메뉴 건너뛰기




Volumn 427, Issue 3, 2012, Pages 587-592

The functional role of UBA1 cysteine-278 in ubiquitination

Author keywords

Hyperoxidized cysteines; UBA1 activity; Ubiquitin activating enzyme E1; Ubiquitination

Indexed keywords

CYSTEINE; PROTEIN; UBIQUITIN ACTIVATING ENZYME E1; UNCLASSIFIED DRUG;

EID: 84867860280     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2012.09.102     Document Type: Article
Times cited : (3)

References (24)
  • 1
    • 0034296394 scopus 로고    scopus 로고
    • Basic Medical Research Award. The ubiquitin system
    • Hershko A., Ciechanover A., Varshavsky A. Basic Medical Research Award. The ubiquitin system. Nat. Med. 2000, 6:1073-1081.
    • (2000) Nat. Med. , vol.6 , pp. 1073-1081
    • Hershko, A.1    Ciechanover, A.2    Varshavsky, A.3
  • 2
    • 0026663539 scopus 로고
    • The ubiquitin system for protein degradation
    • Hershko A., Ciechanover A. The ubiquitin system for protein degradation. Annu. Rev. Biochem. 1992, 61:761-807.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 761-807
    • Hershko, A.1    Ciechanover, A.2
  • 3
    • 0033597126 scopus 로고    scopus 로고
    • Identification of the activating and conjugating enzymes of the NEDD8 conjugation pathway
    • Gong L., Yeh E.T. Identification of the activating and conjugating enzymes of the NEDD8 conjugation pathway. J. Biol. Chem. 1999, 274:12036-12042.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12036-12042
    • Gong, L.1    Yeh, E.T.2
  • 4
    • 0026769411 scopus 로고
    • Multiple forms of ubiquitin-activating enzyme E1 from wheat. Identification of an essential cysteine by in vitro mutagenesis
    • Hatfield P.M., Vierstra R.D. Multiple forms of ubiquitin-activating enzyme E1 from wheat. Identification of an essential cysteine by in vitro mutagenesis. J. Biol. Chem. 1992, 267:14799-14803.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14799-14803
    • Hatfield, P.M.1    Vierstra, R.D.2
  • 8
    • 0028324041 scopus 로고
    • Recognition of oxidatively damaged erythrocytes by a macrophage receptor with specificity for oxidized low density lipoprotein
    • Sambrano G.R., Parthasarathy S., Steinberg D. Recognition of oxidatively damaged erythrocytes by a macrophage receptor with specificity for oxidized low density lipoprotein. Proc. Natl. Acad. Sci. USA 1994, 91:3265-3269.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3265-3269
    • Sambrano, G.R.1    Parthasarathy, S.2    Steinberg, D.3
  • 9
    • 0034653976 scopus 로고    scopus 로고
    • Scavenger receptors on liver Kupffer cells mediate the in vivo uptake of oxidatively damaged red blood cells in mice
    • Terpstra V., van Berkel T.J. Scavenger receptors on liver Kupffer cells mediate the in vivo uptake of oxidatively damaged red blood cells in mice. Blood 2000, 95:2157-2163.
    • (2000) Blood , vol.95 , pp. 2157-2163
    • Terpstra, V.1    van Berkel, T.J.2
  • 10
    • 0031440694 scopus 로고    scopus 로고
    • Independent mechanisms for macrophage binding macrophage phagocytosis of damaged erythrocytes evidence of receptor cooperativity
    • Sambrano G.R., Terpstra V., Steinberg D. Independent mechanisms for macrophage binding macrophage phagocytosis of damaged erythrocytes evidence of receptor cooperativity. Arterioscler. Thromb. Vasc. Biol. 1997, 17:3442-3448.
    • (1997) Arterioscler. Thromb. Vasc. Biol. , vol.17 , pp. 3442-3448
    • Sambrano, G.R.1    Terpstra, V.2    Steinberg, D.3
  • 11
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence N.F., Sampat R.M., Kopito R.R. Impairment of the ubiquitin-proteasome system by protein aggregation. Science 2001, 292:1552-1555.
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 12
    • 80053173420 scopus 로고    scopus 로고
