메뉴 건너뛰기




Volumn 985, Issue , 2013, Pages 249-267

Multiple binding partners

Author keywords

[No Author keywords available]

Indexed keywords

ADENINE; ADENOSINE TRIPHOSPHATASE; ALPHA SYNUCLEIN; AMYLOID BETA PROTEIN; CALCIUM BINDING PROTEIN; CARBOHYDRATE; CARRIER PROTEIN; CHAPERONE; CYTOSKELETON PROTEIN; DIPEPTIDE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; GUANINE NUCLEOTIDE BINDING PROTEIN; LIPID; NUCLEAR PROTEIN; PEROXIDASE; POLYGLUTAMINE; POLYNUCLEOTIDE; TAU PROTEIN;

EID: 84867506834     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-94-007-4716-6_8     Document Type: Article
Times cited : (5)

References (101)
  • 1
    • 34547558087 scopus 로고    scopus 로고
    • GAPDH and the search for alternative energy
    • Song S, Finkel T (2007) GAPDH and the search for alternative energy. Nat Cell Biol 9:869-870
    • (2007) Nat Cell Biol , vol.9 , pp. 869-870
    • Song, S.1    Finkel, T.2
  • 2
    • 10644272564 scopus 로고    scopus 로고
    • Interactions among p22, glyceraldehyde-3-phosphate dehydrogenase and microtubules
    • Andrade J, Pearce ST, Zhao H, et al. (2004) Interactions among p22, glyceraldehyde-3-phosphate dehydrogenase and microtubules. Biochem J 384:327-336
    • (2004) Biochem J , vol.384 , pp. 327-336
    • Andrade, J.1    Pearce, S.T.2    Zhao, H.3
  • 3
    • 0021804407 scopus 로고
    • Interaction of glyceraldehyde-3-phosphate dehydrogenase with isolated microsomal subfractions of skeletal muscle
    • Caswell AH, Corbett AM (1985) Interaction of glyceraldehyde-3-phosphate dehydrogenase with isolated microsomal subfractions of skeletal muscle. J Biol Chem 260:6892-6898
    • (1985) J Biol Chem , vol.260 , pp. 6892-6898
    • Caswell, A.H.1    Corbett, A.M.2
  • 4
    • 79959976468 scopus 로고    scopus 로고
    • The S-nitrosylation of glyceraldehyde-3-phosphate dehydrogenase 2 is reduced by interaction with glutathione peroxidase 3 in Saccharomyces cerevisiae
    • Lee PY, Bae KH, Jeong DG, et al. (2011) The S-nitrosylation of glyceraldehyde-3-phosphate dehydrogenase 2 is reduced by interaction with glutathione peroxidase 3 in Saccharomyces cerevisiae. Mol Cells 31:255-259
    • (2011) Mol Cells , vol.31 , pp. 255-259
    • Lee, P.Y.1    Bae, K.H.2    Jeong, D.G.3
  • 5
    • 46649101876 scopus 로고    scopus 로고
    • Nitric oxide-induced nuclear GAPDH activates p300/CBP and mediates apoptosis
    • Sen N, Hara MR, Kornberg MD, et al. (2008) Nitric oxide-induced nuclear GAPDH activates p300/CBP and mediates apoptosis. Nat Cell Biol 10:866-873
    • (2008) Nat Cell Biol , vol.10 , pp. 866-873
    • Sen, N.1    Hara, M.R.2    Kornberg, M.D.3
  • 6
    • 0345600247 scopus 로고    scopus 로고
    • A protein interaction map of Drosophila melanogaster
    • Giot L, Bader JS, Brouwer C, et al. (2003) A protein interaction map of Drosophila melanogaster. Science 302:1727-1736
    • (2003) Science , vol.302 , pp. 1727-1736
    • Giot, L.1    Bader, J.S.2    Brouwer, C.3
  • 7
    • 0022477471 scopus 로고
    • Autophosphorylation of glyceraldehydephosphate dehydrogenase and phosphorylation of protein from skeletal muscle microsomes
    • Kawamoto RM, Caswell AH (1986) Autophosphorylation of glyceraldehydephosphate dehydrogenase and phosphorylation of protein from skeletal muscle microsomes. Biochemistry 25:657-661
    • (1986) Biochemistry , vol.25 , pp. 657-661
    • Kawamoto, R.M.1    Caswell, A.H.2
  • 8
    • 11844305571 scopus 로고    scopus 로고
    • Oxidative stress-responsive intracellular regulation specific for the angiostatic form of human tryptophanyl-tRNA synthetase
    • Wakasugi K, Nakano T, Morishima I (2005) Oxidative stress-responsive intracellular regulation specific for the angiostatic form of human tryptophanyl-tRNA synthetase. Biochemistry 44:225-232
    • (2005) Biochemistry , vol.44 , pp. 225-232
    • Wakasugi, K.1    Nakano, T.2    Morishima, I.3
  • 9
    • 77955293810 scopus 로고    scopus 로고
    • Haponin (eIF1AD) interacts with glyceraldehyde 3-phosphate dehydrogenase in the CHO-K1 cell line
    • Rakitina TV, Bogatova OV, Smirnova EV, et al. (2010) Haponin (eIF1AD) interacts with glyceraldehyde 3-phosphate dehydrogenase in the CHO-K1 cell line. Bioorg Khim 36:312-318
    • (2010) Bioorg Khim , vol.36 , pp. 312-318
    • Rakitina, T.V.1    Bogatova, O.V.2    Smirnova, E.V.3
  • 10
    • 81355123420 scopus 로고    scopus 로고
    • Novel protein haponin regulates cellular response to oxidative stress
    • Smirnova EV, Rakitina TV, Bogatova OV, et al. (2011) Novel protein haponin regulates cellular response to oxidative stress. Dokl Biochem Biophys 440:225-227
    • (2011) Dokl Biochem Biophys , vol.440 , pp. 225-227
    • Smirnova, E.V.1    Rakitina, T.V.2    Bogatova, O.V.3
  • 11
    • 77954497959 scopus 로고    scopus 로고
    • Oxidatively modified glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and Alzheimer's disease: Many pathways to neurodegeneration
    • Butterfield DA, Hardas SS, Lange ML (2010) Oxidatively modified glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and Alzheimer's disease: many pathways to neurodegeneration. J Alzheimers Dis 20:369-393
    • (2010) J Alzheimers Dis , vol.20 , pp. 369-393
    • Butterfield, D.A.1    Hardas, S.S.2    Lange, M.L.3
  • 12
    • 84856747214 scopus 로고    scopus 로고
    • Establishment of a novel fluorescence-based method to evaluate chaperone-mediated autophagy in a single neuron
