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Volumn 236, Issue 5, 2011, Pages 580-591

Functional 20s proteasomes in mature human red blood cells

Author keywords

2d dige; Atomic force microscopy; Electron microscopy; Erythrocytes; Proteasomes; Proteolysis; Proteomics

Indexed keywords

LACTACYSTIN; MEMBRANE PROTEIN; PROTEASOME;

EID: 79958796521     PISSN: 15353702     EISSN: 15353699     Source Type: Journal    
DOI: 10.1258/ebm.2011.010394     Document Type: Article
Times cited : (53)

References (37)
  • 1
    • 0342265782 scopus 로고
    • A soluble ATP-dependent proteolytic system responsible for degradation of abnormal proteins in reticulocytes
    • Etlinger JD, Goldberg AL. A soluble ATP-dependent proteolytic system responsible for degradation of abnormal proteins in reticulocytes. Proc Natl Acad Sci USA 1977;74:54-58
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 54-58
    • Etlinger, J.D.1    Goldberg, A.L.2
  • 2
    • 0020465451 scopus 로고
    • Loss of ATP-dependent proteolysis with maturation of reticulocytes and erythrocytes
    • Speiser S, Etlinger JD. Loss of ATP-dependent proteolysis with maturation of reticulocytes and erythrocytes. J Biol Chem 1982;257:14122-14127
    • (1982) J Biol Chem , vol.257 , pp. 14122-14127
    • Speiser, S.1    Etlinger, J.D.2
  • 3
    • 0022975889 scopus 로고
    • Red blood cells contain a pathway for the degradation of oxidant-damaged hemoglobin that does not require ATP or ubiquitin
    • Fagan JM, Waxman L, Goldberg AL. Red blood cells contain a pathway for the degradation of oxidant-damaged hemoglobin that does not require ATP or ubiquitin. J Biol Chem 1986;261:5705-5713
    • (1986) J Biol Chem , vol.261 , pp. 5705-5713
    • Fagan, J.M.1    Waxman, L.2    Goldberg, A.L.3
  • 4
    • 0023682264 scopus 로고
    • Levels of active ubiquitin carrier proteins decline during erythroid maturation
    • Pickart CM, Vella AT. Levels of active ubiquitin carrier proteins decline during erythroid maturation. J Biol Chem 1988;263:12028-12035
    • (1988) J Biol Chem , vol.263 , pp. 12028-12035
    • Pickart, C.M.1    Vella, A.T.2
  • 5
    • 0022379602 scopus 로고
    • The immunochemical detection and quantitation of intracellular ubiquitin-protein conjugates
    • Haas AL, Bright PM. The immunochemical detection and quantitation of intracellular ubiquitin-protein conjugates. J Biol Chem 1985;260:12464-12473
    • (1985) J Biol Chem , vol.260 , pp. 12464-12473
    • Haas, A.L.1    Bright, P.M.2
  • 6
    • 20044375595 scopus 로고    scopus 로고
    • Spectrin's E2/E3 ubiquitin conjugating/ligating activity is diminished in sickle cells
    • Chang TL, Kakhniashvili DG, Goodman SR. Spectrin's E2/E3 ubiquitin conjugating/ligating activity is diminished in sickle cells. Am J Hematol 2005;79:89-96
    • (2005) Am J Hematol , vol.79 , pp. 89-96
    • Chang, T.L.1    Kakhniashvili, D.G.2    Goodman, S.R.3
  • 8
    • 33646839008 scopus 로고    scopus 로고
    • Spectrin and ubiquitination: A review
    • Noisy-le-grand, France
    • Hsu YJ, Goodman SR. Spectrin and ubiquitination: a review. Cell Mol Biol (Noisy-le-grand, France) 2005;Suppl. 51:OL801-OL807
    • (2005) Cell Mol Biol , Issue.SUPPL. 51
    • Hsu, Y.J.1    Goodman, S.R.2
  • 9
    • 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 TL, Cubillos FF, Kakhniashvili DG, Goodman SR. 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 2004;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
  • 10
    • 5144230132 scopus 로고    scopus 로고
    • Ankyrin is a target of spectrin's E2/E3 ubiquitin-conjugating/ligating activity
    • Chang TL, Cubillos FF, Kakhniashvili DG, Goodman SR. Ankyrin is a target of spectrin's E2/E3 ubiquitin-conjugating/ligating activity. Cell Mol Biol 2004;50:59-66
    • (2004) Cell Mol Biol , vol.50 , pp. 59-66
    • Chang, T.L.1    Cubillos, F.F.2    Kakhniashvili, D.G.3    Goodman, S.R.4
  • 11
    • 0036746499 scopus 로고    scopus 로고
    • Separation of human erythrocyte membrane associated proteins with one-dimensional and two-dimensional gel electrophoresis followed by identification with matrix-assisted laser desorption/ionization-time of flight mass spectrometry
    • Low TY, Seow TK, Chung MC. Separation of human erythrocyte membrane associated proteins with one-dimensional and two-dimensional gel electrophoresis followed by identification with matrix-assisted laser desorption/ionization-time of flight mass spectrometry. Proteomics 2002;2:1229-1239
    • (2002) Proteomics , vol.2 , pp. 1229-1239
    • Low, T.Y.1    Seow, T.K.2    Chung, M.C.3
  • 12
    • 2642551423 scopus 로고    scopus 로고
    • The human erythrocyte proteome: Analysis by ion trap mass spectrometry
    • Kakhniashvili DG, Bulla LA Jr, Goodman SR. The human erythrocyte proteome: analysis by ion trap mass spectrometry. Mol Cell Proteom 2004;3:501-509
