메뉴 건너뛰기




Volumn 1810, Issue 8, 2011, Pages 741-751

On the functional diversity of glyceraldehyde-3-phosphate dehydrogenase: Biochemical mechanisms and regulatory control

Author keywords

Glyceraldehyde 3 phosphate dehydrogenase; Multifunctional protein; Subcellular translocation

Indexed keywords

ANDROGEN RECEPTOR; ANGIOTENSIN 1 RECEPTOR; COLONY STIMULATING FACTOR 1; DNA (APURINIC OR APYRIMIDINIC SITE) LYASE; ENDOTHELIN 1; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; MESSENGER RNA; PROTEIN SIAH1; RAB PROTEIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 79959226194     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2011.05.010     Document Type: Review
Times cited : (262)

References (110)
  • 1
    • 0032973950 scopus 로고    scopus 로고
    • New insights into an old protein: The functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase
    • DOI 10.1016/S0167-4838(99)00119-3, PII S0167483899001193
    • M.A. Sirover New insight into an old protein: the functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase Biochim. Biophys. Acta 1432 1999 159 184 (Pubitemid 29304525)
    • (1999) Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology , vol.1432 , Issue.2 , pp. 159-184
    • Sirover, M.A.1
  • 2
    • 23844452781 scopus 로고    scopus 로고
    • New nuclear functions of the glycolytic protein, glyceraldehyde-3- phosphate dehydrogenase, in mammalian cells
    • DOI 10.1002/jcb.20399
    • M.A. Sirover New nuclear functions of the glycolytic protein glyceraldehyde-3-phosphate dehydrogenase J. Cell. Biochem. 95 2005 45 52 (Pubitemid 41420214)
    • (2005) Journal of Cellular Biochemistry , vol.95 , Issue.1 , pp. 45-52
    • Sirover, M.A.1
  • 3
    • 0041352962 scopus 로고    scopus 로고
    • S phase activation of the histone H2B promoter by OCA-S, a coactivator complex that contains GAPDH as a key component
    • DOI 10.1016/S0092-8674(03)00552-X
    • I. Zheng, R.G. Roeder, and Y. Luo S phase activation of the histone H2B promoter by OCA-S, a coactivator complex that contains GAPDH as a key component Cell 114 2003 255 266 (Pubitemid 36936918)
    • (2003) Cell , vol.114 , Issue.2 , pp. 255-266
    • Zheng, L.1    Roeder, R.G.2    Luo, Y.3
  • 4
    • 0042698617 scopus 로고    scopus 로고
    • Gene switching by metabolic enzymes - How did you get on the invitation list?
    • DOI 10.1016/S0092-8674(03)00563-4
    • S. McKnight Gene switching by metabolic enzymes - how did you get on the invitation list? Cell 114 2003 150 152 (Pubitemid 36936907)
    • (2003) Cell , vol.114 , Issue.2 , pp. 150-152
    • McKnight, S.1
  • 5
    • 18144423122 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase binds to the AU-rich 3′ untranslated region of colony-stimulating factor-1 (CSF-1) messenger RNA in human ovarian cancer cells: Possible role in CSF-1 posttranscriptional regulation and tumor phenotype
    • DOI 10.1158/0008-5472.CAN-04-3954
    • N. Bonafe, M. Gilmore-Hebert, N.L. Folk, M. Azodi, Y. Zhou, and S.K. Chambers Glyceraldehyde-3-phosphate dehydrogenase binds to the AU-rich 3′untranslated region of colony-stimulating factor-1 (CSF-1) messenger RNA in human ovarian cancer cells: possible role of CSF-1 posttranscriptional regulation and tumor phenotype Cancer Res. 65 2005 3762 3771 (Pubitemid 40616354)
    • (2005) Cancer Research , vol.65 , Issue.9 , pp. 3762-3771
    • Bonafe, N.1    Gilmore-Hebert, M.2    Folk, N.L.3    Azodi, M.4    Zhon, Y.5    Chambers, S.K.6
  • 6
    • 52449119928 scopus 로고    scopus 로고
    • The multifunctional protein glyceraldehyde-3-phosphate dehydrogenase is both regulated and controls colony-stimulating factor-1 messenger RNA stability in ovarian cancer
    • Y. Zhou, X. Yi, J.B. Stofffer, N. Bonafe, M. Gilmore-Hebert, J. McAlpine, and S.K. Chambers The multifunctional protein glyceraldehyde-3-phosphate dehydrogenase is both regulated and controls colony-stimulating factor-1 messenger RNA stability in ovarian cancer Mol. Cancer Res. 6 2008 1375 1384
    • (2008) Mol. Cancer Res. , vol.6 , pp. 1375-1384
    • Zhou, Y.1    Yi, X.2    Stofffer, J.B.3    Bonafe, N.4    Gilmore-Hebert, M.5    McAlpine, J.6    Chambers, S.K.7
  • 9
    • 0035951872 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase is required for vesicular transport in the early secretory pathway
    • E.J. Tisdale Glyceraldehyde-3-phosphate dehydrogenase is required for vesicular transport in the early secretory pathway J. Biol. Chem. 276 2001 2480 2486
    • (2001) J. Biol. Chem. , vol.276 , pp. 2480-2486
    • Tisdale, E.J.1
  • 10
    • 0036479109 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase is phosphorylated by protein kinase Cιλ and plays a role in microtubule dynamics in the early secretory pathway
    • DOI 10.1074/jbc.M109744200
    • E.J. Tisdale Glyceraldehyde-3-phosphate dehydrogenase is phosphorylated by protein kinase Cí/λ and plays a role in microtubule dynamics in the early secretory pathway J. Biol. Chem. 277 2002 3334 3341 (Pubitemid 34953200)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.5 , pp. 3334-3341
    • Tisdale, E.J.1
  • 11
    • 0346732291 scopus 로고    scopus 로고
