvetti, M.2    Pesole, G.3    Attimonelli, M.4    Buttinelli, C.5    Martin, R.6    Riccio, P.7
  • 92
    • 0038605735 scopus 로고    scopus 로고
    • Protein and peptide array analysis of autoimmune disease
    • Robinson, W. H., L. Steinman, and P. J. Utz. 2002. Protein and peptide array analysis of autoimmune disease. Biotechniques (Suppl.):66-69.
    • (2002) Biotechniques , Issue.SUPPL. , pp. 66-69
    • Robinson, W.H.1    Steinman, L.2    Utz, P.J.3
  • 93
    • 0036269973 scopus 로고    scopus 로고
    • Proteomics of the eukaryotic transcription machinery: Identification of proteins associated with components of yeast TFIID by multidimensional mass spectrometry
    • Sanders, S. L., J. Jennings, A. Canutescu, A. J. Link, and P. A. Weil. 2002. Proteomics of the eukaryotic transcription machinery: Identification of proteins associated with components of yeast TFIID by multidimensional mass spectrometry. Mol. Cell Biol. 22:4723-4738.
    • (2002) Mol. Cell Biol. , vol.22 , pp. 4723-4738
    • Sanders, S.L.1    Jennings, J.2    Canutescu, A.3    Link, A.J.4    Weil, P.A.5
  • 94
    • 0037102411 scopus 로고    scopus 로고
    • High-efficiency nanoscale liquid chromatography coupled on-line with mass spectrometry using nanoelectrospray ionization for proteomics
    • Shen, Y., R. Zhao, S. J. Berger, G. A. Anderson, N. Rodriguez, and R. D. Smith. 2002. High-efficiency nanoscale liquid chromatography coupled on-line with mass spectrometry using nanoelectrospray ionization for proteomics. Anal. Chem. 74:4235-4249.
    • (2002) Anal. Chem. , vol.74 , pp. 4235-4249
    • Shen, Y.1    Zhao, R.2    Berger, S.J.3    Anderson, G.A.4    Rodriguez, N.5    Smith, R.D.6
  • 96
    • 0035408587 scopus 로고    scopus 로고
    • Genome annotation: From sequence to biology
    • Stein, L. 2001. Genome annotation: from sequence to biology. Nat. Rev. Genet. 2:493-503.
    • (2001) Nat. Rev. Genet. , vol.2 , pp. 493-503
    • Stein, L.1
  • 97
    • 0033238005 scopus 로고    scopus 로고
    • Automated mass spectrometry imaging with a matrix-assisted laser desorption ionization time-of-flight instrument
    • Stoeckli, M., T. B. Farmer, and R. M. Caprioli. 1999. Automated mass spectrometry imaging with a matrix-assisted laser desorption ionization time-of-flight instrument. J. Am. Soc. Mass Spectrom. 10:67-71.
    • (1999) J. Am. Soc. Mass Spectrom. , vol.10 , pp. 67-71
    • Stoeckli, M.1    Farmer, T.B.2    Caprioli, R.M.3
  • 99
    • 0032804117 scopus 로고    scopus 로고
    • Diversity and evolution of T-cell receptor variable region genes in mammals and birds
    • Su, C., I. Jakobsen, X. Gu, and M. Nei. 1999. Diversity and evolution of T-cell receptor variable region genes in mammals and birds. Immunogenetics 50:301-308.
    • (1999) Immunogenetics , vol.50 , pp. 301-308
    • Su, C.1    Jakobsen, I.2    Gu, X.3    Nei, M.4
  • 100
    • 0034980873 scopus 로고    scopus 로고
    • Vectors and gene targeting modules for tandem affinity purification in Schizosaccharomyces pombe
    • Tasto, J. J., R. H. Carnahan, W. H. McDonald, and K. L. Gould. 2001. Vectors and gene targeting modules for tandem affinity purification in Schizosaccharomyces pombe. Yeast 18:657-662.