    • Seki T, Yoshino KI, Tanaka S, et al. (2012) Establishment of a novel fluorescence-based method to evaluate chaperone-mediated autophagy in a single neuron. PLoS One 7:e31232
    • (2012) PLoS One , vol.7
    • Seki, T.1    Yoshino, K.I.2    Tanaka, S.3
  • 13
    • 33751117197 scopus 로고    scopus 로고
    • Mapping of glycolytic enzyme-binding sites on human erythrocyte band 3
    • Chu H, Low PS (2006) Mapping of glycolytic enzyme-binding sites on human erythrocyte band 3. Biochem J 400:143-151
    • (2006) Biochem J 400 , pp. 143-151
    • Chu, H.1    Low, P.S.2
  • 14
    • 33645798376 scopus 로고    scopus 로고
    • Glycolytic enzyme interactions with yeast and skeletal muscle F-actin
    • Waingeh VF, Gustafson CD, Kozliak EI, et al. (2006) Glycolytic enzyme interactions with yeast and skeletal muscle F-actin. Biophys J 90:1371-1384
    • (2006) Biophys J , vol.90 , pp. 1371-1384
    • Waingeh, V.F.1    Gustafson, C.D.2    Kozliak, E.I.3
  • 15
    • 0024788703 scopus 로고
    • Antigenic probes locate binding sites for the glycolytic enzymes glyceraldehyde-3-phosphate dehydrogenase, aldolase and phosphofructokinase on the actin monomer in microfilaments
    • Me'jean C, Pons F, Benyamin Y, et al. (1989) Antigenic probes locate binding sites for the glycolytic enzymes glyceraldehyde-3-phosphate dehydrogenase, aldolase and phosphofructokinase on the actin monomer in microfilaments. Biochem J 264:671-677
    • (1989) Biochem J , vol.264 , pp. 671-677
    • Mejean, C.1    Pons, F.2    Benyamin, Y.3
  • 17
    • 0036914106 scopus 로고    scopus 로고
    • Analysing protein-protein interactions with the yeast two-hybrid system
    • Causier B, Davies B (2002) Analysing protein-protein interactions with the yeast two-hybrid system. Plant Mol Biol 50:855-870
    • (2002) Plant Mol Biol , vol.50 , pp. 855-870
    • Causier, B.1    Davies, B.2
  • 18
    • 77950295912 scopus 로고    scopus 로고
    • Summary of usefulmethods for two-component system research
    • Scharf BE (2010) Summary of usefulmethods for two-component system research. Curr OpinMicrobiol 13:246-252
    • (2010) Curr OpinMicrobiol , vol.13 , pp. 246-252
    • Scharf, B.E.1
  • 19
    • 0034802539 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer microscopy of localized protein interactions in the living cell nucleus
    • Day RN, Periasamy A, Schaufele F (2001) Fluorescence resonance energy transfer microscopy of localized protein interactions in the living cell nucleus. Methods 25:4-18
    • (2001) Methods , vol.25 , pp. 4-18
    • Day, R.N.1    Periasamy, A.2    Schaufele, F.3
  • 20
    • 4444313326 scopus 로고    scopus 로고
    • Glyceraldehyde-derived advanced glycation end products in Alzheimer's disease
    • Choei H, Sasaki N, Takeuchi M, et al. (2004) Glyceraldehyde-derived advanced glycation end products in Alzheimer's disease. Acta Neuropathol 108:189-193
    • (2004) Acta Neuropathol , vol.108 , pp. 189-193
    • Choei, H.1    Sasaki, N.2    Takeuchi, M.3
  • 21
    • 0033454650 scopus 로고    scopus 로고
    • Non-enzymatic glycosylation (or glycation) and inhibition of the pig heart cytosolic aspartate aminotransferase by glyceraldehyde 3-phosphate
    • Fitzgerald C, Swearengin TA, Yeargans G, et al. (2000) Non-enzymatic glycosylation (or glycation) and inhibition of the pig heart cytosolic aspartate aminotransferase by glyceraldehyde 3-phosphate. J Enzyme Inhib 15:79-89
    • (2000) J Enzyme Inhib , vol.15 , pp. 79-89
    • Fitzgerald, C.1    Swearengin, T.A.2    Yeargans, G.3
  • 22
    • 0033660761 scopus 로고    scopus 로고
    • Carnosine prevents the glycation-induced changes in electrophoretic mobility of aspartate aminotransferase
    • Seidler NW (2000) Carnosine prevents the glycation-induced changes in electrophoretic mobility of aspartate aminotransferase. J Biochem Mol Toxicol 14:215-220
    • (2000) J Biochem Mol Toxicol , vol.14 , pp. 215-220
    • Seidler, N.W.1
  • 23
    • 0034649197 scopus 로고    scopus 로고
    • Glycation of aspartate aminotransferase and conformational flexibility
    • Seidler NW, Seibel I (2000) Glycation of aspartate aminotransferase and conformational flexibility. Biochem Biophys Res Commun 277:47-50
    • (2000) Biochem Biophys Res Commun , vol.277 , pp. 47-50
    • Seidler, N.W.1    Seibel, I.2
  • 24
    • 0036498983 scopus 로고    scopus 로고
    • Effects of thermal denaturation on protein glycation
    • Seidler NW, Yeargans GS (2002) Effects of thermal denaturation on protein glycation. Life Sci 70:1789-1799
    • (2002) Life Sci , vol.70 , pp. 1789-1799
    • Seidler, N.W.1    Yeargans, G.S.2
  • 25
    • 78851471598 scopus 로고    scopus 로고
    • Proteomics analysis of methylglyoxal-induced neurotoxic effects in SH-SY5Y cells
    • Li G, Chang M, Jiang H, et al. (2011) Proteomics analysis of methylglyoxal-induced neurotoxic effects in SH-SY5Y cells. Cell Biochem Funct 29:30-35
    • (2011) Cell Biochem Funct , vol.29 , pp. 30-35
    • Li, G.1    Chang, M.2    Jiang, H.3
  • 26
    • 84855887867 scopus 로고    scopus 로고
    • Serumconcentration of an inflammatory glycotoxin, methylglyoxal, is associated with increased cognitive decline in elderly individuals
    • BeeriMS,Moshier E, Schmeidler J, et al. (2011) Serumconcentration of an inflammatory glycotoxin, methylglyoxal, is associated with increased cognitive decline in elderly individuals. Mech Ageing Dev 132:583-587
    • (2011) Mech Ageing Dev , vol.132 , pp. 583-587
    • Beeri, M.S.1    Moshier, E.2    Schmeidler, J.3
  • 27
    • 83455179184 scopus 로고    scopus 로고