    • Rab2 Interacts Directly with Atypical Protein Kinase C (aPKC) ι/λ and Inhibits aPKCι/λ-dependent Glyceraldehyde-3- phosphate Dehydrogenase Phosphorylation
    • DOI 10.1074/jbc.M309343200
    • E.J. Tisdale Rab2 interacts directly with atypical protein kinase C (aPKC) í/λ and inhibits aPKCí/λ-dependent glyceraldehyde-3-phosphate dehydrogenase phosphorylation J. Biol. Chem. 278 2003 52524 52530 (Pubitemid 38035847)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.52 , pp. 52524-52530
    • Tisdale, E.J.1
  • 12
    • 11144234184 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase interacts with Rab2 and plays an essential role in endoplasmic reticulum to golgi transport exclusive of its glycolytic activity
    • DOI 10.1074/jbc.M409472200
    • E.J. Tisdale, C. Kelly, and C.R. Artalejo Glyceraldehyde-3-phosphate dehydrogenase interacts with Rab2 and plays an essential role in endoplasmic reticulum to golgi transport exclusive of its glycolytic activity J. Biol. Chem. 279 2004 54046 54052 (Pubitemid 40053138)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.52 , pp. 54046-54052
    • Tisdale, E.J.1    Kelly, C.2    Artalejo, C.E.3
  • 13
    • 33646835100 scopus 로고    scopus 로고
    • Src-dependent aprotein kinase C ι/λ (aPKCι/λ) tyrosine phosphorylation is required for aPKCι/λ association with Rab2 and glyceraldehyde-3-phosphate dehydrogenase on pre-Golgi intermediates
    • DOI 10.1074/jbc.M513031200
    • E.J. Tisdale, and C.R. Artalejo Src-dependent aprotein kinase C í/λ (aPKCí/λ) tyrosine phosphorylation is required for aPKCí/λ association with Rab2 and glyceraldehyde-3-phosphate dehydrogenase on pre-golgi intermediates J. Biol. Chem. 281 2006 2006 8436 8442 (Pubitemid 43847945)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.13 , pp. 8436-8442
    • Tisdale, E.J.1    Artalejo, C.R.2
  • 14
    • 34249003714 scopus 로고    scopus 로고
    • A GAPDH mutant defective in Src-dependent tyrosine phosphorylation impedes Rab2-mediated events
    • DOI 10.1111/j.1600-0854.2007.00569.x
    • E.J. Tisdale, and C.R. Artalejo A GAPDH mutant defective in src-dependent tyrosine phosphorylation impedes Rab2-mediated events Traffic 8 2007 733 741 (Pubitemid 46785154)
    • (2007) Traffic , vol.8 , Issue.6 , pp. 733-741
    • Tisdale, E.J.1    Artalejo, C.R.2
  • 15
    • 65549112190 scopus 로고    scopus 로고
    • Rab2 utilizes glyceraldehyde-3-phosphate dehydrogenase and protein kinase Cí to associate with microtubules and to recruit dynein
    • E.J. Tisdale, F. Azizi, and C.R. Artalejo Rab2 utilizes glyceraldehyde-3-phosphate dehydrogenase and protein kinase Cí to associate with microtubules and to recruit dynein J. Biol. Chem. 284 2009 5876 5884
    • (2009) J. Biol. Chem. , vol.284 , pp. 5876-5884
    • Tisdale, E.J.1    Azizi, F.2    Artalejo, C.R.3
  • 16
    • 34547957476 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase enhances transcriptional activity of androgen receptor in prostate cancer cells
    • DOI 10.1074/jbc.M610724200
    • N. Harada, R. Yasunaga, Y. Higashimura, R. Yamaji, K. Fujimoto, J. Moss, H. Inui, and Y. Nakano Glyceraldehyde-3-phosphate dehydrogenase enhances transcriptional activity of androgen receptor in prostate cancer cells J. Biol. Chem. 282 2007 22651 22661 (Pubitemid 47267369)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.31 , pp. 22651-22661
    • Harada, N.1    Yasunaga, R.2    Higashimura, Y.3    Yamaji, R.4    Fujimoto, K.5    Moss, J.6    Inui, H.7    Nakano, Y.8
  • 17
    • 34047254111 scopus 로고    scopus 로고
    • The macrophage cell surface glyceraldehyde-3-phosphate dehydrogenase is a novel transferrin receptor
    • DOI 10.1074/jbc.M608328200
    • C.I. Raje, S. Kumar, A. Harle, J.S. Nanda, and M. Raje The macrophage cell surface glyceraldehyde-3-phosphate dehydrogenase is a novel transferrin receptor J. Biol. Chem. 282 2007 3252 3261 (Pubitemid 47084366)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.5 , pp. 3252-3261
    • Raje, C.I.1    Kumar, S.2    Harle, A.3    Nanda, J.S.4    Raje, M.5
  • 18
    • 1242294390 scopus 로고    scopus 로고
    • Rapid Shortening of Telomere Length in Response to Ceramide Involves the Inhibition of Telomere Binding Activity of Nuclear Glyceraldehyde-3-phosphate Dehydrogenase
    • DOI 10.1074/jbc.M310549200
    • K.P. Sundararaj, R.E. Wood, S. Ponnusamy, A.M. Salas, Z. Szulc, A. Bielawska, L.M. Obeid, Y.A. Hannun, and B. Ogretmen Rapid shortening of telomere length in response to ceramide involves the inhibition of telomere binding activity of nuclear glyceraldehyde-3-phosphate dehydrogenase J. Biol. Chem. 279 2004 6152 6162 (Pubitemid 38220648)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.7 , pp. 6152-6162
    • Sundararaj, K.P.1    Wood, R.E.2    Ponnusamy, S.3    Salas, A.M.4    Szulc, Z.5    Bielawska, A.6    Obeid, L.M.7    Hannun, Y.A.8    Ogretmen, B.9
  • 19
    • 70449525136 scopus 로고    scopus 로고
    • Direct binding of glyceraldehyde-3-phosphate dehydrogenase to telomeric DNA protects telomeres against chemotherapy-induced rapid degradation