    • (2001) Yeast , vol.18 , pp. 657-662
    • Tasto, J.J.1    Carnahan, R.H.2    McDonald, W.H.3    Gould, K.L.4
  • 101
    • 0037337307 scopus 로고    scopus 로고
    • A systematic approach to modeling, capturing, and disseminating proteomics experimental data
    • Taylor, C. F., N. W. Paton, K. L. Garwood, P. D. Kirby, et al. 2003. A systematic approach to modeling, capturing, and disseminating proteomics experimental data. Nat. Biotechnol. 21:247-254.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 247-254
    • Taylor, C.F.1    Paton, N.W.2    Garwood, K.L.3    Kirby, P.D.4
  • 102
    • 0036784621 scopus 로고    scopus 로고
    • Orderly pattern of development of the autoantibody response in (New Zealand White x BXSB)F1 lupus mice: Characterization of target antigens and antigen spreading by two-dimensional gel electrophoresis and mass spectrometry
    • Thebault, S., D. Gilbert, M. Hubert, L. Drouot, N. Machour, C. Lange, R. Charlionet, and F. Tron. 2002. Orderly pattern of development of the autoantibody response in (New Zealand White x BXSB)F1 lupus mice: Characterization of target antigens and antigen spreading by two-dimensional gel electrophoresis and mass spectrometry. J. Immunol. 169:4046-4053.
    • (2002) J. Immunol. , vol.169 , pp. 4046-4053
    • Thebault, S.1    Gilbert, D.2    Hubert, M.3    Drouot, L.4    Machour, N.5    Lange, C.6    Charlionet, R.7    Tron, F.8
  • 103
    • 0035877018 scopus 로고    scopus 로고
    • Proteomic analysis of dendritic cell-derived exosomes: A secreted subcellular compartment distinct from apoptotic vesicles
    • Thery, C., M. Boussac, P. Veron, P. Ricciardi-Castagnoli, G. Raposo, J. Garin, and S. Amigorena. 2001. Proteomic analysis of dendritic cell-derived exosomes: a secreted subcellular compartment distinct from apoptotic vesicles. J. Immunol. 166:7309-7318.
    • (2001) J. Immunol. , vol.166 , pp. 7309-7318
    • Thery, C.1    Boussac, M.2    Veron, P.3    Ricciardi-Castagnoli, P.4    Raposo, G.5    Garin, J.6    Amigorena, S.7
  • 106
    • 0033861430 scopus 로고    scopus 로고
    • Proteomic analysis of T cell activation in the presence of cyclosporin A: Immunosuppressor and activator removal induces de novo protein synthesis
    • Truffa-Bachi, P., I. I. Lefkovits, and J. Rudolf Frey. 2000. Proteomic analysis of T cell activation in the presence of cyclosporin A: immunosuppressor and activator removal induces de novo protein synthesis. Mol. Immunol. 37:261.
    • (2000) Mol. Immunol. , vol.37 , pp. 261
    • Truffa-Bachi, P.1    Lefkovits, I.I.2    Rudolf Frey, J.3
  • 107
    • 0034628508 scopus 로고    scopus 로고
    • A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae
    • Uetz, P., L. Giot, G. Cagney, T. A. Mansfield, et al. 2000. A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae. Nature 403:623-627.
    • (2000) Nature , vol.403 , pp. 623-627
    • Uetz, P.1    Giot, L.2    Cagney, G.3    Mansfield, T.A.4
  • 108
    • 0028969264 scopus 로고
    • Cartography of neurexins: More than 1000 isoforms generated by alternative splicing and expressed in distinct subsets of neurons
    • Ullrich, B., Y. A. Ushkaryov, and T. C. Sudhof. 1995. Cartography of neurexins: more than 1000 isoforms generated by alternative splicing and expressed in distinct subsets of neurons. Neuron 14:497-507.