    • Brain region specific mitophagy capacity could contribute to selective neuronal vulnerability in Parkinson's disease
    • Diedrich M., Kitada T., Nebrich G., Koppelstaetter A., Shen J., Zabel C., Klose J., Mao L. Brain region specific mitophagy capacity could contribute to selective neuronal vulnerability in Parkinson's disease. Proteome Sci. 2011, 9:59.
    • (2011) Proteome Sci. , vol.9 , pp. 59
    • Diedrich, M.1    Kitada, T.2    Nebrich, G.3    Koppelstaetter, A.4    Shen, J.5    Zabel, C.6    Klose, J.7    Mao, L.8
  • 13
    • 77951228584 scopus 로고    scopus 로고
    • Alterations in the red blood cell membrane proteome in Alzheimer's subjects reflect disease-related changes and provide insight into altered cell morphology
    • Mohanty J.G., Shukla H.D., Williamson J.D., Launer L.J., Saxena S., Rifkind J.M. Alterations in the red blood cell membrane proteome in Alzheimer's subjects reflect disease-related changes and provide insight into altered cell morphology. Proteome Sci. 2010, 8:11.
    • (2010) Proteome Sci. , vol.8 , pp. 11
    • Mohanty, J.G.1    Shukla, H.D.2    Williamson, J.D.3    Launer, L.J.4    Saxena, S.5    Rifkind, J.M.6
  • 16
    • 79952407243 scopus 로고    scopus 로고
    • Ubiquitin in motion: structural studies of the ubiquitin-conjugating enzyme approximately ubiquitin conjugate
    • Pruneda J.N., Stoll K.E., Bolton L.J., Brzovic P.S., Klevit R.E. Ubiquitin in motion: structural studies of the ubiquitin-conjugating enzyme approximately ubiquitin conjugate. Biochemistry 2011, 50:1624-1633.
    • (2011) Biochemistry , vol.50 , pp. 1624-1633
    • Pruneda, J.N.1    Stoll, K.E.2    Bolton, L.J.3    Brzovic, P.S.4    Klevit, R.E.5
  • 18
    • 84862908377 scopus 로고    scopus 로고
    • Changes in the ratio of free NEDD8 to ubiquitin triggers NEDDylation by ubiquitin enzymes
    • Hjerpe R., Thomas Y., Chen J., Zemla A., Curran S., Shpiro N., Dick L.R., Kurz T. Changes in the ratio of free NEDD8 to ubiquitin triggers NEDDylation by ubiquitin enzymes. Biochem. J. 2012, 441:927-936.
    • (2012) Biochem. J. , vol.441 , pp. 927-936
    • Hjerpe, R.1    Thomas, Y.2    Chen, J.3    Zemla, A.4    Curran, S.5    Shpiro, N.6    Dick, L.R.7    Kurz, T.8
  • 19
    • 34347329214 scopus 로고    scopus 로고
    • Dual E1 activation systems for ubiquitin differentially regulate E2 enzyme charging
    • Jin J., Li X., Gygi S.P., Harper J.W. Dual E1 activation systems for ubiquitin differentially regulate E2 enzyme charging. Nature 2007, 447:1135-1138.
    • (2007) Nature , vol.447 , pp. 1135-1138
    • Jin, J.1    Li, X.2    Gygi, S.P.3    Harper, J.W.4
  • 20
    • 0023802469 scopus 로고
    • The resolution and characterization of putative ubiquitin carrier protein isozymes from rabbit reticulocytes
    • Haas A.L., Bright P.M. The resolution and characterization of putative ubiquitin carrier protein isozymes from rabbit reticulocytes. J. Biol. Chem. 1988, 263:13258-13267.
    • (1988) J. Biol. Chem. , vol.263 , pp. 13258-13267
    • Haas, A.L.1    Bright, P.M.2
  • 21
    • 20444456668 scopus 로고    scopus 로고
    • Crystal structure of a fragment of mouse ubiquitin-activating enzyme
    • Szczepanowski R.H., Filipek R., Bochtler M. Crystal structure of a fragment of mouse ubiquitin-activating enzyme. J. Biol. Chem. 2005, 280:22006-22011.
    • (2005) J. Biol. Chem. , vol.280 , pp. 22006-22011
    • Szczepanowski, R.H.1    Filipek, R.2    Bochtler, M.3
  • 23
    • 47549111312 scopus 로고    scopus 로고
    • Structural insights into E1-catalyzed ubiquitin activation and transfer to conjugating enzymes
    • Lee I., Schindelin H. Structural insights into E1-catalyzed ubiquitin activation and transfer to conjugating enzymes. Cell 2008, 134:268-278.
    • (2008) Cell , vol.134 , pp. 268-278
    • Lee, I.1    Schindelin, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.