    • N.A. Demarse, S. Ponnusamy, E.K. Spicer, E. Apohan, J.E. Baatz, B. Ogretman, and B.C. Davies Direct binding of glyceraldehyde-3-phosphate dehydrogenase to telomeric DNA protects telomeres against chemotherapy-induced rapid degradation J. Mol. Biol. 394 2009 789 803
    • (2009) J. Mol. Biol. , vol.394 , pp. 789-803
    • Demarse, N.A.1    Ponnusamy, S.2    Spicer, E.K.3    Apohan, E.4    Baatz, J.E.5    Ogretman, B.6    Davies, B.C.7
  • 20
    • 57649171241 scopus 로고    scopus 로고
    • Human glyceraldehyde-3-phosphate dehydrogenase plays a direct role in reactivating oxidized forms of the DNA repair enzyme APE1
    • S. Azam, N. Jouvet, A. Jilani, R. Vongsamphanh, X. Yang, S. Yang, and D. Ramotar Human glyceraldehyde-3-phosphate dehydrogenase plays a direct role in reactivating oxidized forms of the DNA repair enzyme APE1 J. Biol. Chem. 283 2008 30632 30641
    • (2008) J. Biol. Chem. , vol.283 , pp. 30632-30641
    • Azam, S.1    Jouvet, N.2    Jilani, A.3    Vongsamphanh, R.4    Yang, X.5    Yang, S.6    Ramotar, D.7
  • 21
    • 22144444152 scopus 로고    scopus 로고
    • A central role for S-nitrosylation in apoptosis
    • DOI 10.1038/ncb0705-645
    • M. Benhar, and J.S. Stamler A central role for S-nitrosylation in apoptosis Nat. Cell Biol. 7 2005 645 646 (Pubitemid 40975742)
    • (2005) Nature Cell Biology , vol.7 , Issue.7 , pp. 645-646
    • Benhar, M.1    Stamler, J.S.2
  • 23
    • 33746445177 scopus 로고    scopus 로고
    • Nitric oxide-GAPDH-Siah: A novel cell death cascade
    • M.R. Hara, and S.H. Snyder Nitric oxide-GAPDH-Siah: a novel cell death cascade Cell. Mol. Neurobiol. 26 2006 525 536
    • (2006) Cell. Mol. Neurobiol. , vol.26 , pp. 525-536
    • Hara, M.R.1    Snyder, S.H.2
  • 29
    • 68349109656 scopus 로고    scopus 로고
    • According to GOSPEL: Filling in the GAP(DH) of NO-mediated neurotoxicity
    • T. Nakamura, and S.A. Lipton According to GOSPEL: filling in the GAP(DH) of NO-mediated neurotoxicity Neuron 63 2009 3 6
    • (2009) Neuron , vol.63 , pp. 3-6
    • Nakamura, T.1    Lipton, S.A.2
  • 30
    • 34548845570 scopus 로고    scopus 로고
    • The active site cysteine of the proapoptotic protein glyceraldehyde-3- phosphate dehydrogenase is essential in oxidative stress-induced aggregation and cell death
    • DOI 10.1074/jbc.M704199200
    • H. Nakajima, W. Amano, A. Fujita, A. Fukuhara, Y.-T. Azuma, F. Hata, T. Inui, and T. Takeuchi The active site cysteine of the proapoptotic protein glyceraldehyde-3-phosphate dehydrogenase is essential in oxidative stress-induced aggregation and cell death J. Biol. Chem. 282 2007 26562 26574 (Pubitemid 47443820)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.36 , pp. 26562-26574
    • Nakajima, H.1    Amano, W.2    Fujita, A.3    Fukuhara, A.4    Azuma, Y.-T.5    Hata, F.6    Inui, T.7    Takeuchi, T.8
  • 31
    • 34250014485 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase exerts different biologic activities in apoptotic and proliferating hepatocytes according to its subcellular localization
    • DOI 10.1007/s11010-006-9341-1
    • L. Barbini, J. Rodriguez, F. Dominguez, and F. Vega Glyceraldehyde-3- phosphate dehydrogenase exerts different biologic activities in apoptotic and proliferating hepatocytes according to its subcellular localization Mol. Cell. Biochem. 300 2007 19 28 (Pubitemid 46881812)
    • (2007) Molecular and Cellular Biochemistry , vol.300 , Issue.1-2 , pp. 19-28
    • Barbini, L.1    Rodriguez, J.2    Dominguez, F.3    Vega, F.4
  • 32
    • 34548101969 scopus 로고    scopus 로고
    • Involvement of glyceraldehyde-3-phosphate dehydrogenase in tumor necrosis factor-related apoptosis-inducing ligand-mediated death of thyroid cancer cells
    • DOI 10.1210/en.2006-1511
    • Z.-X. Du, H.-Q. Wang, H.-Y. Zhang, and D.-X. Gao Involvement of glyceraldehyde-3-phosphate dehydrogenase in tumor necrosis factor-related apoptosis-inducing ligand-mediated death of thyroid cancer cells Endocrinology 148 2007 4352 4361 (Pubitemid 47295684)
    • (2007) Endocrinology , vol.148 , Issue.9 , pp. 4352-4361
    • Du, Z.-X.1    Wang, H.-Q.2    Zhang, H.-Y.3    Gao, D.-X.4
  • 35
    • 70449703211 scopus 로고    scopus 로고
    • An aggregate-prone mutant of human glyceraldehyde-3-phosphate dehydrogenase augments oxidative-stress induced cell death in SH-SY5Y cells
    • H. Nakajima, W. Amano, A. Fukuhara, T. Kubo, S. Misaki, Y.-T. Azuma, T. Inui, and T. Takeuchi An aggregate-prone mutant of human glyceraldehyde-3- phosphate dehydrogenase augments oxidative-stress induced cell death in SH-SY5Y cells Biochem. Biophys. Res. Commun. 390 2009 1066 1071
    • (2009) Biochem. Biophys. Res. Commun. , vol.390 , pp. 1066-1071
    • Nakajima, H.1    Amano, W.2    Fukuhara, A.3    Kubo, T.4    Misaki, S.5    Azuma, Y.-T.6    Inui, T.7    Takeuchi, T.8
  • 37
    • 67649410138 scopus 로고    scopus 로고
    • Involvement of glyceraldehyde-3-phosphate dehydrogenase in rotenone-induced cell apoptosis: Relevance to protein misfolding and aggregation
    • J. Huang, L. Hao, N. Xiong, X. Cao, Z. Liang, S. Sun, and T. Wang Involvement of glyceraldehyde-3-phosphate dehydrogenase in rotenone-induced cell apoptosis: relevance to protein misfolding and aggregation Brain Res. 1279 2009 1 8