    • Role of the glyoxalase system in astrocyte-mediated neuroprotection
    • Be'langer M, Yang J, Petit JM, et al. (2011) Role of the glyoxalase system in astrocyte-mediated neuroprotection. J Neurosci 31:18338-18352
    • (2011) J Neurosci , vol.31 , pp. 18338-18352
    • Belanger, M.1    Yang, J.2    Petit, J.M.3
  • 28
    • 33646482095 scopus 로고    scopus 로고
    • Age-dependent changes of glyoxalase i expression in human brain
    • Kuhla B, Boeck K, Luth HJ, et al. (2006) Age-dependent changes of glyoxalase I expression in human brain. Neurobiol Aging 27:815-822
    • (2006) Neurobiol Aging , vol.27 , pp. 815-822
    • Kuhla, B.1    Boeck, K.2    Luth, H.J.3
  • 29
    • 0037454697 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase activity as an independent modifier of methylglyoxal levels in diabetes
    • Beisswenger PJ, Howell SK, Smith K, et al. (2003) Glyceraldehyde-3- phosphate dehydrogenase activity as an independent modifier of methylglyoxal levels in diabetes. Biochim Biophys Acta 1637:98-106
    • (2003) Biochim Biophys Acta , vol.1637 , pp. 98-106
    • Beisswenger, P.J.1    Howell, S.K.2    Smith, K.3
  • 30
    • 77952958379 scopus 로고    scopus 로고
    • Isoflurane's effect on interfacial dynamics in GAPDH influences methylglyoxal reactivity
    • Pattin AE, Ochs S, Theisen CS, et al. (2010) Isoflurane's effect on interfacial dynamics in GAPDH influences methylglyoxal reactivity. Arch Biochem Biophys 498:7-12
    • (2010) Arch Biochem Biophys , vol.498 , pp. 7-12
    • Pattin, A.E.1    Ochs, S.2    Theisen, C.S.3
  • 31
    • 23744495847 scopus 로고    scopus 로고
    • Methylglyoxal can modify GAPDH activity and structure
    • Lee HJ, Howell SK, Sanford RJ, et al. (2005) Methylglyoxal can modify GAPDH activity and structure. Ann N Y Acad Sci 1043:135-145
    • (2005) Ann N y Acad Sci , vol.1043 , pp. 135-145
    • Lee, H.J.1    Howell, S.K.2    Sanford, R.J.3
  • 32
    • 0028865070 scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase is over-expressed during apoptotic death of neuronal cultures and is recognized by a monoclonal antibody against amyloid plaques from Alzheimer's brain
    • Sunaga K, Takahashi H, Chuang DM, et al. (1995) Glyceraldehyde-3- phosphate dehydrogenase is over-expressed during apoptotic death of neuronal cultures and is recognized by a monoclonal antibody against amyloid plaques from Alzheimer's brain. Neurosci Lett 200:133-136
    • (1995) Neurosci Lett , vol.200 , pp. 133-136
    • Sunaga, K.1    Takahashi, H.2    Chuang, D.M.3
  • 33
    • 0027314334 scopus 로고
    • Rat brain glyceraldehyde-3-phosphate dehydrogenase interacts with the recombinant cytoplasmic domain of Alzheimer's beta-amyloid precursor protein
    • Schulze H, Schuler A, Stuber D, et al. (1993) Rat brain glyceraldehyde-3-phosphate dehydrogenase interacts with the recombinant cytoplasmic domain of Alzheimer's beta-amyloid precursor protein. J Neurochem 60:1915-1922
    • (1993) J Neurochem , vol.60 , pp. 1915-1922
    • Schulze, H.1    Schuler, A.2    Stuber, D.3
  • 34
    • 13444251318 scopus 로고    scopus 로고
    • Pro-apoptotic protein glyceraldehyde-3-phosphate dehydrogenase promotes the formation of Lewy body-like inclusions
    • Tsuchiya K, Tajima H, Kuwae T, et al. (2005) Pro-apoptotic protein glyceraldehyde-3-phosphate dehydrogenase promotes the formation of Lewy body-like inclusions. Eur J Neurosci 21:317-326
    • (2005) Eur J Neurosci , vol.21 , pp. 317-326
    • Tsuchiya, K.1    Tajima, H.2    Kuwae, T.3
  • 35
    • 18144406844 scopus 로고    scopus 로고
    • Proteomic analysis of neurofibrillary tangles in Alzheimer disease identifies GAPDH as a detergent-insoluble paired helical filament tau binding protein
    • Wang Q, Woltjer RL, Cimino PJ, et al. (2005) Proteomic analysis of neurofibrillary tangles in Alzheimer disease identifies GAPDH as a detergent-insoluble paired helical filament tau binding protein. FASEB J 19:869-871
    • (2005) FASEB J , vol.19 , pp. 869-871
    • Wang, Q.1    Woltjer, R.L.2    Cimino, P.J.3
  • 36
    • 18544410106 scopus 로고    scopus 로고
    • Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation
    • Davies SW, Turmaine M, Cozens BA, et al. (1997) Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation. Cell 90:537-548
    • (1997) Cell , vol.90 , pp. 537-548
    • Davies, S.W.1    Turmaine, M.2    Cozens, B.A.3
  • 37
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • DiFiglia M, Sapp E, Chase KO, et al. (1997) Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 277:1990-1993
    • (1997) Science , vol.277 , pp. 1990-1993
    • Difiglia, M.1    Sapp, E.2    Chase, K.O.3
  • 38
    • 80051950364 scopus 로고    scopus 로고
    • Proteomic analysis of human age-related nuclear cataracts and normal lens nuclei
    • Su S, Liu P, Zhang H, et al. (2011) Proteomic analysis of human age-related nuclear cataracts and normal lens nuclei. Invest Ophthalmol Vis Sci 52:4182-4191
    • (2011) Invest Ophthalmol Vis Sci , vol.52 , pp. 4182-4191
    • Su, S.1    Liu, P.2    Zhang, H.3
  • 39
    • 61449148337 scopus 로고    scopus 로고
    • Proteomic and histochemical analysis of proteins involved in the dyingback- type of axonal degeneration in the gracile axonal dystrophy (gad) mouse
    • Goto A, Wang YL, Kabuta T, et al. (2009) Proteomic and histochemical analysis of proteins involved in the dyingback- type of axonal degeneration in the gracile axonal dystrophy (gad) mouse. Neurochem Int 54:330-338
