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Volumn 59, Issue 5, 2015, Pages 850-857

Lack of Evidence for PKM2 Protein Kinase Activity

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; PHOSPHATE; PHOSPHORUS 32; PYRUVATE KINASE; PYRUVATE KINASE M2; RECOMBINANT ENZYME; UNCLASSIFIED DRUG; CARRIER PROTEIN; MEMBRANE PROTEIN; PHOSPHOENOLPYRUVATE; PROTEIN KINASE; RECOMBINANT PROTEIN; THYROID HORMONE; THYROID HORMONE-BINDING PROTEINS;

EID: 84940900111     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2015.07.013     Document Type: Article
Times cited : (84)

References (30)
  • 3
    • 0020491881 scopus 로고
    • Effect of vanadate on the formation and stability of the phosphoenzyme forms of 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase and of phosphoglucomutase
    • Carreras J., Climent F., Bartrons R., Pons G. Effect of vanadate on the formation and stability of the phosphoenzyme forms of 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase and of phosphoglucomutase. Biochim. Biophys. Acta 1982, 705:238-242.
    • (1982) Biochim. Biophys. Acta , vol.705 , pp. 238-242
    • Carreras, J.1    Climent, F.2    Bartrons, R.3    Pons, G.4
  • 7
    • 33845626641 scopus 로고    scopus 로고
    • How phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteria
    • Deutscher J., Francke C., Postma P.W. How phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteria. Microbiol. Mol. Biol. Rev. 2006, 70:939-1031.
    • (2006) Microbiol. Mol. Biol. Rev. , vol.70 , pp. 939-1031
    • Deutscher, J.1    Francke, C.2    Postma, P.W.3
  • 8
    • 21844468220 scopus 로고    scopus 로고
    • Structural basis for tumor pyruvate kinase M2 allosteric regulation and catalysis
    • Dombrauckas J.D., Santarsiero B.D., Mesecar A.D. Structural basis for tumor pyruvate kinase M2 allosteric regulation and catalysis. Biochemistry 2005, 44:9417-9429.
    • (2005) Biochemistry , vol.44 , pp. 9417-9429
    • Dombrauckas, J.D.1    Santarsiero, B.D.2    Mesecar, A.D.3
  • 9
    • 84862776933 scopus 로고    scopus 로고
    • Pyruvate kinase M2 regulates gene transcription by acting as a protein kinase
    • Gao X., Wang H., Yang J.J., Liu X., Liu Z.R. Pyruvate kinase M2 regulates gene transcription by acting as a protein kinase. Mol. Cell 2012, 45:598-609.
    • (2012) Mol. Cell , vol.45 , pp. 598-609
    • Gao, X.1    Wang, H.2    Yang, J.J.3    Liu, X.4    Liu, Z.R.5
  • 13
    • 84869888609 scopus 로고    scopus 로고
    • SAICAR stimulates pyruvate kinase isoform M2 and promotes cancer cell survival in glucose-limited conditions
    • Keller K.E., Tan I.S., Lee Y.S. SAICAR stimulates pyruvate kinase isoform M2 and promotes cancer cell survival in glucose-limited conditions. Science 2012, 338:1069-1072.
    • (2012) Science , vol.338 , pp. 1069-1072
    • Keller, K.E.1    Tan, I.S.2    Lee, Y.S.3
  • 14
    • 84896764451 scopus 로고    scopus 로고
    • SAICAR induces protein kinase activity of PKM2 that is necessary for sustained proliferative signaling of cancer cells
    • Keller K.E., Doctor Z.M., Dwyer Z.W., Lee Y.S. SAICAR induces protein kinase activity of PKM2 that is necessary for sustained proliferative signaling of cancer cells. Mol. Cell 2014, 53:700-709.
    • (2014) Mol. Cell , vol.53 , pp. 700-709