    • (2009) Brain Res. , vol.1279 , pp. 1-8
    • Huang, J.1    Hao, L.2    Xiong, N.3    Cao, X.4    Liang, Z.5    Sun, S.6    Wang, T.7
  • 38
    • 78649842470 scopus 로고    scopus 로고
    • The diverse functions of GAPDH: Views from different subcellular compartments
    • C. Tristan, N. Shahani, T.W. Sedlak, and A. Sawa The diverse functions of GAPDH: views from different subcellular compartments Cell. Signal. 23 2011 317 323
    • (2011) Cell. Signal. , vol.23 , pp. 317-323
    • Tristan, C.1    Shahani, N.2    Sedlak, T.W.3    Sawa, A.4
  • 40
    • 34547558087 scopus 로고    scopus 로고
    • GAPDH and the search for alternative energy
    • DOI 10.1038/ncb0807-869, PII NCB0807-869
    • S. Song, and T. Finkel GAPDH and the search for alternative energy Nat. Cell Biol. 9 2007 869 870 (Pubitemid 47190437)
    • (2007) Nature Cell Biology , vol.9 , Issue.8 , pp. 869-870
    • Song, S.1    Finkel, T.2
  • 42
    • 0034710891 scopus 로고    scopus 로고
    • Hyperglycemia-induced mitochondrial superoxide overproduction activates the hexosamine pathway and induces plasminogen activator inhibitor-1 expression by increasing Sp1 glycosylation
    • X.-L. Du, D. Edelstein, L. Rossetti, I.G. Fantus, H. Goldberg, F. Ziyadeh, J. Wu, and M. Brownlee Hyperglycemia-induced mitochondrial superoxide overproduction activates the hexosamine pathway and induces plasminogen activator inhibitor-1 expression by increasing Sp1 glycosylation Proc. Natl. Acad. Sci. U. S. A. 97 2000 12222 12226
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 12222-12226
    • Du, X.-L.1    Edelstein, D.2    Rossetti, L.3    Fantus, I.G.4    Goldberg, H.5    Ziyadeh, F.6    Wu, J.7    Brownlee, M.8
  • 43
    • 85047691537 scopus 로고    scopus 로고
    • Inhibition of GAPDH activity by poly(ADP-ribose) polymerase activates three major pathways of hyperglycemic damage in endothelial cells
    • DOI 10.1172/JCI200318127
    • X. Du, T. Matsumura, D. Edelstein, L. Rossetti, Z. Zsengeller, C. Szabo, and M. Brownlee Inhibition of GAPDH activity by poly (ADP-ribose) polymerase activates three major pathways of hyperglycemic damage in endothelial cells J. Clin. Invest. 112 2003 1049 1057 (Pubitemid 38056320)
    • (2003) Journal of Clinical Investigation , vol.112 , Issue.7 , pp. 1049-1057
    • Du, X.1    Matsumura, T.2    Edelstein, D.3    Rossetti, L.4    Zsengeller, Z.5    Szabo, C.6    Brownlee, M.7
  • 44
    • 0242380324 scopus 로고    scopus 로고
    • Diabetes, microvascular complications, and cardiovascular complications: What is it about glucose?
    • DOI 10.1172/JCI200319902
    • J.E.B. Reusch Diabetes, microvascular complications, and cardiovascular complications: what is it about glucose? J. Clin. Invest. 112 2003 986 988 (Pubitemid 38056313)
    • (2003) Journal of Clinical Investigation , vol.112 , Issue.7 , pp. 986-988
    • Reusch, J.E.B.1
  • 45
    • 64149103180 scopus 로고    scopus 로고
    • Role of nitrosative stress in the pathogenesis of diabetic vascular dysfunction
    • C. Szabo Role of nitrosative stress in the pathogenesis of diabetic vascular dysfunction Br. J. Pharmacol. 156 2009 713 727
    • (2009) Br. J. Pharmacol. , vol.156 , pp. 713-727
    • Szabo, C.1
  • 46
    • 64049105963 scopus 로고    scopus 로고
    • Differential regulation of high glucose-induced glyceraldehyde-3- phosphate dehydrogenase nuclear accumulation in Muller cells by IL-1beta and IL-6
    • E.C.K. Yego, J.A. Vincent, V.P. Sarthy, I. Busik, and S. Mohr Differential regulation of high glucose-induced glyceraldehyde-3-phosphate dehydrogenase nuclear accumulation in Muller cells by IL-1beta and IL-6 Invest. Ophthalmol. Vis. Sci. 50 2009 1920 1928
    • (2009) Invest. Ophthalmol. Vis. Sci. , vol.50 , pp. 1920-1928
    • Yego, E.C.K.1    Vincent, J.A.2    Sarthy, V.P.3    Busik, I.4    Mohr, S.5
  • 47
    • 77449121531 scopus 로고    scopus 로고
    • Siah-1 protein is necessary for high glucose-induced glyceraldehydes-3- phosphate dehydrogenase nuclear accumulation and cell death in Muller cells
    • E.C.K. Yego, and S. Mohr Siah-1 protein is necessary for high glucose-induced glyceraldehydes-3-phosphate dehydrogenase nuclear accumulation and cell death in Muller cells J. Biol. Chem. 285 2010 3181 3190
    • (2010) J. Biol. Chem. , vol.285 , pp. 3181-3190
    • Yego, E.C.K.1    Mohr, S.2
  • 48
    • 42549083245 scopus 로고    scopus 로고
    • Succination of proteins by fumarate: Mechanism of inactivation of glyceraldehyde-3-phosphate dehydrogenase in diabetes
    • DOI 10.1196/annals.1433.047, The Maillard Reaction Recent Advances in Food and Biomedical Sciences
    • M. Blatnik, S.R. Thorpe, and J.W. Baynes Succination of proteins by fumarate: mechanism of inactivation of glyceraldehyde-3-phosphate dehydrogenase in diabetes Ann. N. Y. Acad. Sci. 1126 2008 272 275 (Pubitemid 351589309)
    • (2008) Annals of the New York Academy of Sciences , vol.1126 , pp. 272-275
    • Blatnik, M.1    Thorpe, S.R.2    Baynes, J.W.3
  • 49
    • 0036778378 scopus 로고    scopus 로고
    • Alteration of intracellular structure and function of glyceraldehyde-3-phosphate dehydrogenase: A common phenotype of neurodegenerative disorders?
