메뉴 건너뛰기




Volumn 3, Issue 1, 2004, Pages 56-65

Expression profiling of lymphocyte plasma membrane proteins

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM IONOPHORE; CD69 ANTIGEN; GENE PRODUCT; GLUCOCORTICOID; IMMUNOGLOBULIN D; IMMUNOGLOBULIN M; LECTIN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; MEMBRANE PROTEIN; NICASTRIN; PHORBOL ESTER; TUMOR NECROSIS FACTOR RECEPTOR;

EID: 2542573212     PISSN: 15359476     EISSN: None     Source Type: Journal    
DOI: 10.1074/mcp.M300064-MCP200     Document Type: Article
Times cited : (78)

References (47)
  • 1
    • 0035057790 scopus 로고    scopus 로고
    • Monoclonal antibodies targeting cancer: "Magic bullets" or just the trigger?
    • Eccles, S. A. (2001) Monoclonal antibodies targeting cancer: "Magic bullets" or just the trigger? Breast Cancer Res. 3, 86-90
    • (2001) Breast Cancer Res. , vol.3 , pp. 86-90
    • Eccles, S.A.1
  • 2
    • 0034066471 scopus 로고    scopus 로고
    • Membrane proteins and proteomics: Un amour impossible?
    • Santoni, V., Molloy, M., and Rabilloud, T. (2000) Membrane proteins and proteomics: Un amour impossible? Electrophoresis 21, 1054-1070
    • (2000) Electrophoresis , vol.21 , pp. 1054-1070
    • Santoni, V.1    Molloy, M.2    Rabilloud, T.3
  • 3
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • Krogh, A., Larsson, B., von Heijne, G., and Sonnhammer, E. L. (2001) Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes. J. Mol. Biol. 305, 567-580
    • (2001) J. Mol. Biol. , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    von Heijne, G.3    Sonnhammer, E.L.4
  • 4
    • 0031026920 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis of membrane proteins: A current challenge for immobilized pH gradients
    • Adessi, C., Miege, C., Albrieux, C., and Rabilloud, T. (1997) Two-dimensional electrophoresis of membrane proteins: A current challenge for immobilized pH gradients. Electrophoresis 18, 127-135
    • (1997) Electrophoresis , vol.18 , pp. 127-135
    • Adessi, C.1    Miege, C.2    Albrieux, C.3    Rabilloud, T.4
  • 6
    • 0033404839 scopus 로고    scopus 로고
    • Analysis of membrane proteins by two-dimensional electrophoresis: Comparison of the proteins extracted from normal or Plasmodium falciparum-infected erythrocyte ghosts
    • Rabilloud, T., Blisnick, T., Heller, M., Luche, S., Aebersold, R., Lunardi, J., and Braun-Breton, C. (1999) Analysis of membrane proteins by two-dimensional electrophoresis: Comparison of the proteins extracted from normal or Plasmodium falciparum-infected erythrocyte ghosts. Electrophoresis 20, 3603-3610
    • (1999) Electrophoresis , vol.20 , pp. 3603-3610
    • Rabilloud, T.1    Blisnick, T.2    Heller, M.3    Luche, S.4    Aebersold, R.5    Lunardi, J.6    Braun-Breton, C.7
  • 8
    • 0030957650 scopus 로고    scopus 로고
    • Improvement of the solubilization of proteins in two-dimensional electrophoresis with immobilized pH gradients
    • Rabilloud, T., Adessi, C., Giraudel, A., and Lunardi, J. (1997) Improvement of the solubilization of proteins in two-dimensional electrophoresis with immobilized pH gradients. Electrophoresis 18, 307-316
    • (1997) Electrophoresis , vol.18 , pp. 307-316
    • Rabilloud, T.1    Adessi, C.2    Giraudel, A.3    Lunardi, J.4
  • 9
    • 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
  • 10
    • 0022396827 scopus 로고
    • Identification of surface proteins on bovine leukocytes by a botin-avidin protein blotting technique