    • (2009) Neurochem Int , vol.54 , pp. 330-338
    • Goto, A.1    Wang, Y.L.2    Kabuta, T.3
  • 40
    • 21244477130 scopus 로고    scopus 로고
    • Axon reactive B cells clonally expanded in the cerebrospinal fluid of patients with multiple sclerosis
    • Zhang Y, Da RR, GuoWet al (2005) Axon reactive B cells clonally expanded in the cerebrospinal fluid of patients with multiple sclerosis. J Clin Immunol 25:254-264
    • (2005) J Clin Immunol , vol.25 , pp. 254-264
    • Zhang, Y.1    Da, R.R.2    Guo, W.3
  • 41
    • 24344433564 scopus 로고    scopus 로고
    • Clonal expansion of IgA-positive plasma cells and axon-reactive antibodies in MS lesions
    • Zhang Y, Da RR, Hilgenberg LG, et al. (2005) Clonal expansion of IgA-positive plasma cells and axon-reactive antibodies in MS lesions. J Neuroimmunol 167:120-130
    • (2005) J Neuroimmunol , vol.167 , pp. 120-130
    • Zhang, Y.1    Da, R.R.2    Hilgenberg, L.G.3
  • 42
    • 33749528961 scopus 로고    scopus 로고
    • Triosephosphate isomerase- and glyceraldehyde-3-phosphate dehydrogenase-reactive autoantibodies in the cerebrospinal fluid of patients with multiple sclerosis
    • Kolln J, Ren HM, Da RR, et al. (2006) Triosephosphate isomerase- and glyceraldehyde-3-phosphate dehydrogenase-reactive autoantibodies in the cerebrospinal fluid of patients with multiple sclerosis. J Immunol 177:5652-5658
    • (2006) J Immunol , vol.177 , pp. 5652-5658
    • Kolln, J.1    Ren, H.M.2    Da, R.R.3
  • 43
    • 77956409953 scopus 로고    scopus 로고
    • Inhibition of glyceraldehyde-3-phosphate dehydrogenase activity by antibodies present in the cerebrospinal fluid of patients with multiple sclerosis
    • Kolln J, Zhang Y, Thai G, et al. (2010) Inhibition of glyceraldehyde-3-phosphate dehydrogenase activity by antibodies present in the cerebrospinal fluid of patients with multiple sclerosis. J Immunol 185:1968-1975
    • (2010) J Immunol , vol.185 , pp. 1968-1975
    • Kolln, J.1    Zhang, Y.2    Thai, G.3
  • 44
    • 34347332414 scopus 로고    scopus 로고
    • Proteomics analysis of the Alzheimer's disease hippocampal proteome
    • Sultana R, Boyd-Kimball D, Cai J, et al. (2007) Proteomics analysis of the Alzheimer's disease hippocampal proteome. J Alzheimers Dis 11:153-164
    • (2007) J Alzheimers Dis , vol.11 , pp. 153-164
    • Sultana, R.1    Boyd-Kimball, D.2    Cai, J.3
  • 45
    • 33845892752 scopus 로고    scopus 로고
    • Systematic meta-analyses of Alzheimer disease genetic association studies: The AlzGene database
    • Bertram L, McQueen MB, Mullin K, et al. (2007) Systematic meta-analyses of Alzheimer disease genetic association studies: the AlzGene database. Nat Genet 39:17-23
    • (2007) Nat Genet , vol.39 , pp. 17-23
    • Bertram, L.1    McQueen, M.B.2    Mullin, K.3
  • 46
    • 8144228132 scopus 로고    scopus 로고
    • Association of late-onset Alzheimer's disease with genetic variation in multiple members of the GAPD gene family
    • Li Y, Nowotny P, Holmans P, et al. (2004) Association of late-onset Alzheimer's disease with genetic variation in multiple members of the GAPD gene family. Proc Natl Acad Sci USA 101:15688-15693
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 15688-15693
    • Li, Y.1    Nowotny, P.2    Holmans, P.3
  • 47
    • 0029898223 scopus 로고    scopus 로고
    • Antibodies to amyloid β protein (Aβ) crossreact with glyceraldehyde- 3-phosphate dehydrogenase (GAPDH)
    • Tamaoka A, Endoh R, Shoji S, et al. (1996) Antibodies to amyloid β protein (Aβ) crossreact with glyceraldehyde- 3-phosphate dehydrogenase (GAPDH). Neurobiol Aging 17:405-414
    • (1996) Neurobiol Aging , vol.17 , pp. 405-414
    • Tamaoka, A.1    Endoh, R.2    Shoji, S.3
  • 48
    • 0035145627 scopus 로고    scopus 로고
    • Reduction of glyceraldehyde-3-phosphate dehydrogenase activity in Alzheimer's disease and in Huntington's disease fibroblasts
    • Mazzola JL, Sirover MA (2001) Reduction of glyceraldehyde-3-phosphate dehydrogenase activity in Alzheimer's disease and in Huntington's disease fibroblasts. J Neurochem 76:442-449
    • (2001) J Neurochem , vol.76 , pp. 442-449
    • Mazzola, J.L.1    Sirover, M.A.2
  • 49
    • 0035017658 scopus 로고    scopus 로고
    • Potential role of nuclear translocation of glyceraldehyde-3-phosphate dehydrogenase in apoptosis and oxidative stress
    • Dastoor Z, Dreyer JL (2001) Potential role of nuclear translocation of glyceraldehyde-3-phosphate dehydrogenase in apoptosis and oxidative stress. J Cell Sci 114:1643-1653
    • (2001) J Cell Sci , vol.114 , pp. 1643-1653
    • Dastoor, Z.1    Dreyer, J.L.2
  • 50
    • 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
    • Nakajima H, Amano W, Fukuhara A, et al. (2009) An aggregate-prone mutant of human glyceraldehyde- 3-phosphate dehydrogenase augments oxidative stress-induced cell death in SH-SY5Y cells. Biochem Biophys Res Commun 390:1066-1071
    • (2009) Biochem Biophys Res Commun , vol.390 , pp. 1066-1071
    • Nakajima, H.1    Amano, W.2    Fukuhara, A.3
  • 51
    • 54549093577 scopus 로고    scopus 로고
    • Non-native glyceraldehyde-3-phosphate dehydrogenase can be an intrinsic component of amyloid structures
    • Naletova I, Schmalhausen E, Kharitonov A, et al. (2008) Non-native glyceraldehyde-3-phosphate dehydrogenase can be an intrinsic component of amyloid structures. Biochim Biophys Acta 1784:2052-2058
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 2052-2058
    • Naletova, I.1    Schmalhausen, E.2    Kharitonov, A.3