    • DOI 10.1016/S0161-813X(02)00062-1, PII S0161813X02000621
    • J.L. Mazzola, and M.A. Sirover Alteration of intracellular structure and function of glyceraldehyde-3-phosphate dehydrogenase: a common phenotype of neurodegenerative disorders? Neurotoxicology 23 2002 603 609 (Pubitemid 36527680)
    • (2002) NeuroToxicology , vol.23 , Issue.4-5 , pp. 603-609
    • Mazzola, J.L.1    Sirover, M.A.2
  • 50
    • 77954497959 scopus 로고    scopus 로고
    • Oxidatively modified glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and Alzheimer's disease: Many pathways to Neurodegeneration
    • D.A. Butterfield, S.S. Hardas, and M.L. Bader Lange Oxidatively modified glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and Alzheimer's disease: many pathways to Neurodegeneration J. Alzheimers Dis. 20 2010 369 393
    • (2010) J. Alzheimers Dis. , vol.20 , pp. 369-393
    • Butterfield, D.A.1    Hardas, S.S.2    Bader Lange, M.L.3
  • 51
    • 33750063178 scopus 로고    scopus 로고
    • Interaction of TPPP/p25 protein with glyceraldehyde-3-phosphate dehydrogenase and their co-localization in Lewy bodies
    • DOI 10.1016/j.febslet.2006.09.037, PII S001457930601146X
    • J. Oláh, N. Tokési, O. Vincze, I. Horváth, A. Lehotzky, A. Erdei, E. Szájli, K.F. Medzihradszky, F. Orosz Gabor, G. Kovács, and J. Ovádi Interaction of TPPP/p25 protein with glyceraldehyde-3-phosphate dehydrogenase and their co-localization in Lewy bodies FEBS Lett. 580 2006 5807 5814 (Pubitemid 44584278)
    • (2006) FEBS Letters , vol.580 , Issue.25 , pp. 5807-5814
    • Olah, J.1    Tokesi, N.2    Vincze, O.3    Horvath, I.4    Lehotzky, A.5    Erdei, A.6    Szajli, E.7    Medzihradszky, K.F.8    Orosz, F.9    Kovacs, G.G.10    Ovadi, J.11
  • 56
    • 10744231179 scopus 로고    scopus 로고
    • The N'-terminal domain of glyceraldehyde-3-phosphate dehydrogenase of the apicomplexan Plasmodium falciparum mediates GTPase Rab2-dependent recruitment to membranes
    • DOI 10.1515/BC.2003.135
    • C.A. Daubenberger, E.J. Tisdale, M. Curcic, D. Diaz, O. Silvie, D. Mazier, W. Eling, B. Bohrmann, H. Matile, and G. Pluschke The N'terminal domain of glyceraldehyde-3-phosphate dehydrogenase of the apicomplexan Plasmodium falciparum mediates GTPase Rab2-recruitment to membranes Biol. Chem. 384 2003 1227 1237 (Pubitemid 37121194)
    • (2003) Biological Chemistry , vol.384 , Issue.8 , pp. 1227-1237
    • Daubenberger, C.A.1    Tisdale, E.J.2    Curcic, M.3    Diaz, D.4    Silvie, O.5    Mazier, D.6    Eling, W.7    Bohrmann, B.8    Matile, H.9    Pluschke, G.10
  • 58
    • 0013999607 scopus 로고
    • Comparison of glycolytic enzyme activities in a series of human and rodent hepatomas
    • G.E. Boxer, and C.E. Shonk Comparison of glycolytic enzyme activities in a series of human and rodent hepatomas Adv. Enzyme Regul. 4 1966 107 114
    • (1966) Adv. Enzyme Regul. , vol.4 , pp. 107-114
    • Boxer, G.E.1    Shonk, C.E.2
  • 59
    • 0015251175 scopus 로고
    • Bioenergetics and the problem of tumor growth
    • E. Racker Bioenergetics and the problem of tumor growth Am. Sci. 60 1972 56 63
    • (1972) Am. Sci. , vol.60 , pp. 56-63
    • Racker, E.1
  • 60
    • 70449712602 scopus 로고    scopus 로고
    • Novel roles for GAPDH in cell death and carcinogenesis
    • A. Colell, D.R. Green, and J.-E. Ricci Novel roles for GAPDH in cell death and carcinogenesis Cell Death Diff. 16 2009 1573 1581
    • (2009) Cell Death Diff. , vol.16 , pp. 1573-1581
    • Colell, A.1    Green, D.R.2    Ricci, J.-E.3
  • 61
    • 33644750203 scopus 로고    scopus 로고
    • Effects of Histone Deacetylase Inhibitor (HDACi); Trichostatin-A (TSA) on the expression of housekeeping genes
    • A. Mogal, and S.A. Abdulkadir Effects of Histone Deacetylase Inhibitor (HDACi); Trichostatin-A (TSA) on the expression of housekeeping genes Mol. Cell. Probes 20 2005 81 86
    • (2005) Mol. Cell. Probes , vol.20 , pp. 81-86
    • Mogal, A.1    Abdulkadir, S.A.2
  • 62
    • 34548034236 scopus 로고    scopus 로고
    • De-regulation of common housekeeping genes in hepatocellular carcinoma
    • S. Waxman, and E. Wurmbach De-regulation of common housekeeping genes in hepatocellular carcinoma BMC Genomics 8 2007 243
    • (2007) BMC Genomics , vol.8 , pp. 243
    • Waxman, S.1    Wurmbach, E.2
  • 64
    • 0343619342 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase gene expression in human breast cancer
    • DOI 10.1016/S0959-8049(00)00051-4, PII S0959804900000514
    • F. Revillion, V. Pawlowski, L. Hornez, and J.P. Peyrat Glyceraldehyde-3-phosphate dehydrogenase gene expression in human breast cancer Eur. J. Cancer 36 2000 1038 1042 (Pubitemid 30316430)
    • (2000) European Journal of Cancer , vol.36 , Issue.8 , pp. 1038-1042
    • Revillion, F.1    Pawlowski, V.2    Hornez, L.3    Peyrat, J.-P.4
  • 65
    • 78649976904 scopus 로고    scopus 로고
    • Identification of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) as a binding protein for a 68-kDa Bacillus thuringiensis parasporal protein cytotoxic against leukaemic cells