    • Hurley, W. L., Finkelstein, E., and Holst, B. D. (1985) Identification of surface proteins on bovine leukocytes by a botin-avidin protein blotting technique. J. Immunol. Methods 85, 195-202
    • (1985) J. Immunol. Methods , vol.85 , pp. 195-202
    • Hurley, W.L.1    Finkelstein, E.2    Holst, B.D.3
  • 11
    • 0037008715 scopus 로고    scopus 로고
    • Identification of surface proteins of Helicobacter pylori by selective biotinylation, affinity purification, and two-dimensional gel electrophoresis
    • Sabarth, N., Lamer, S., Zimny-Arndt, U., Jungblut, P. R., Meyer, T. F., and Bumann, D. (2002) Identification of surface proteins of Helicobacter pylori by selective biotinylation, affinity purification, and two-dimensional gel electrophoresis. J. Biol. Chem. 277, 27896-27902
    • (2002) J. Biol. Chem. , vol.277 , pp. 27896-27902
    • Sabarth, N.1    Lamer, S.2    Zimny-Arndt, U.3    Jungblut, P.R.4    Meyer, T.F.5    Bumann, D.6
  • 12
    • 0035049237 scopus 로고    scopus 로고
    • Identification of tumour-induced changes in endothelial cell surface protein expression: An in vitro model
    • Hewett, P. W. (2001) Identification of tumour-induced changes in endothelial cell surface protein expression: An in vitro model. Int. J. Biochem. Cell Biol. 33, 325-335
    • (2001) Int. J. Biochem. Cell Biol. , vol.33 , pp. 325-335
    • Hewett, P.W.1
  • 15
    • 0034120122 scopus 로고    scopus 로고
    • Proteomic analysis of the human colon carcinoma cell line (LIM 1215): Development of a membrane protein database
    • Simpson, R. J., Connolly, L. M., Eddes, J. S., Pereira, J. J., Moritz, R. L., and Reid, G. E. (2000) Proteomic analysis of the human colon carcinoma cell line (LIM 1215): Development of a membrane protein database. Electrophoresis 21, 1707-1732
    • (2000) Electrophoresis , vol.21 , pp. 1707-1732
    • Simpson, R.J.1    Connolly, L.M.2    Eddes, J.S.3    Pereira, J.J.4    Moritz, R.L.5    Reid, G.E.6
  • 17
    • 0038561131 scopus 로고    scopus 로고
    • A method for the comprehensive proteomic analysis of membrane proteins
    • Wu, C. C., MacCoss, M. J., Howell, K. E., and Yates, J. R. (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
  • 18
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
    • Gygi, S. P., Rist, B., Gerber, S. A., Turecek, F., Gelb, M. H., and Aebersold, R. (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
  • 19
    • 0034789979 scopus 로고    scopus 로고
    • Quantitative profiling of differentiation-induced microsomal proteins using isotope-coded affinity tags and mass spectrometry
    • Han, D. K., Eng, J., Zhou, H., and Aebersold, R. (2001) Quantitative profiling of differentiation-induced microsomal proteins using isotope-coded affinity tags and mass spectrometry. Nat. Biotechnol. 19, 946-951
    • (2001) Nat. Biotechnol. , vol.19 , pp. 946-951
    • Han, D.K.1    Eng, J.2    Zhou, H.3    Aebersold, R.4
  • 22
    • 0028266949 scopus 로고
    • Non-radioactive labelling and immuno-precipitation analysis of leukocyte surface proteins using different methods of protein biotinylation
    • Kahne, T., and Ansorge, S. (1994) Non-radioactive labelling and immuno-precipitation analysis of leukocyte surface proteins using different methods of protein biotinylation. J. Immunol. Methods 168, 209-218
    • (1994) J. Immunol. Methods , vol.168 , pp. 209-218
    • Kahne, T.1    Ansorge, S.2
  • 23
    • 0019325639 scopus 로고
    • Preparation of resealed pig lymphocyte plasma-membrane vesicles
    • Johnstone, A. P., and Crumpton, M. J. (1980) Preparation of resealed pig lymphocyte plasma-membrane vesicles. Biochem. J. 190, 45-50
