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Volumn 8, Issue 2, 2013, Pages

Transiently Transfected Purine Biosynthetic Enzymes Form Stress Bodies

Author keywords

[No Author keywords available]

Indexed keywords

PURINE; RECOMBINANT ENZYME;

EID: 84873560858     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0056203     Document Type: Article
Times cited : (10)

References (20)
  • 1
    • 27144515901 scopus 로고    scopus 로고
    • Movement of eukaryotic mRNAs between polysomes and cytoplasmic processing bodies
    • Brengues M, Teixeira D, Parker R, (2005) Movement of eukaryotic mRNAs between polysomes and cytoplasmic processing bodies. Science 310: 486-489.
    • (2005) Science , vol.310 , pp. 486-489
    • Brengues, M.1    Teixeira, D.2    Parker, R.3
  • 2
    • 33750522651 scopus 로고    scopus 로고
    • Actin bodies in yeast quiescent cells: an immediately available actin reserve?
    • Sagot I, Pinson B, Salin B, Daignan-Fornier B, (2006) Actin bodies in yeast quiescent cells: an immediately available actin reserve? Mol Biol Cell 17: 4645-4655.
    • (2006) Mol Biol Cell , vol.17 , pp. 4645-4655
    • Sagot, I.1    Pinson, B.2    Salin, B.3    Daignan-Fornier, B.4
  • 3
    • 63049091236 scopus 로고    scopus 로고
    • A systematic survey identifies prions and illuminates sequence features of prionogenic proteins
    • Alberti S, Halfmann R, King O, Kapila A, Lindquist S, (2009) A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell 137: 146-158.
    • (2009) Cell , vol.137 , pp. 146-158
    • Alberti, S.1    Halfmann, R.2    King, O.3    Kapila, A.4    Lindquist, S.5
  • 4
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: a cellular response to misfolded proteins
    • Johnston JA, Ward CL, Kopito RR, (1998) Aggresomes: a cellular response to misfolded proteins. J Cell Biol 143: 1883-1898.
    • (1998) J Cell Biol , vol.143 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 5
    • 67649875630 scopus 로고    scopus 로고
    • Widespread reorganization of metabolic enzymes into reversible assemblies upon nutrient starvation
    • Narayanaswamy R, Levy M, Tsechansky M, Stovall GM, O'Connell JD, et al. (2009) Widespread reorganization of metabolic enzymes into reversible assemblies upon nutrient starvation. Proc Natl Acad Sci U S A 106: 10147-10152.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 10147-10152
    • Narayanaswamy, R.1    Levy, M.2    Tsechansky, M.3    Stovall, G.M.4    O'Connell, J.D.5
  • 6
    • 41749092312 scopus 로고    scopus 로고
    • Reversible compartmentalization of de novo purine biosynthetic complexes in living cells
    • An S, Kumar R, Sheets ED, Benkovic SJ, (2008) Reversible compartmentalization of de novo purine biosynthetic complexes in living cells. Science 320: 103-106.
    • (2008) Science , vol.320 , pp. 103-106
    • An, S.1    Kumar, R.2    Sheets, E.D.3    Benkovic, S.J.4
  • 7
    • 77955593994 scopus 로고    scopus 로고
    • Microtubule-assisted mechanism for functional metabolic macromolecular complex formation
    • An S, Deng Y, Tomsho JW, Kyoung M, Benkovic SJ, (2010) Microtubule-assisted mechanism for functional metabolic macromolecular complex formation. Proc Natl Acad Sci U S A 107: 12872-12876.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 12872-12876
    • An, S.1    Deng, Y.2    Tomsho, J.W.3    Kyoung, M.4    Benkovic, S.J.5
  • 8
    • 77951236102 scopus 로고    scopus 로고
    • Dynamic regulation of a metabolic multi-enzyme complex by protein kinase CK2
    • An S, Kyoung M, Allen JJ, Shokat KM, Benkovic SJ, (2010) Dynamic regulation of a metabolic multi-enzyme complex by protein kinase CK2. J Biol Chem 285: 11093-11099.
    • (2010) J Biol Chem , vol.285 , pp. 11093-11099
    • An, S.1    Kyoung, M.2    Allen, J.J.3    Shokat, K.M.4    Benkovic, S.J.5
  • 9
    • 81355148507 scopus 로고    scopus 로고