    • E. Krishnan, J.E. Ker, S.M. Mohammed, and V.D. Nadarajah Identification of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) as a binding protein for a 68-kDa Bacillus thuringiensis parasporal protein cytotoxic against leukaemic cells J. Biomed. Sci. 17 2010 86
    • (2010) J. Biomed. Sci. , vol.17 , pp. 86
    • Krishnan, E.1    Ker, J.E.2    Mohammed, S.M.3    Nadarajah, V.D.4
  • 66
    • 77956337524 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase as a surface associated antigen on human breast cancer cell lines MACL-1 and MGSO-3
    • C.R. Correa, C.M. Bertollo, C.S. Zouain, and A.M. Goes Glyceraldehyde-3-phosphate dehydrogenase as a surface associated antigen on human breast cancer cell lines MACL-1 and MGSO-3 Oncol. Rep. 24 2010 677 685
    • (2010) Oncol. Rep. , vol.24 , pp. 677-685
    • Correa, C.R.1    Bertollo, C.M.2    Zouain, C.S.3    Goes, A.M.4
  • 67
    • 34249821909 scopus 로고    scopus 로고
    • II68-TEC activity by human glyceraldehyde-3-phosphate dehydrogenase (GAPDH)
    • DOI 10.1042/BJ20061297
    • S. Kim, J. Lee, and J. Kim Regulation of oncogenic transcription factor hTAF(II)68-TEC activity by human glyceraldehyde-3-phosphate dehydrogenase (GAPDH) Biochem. J. 404 2007 197 206 (Pubitemid 46849591)
    • (2007) Biochemical Journal , vol.404 , Issue.2 , pp. 197-206
    • Kim, S.1    Lee, J.2    Kim, J.3
  • 69
    • 0017255365 scopus 로고
    • Human glyceraldehyde-3-phosphate dehydrogenase in man-rodent somatic cell hybrids
    • G.A.P. Bruns, and P.S. Gerald Human glyceraldehyde-3-phosphate dehydrogenase in man-rodent somatic cell hybrids Science 192 1976 54 56
    • (1976) Science , vol.192 , pp. 54-56
    • Bruns, G.A.P.1    Gerald, P.S.2
  • 72
    • 0032188955 scopus 로고    scopus 로고
    • Several novel transcripts of glyceraldehyde-3-phosphate dehydrogenase expressed in adult chicken testis
    • DOI 10.1002/(SICI)1097-4644(19981001)71:1<127::AID-JCB13>3.0.CO;2-K
    • J. Mezquita, M. Pau, and C. Mezquita Several novel transcripts of glyceraldehyde-3-phosphate dehydrogenase expressed in adult chicken testis J. Cell. Biochem. 71 1998 127 139 (Pubitemid 28402551)
    • (1998) Journal of Cellular Biochemistry , vol.71 , Issue.1 , pp. 127-139
    • Mezquita, J.1    Pau, M.2    Mezquita, C.3
  • 73
    • 0034213740 scopus 로고    scopus 로고
    • Protein complexes in transport vesicle targeting
    • DOI 10.1016/S0962-8924(00)01754-2, PII S0962892400017542
    • W. Guo, M. Sacher, J. Barrowman, S. Ferro-Novick, and P. Novick Protein complexes in transport vesicle targeting Trends Cell Biol. 10 2000 251 255 (Pubitemid 30251987)
    • (2000) Trends in Cell Biology , vol.10 , Issue.6 , pp. 251-255
    • Guo, W.1    Sacher, M.2    Barrowman, J.3    Ferro-Novick, S.4    Novick, P.5
  • 74
    • 0036629335 scopus 로고    scopus 로고
    • Vesicle tethering complexes in membrane traffic
    • J.R.C. Whyte, and S. Munro Vesicle tethering complexes in membrane traffic J. Cell Sci. 115 2002 2627 2637 (Pubitemid 34846504)
    • (2002) Journal of Cell Science , vol.115 , Issue.13 , pp. 2627-2637
    • Whyte, J.R.C.1    Munro, S.2
  • 75
    • 77951645885 scopus 로고    scopus 로고
    • Androgen regulation of gene expression
    • K.R. Lamont, and D.J. Tindall Androgen regulation of gene expression Adv. Cancer Res. 107 2010 137 162
    • (2010) Adv. Cancer Res. , vol.107 , pp. 137-162
    • Lamont, K.R.1    Tindall, D.J.2
  • 77
    • 75449091373 scopus 로고    scopus 로고
    • Regulation of heat shock protein 70-1 expression by androgen receptor and its signaling in human prostate cancer cells
    • S. Lui, Z. Tan, M. Wortman, and Z. Dong Regulation of heat shock protein 70-1 expression by androgen receptor and its signaling in human prostate cancer cells Int. J. Oncol. 36 2010 459 467
    • (2010) Int. J. Oncol. , vol.36 , pp. 459-467
    • Lui, S.1    Tan, Z.2    Wortman, M.3    Dong, Z.4
  • 78
    • 0036786205 scopus 로고    scopus 로고
    • Mechanism of antiandrogen action: Key role of Hsp90 in conformational change and transcriptional activity of the androgen receptor
    • V. Georget, B. Terouanne, J.-C. Nicolas, and C. Sultan Mechanism of antiandrogen action: key role of Hsp90 in conformational change and transcriptional activity of the androgen receptor Biochemistry 41 2002 11824 11831
    • (2002) Biochemistry , vol.41 , pp. 11824-11831
    • Georget, V.1    Terouanne, B.2    Nicolas, J.-C.3    Sultan, C.4
  • 80
    • 33846691564 scopus 로고    scopus 로고
    • Iron uptake and metabolism in the new millennium
    • DOI 10.1016/j.tcb.2006.12.003, PII S0962892406003400
    • L.L. Dunn, Y.S. Rahmanto, and D.R. Richardson Iron uptake and metabolism in the new millennium Trends Cell Biol. 17 2007 93 100 (Pubitemid 46199183)
    • (2007) Trends in Cell Biology , vol.17 , Issue.2 , pp. 93-100
    • Dunn, L.L.1    Rahmanto, Y.S.2    Richardson, D.R.3
  • 81
    • 33750008791 scopus 로고    scopus 로고
    • The transferrin receptor part I: Biology and targeting with cytotoxic antibodies for the treatment of cancer
    • DOI 10.1016/j.clim.2006.06.010, PII S1521661606007807