    • (1980) Biochem. J. , vol.190 , pp. 45-50
    • Johnstone, A.P.1    Crumpton, M.J.2
  • 24
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O., and Mann, M. (1996) Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal. Chem. 68, 850-858
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 26
    • 0023270053 scopus 로고
    • CD4 monoclonal antibody pairs for immunosuppression and tolerance induction
    • Qin, S., Cobbold, S., Tighe, H., Benjamin, R., and Waldmann, H. (1987) CD4 monoclonal antibody pairs for immunosuppression and tolerance induction. Eur. J. Immunol. 17, 1159-1165
    • (1987) Eur. J. Immunol. , vol.17 , pp. 1159-1165
    • Qin, S.1    Cobbold, S.2    Tighe, H.3    Benjamin, R.4    Waldmann, H.5
  • 27
    • 0034848903 scopus 로고    scopus 로고
    • Proteins of rat serum, urine, and cerebrospinal fluid: VI. Further protein identifications and interstrain comparison
    • Wait, R., Gianazza, E., Eberini, I., Sironi, L., Dunn, M. J., Gemeiner, M., and Miller, I. (2001) Proteins of rat serum, urine, and cerebrospinal fluid: VI. Further protein identifications and interstrain comparison. Electrophoresis 22, 3043-3052
    • (2001) Electrophoresis , vol.22 , pp. 3043-3052
    • Wait, R.1    Gianazza, E.2    Eberini, I.3    Sironi, L.4    Dunn, M.J.5    Gemeiner, M.6    Miller, I.7
  • 30
    • 0037144422 scopus 로고    scopus 로고
    • Complex N-linked glycosylated nicastrin associates with active gamma-secretase and undergoes tight cellular regulation
    • Kimberly, W. T., LaVoie, M. J., Ostaszewski, B. L., Ye, W., Wolfe, M. S., and Selkoe, D. J. (2002) Complex N-linked glycosylated nicastrin associates with active gamma-secretase and undergoes tight cellular regulation. J. Biol. Chem. 277, 35113-35117
    • (2002) J. Biol. Chem. , vol.277 , pp. 35113-35117
    • Kimberly, W.T.1    LaVoie, M.J.2    Ostaszewski, B.L.3    Ye, W.4    Wolfe, M.S.5    Selkoe, D.J.6
  • 31
    • 0036007117 scopus 로고    scopus 로고
    • Nicastrin is required for gamma-secretase cleavage of the Drosophila Notch receptor
    • Hu, Y., Ye, Y., and Fortini, M. E. (2002) Nicastrin is required for gamma-secretase cleavage of the Drosophila Notch receptor. Dev. Cell 2, 69-78
    • (2002) Dev. Cell , vol.2 , pp. 69-78
    • Hu, Y.1    Ye, Y.2    Fortini, M.E.3
  • 33
    • 0032211830 scopus 로고    scopus 로고
    • The cell biology of beta-amyloid precursor protein and presenilin in Alzheimer's disease
    • Selkoe, D. J. (1998) The cell biology of beta-amyloid precursor protein and presenilin in Alzheimer's disease. Trends. Cell Biol. 8, 447-453
    • (1998) Trends. Cell Biol. , vol.8 , pp. 447-453
    • Selkoe, D.J.1
  • 34
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy, J., and Selkoe, D. J. (2002) The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297, 353-356
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 36
    • 0012721724 scopus 로고    scopus 로고
    • Notch cleavage: Nicastrin helps Presenilin make the final cut
    • Lai, E. C. (2002) Notch cleavage: Nicastrin helps Presenilin make the final cut. Curr. Biol. 12, R200-202
    • (2002) Curr. Biol. , vol.12
    • Lai, E.C.1
  • 37
    • 0036236895 scopus 로고    scopus 로고
    • An invitation to T and more: Notch signaling in lymphopoiesis
    • Allman, D., Punt, J. A., Izon, D. J., Aster, J. C., and Pear, W. S. (2002). An invitation to T and more: notch signaling in lymphopoiesis. Cell 109, (suppl.) S1-11
    • (2002) Cell , vol.109 , Issue.SUPPL.