    • (1995) Neuron , vol.14 , pp. 497-507
    • Ullrich, B.1    Ushkaryov, Y.A.2    Sudhof, T.C.3
  • 109
    • 0343376097 scopus 로고    scopus 로고
    • Difference gel electrophoresis: A single gel method for detecting changes in protein extracts
    • Unlu, M., M. E. Morgan, and J. S. Minden. 1997. Difference gel electrophoresis: a single gel method for detecting changes in protein extracts. Electrophoresis 18:2071-2077.
    • (1997) Electrophoresis , vol.18 , pp. 2071-2077
    • Unlu, M.1    Morgan, M.E.2    Minden, J.S.3
  • 110
    • 4444344532 scopus 로고    scopus 로고
    • Computational methods and bioinformational tools
    • S. Lorkowski and P. Cullen, ed. S. Wiley-VCH, New York
    • Various. 2003. Computational methods and bioinformational tools. Pages 769-904 in Analysing Gene Expression: a Handbook of Methods, Possibilities, and Pitfalls. Vol. 2. S. Lorkowski and P. Cullen, ed. S. Wiley-VCH, New York.
    • (2003) Analysing Gene Expression: A Handbook of Methods, Possibilities, and Pitfalls , vol.2 , pp. 769-904
    • Various1
  • 111
    • 0037332128 scopus 로고    scopus 로고
    • Sequential waves of functionally related proteins are expressed when B cells prepare for antibody secretion
    • van Anken, E., E. P. Romijn, C. Maggioni, A. Mezghrani, R. Sitia, I. Braakman, and A. J. Heck. 2003. Sequential waves of functionally related proteins are expressed when B cells prepare for antibody secretion. Immunity 18:243-253.
    • (2003) Immunity , vol.18 , pp. 243-253
    • Van Anken, E.1    Romijn, E.P.2    Maggioni, C.3    Mezghrani, A.4    Sitia, R.5    Braakman, I.6    Heck, A.J.7
  • 112
    • 0036533761 scopus 로고    scopus 로고
    • Major outer membrane proteins and proteolytic processing of RgpA and Kgp of Porphyromonas gingivalis W50
    • Veith, P. D., G. H. Talbo, N. Slakeski, S. G. Dashper, C. Moore, R. A. Paolini, and E. C. Reynolds. 2002. Major outer membrane proteins and proteolytic processing of RgpA and Kgp of Porphyromonas gingivalis W50. Biochem. J. 363:105-115.
    • (2002) Biochem. J. , vol.363 , pp. 105-115
    • Veith, P.D.1    Talbo, G.H.2    Slakeski, N.3    Dashper, S.G.4    Moore, C.5    Paolini, R.A.6    Reynolds, E.C.7
  • 113
    • 0035895505 scopus 로고    scopus 로고
    • The sequence of the human genome
    • Venter, J. C., M. D. Adams, E. W. Myers, P. W. Li, et al. 2001. The sequence of the human genome. Science 291:1304-1351.
    • (2001) Science , vol.291 , pp. 1304-1351
    • Venter, J.C.1    Adams, M.D.2    Myers, E.W.3    Li, P.W.4
  • 116
    • 0035055142 scopus 로고    scopus 로고
    • Mass spectrometric imaging of immobilized pH gradient gels and creation of "virtual" two-dimensional gels
    • Walker, A. K., G. Rymar, and P. C. Andrews. 2001. Mass spectrometric imaging of immobilized pH gradient gels and creation of "virtual" two-dimensional gels. Electrophoresis 22:933-945.