    • Keller, K.E.1    Doctor, Z.M.2    Dwyer, Z.W.3    Lee, Y.S.4
  • 17
    • 0030333069 scopus 로고    scopus 로고
    • Cell cycle-dependent regulation of cellular ATP concentration, and depolymerization of the interphase microtubular network induced by elevated cellular ATP concentration in whole fibroblasts
    • Marcussen M., Larsen P.J. Cell cycle-dependent regulation of cellular ATP concentration, and depolymerization of the interphase microtubular network induced by elevated cellular ATP concentration in whole fibroblasts. Cell Motil. Cytoskeleton 1996, 35:94-99.
    • (1996) Cell Motil. Cytoskeleton , vol.35 , pp. 94-99
    • Marcussen, M.1    Larsen, P.J.2
  • 18
    • 0020651272 scopus 로고
    • An enzymatic method for [32P]phosphoenolpyruvate synthesis
    • Mattoo R.L., Waygood E.B. An enzymatic method for [32P]phosphoenolpyruvate synthesis. Anal. Biochem. 1983, 128:245-249.
    • (1983) Anal. Biochem. , vol.128 , pp. 245-249
    • Mattoo, R.L.1    Waygood, E.B.2
  • 19
    • 0031730047 scopus 로고    scopus 로고
    • Metabolic characteristics of different malignant cancer cell lines
    • Mazurek S., Grimm H., Wilker S., Leib S., Eigenbrodt E. Metabolic characteristics of different malignant cancer cell lines. Anticancer Res. 1998, 18(5A):3275-3282.
    • (1998) Anticancer Res. , vol.18 , Issue.5 A , pp. 3275-3282
    • Mazurek, S.1    Grimm, H.2    Wilker, S.3    Leib, S.4    Eigenbrodt, E.5
  • 20
    • 84896761915 scopus 로고    scopus 로고
    • Please keep me 2uned to PKM2
    • McKnight S.L. Please keep me 2uned to PKM2. Mol. Cell 2014, 53:683-684.
    • (2014) Mol. Cell , vol.53 , pp. 683-684
    • McKnight, S.L.1
  • 21
    • 84881077601 scopus 로고    scopus 로고
    • Functional lysine modification by an intrinsically reactive primary glycolytic metabolite
    • Moellering R.E., Cravatt B.F. Functional lysine modification by an intrinsically reactive primary glycolytic metabolite. Science 2013, 341:549-553.
    • (2013) Science , vol.341 , pp. 549-553
    • Moellering, R.E.1    Cravatt, B.F.2
  • 23
    • 0013841130 scopus 로고
    • A kinetic study of nucleotide interactions with pyruvate kinase
    • Plowman K.M., Krall A.R. A kinetic study of nucleotide interactions with pyruvate kinase. Biochemistry 1965, 4:2809-2814.
    • (1965) Biochemistry , vol.4 , pp. 2809-2814
    • Plowman, K.M.1    Krall, A.R.2
  • 24
    • 0023796705 scopus 로고
    • Nonenzymatic phosphorylation of tyrosine and serine by ATP is catalyzed by manganese but not magnesium
    • Schieven G., Martin G.S. Nonenzymatic phosphorylation of tyrosine and serine by ATP is catalyzed by manganese but not magnesium. J. Biol. Chem. 1988, 263:15590-15593.
    • (1988) J. Biol. Chem. , vol.263 , pp. 15590-15593
    • Schieven, G.1    Martin, G.S.2
  • 27
    • 0028225462 scopus 로고
    • SREBP-1, a membrane-bound transcription factor released by sterol-regulated proteolysis
    • Wang X., Sato R., Brown M.S., Hua X., Goldstein J.L. SREBP-1, a membrane-bound transcription factor released by sterol-regulated proteolysis. Cell 1994, 77:53-62.
    • (1994) Cell , vol.77 , pp. 53-62
    • Wang, X.1    Sato, R.2    Brown, M.S.3    Hua, X.4    Goldstein, J.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.