    • Allman, D.1    Punt, J.A.2    Izon, D.J.3    Aster, J.C.4    Pear, W.S.5
  • 42
    • 0024414103 scopus 로고
    • A B-lymphocyte activation molecule related to the nerve growth factor receptor and induced by cytokines in carcinomas
    • Stamenkovic, I., Clark, E. A., and Seed, B. (1989) A B-lymphocyte activation molecule related to the nerve growth factor receptor and induced by cytokines in carcinomas. EMBO J. 8, 1403-1410
    • (1989) EMBO J. , vol.8 , pp. 1403-1410
    • Stamenkovic, I.1    Clark, E.A.2    Seed, B.3
  • 43
    • 0030918905 scopus 로고    scopus 로고
    • Characterization of mouse ALCAM (CD166): The CD6-binding domain is conserved in different homologs and mediates cross-species binding
    • Bowen, M. A., Bajorath, J., D'Egidio, M., Whitney, G. S., Palmer, D., Kobarg, J., Starling, G. C., Siadak, A. W., and Aruffo, A. (1997) Characterization of mouse ALCAM (CD166): The CD6-binding domain is conserved in different homologs and mediates cross-species binding. Eur. J. Immunol. 27, 1469-1478
    • (1997) Eur. J. Immunol. , vol.27 , pp. 1469-1478
    • Bowen, M.A.1    Bajorath, J.2    D'Egidio, M.3    Whitney, G.S.4    Palmer, D.5    Kobarg, J.6    Starling, G.C.7    Siadak, A.W.8    Aruffo, A.9
  • 44
    • 0031932784 scopus 로고    scopus 로고
    • Dipeptidyl-peptidase IV/CD26 on T cells: Analysis of an alternative T-cell activation pathway
    • von Bonin, A., Huhn, J., and Fleischer, B. (1998) Dipeptidyl-peptidase IV/CD26 on T cells: Analysis of an alternative T-cell activation pathway. Immunol. Rev. 161, 43-53
    • (1998) Immunol. Rev. , vol.161 , pp. 43-53
    • von Bonin, A.1    Huhn, J.2    Fleischer, B.3
  • 45
    • 0037080024 scopus 로고    scopus 로고
    • Tissue expression of human Toll-like receptors and differential regulation of Toll-like receptor mRNAs in leukocytes in response to microbes, their products, and cytokines
    • Zarember, K. A., and Godowski, P. J. (2002) Tissue expression of human Toll-like receptors and differential regulation of Toll-like receptor mRNAs in leukocytes in response to microbes, their products, and cytokines. J. Immunol. 168, 554-561
    • (2002) J. Immunol. , vol.168 , pp. 554-561
    • Zarember, K.A.1    Godowski, P.J.2
  • 46
    • 0018167339 scopus 로고
    • Analytical techniques for cell fractions. XII. Two-dimensional analysis of serum and tissue proteins: Multiple gradient-slab gel electrophoresis
    • Anderson, N. L., and Anderson, N. G. (1978) Analytical techniques for cell fractions. XII. Two-dimensional analysis of serum and tissue proteins: Multiple gradient-slab gel electrophoresis. Anal. Biochem. 85, 341-354
    • (1978) Anal. Biochem. , vol.85 , pp. 341-354
    • Anderson, N.L.1    Anderson, N.G.2
  • 47
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching databases using mass spectrometry data
    • Perkins, D. N., Pappin, D. J., Creasey, D. M., and Cottrell, J. S. (1999) Probability-based protein identification by searching databases using mass spectrometry data. Electrophoresis 18, 3551-3567
    • (1999) Electrophoresis , vol.18 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasey, D.M.3    Cottrell, J.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.