  • 52
    • 79952784842 scopus 로고    scopus 로고
    • Proteomic identification of protein targets for 15-deoxy-D(12,14)- prostaglandin J2 in neuronal plasma membrane
    • Yamamoto Y, Takase K, Kishino J, et al. (2011) Proteomic identification of protein targets for 15-deoxy-D(12,14)- prostaglandin J2 in neuronal plasma membrane. PLoS One 6:e17552
    • (2011) PLoS One , vol.6
    • Yamamoto, Y.1    Takase, K.2    Kishino, J.3
  • 53
    • 0034306109 scopus 로고    scopus 로고
    • Effect of human neuronal tau on denaturation and reactivation of rabbit muscle D-glyceraldehyde-3-phosphate dehydrogenase
    • Chen YH, He RQ, Liu Y, et al. (2000) Effect of human neuronal tau on denaturation and reactivation of rabbit muscle D-glyceraldehyde-3-phosphate dehydrogenase. Biochem J 351:233-240
    • (2000) Biochem J , vol.351 , pp. 233-240
    • Chen, Y.H.1    He, R.Q.2    Liu, Y.3
  • 54
    • 0034845915 scopus 로고    scopus 로고
    • Aggregated proteins accelerate but do not increase the aggregation of D-glyceraldehyde-3-phosphate dehydrogenase. Specificity of protein aggregation
    • Li J, Lin Z, Wang CC (2001) Aggregated proteins accelerate but do not increase the aggregation of D-glyceraldehyde-3-phosphate dehydrogenase. Specificity of protein aggregation. J Protein Chem 20:155-163
    • (2001) J Protein Chem , vol.20 , pp. 155-163
    • Li, J.1    Lin, Z.2    Wang, C.C.3
  • 55
    • 0035949542 scopus 로고    scopus 로고
    • Effect of familial Parkinson's disease point mutations A30P and A53T on the structural properties, aggregation, and fibrillation of human alpha-synuclein
    • Li J, Uversky VN, Fink AL (2001) Effect of familial Parkinson's disease point mutations A30P and A53T on the structural properties, aggregation, and fibrillation of human alpha-synuclein. Biochemistry 40:11604-11613
    • (2001) Biochemistry , vol.40 , pp. 11604-11613
    • Li, J.1    Uversky, V.N.2    Fink, A.L.3
  • 56
  • 57
    • 79955694568 scopus 로고    scopus 로고
    • Lysosomal enzyme cathepsin D protects against alpha-synuclein aggregation and toxicity
    • Qiao L, Hamamichi S, Caldwell KA, et al. (2008) Lysosomal enzyme cathepsin D protects against alpha-synuclein aggregation and toxicity. Mol Brain 1:17
    • (2008) Mol Brain , vol.1 , pp. 17
    • Qiao, L.1    Hamamichi, S.2    Caldwell, K.A.3
  • 58
    • 0035662941 scopus 로고    scopus 로고
    • Estradiol, in the CNS, targets several physiologically relevant membrane associated proteins
    • Ramirez VD, Kipp JL, Joe I (2001) Estradiol, in the CNS, targets several physiologically relevant membrane associated proteins. Brain Res Brain Res Rev 37:141-152
    • (2001) Brain Res Brain Res Rev , vol.37 , pp. 141-152
    • Ramirez, V.D.1    Kipp, J.L.2    Joe, I.3
  • 59
    • 0032489392 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase, the putative target of the antiapoptotic compounds CGP 3466 and R-(-)-deprenyl
    • Kragten E, Lalande I, Zimmermann K, et al. (1998) Glyceraldehyde-3- phosphate dehydrogenase, the putative target of the antiapoptotic compounds CGP 3466 and R-(-)-deprenyl. J Biol Chem 273:5821-5828
    • (1998) J Biol Chem , vol.273 , pp. 5821-5828
    • Kragten, E.1    Lalande, I.2    Zimmermann, K.3
  • 60
    • 9644270583 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase as a target for small-molecule disease-modifying therapies in human neurodegenerative disorders
    • Berry MD (2004) Glyceraldehyde-3-phosphate dehydrogenase as a target for small-molecule disease-modifying therapies in human neurodegenerative disorders. J Psychiatry Neurosci 29:337-345
    • (2004) J Psychiatry Neurosci , vol.29 , pp. 337-345
    • Berry, M.D.1
  • 61
    • 0033989493 scopus 로고    scopus 로고
    • Reduced apoptosis after nerve growth factor and serum withdrawal: Conversion of tetrameric glyceraldehyde-3-phosphate dehydrogenase to a dimer
    • Carlile GW, Chalmers-Redman RME, Tatton NA, et al. (2000) Reduced apoptosis after nerve growth factor and serum withdrawal: conversion of tetrameric glyceraldehyde-3-phosphate dehydrogenase to a dimer. Mol Pharmacol 57:2-12
    • (2000) Mol Pharmacol , vol.57 , pp. 2-12
    • Carlile, G.W.1    Rme, C.2    Tatton, N.A.3
  • 62
    • 80053144772 scopus 로고    scopus 로고
    • Novel mechanism of Hsp70 chaperone-mediated prevention of polyglutamine aggregates in a cellular model of huntington disease
    • Guzhova IV, Lazarev VF, Kaznacheeva AV, et al. (2011) Novel mechanism of Hsp70 chaperone-mediated prevention of polyglutamine aggregates in a cellular model of huntington disease. Hum Mol Genet 20:3953-3963
    • (2011) Hum Mol Genet , vol.20 , pp. 3953-3963
    • Guzhova, I.V.1    Lazarev, V.F.2    Kaznacheeva, A.V.3
  • 63
    • 83455199097 scopus 로고    scopus 로고
    • Constitutive upregulation of chaperone-mediated autophagy in Huntington's disease
    • Koga H, Martinez-Vicente M, Arias E, et al. (2011) Constitutive upregulation of chaperone-mediated autophagy in Huntington's disease. J Neurosci 31:18492-18505
    • (2011) J Neurosci , vol.31 , pp. 18492-18505
    • Koga, H.1    Martinez-Vicente, M.2    Arias, E.3
  • 64
    • 0029664992 scopus 로고    scopus 로고
    • Huntingtin and DRPLA proteins selectively interact with the enzyme GAPDH
    • Burke JR, Enghild JJ, Martin ME, et al. (1996) Huntingtin and DRPLA proteins selectively interact with the enzyme GAPDH. Nat Med 2:347-350
    • (1996) Nat Med , vol.2 , pp. 347-350
    • Burke, J.R.1    Enghild, J.J.2    Martin, M.E.3