    • (2001) Electrophoresis , vol.22 , pp. 933-945
    • Walker, A.K.1    Rymar, G.2    Andrews, P.C.3
  • 117
    • 0036169299 scopus 로고    scopus 로고
    • Studies on the immuno-modulating and antitumor activities of Ganoderma lucidum (Reishi) polysaccharides: Functional and proteomic analyses of a fucose-containing glycoprotein fraction responsible for the activities
    • Wang, Y. Y., K. H. Khoo, S. T. Chen, C. C. Lin, C. H. Wong, and C. H. Lin. 2002. Studies on the immuno-modulating and antitumor activities of Ganoderma lucidum (Reishi) polysaccharides: functional and proteomic analyses of a fucose-containing glycoprotein fraction responsible for the activities. Bioorg. Med. Chem. 10:1057-1062.
    • (2002) Bioorg. Med. Chem. , vol.10 , pp. 1057-1062
    • Wang, Y.Y.1    Khoo, K.H.2    Chen, S.T.3    Lin, C.C.4    Wong, C.H.5    Lin, C.H.6
  • 119
    • 33749048664 scopus 로고
    • Genetical Implications of the structure of deoxyribonucleic acid
    • Watson, J. D., and F. H. C. Crick. 1953. Genetical Implications of the structure of deoxyribonucleic acid. Nature 171:964-967.
    • (1953) Nature , vol.171 , pp. 964-967
    • Watson, J.D.1    Crick, F.H.C.2
  • 121
    • 0035582244 scopus 로고    scopus 로고
    • An automated multidimensional protein identification technology for shotgun proteomics
    • Wolters, D. A., M. P. Washburn, and J. R. Yates, 3rd. 2001. An automated multidimensional protein identification technology for shotgun proteomics. Anal. Chem. 73:5683-5690.
    • (2001) Anal. Chem. , vol.73 , pp. 5683-5690
    • Wolters, D.A.1    Washburn, M.P.2    Yates III, J.R.3
  • 122
    • 0038561131 scopus 로고    scopus 로고
    • A method for the comprehensive proteomic analysis of membrane proteins
    • Wu, C. C., M. J. MacCoss, K. E. Howell, and J. R. Yates. 2003. A method for the comprehensive proteomic analysis of membrane proteins. Nat. Biotechnol. 21:532-538.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 532-538
    • Wu, C.C.1    MacCoss, M.J.2    Howell, K.E.3    Yates, J.R.4
  • 123
    • 0029644596 scopus 로고
    • Method to correlate tandem mass spectra of modified peptides to amino acid sequences in the protein database
    • Yates, J. R., III, J. K. Eng, A. L. McCormack, and D. Schieltz. 1995. Method to correlate tandem mass spectra of modified peptides to amino acid sequences in the protein database. Anal. Chem. 67:1426-1436.
    • (1995) Anal. Chem. , vol.67 , pp. 1426-1436
    • Yates III, J.R.1    Eng, J.K.2    McCormack, A.L.3    Schieltz, D.4
  • 124
    • 0038608023 scopus 로고    scopus 로고
    • Comprehensive analysis of the secreted proteins of the parasite Haemonchus contortus reveals extensive sequence variation and differential immune recognition
    • Yatsuda, A. P., J. Krijgsveld, A. W. Cornelissen, A. J. Heck, and E. de Vries. 2003. Comprehensive analysis of the secreted proteins of the parasite Haemonchus contortus reveals extensive sequence variation and differential immune recognition. J. Biol. Chem. 278:16941-16951.
    • (2003) J. Biol. Chem. , vol.278 , pp. 16941-16951
    • Yatsuda, A.P.1    Krijgsveld, J.2    Cornelissen, A.W.3    Heck, A.J.4    De Vries, E.5
  • 126
    • 0037223013 scopus 로고    scopus 로고
    • Proteomics and immunological analysis of a novel shrimp allergen, Pen m 2
    • Yu, C. J., Y. F. Lin, B. L. Chiang, and L. P. Chow. 2003. Proteomics and immunological analysis of a novel shrimp allergen, Pen m 2. J. Immunol. 170:445-453.
    • (2003) J. Immunol. , vol.170 , pp. 445-453
    • Yu, C.J.1    Lin, Y.F.2    Chiang, B.L.3    Chow, L.P.4


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