    • T.R. Daniels, T. Delgado, J.A. Rodriguez, G. Helguera, and M.L. Penichet The transferrin receptor part I: biology and targeting with cytotoxic antibodies for the treatment of cancer Clin. Immunol. 121 2006 144 158 (Pubitemid 44592578)
    • (2006) Clinical Immunology , vol.121 , Issue.2 , pp. 144-158
    • Daniels, T.R.1    Delgado, T.2    Rodriguez, J.A.3    Helguera, G.4    Penichet, M.L.5
  • 82
    • 0029095105 scopus 로고
    • A mutation in glyceraldehyde-3-phosphate dehydrogenase alters endocytosis in CHO Cells
    • A.R. Robbins, R.D. Ward, and C. Oliver A mutation in glyceraldehyde-3- phosphate dehydrogenase alters endocytosis in CHO Cells J. Cell Biol. 130 1995 1093 1104
    • (1995) J. Cell Biol. , vol.130 , pp. 1093-1104
    • Robbins, A.R.1    Ward, R.D.2    Oliver, C.3
  • 83
    • 0030887909 scopus 로고    scopus 로고
    • Glutathione conjugates recognize the Rossmann fold of glyceraldehyde-3-phosphate dehydrogenase
    • M. Puder, and R.J. Soberman Glutathione conjugates recognize the Rossmann fold of glyceraldehyde-3-phosphate dehydrogenase J. Biol. Chem. 272 1997 10936 10940
    • (1997) J. Biol. Chem. , vol.272 , pp. 10936-10940
    • Puder, M.1    Soberman, R.J.2
  • 84
    • 0032975361 scopus 로고    scopus 로고
    • The staphylococcal transferrin-binding protein is a cell wall glyceraldehyde-3-phosphate dehydrogenase
    • B. Modun, and P. Williams The staphylococcal transferrin-binding protein is a cell wall glyceraldehyde-3-phosphate dehydrogenase Infect. Immun. 67 1999 1086 1092 (Pubitemid 29108481)
    • (1999) Infection and Immunity , vol.67 , Issue.3 , pp. 1086-1092
    • Modun, B.1    Williams, P.2
  • 85
    • 0034193246 scopus 로고    scopus 로고
    • The staphylococcal transferrin receptor: A glycolytic enzyme with novel functions
    • DOI 10.1016/S0966-842X(00)01728-5, PII S0966842X00017285
    • B. Modun, J. Morrissey, and P. Williams The staphylococcal transferrin receptor: a glycolytic enzyme with novel functions Trends Microbiol. 8 2000 231 237 (Pubitemid 30236244)
    • (2000) Trends in Microbiology , vol.8 , Issue.5 , pp. 231-237
    • Modun, B.1    Morrissey, J.2    Williams, P.3
  • 86
    • 1842687737 scopus 로고    scopus 로고
    • Characterization of two proteins of Staphylococcus aureus isolated from bovine clinical mastitis with homology to glyceraldehyde-3-phosphate dehydrogenase
    • DOI 10.1016/j.vetmic.2003.12.009, PII S037811350400029X
    • N. Goji, A.A. Potter, and J. Perez-Casal Characterization of two proteins of Staphylococcus aureus isolated from bovine clinical mastitis with homology to glyceraldehyde-3-phosphate dehydrogenase Vet. Microbiol. 99 2004 269 279 (Pubitemid 38471660)
    • (2004) Veterinary Microbiology , vol.99 , Issue.3-4 , pp. 269-279
    • Goji, N.1    Potter, A.A.2    Perez-Casal, J.3
  • 87
    • 0024399951 scopus 로고
    • Physical association of base excision repair enzymes with parental and replicating DNA in BHK-21 cells
    • K.A. Lee, and M.A. Sirover Physical association of base excision repair enzymes with parental or replicating DNA in BHK-21 cells Cancer Res. 49 1989 3037 3044 (Pubitemid 19148645)
    • (1989) Cancer Research , vol.49 , Issue.11 , pp. 3037-3044
    • Lee, K.A.1    Sirover, M.A.2
  • 88
    • 0024308384 scopus 로고
    • Immunocytochemical localization of the base excision repair enzyme uracil DNA glycosylase in quiescent and proliferating normal human cells
    • B.L. Cool, and M.A. Sirover Immunocytochemical analysis of the base excision repair enzyme uracil DNA glycosylase in quiescent and proliferating normal human cells Cancer Res. 49 1989 3029 3036 (Pubitemid 19148644)
    • (1989) Cancer Research , vol.49 , Issue.11 , pp. 3029-3036
    • Cool, B.L.1    Sirover, M.A.2
  • 89
    • 0034957426 scopus 로고    scopus 로고
    • Reversible nuclear translocation of glyceraldehyde-3-phosphate dehydrogenase upon serum depletion
    • H.-D. Schmitz Reversible nuclear translocation of glyceraldehyde-3- phosphate dehydrogenase upon serum depletion Eur. J. Cell Biol. 80 2001 419 427 (Pubitemid 32605785)
    • (2001) European Journal of Cell Biology , vol.80 , Issue.6 , pp. 419-427
    • Schmitz, H.-D.1
  • 90
    • 0038386268 scopus 로고    scopus 로고
    • Exportin 1-independent nuclear export of GAPDH
    • DOI 10.1016/S1065-6995(03)00096-9
    • H.-D. Schmitz, C. Dutine, and J. Bereiter-Hahn Exportin 1-independent nuclear export of GAPDH Cell Biol. Int. 27 2003 511 517 (Pubitemid 36808669)
    • (2003) Cell Biology International , vol.27 , Issue.7 , pp. 511-517
    • Schmitz, H.-D.1    Dutine, C.2    Bereiter-Hahn, J.3
  • 91
    • 77951969800 scopus 로고    scopus 로고
    • Activation of AMP-activated protein kinase stimulates the nuclear localization of glyceraldehyde-3-phosphate dehydrogenase in human diploid fibroblasts
    • H.J. Kwon, J.H. Rhim, I.-S. Jang, G.-E. Kim, S.C. Park, and E.-J. Yeo Activation of AMP-activated protein kinase stimulates the nuclear localization of glyceraldehyde-3-phosphate dehydrogenase in human diploid fibroblasts Exp. Mol. Med. 42 2010 254 269
    • (2010) Exp. Mol. Med. , vol.42 , pp. 254-269
    • Kwon, H.J.1    Rhim, J.H.2    Jang, I.-S.3    Kim, G.-E.4    Park, S.C.5    Yeo, E.-J.6
  • 92