  • 65
    • 0030850412 scopus 로고    scopus 로고
    • Intranuclear inclusions of expanded polyglutamine protein in spinocerebellar ataxia type 3
    • Paulson HL, Perez MK, Trottier Y, et al. (1997) Intranuclear inclusions of expanded polyglutamine protein in spinocerebellar ataxia type 3. Neuron 19:333-344
    • (1997) Neuron , vol.19 , pp. 333-344
    • Paulson, H.L.1    Perez, M.K.2    Trottier, Y.3
  • 66
    • 0033232529 scopus 로고    scopus 로고
    • Involvement of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and p53 in neuronal apoptosis: Evidence that GAPDH is upregulated by p53
    • Chen RW, Saunders PA, Wei H, et al. (1999) Involvement of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and p53 in neuronal apoptosis: evidence that GAPDH is upregulated by p53. J Neurosci 19:9654-9662
    • (1999) J Neurosci , vol.19 , pp. 9654-9662
    • Chen, R.W.1    Saunders, P.A.2    Wei, H.3
  • 67
    • 33644775636 scopus 로고    scopus 로고
    • Mutant huntingtin: Nuclear translocation and cytotoxicity mediated by GAPDH
    • Bae BI, Hara MR, Cascio MB, et al. (2006) Mutant huntingtin: nuclear translocation and cytotoxicity mediated by GAPDH. Proc Natl Acad Sci USA 103:3405-3409
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 3405-3409
    • Bae, B.I.1    Hara, M.R.2    Cascio, M.B.3
  • 68
    • 0031968628 scopus 로고    scopus 로고
    • Nuclear localization of overexpressed glyceraldehyde-3-phosphate dehydrogenase in cultured cerebellar neurons undergoing apoptosis
    • Ishitani R, Tanaka M, Sunaga K, et al. (1998) Nuclear localization of overexpressed glyceraldehyde-3-phosphate dehydrogenase in cultured cerebellar neurons undergoing apoptosis. Mol Pharmacol 53:701-707
    • (1998) Mol Pharmacol , vol.53 , pp. 701-707
    • Ishitani, R.1    Tanaka, M.2    Sunaga, K.3
  • 69
    • 0029838525 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase antisense oligodeoxynucleotides protect against cytosine arabinonucleoside-induced apoptosis in cultured cerebellar neurons
    • Ishitani R, Chuang DM (1996) Glyceraldehyde-3-phosphate dehydrogenase antisense oligodeoxynucleotides protect against cytosine arabinonucleoside- induced apoptosis in cultured cerebellar neurons. Proc Natl Acad Sci USA 93:9937-9941
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 9937-9941
    • Ishitani, R.1    Chuang, D.M.2
  • 70
    • 0029833062 scopus 로고    scopus 로고
    • Spinocerebellar ataxia type-1 and spinobulbar muscular atrophy gene products interact with glyceraldehyde-3-phosphate dehydrogenase
    • Koshy B, Matilla T, Burright EN, et al. (1996) Spinocerebellar ataxia type-1 and spinobulbar muscular atrophy gene products interact with glyceraldehyde-3-phosphate dehydrogenase. Hum Mol Genet 5:1311-1318
    • (1996) Hum Mol Genet , vol.5 , pp. 1311-1318
    • Koshy, B.1    Matilla, T.2    Burright, E.N.3
  • 71
    • 0041353535 scopus 로고    scopus 로고
    • Huntingtin interacts with REST/NRSF to modulate the transcription of NRSE-controlled neuronal genes
    • Zuccato C, Tartari M, Crotti A, et al. (2003) Huntingtin interacts with REST/NRSF to modulate the transcription of NRSE-controlled neuronal genes. Nat Genet 35:76-83
    • (2003) Nat Genet , vol.35 , pp. 76-83
    • Zuccato, C.1    Tartari, M.2    Crotti, A.3
  • 72
    • 58049197863 scopus 로고    scopus 로고
    • Huntingtin regulates RE1-silencing transcription factor/neuron- restrictive silencer factor (REST/NRSF) nuclear trafficking indirectly through a complex with REST/NRSF-interacting LIM domain protein (RILP) and dynactin p150 Glued
    • Shimojo M (2008) Huntingtin regulates RE1-silencing transcription factor/neuron-restrictive silencer factor (REST/NRSF) nuclear trafficking indirectly through a complex with REST/NRSF-interacting LIM domain protein (RILP) and dynactin p150 Glued. J Biol Chem 283:34880-34886
    • (2008) J Biol Chem , vol.283 , pp. 34880-34886
    • Shimojo, M.1
  • 73
    • 0028293240 scopus 로고
    • Characterization of the alpha-gamma and alpha-beta complex: Evidence for an in vivo functional role of alpha-crystallin as a molecular chaperone
    • Boyle D, Takemoto L (1994) Characterization of the alpha-gamma and alpha-beta complex: evidence for an in vivo functional role of alpha-crystallin as a molecular chaperone. Exp Eye Res 58:9-15
    • (1994) Exp Eye Res , vol.58 , pp. 9-15
    • Boyle, D.1    Takemoto, L.2
  • 74
    • 0032986520 scopus 로고    scopus 로고
    • Alpha-crystallin as a molecular chaperone
    • Derham BK, Harding JJ (1999) Alpha-crystallin as a molecular chaperone. Prog Retin Eye Res 18:463-509
    • (1999) Prog Retin Eye Res , vol.18 , pp. 463-509
    • Derham, B.K.1    Harding, J.J.2
  • 75
    • 5644275139 scopus 로고    scopus 로고
    • Role of ATP on the interaction of alpha-crystallin with its substrates and its implications for the molecular chaperone function
    • Biswas A, Das KP (2004) Role of ATP on the interaction of alpha-crystallin with its substrates and its implications for the molecular chaperone function. J Biol Chem 279:42648-42657
    • (2004) J Biol Chem , vol.279 , pp. 42648-42657
    • Biswas, A.1    Das, K.P.2
  • 76
    • 2942619847 scopus 로고
    • Enzyme activity patterns in clear human lenses and in different types of human senile cataract
    • Friedburg D (1973) Enzyme activity patterns in clear human lenses and in different types of human senile cataract. Ciba Found Symp 19:117-133
    • (1973) Ciba Found Symp , vol.19 , pp. 117-133