    • (2004) Mol Cell Proteom , vol.3 , pp. 501-509
    • Kakhniashvili, D.G.1    Bulla Jr., L.A.2    Goodman, S.R.3
  • 15
    • 72149104586 scopus 로고    scopus 로고
    • In vivo pharmaco-proteomic analysis of hydroxyurea induced changes in the sickle red blood cell membrane proteome
    • Ghatpande SS, Choudhary PK, Quinn CT, Goodman SR. In vivo pharmaco-proteomic analysis of hydroxyurea induced changes in the sickle red blood cell membrane proteome. J Proteom 2010;73:619-626
    • (2010) J Proteom , vol.73 , pp. 619-626
    • Ghatpande, S.S.1    Choudhary, P.K.2    Quinn, C.T.3    Goodman, S.R.4
  • 20
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single-particle reconstructions
    • Ludtke SJ, Baldwin PR, Chiu W. EMAN: semiautomated software for high-resolution single-particle reconstructions. J Struct Biol 1999;128:82-97
    • (1999) J Struct Biol , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 25
    • 0037013955 scopus 로고    scopus 로고
    • Properties of the hybrid form of the 26S proteasome containing both 19S and PA28 complexes
    • Cascio P, Call M, Pete BM, Walz T, Goldberg AL. Properties of the hybrid form of the 26S proteasome containing both 19S and PA28 complexes. EMBO J 2002;21:2636-2645
    • (2002) EMBO J , vol.21 , pp. 2636-2645
    • Cascio, P.1    Call, M.2    Pete, B.M.3    Walz, T.4    Goldberg, A.L.5
  • 27
    • 77956527512 scopus 로고    scopus 로고
    • Syntaxin 16: Unraveling cellular physiology through a ubiquitous SNARE molecule
    • Chen Y, Gan BQ, Tang BL. Syntaxin 16: unraveling cellular physiology through a ubiquitous SNARE molecule. J Cell Physiol 2010;225:326-332
    • (2010) J Cell Physiol , vol.225 , pp. 326-332
    • Chen, Y.1    Gan, B.Q.2    Tang, B.L.3
  • 31
    • 0033553570 scopus 로고    scopus 로고
    • A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A
    • Ogris E, Du X, Nelson KC, Mak EK, Yu XX, Lane WS, Pallas DC. A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A. J Biol Chem 1999;274:14382-14391
    • (1999) J Biol Chem , vol.274 , pp. 14382-14391
    • Ogris, E.1    Du, X.2    Nelson, K.C.3    Mak, E.K.4    Yu, X.X.5    Lane, W.S.6    Pallas, D.C.7
  • 32
    • 0034194227 scopus 로고    scopus 로고
    • Differential impairment of 20S and 26S proteasome activities in human hematopoietic K562 cells during oxidative stress
    • Reinheckel T, Ullrich O, Sitte N, Grune T. Differential impairment of 20S and 26S proteasome activities in human hematopoietic K562 cells during oxidative stress. Arch Biochem Biophys 2000;377:65-68
    • (2000) Arch Biochem Biophys , vol.377 , pp. 65-68
    • Reinheckel, T.1    Ullrich, O.2    Sitte, N.3    Grune, T.4
  • 33
    • 0035072229 scopus 로고    scopus 로고
    • Degradation of oxidized proteins by the 20S proteasome
    • Davies JA. Degradation of oxidized proteins by the 20S proteasome. Biochimie 2001;83:301-310
    • (2001) Biochimie , vol.83 , pp. 301-310
    • Davies, J.A.1
  • 34
    • 0034640520 scopus 로고    scopus 로고
    • Hybrid proteasomes. Induction by interferon-gamma and contribution to ATP-dependent proteolysis
    • Tanahashi N, Murakami Y, Minami Y, Shimbara N, Hendil KB, Tanaka K. Hybrid proteasomes. Induction by interferon-gamma and contribution to ATP-dependent proteolysis. J Biol Chem 2000;275:14336-14345
    • (2000) J Biol Chem , vol.275 , pp. 14336-14345
    • Tanahashi, N.1    Murakami, Y.2    Minami, Y.3    Shimbara, N.4    Hendil, K.B.5    Tanaka, K.6
  • 35
    • 0020031293 scopus 로고
    • Oxidized proteins in erythrocytes are rapidly degraded by the adenosine triphosphate-dependent proteolytic system
    • Goldberg AL, Boches FS. Oxidized proteins in erythrocytes are rapidly degraded by the adenosine triphosphate-dependent proteolytic system. Science 1982;215:1107-1009
    • (1982) Science , vol.215 , pp. 1009-1107
    • Goldberg, A.L.1    Boches, F.S.2
  • 36
    • 26444577079 scopus 로고    scopus 로고
    • Selectivity of the ubiquitin pathway for oxidatively modified proteins: Relevance to protein precipitation diseases
    • Dudel EJ, Shang F, Valverde P, Liu Q, Hobbs M, Taylor A. Selectivity of the ubiquitin pathway for oxidatively modified proteins: relevance to protein precipitation diseases. FASEB J 2005;19:1707-1709
    • (2005) FASEB J , vol.19 , pp. 1707-1709
    • Dudel, E.J.1    Shang, F.2    Valverde, P.3    Liu, Q.4    Hobbs, M.5    Taylor, A.6
  • 37
    • 77953467032 scopus 로고    scopus 로고
    • Characterization of the brain 26S proteasome and its interacting proteins
    • Tai HC, Besche H, Goldberg AL, Schuman EM. Characterization of the brain 26S proteasome and its interacting proteins. Front Mol Neurosci 2010;3:1-12
    • (2010) Front Mol Neurosci , vol.3 , pp. 1-12
    • Tai, H.C.1    Besche, H.2    Goldberg, A.L.3    Schuman, E.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.