    • 0028342951 scopus 로고
    • Repair of oxidative damage to DNA: Enzymology and biology
    • B. Demple, and L. Harrison Repair of oxidative damage to DNA: enzymology and biology Annu. Rev. Biochem. 63 1994 915 940
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 915-940
    • Demple, B.1    Harrison, L.2
  • 94
  • 95
    • 0033068028 scopus 로고    scopus 로고
    • Pathophysiology of endothelin in the cardiovascular system
    • DOI 10.1146/annurev.physiol.61.1.391
    • T. Miyauchi, and T. Masaki Pathophysiology of endothelin in the cardiovascular system Annu. Rev. Physiol. 61 1999 391 415 (Pubitemid 29143176)
    • (1999) Annual Review of Physiology , vol.61 , pp. 391-415
    • Miyauchi, T.1    Masaki, T.2
  • 96
    • 18844362863 scopus 로고    scopus 로고
    • Endothelin-1 expression is strongly repressed by AU-rich elements in the 3́-untranslated region of the gene
    • DOI 10.1042/BJ20041687
    • F.M. Reimunde, C. Castanares, M. Redondo-Horcajo, S. Lamas, and F. Rodriguez-Pascual Endothelin-1 expression is strongly repressed by AU-rich elements in the 3′-untranslated region of the gene Biochem. J. 387 2005 763 772 (Pubitemid 40685711)
    • (2005) Biochemical Journal , vol.387 , Issue.3 , pp. 763-772
    • Reimunde, F.M.1    Castanares, C.2    Redondo-Horcajo, M.3    Lamas, S.4    Rodriguez-Pascual, F.5
  • 97
    • 0029927267 scopus 로고    scopus 로고
    • Specific interaction of glyceraldehyde-3-phosphate dehydrogenase with the 5′-nontranslated region of hepatitis A virus
    • D.E. Schultz, C.C. Hardin, and S. Lemon Specific interaction of glyceraldehyde-3-phosphate dehydrogenase with the 5′-nontranslated region of hepatitis A virus J. Biol. Chem. 271 1996 14134 14142
    • (1996) J. Biol. Chem. , vol.271 , pp. 14134-14142
    • Schultz, D.E.1    Hardin, C.C.2    Lemon, S.3
  • 99
    • 74949093638 scopus 로고    scopus 로고
    • Role of CSF-1 in progression of epithelial ovarian cancer
    • S.K. Chambers Role of CSF-1 in progression of epithelial ovarian cancer Future Oncol. 5 2009 1429 1440
    • (2009) Future Oncol. , vol.5 , pp. 1429-1440
    • Chambers, S.K.1
  • 100
    • 0030849728 scopus 로고    scopus 로고
    • PHYL acts to down-regulate TTK88, a transcriptional repressor of neuronal cell fates, by a SINA-dependent mechanism
    • DOI 10.1016/S0092-8674(00)80506-1
    • A.H. Tang, T.P. Neufeld, E. Kwan, and G.M. Rubin PHYL Acts to down-regulate TTK88, a transcriptional repressor of neuronal cell fates, by a SINA-dependent mechanism Cell 90 1997 459 467 (Pubitemid 27347236)
    • (1997) Cell , vol.90 , Issue.3 , pp. 459-467
    • Tang, A.H.1    Neufeld, T.P.2    Kwan, E.3    Rubin, G.M.4
  • 101
    • 0030790796 scopus 로고    scopus 로고
    • Photoreceptor cell differentiation requires regulated proteolysis of the transcriptional repressor Tramtrack
    • DOI 10.1016/S0092-8674(00)80507-3
    • S. Li, Y. Li, R.W. Carthew, and Z.-C. Lai Photoreceptor cell differentiation requires regulated proteolysis of the transcriptional repressor Tramtrack Cell 90 1997 469 478 (Pubitemid 27347237)
    • (1997) Cell , vol.90 , Issue.3 , pp. 469-478
    • Li, S.1    Li, Y.2    Carthew, R.W.3    Lai, Z.-C.4
  • 102
    • 0031573441 scopus 로고    scopus 로고
    • Characterization of human homologs of the Drosophila seven in absentia (sina) gene
    • DOI 10.1006/geno.1997.4997
    • G. Hu, Y.-L. Chung, T. Glover, V. Valentine, A.T. Look, and E.R. Fearon Characterization of human homologs of the Drosophila seven in absentia (sina) gene Genomics 46 1997 103 111 (Pubitemid 27527697)
    • (1997) Genomics , vol.46 , Issue.1 , pp. 103-111
    • Hu, G.1    Chung, Y.-L.2    Glover, T.3    Valentine, V.4    Look, A.T.5    Fearon, E.R.6
  • 106
    • 72549095406 scopus 로고    scopus 로고
    • Regulation and signaling pathways of autophagy
    • C. He, and D.J. Klionsky Regulation and signaling pathways of autophagy Annu. Rev. Genet. 43 2009 67 93
    • (2009) Annu. Rev. Genet. , vol.43 , pp. 67-93
    • He, C.1    Klionsky, D.J.2
  • 107
    • 0033048066 scopus 로고    scopus 로고
    • Moonlighting proteins
    • DOI 10.1016/S0968-0004(98)01335-8, PII S0968000498013358
    • C.J. Jeffery Moonlighting proteins Trends Biochem. Sci. 24 1999 8 11 (Pubitemid 29074455)
    • (1999) Trends in Biochemical Sciences , vol.24 , Issue.1 , pp. 8-11
    • Jeffery, C.J.1
  • 108
    • 70449706229 scopus 로고    scopus 로고
    • Comprehensive analysis of the pseudogenes of glycolytic enzymes in vertebrates: The anomalously high number of GAPDH pseudogenes highlights a recent burst of retrotrans-positional activity
    • Y.-J. Liu, D. Zheng, S. Balasubramanian, N. Carriero, E. Khurana, R. Robilotto, and M.B. Gersetein Comprehensive analysis of the pseudogenes of glycolytic enzymes in vertebrates: the anomalously high number of GAPDH pseudogenes highlights a recent burst of retrotrans-positional activity BMC Genomics 10 2009 480
    • (2009) BMC Genomics , vol.10 , pp. 480
    • Liu, Y.-J.1    Zheng, D.2    Balasubramanian, S.3    Carriero, N.4    Khurana, E.5    Robilotto, R.6    Gersetein, M.B.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.