    • Friedburg, D.1
  • 77
    • 33749447728 scopus 로고    scopus 로고
    • Thioredoxin, thioredoxin reductase, and alpha-crystallin revive inactivated glyceraldehyde 3-phosphate dehydrogenase in human aged and cataract lens extracts
    • Yan H, Lou MF, Fernando MR, et al. (2006) Thioredoxin, thioredoxin reductase, and alpha-crystallin revive inactivated glyceraldehyde 3-phosphate dehydrogenase in human aged and cataract lens extracts. Mol Vis 12:1153-1159
    • (2006) Mol Vis , vol.12 , pp. 1153-1159
    • Yan, H.1    Lou, M.F.2    Fernando, M.R.3
  • 78
    • 0015813698 scopus 로고
    • Reactive lysines of yeast glyceraldehyde 3-phosphate dehydrogenase. Attachment of a reporter group to a specific non-essential residue
    • Stallcup WB, Koshland DE Jr (1973) Reactive lysines of yeast glyceraldehyde 3-phosphate dehydrogenase. Attachment of a reporter group to a specific non-essential residue. J Mol Biol 80:63-75
    • (1973) J Mol Biol , vol.80 , pp. 63-75
    • Stallcup, W.B.1    Koshland Jr., D.E.2
  • 79
    • 0014199201 scopus 로고
    • The enzymatic significance of S-acetylation and N-acetylation of 3-phosphoglyceraldehyde dehydrogenase
    • Mathew E, Meriwether BP, Park JH (1967) The enzymatic significance of S-acetylation and N-acetylation of 3-phosphoglyceraldehyde dehydrogenase. J Biol Chem 242:5024-5033
    • (1967) J Biol Chem , vol.242 , pp. 5024-5033
    • Mathew, E.1    Meriwether, B.P.2    Park, J.H.3
  • 80
    • 8244261090 scopus 로고
    • The hydrolysis of p-nitrophenyl acetate catalyzed by 3- phosphoglyceraldehyde dehydrogenase
    • Park JH, Meriwether BP, Clodfelder P, et al. (1961) The hydrolysis of p-nitrophenyl acetate catalyzed by 3-phosphoglyceraldehyde dehydrogenase. J Biol Chem 236:136-141
    • (1961) J Biol Chem , vol.236 , pp. 136-141
    • Park, J.H.1    Meriwether, B.P.2    Clodfelder, P.3
  • 81
    • 78649486199 scopus 로고    scopus 로고
    • Glyceraldehyde 3-phosphate dehydrogenase is unlikely to mediate hydrogen peroxide signaling: Studies with a novel anti-dimedone sulfenic acid antibody
    • Maller C, Schroder E, Eaton P (2011) Glyceraldehyde 3-phosphate dehydrogenase is unlikely to mediate hydrogen peroxide signaling: studies with a novel anti-dimedone sulfenic acid antibody. Antioxid Redox Signal 14:49-60
    • (2011) Antioxid Redox Signal , vol.14 , pp. 49-60
    • Maller, C.1    Schroder, E.2    Eaton, P.3
  • 82
    • 34447638199 scopus 로고    scopus 로고
    • Hyperoxidized peroxiredoxins and glyceraldehyde-3-phosphate dehydrogenase immunoreactivity and protein levels are changed in the gerbil hippocampal CA1 region after transient forebrain ischemia
    • Hwang IK, Yoo KY, Kim DW, et al. (2007) Hyperoxidized peroxiredoxins and glyceraldehyde-3-phosphate dehydrogenase immunoreactivity and protein levels are changed in the gerbil hippocampal CA1 region after transient forebrain ischemia. Neurochem Res 32:1530-1538
    • (2007) Neurochem Res , vol.32 , pp. 1530-1538
    • Hwang, I.K.1    Yoo, K.Y.2    Kim, D.W.3
  • 83
    • 70350091586 scopus 로고    scopus 로고
    • Oxidative modifications of glyceraldehyde-3-phosphate dehydrogenase play a key role in its multiple cellular functions
    • Hwang NR, Yim SH, Kim YM, et al. (2009) Oxidative modifications of glyceraldehyde-3-phosphate dehydrogenase play a key role in its multiple cellular functions. Biochem J 423:253-264
    • (2009) Biochem J , vol.423 , pp. 253-264
    • Hwang, N.R.1    Yim, S.H.2    Kim, Y.M.3
  • 84
    • 0031760530 scopus 로고    scopus 로고
    • Substituting selenocysteine for active site cysteine 149 of phosphorylating glyceraldehyde 3-phosphate dehydrogenase reveals a peroxidase activity
    • Boschi-Muller S, Muller S, Van Dorsselaer A, et al. (1998) Substituting selenocysteine for active site cysteine 149 of phosphorylating glyceraldehyde 3-phosphate dehydrogenase reveals a peroxidase activity. FEBS Lett 439:241-245
    • (1998) FEBS Lett , vol.439 , pp. 241-245
    • Boschi-Muller, S.1    Muller, S.2    Van Dorsselaer, A.3
  • 86
    • 78149284226 scopus 로고    scopus 로고
    • GAPDH mediates nitrosylation of nuclear proteins
    • Kornberg MD, Sen N, Hara MR, et al. (2010) GAPDH mediates nitrosylation of nuclear proteins. Nat Cell Biol 12:1094-1100
    • (2010) Nat Cell Biol , vol.12 , pp. 1094-1100
    • Kornberg, M.D.1    Sen, N.2    Hara, M.R.3
  • 87
    • 4444346023 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase is a GABAA receptor kinase linking glycolysis to neuronal inhibition
    • Laschet JJ, Minier F, Kurcewicz I, et al. (2004) Glyceraldehyde-3- phosphate dehydrogenase is a GABAA receptor kinase linking glycolysis to neuronal inhibition. J Neurosci 24:7614-7622
    • (2004) J Neurosci , vol.24 , pp. 7614-7622
    • Laschet, J.J.1    Minier, F.2    Kurcewicz, I.3
  • 88
    • 38149103777 scopus 로고    scopus 로고
    • Genetic evidence for a link between glycolysis and DNA replication
    • Janniere L, Canceill D, Suski C, et al. (2007) Genetic evidence for a link between glycolysis and DNA replication. PLoS One 2:e447
    • (2007) PLoS One , vol.2
    • Janniere, L.1    Canceill, D.2    Suski, C.3
  • 89
    • 0032053510 scopus 로고    scopus 로고
    • Modulation of DNA polymerases alpha, delta and epsilon by lactate dehydrogenase and 3-phosphoglycerate kinase
    • Popanda O, Fox G, Thielmann HW (1998) Modulation of DNA polymerases alpha, delta and epsilon by lactate dehydrogenase and 3-phosphoglycerate kinase. Biochim Biophys Acta 1397:102-117
