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Volumn 3, Issue 5, 2004, Pages 501-509

The human erythrocyte proteome: Analysis by ion trap mass spectrometry

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CARRIER PROTEIN; CELL ADHESION MOLECULE; CELL ENZYME; CELL MEMBRANE PROTEIN; CHAPERONE; CYTOPLASM PROTEIN; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; GUANINE NUCLEOTIDE BINDING PROTEIN; HEMOGLOBIN; INITIATION FACTOR; PROTEIN KINASE; PROTEINASE; PROTEOME; RAS PROTEIN; SPECTRIN; TRYPSIN; UBIQUITIN;

EID: 2642551423     PISSN: 15359476     EISSN: None     Source Type: Journal    
DOI: 10.1074/mcp.M300132-MCP200     Document Type: Article
Times cited : (205)

References (16)
  • 2
    • 0016226796 scopus 로고
    • The organization of proteins in the human red blood cell membrane
    • Steck, T. L. (1974) The organization of proteins in the human red blood cell membrane. J. Cell Biol. 62, 1-19
    • (1974) J. Cell Biol. , vol.62 , pp. 1-19
    • Steck, T.L.1
  • 3
    • 0036746499 scopus 로고    scopus 로고
    • Separation of human erythrocyte membrane associated proteins with one dimensional and two-dimensional gel eletrophoresis followed by identification with matrix assisted laser desorption/ionization-time of flight mass spectrometry
    • Low, T. Y., Seow, T. K., and Chung, M. C. M. (2002) Separation of human erythrocyte membrane associated proteins with one dimensional and two-dimensional gel eletrophoresis followed by identification with matrix assisted laser desorption/ionization-time of flight mass spectrometry. Proteomics 2, 1229-1239
    • (2002) Proteomics , vol.2 , pp. 1229-1239
    • Low, T.Y.1    Seow, T.K.2    Chung, M.C.M.3
  • 4
    • 0025290039 scopus 로고
    • The identification and sequence of the actin-binding domain of human red cell β-spectrin
    • Karinch, A. M., Zimmer, W. E., and Goodman, S. R. (1990) The identification and sequence of the actin-binding domain of human red cell β-spectrin. J. Biol. Chem. 65, 11833-11840
    • (1990) J. Biol. Chem. , vol.65 , pp. 11833-11840
    • Karinch, A.M.1    Zimmer, W.E.2    Goodman, S.R.3
  • 5
    • 0019887744 scopus 로고
    • Phase separation of integral membrane proteins in Triton X-114 solution
    • Bordier, C. (1981) Phase separation of integral membrane proteins in Triton X-114 solution. J. Biol. Chem. 256, 1604-1607
    • (1981) J. Biol. Chem. , vol.256 , pp. 1604-1607
    • Bordier, C.1
  • 6
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng, J. K., McCormack, A. L., and Yates, J. R., 3rd. (1994) An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J. Am. Soc. Mass Spectrom. 5, 976-989
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates III, J.R.3
  • 7
    • 0029644596 scopus 로고
    • Method to correlate tandem mass spectra of modified peptides to amino acid sequences in the protein database
    • Yates, J. R., 3rd, Eng, J. K., McCormack, A. L., and Schieltz, D. (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
  • 8
    • 0031888036 scopus 로고    scopus 로고
    • High throughput protein characterization by automated reverse-phase chromatography/electrospray tandem mass spectrometry
    • Ducret, A., Van Oostveen, I., Eng, J. K., Yates, J. R., 3rd, and Aebersold, R. (1998) High throughput protein characterization by automated reverse-phase chromatography/electrospray tandem mass spectrometry. Prot. Sci. 7, 706-719
    • (1998) Prot. Sci. , vol.7 , pp. 706-719
    • Ducret, A.1    Van Oostveen, I.2    Eng, J.K.3    Yates III, J.R.4    Aebersold, R.5
  • 9
    • 0035865744 scopus 로고    scopus 로고
    • Stomatin, flotillin-1, and flotillin-2 are major integral proteins of erythrocyte lipid rafts
    • Salser, U., and Prohaska R. (2001) Stomatin, flotillin-1, and flotillin-2 are major integral proteins of erythrocyte lipid rafts. Blood 97, 1141-1143
    • (2001) Blood , vol.97 , pp. 1141-1143
    • Salser, U.1    Prohaska, R.2
  • 11
    • 5144230132 scopus 로고    scopus 로고
    • Ankyrin is a target of spectrin's E2/E3 ubiquitin-conjugating/ligating activity
    • Chang, T. L., Cubillos, F. F., Kakhniashvili, D. G., and Goodman, S. R. (2003) Ankyrin is a target of spectrin's E2/E3 ubiquitin-conjugating/ligating activity. Cell Mol. Biol. 50, 59-66
    • (2003) Cell Mol. Biol. , vol.50 , pp. 59-66
    • Chang, T.L.1    Cubillos, F.F.2    Kakhniashvili, D.G.3    Goodman, S.R.4
  • 12
    • 2642524773 scopus 로고    scopus 로고
    • Band 3 is a target protein of spectrin's E2/E3 activity: Implication for sickle cell disease and normal red blood cell aging
    • Chang, T. L., Cubillos, F. F., Kakhniashvili, D. G., and Goodman, S. R. (2004) Band 3 is a target protein of spectrin's E2/E3 activity: Implication for sickle cell disease and normal red blood cell aging. Cell Mol. Biol. 50, 171-177
    • (2004) Cell Mol. Biol. , vol.50 , pp. 171-177
    • Chang, T.L.1    Cubillos, F.F.2    Kakhniashvili, D.G.3    Goodman, S.R.4
  • 13
    • 5144222293 scopus 로고    scopus 로고
    • Ubiquitination of spectrin regulates the erythrocyte spectrin-protein 4.1-actin ternary complex dissociation: Implications for the sickle cell membrane skeletons
    • Ghatpande, S., and Goodman, S. R. (2003) Ubiquitination of spectrin regulates the erythrocyte spectrin-protein 4.1-actin ternary complex dissociation: Implications for the sickle cell membrane skeletons. Cell Mol. Biol. 50, 67-74
    • (2003) Cell Mol. Biol. , vol.50 , pp. 67-74
    • Ghatpande, S.1    Goodman, S.R.2
  • 14
    • 5144227414 scopus 로고    scopus 로고
    • Ubiquitination of spectrin regulates the dissociation of spectrin-adducin-F-actin ternary complex in vitro
    • Mishra, R., and Goodman, S. R. (2003) Ubiquitination of spectrin regulates the dissociation of spectrin-adducin-F-actin ternary complex in vitro. Cell Mol. Biol. 50, 75-80
    • (2003) Cell Mol. Biol. , vol.50 , pp. 75-80
    • Mishra, R.1    Goodman, S.R.2
  • 15
    • 0023682264 scopus 로고
    • Levels of active ubiquitin carrier proteins decline during erythroid maturation
    • Pickart, C. M., and Vella, A. T. (1988) Levels of active ubiquitin carrier proteins decline during erythroid maturation. J. Biol. Chem. 263, 12028-12035
    • (1988) J. Biol. Chem. , vol.263 , pp. 12028-12035
    • Pickart, C.M.1    Vella, A.T.2
  • 16
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.