    • GPCRs regulate the assembly of a multienzyme complex for purine biosynthesis
    • Verrier F, An S, Ferrie AM, Sun H, Kyoung M, et al. (2011) GPCRs regulate the assembly of a multienzyme complex for purine biosynthesis. Nat Chem Biol 7: 909-915.
    • (2011) Nat Chem Biol , vol.7 , pp. 909-915
    • Verrier, F.1    An, S.2    Ferrie, A.M.3    Sun, H.4    Kyoung, M.5
  • 10
    • 5044235541 scopus 로고    scopus 로고
    • Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins
    • Fernandez-Escamilla AM, Rousseau F, Schymkowitz J, Serrano L, (2004) Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins. Nat Biotechnol 22: 1302-1306.
    • (2004) Nat Biotechnol , vol.22 , pp. 1302-1306
    • Fernandez-Escamilla, A.M.1    Rousseau, F.2    Schymkowitz, J.3    Serrano, L.4
  • 11
    • 4344569643 scopus 로고    scopus 로고
    • Geldanamycin induces Hsp70 and prevents alpha-synuclein aggregation and toxicity in vitro
    • McLean PJ, Klucken J, Shin Y, Hyman BT, (2004) Geldanamycin induces Hsp70 and prevents alpha-synuclein aggregation and toxicity in vitro. Biochem Biophys Res Commun 321: 665-669.
    • (2004) Biochem Biophys Res Commun , vol.321 , pp. 665-669
    • McLean, P.J.1    Klucken, J.2    Shin, Y.3    Hyman, B.T.4
  • 13
  • 14
    • 0038307156 scopus 로고    scopus 로고
    • Ubiquitination of alpha-synuclein is not required for formation of pathological inclusions in alpha-synucleinopathies
    • Sampathu DM, Giasson BI, Pawlyk AC, Trojanowski JQ, Lee VM, (2003) Ubiquitination of alpha-synuclein is not required for formation of pathological inclusions in alpha-synucleinopathies. Am J Pathol 163: 91-100.
    • (2003) Am J Pathol , vol.163 , pp. 91-100
    • Sampathu, D.M.1    Giasson, B.I.2    Pawlyk, A.C.3    Trojanowski, J.Q.4    Lee, V.M.5
  • 16
    • 79960337702 scopus 로고    scopus 로고
    • Modelling the role of the Hsp70/Hsp90 system in the maintenance of protein homeostasis
    • Proctor CJ, Lorimer IA, (2011) Modelling the role of the Hsp70/Hsp90 system in the maintenance of protein homeostasis. PLoS One 6: e22038.
    • (2011) PLoS One , vol.6
    • Proctor, C.J.1    Lorimer, I.A.2
  • 18
    • 84858214646 scopus 로고    scopus 로고
    • Mutations of ATIC and ADSL affect purinosome assembly in cultured skin fibroblasts from patients with AICA-ribosiduria and ADSL deficiency
    • Baresova V, Skopova V, Sikora J, Patterson D, Sovova J, et al. (2012) Mutations of ATIC and ADSL affect purinosome assembly in cultured skin fibroblasts from patients with AICA-ribosiduria and ADSL deficiency. Hum Mol Genet 21: 1534-1543.
    • (2012) Hum Mol Genet , vol.21 , pp. 1534-1543
    • Baresova, V.1    Skopova, V.2    Sikora, J.3    Patterson, D.4    Sovova, J.5
  • 19
    • 0030859943 scopus 로고    scopus 로고
    • Amidophosphoribosyltransferase limits the rate of cell growth-linked de novo purine biosynthesis in the presence of constant capacity of salvage purine biosynthesis
    • Yamaoka T, Kondo M, Honda S, Iwahana H, Moritani M, et al. (1997) Amidophosphoribosyltransferase limits the rate of cell growth-linked de novo purine biosynthesis in the presence of constant capacity of salvage purine biosynthesis. J Biol Chem 272: 17719-17725.
    • (1997) J Biol Chem , vol.272 , pp. 17719-17725
    • Yamaoka, T.1    Kondo, M.2    Honda, S.3    Iwahana, H.4    Moritani, M.5
  • 20
    • 0035877810 scopus 로고    scopus 로고
    • Feedback inhibition of amidophosphoribosyltransferase regulates the rate of cell growth via purine nucleotide, DNA, and protein syntheses
    • Yamaoka T, Yano M, Kondo M, Sasaki H, Hino S, et al. (2001) Feedback inhibition of amidophosphoribosyltransferase regulates the rate of cell growth via purine nucleotide, DNA, and protein syntheses. J Biol Chem 276: 21285-21291.
    • (2001) J Biol Chem , vol.276 , pp. 21285-21291
    • Yamaoka, T.1    Yano, M.2    Kondo, M.3    Sasaki, H.4    Hino, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.