    • (1998) Biochim Biophys Acta , vol.1397 , pp. 102-117
    • Popanda, O.1    Fox, G.2    Thielmann, H.W.3
  • 90
    • 0032493656 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase and Nm23-H1/ nucleoside diphosphate kinase A. Two old enzymes combine for the novel Nm23 protein phosphotransferase function
    • Engel M, Seifert M, Theisinger B, et al. (1998) Glyceraldehyde-3- phosphate dehydrogenase and Nm23-H1/ nucleoside diphosphate kinase A. Two old enzymes combine for the novel Nm23 protein phosphotransferase function. J Biol Chem 273:20058-20065
    • (1998) J Biol Chem , vol.273 , pp. 20058-20065
    • Engel, M.1    Seifert, M.2    Theisinger, B.3
  • 91
    • 0024324347 scopus 로고
    • Activation of a cytosolic ADP-ribosyltransferase by nitric oxide-generating agents
    • Brune B, Lapetina EG (1989) Activation of a cytosolic ADP-ribosyltransferase by nitric oxide-generating agents. J Biol Chem 264:8455-8458
    • (1989) J Biol Chem , vol.264 , pp. 8455-8458
    • Brune, B.1    Lapetina, E.G.2
  • 92
    • 0026575447 scopus 로고
    • Nitroprusside stimulates the cysteine-specific mono(ADPribosylation) of glyceraldehyde-3-phosphate dehydrogenase from human erythrocytes
    • Kots AY, Skurat AV, Sergienko EA, et al. (1992) Nitroprusside stimulates the cysteine-specific mono(ADPribosylation) of glyceraldehyde-3-phosphate dehydrogenase from human erythrocytes. FEBS Lett 300:9-12
    • (1992) FEBS Lett , vol.300 , pp. 9-12
    • Kots, A.Y.1    Skurat, A.V.2    Sergienko, E.A.3
  • 93
    • 0026686667 scopus 로고
    • Nitric oxide stimulates auto-ADP-ribosylation of glyceraldehyde-3- phosphate dehydrogenase
    • Zhang J, Snyder SH (1992) Nitric oxide stimulates auto-ADP-ribosylation of glyceraldehyde-3-phosphate dehydrogenase. Proc Natl Acad Sci USA 89:9382-9385
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 9382-9385
    • Zhang, J.1    Snyder, S.H.2
  • 94
    • 0024463862 scopus 로고
    • Enzymic and nonenzymic mono ADP-ribosylation of proteins in skeletal muscle
    • Tanaka Y, Yoshihara K, Kamiya T (1989) Enzymic and nonenzymic mono ADP-ribosylation of proteins in skeletal muscle. Biochem Biophys Res Commun 163:1063-1070
    • (1989) Biochem Biophys Res Commun , vol.163 , pp. 1063-1070
    • Tanaka, Y.1    Yoshihara, K.2    Kamiya, T.3
  • 95
    • 38849091401 scopus 로고    scopus 로고
    • Characterization of a Listeria monocytogenes protein interfering with Rab5a
    • Alvarez-Dominguez C, Madrazo-Toca F, Fernandez-Prieto L, et al. (2008) Characterization of a Listeria monocytogenes protein interfering with Rab5a. Traffic 9:325-337
    • (2008) Traffic , vol.9 , pp. 325-337
    • Alvarez-Dominguez, C.1    Madrazo-Toca, F.2    Fernandez-Prieto, L.3
  • 96
    • 0027249488 scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase on the surface of group A streptococci is also an ADP-ribosylating enzyme
    • Pancholi V, Fischetti VA (1993) Glyceraldehyde-3-phosphate dehydrogenase on the surface of group A streptococci is also an ADP-ribosylating enzyme. Proc Natl Acad Sci USA 90:8154-8158
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 8154-8158
    • Pancholi, V.1    Fischetti, V.A.2
  • 97
    • 0023742061 scopus 로고
    • ADP-ribosylation of guanyl nucleotide-binding regulatory proteins by bacterial toxins
    • Moss J, VaughanM(1988) ADP-ribosylation of guanyl nucleotide-binding regulatory proteins by bacterial toxins. Adv Enzymol Relat Areas Mol Biol 61:303-379
    • (1988) Adv Enzymol Relat Areas Mol Biol , vol.61 , pp. 303-379
    • Moss, J.1    Vaughan, M.2
  • 98
    • 0025291837 scopus 로고
    • Modification of plasma membrane protein cysteine residues by ADP-ribose in vivo
    • Jacobson MK, Loflin PT, Aboul-Ela N, et al. (1990) Modification of plasma membrane protein cysteine residues by ADP-ribose in vivo. J Biol Chem 265:10825-10828
    • (1990) J Biol Chem , vol.265 , pp. 10825-10828
    • Jacobson, M.K.1    Loflin, P.T.2    Aboul-Ela, N.3
  • 99
    • 70349873656 scopus 로고    scopus 로고
    • NAD+-dependent post-translational modification of Escherichia coli glyceraldehyde-3-phosphate dehydrogenase
    • Aguilera L, Gime'nez R, Badia J, et al. (2009) NAD+-dependent post-translational modification of Escherichia coli glyceraldehyde-3-phosphate dehydrogenase. Int Microbiol 12:187-192
    • (2009) Int Microbiol , vol.12 , pp. 187-192
    • Aguilera, L.1    Gimenez, R.2    Badia, J.3
  • 100
    • 35748951013 scopus 로고    scopus 로고
    • Entamoeba histolytica: ADP-ribosylation of secreted glyceraldehyde-3- phosphate dehydrogenase
    • Alvarez AH, Martinez-Cadena G, Silva ME, et al. (2007) Entamoeba histolytica: ADP-ribosylation of secreted glyceraldehyde-3-phosphate dehydrogenase. Exp Parasitol 117:349-356
    • (2007) Exp Parasitol , vol.117 , pp. 349-356
    • Alvarez, A.H.1    Martinez-Cadena, G.2    Silva, M.E.3
  • 101
    • 0026453106 scopus 로고
    • Nitric oxide-induced S-nitrosylation of glyceraldehyde- 3-phosphate dehydrogenase inhibits enzymatic activity and increases endogenous ADP-ribosylation
    • Molina y Vedia L, McDonald B, Reep B, et al. (1992) Nitric oxide-induced S-nitrosylation of glyceraldehyde- 3-phosphate dehydrogenase inhibits enzymatic activity and increases endogenous ADP-ribosylation. J Biol Chem 267:24929-24932
    • (1992) J Biol Chem , vol.267 , pp. 24929-24932
    • Molina, Y.1    Vedia, L.2    McDonald, B.3    Reep, B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.