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Volumn 589, Issue 5, 2015, Pages 581-587

GAPDH binders as potential drugs for the therapy of polyglutamine diseases: Design of a new screening assay

Author keywords

Aggregation assay; dehydrogenase; Drug; Glyceraldehydes 3 phosphate; Polyglutamine diseases; Small molecule; Therapeutic target; Transgenic Drosophila; Transglutaminase

Indexed keywords

BENZOTHIAZOLE DERIVATIVE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; HYDROXYNONENAL; NEUROPROTECTIVE AGENT; PGL 135; POLYGLUTAMINE; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; SELEGILINE; UNCLASSIFIED DRUG; PEPTIDE;

EID: 84922714714     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2015.01.018     Document Type: Article
Times cited : (22)

References (30)
  • 1
    • 77955643169 scopus 로고    scopus 로고
    • Molecular mechanisms and potential therapeutical targets in Huntington's disease
    • C. Zuccato, M. Valenza, and E. Cattaneo Molecular mechanisms and potential therapeutical targets in Huntington's disease Physiol. Rev. 90 2010 905 981
    • (2010) Physiol. Rev. , vol.90 , pp. 905-981
    • Zuccato, C.1    Valenza, M.2    Cattaneo, E.3
  • 2
    • 84878926416 scopus 로고    scopus 로고
    • Pharmacological protein targets in polyglutamine diseases: Mutant polypeptides and their interactors
    • B.A. Margulis, V. Vigont, V.F. Lazarev, E.V. Kaznacheyeva, and I.V. Guzhova Pharmacological protein targets in polyglutamine diseases: mutant polypeptides and their interactors FEBS Lett. 587 2013 1997 2007
    • (2013) FEBS Lett. , vol.587 , pp. 1997-2007
    • Margulis, B.A.1    Vigont, V.2    Lazarev, V.F.3    Kaznacheyeva, E.V.4    Guzhova, I.V.5
  • 3
    • 84906096688 scopus 로고    scopus 로고
    • Therapeutic approaches for inhibition of protein aggregation in Huntington's disease
    • S. Kim, and K.T. Kim Therapeutic approaches for inhibition of protein aggregation in Huntington's disease Exp. Neurobiol. 23 2014 36 44
    • (2014) Exp. Neurobiol. , vol.23 , pp. 36-44
    • Kim, S.1    Kim, K.T.2
  • 4
    • 0036172346 scopus 로고    scopus 로고
    • Prolonged survival and decreased abnormal movements in transgenic model of Huntington disease, with administration of the transglutaminase inhibitor cystamine
    • M.V. Karpuj, M.W. Becher, J.E. Springer, D. Chabas, S. Youssef, R. Pedotti, D. Mitchell, and L. Steinman Prolonged survival and decreased abnormal movements in transgenic model of Huntington disease, with administration of the transglutaminase inhibitor cystamine Nat. Med. 8 2012 143 149
    • (2012) Nat. Med. , vol.8 , pp. 143-149
    • Karpuj, M.V.1    Becher, M.W.2    Springer, J.E.3    Chabas, D.4    Youssef, S.5    Pedotti, R.6    Mitchell, D.7    Steinman, L.8
  • 5
    • 0037197778 scopus 로고    scopus 로고
    • Alteration of nuclear glyceraldehyde-3-phosphate dehydrogenase structure in Huntington's disease fibroblasts
    • J.L. Mazzola, and M.A. Sirover Alteration of nuclear glyceraldehyde-3-phosphate dehydrogenase structure in Huntington's disease fibroblasts Brain Res. Mol. Brain Res. 100 2002 95 101
    • (2002) Brain Res. Mol. Brain Res. , vol.100 , pp. 95-101
    • Mazzola, J.L.1    Sirover, M.A.2
  • 6
    • 0037216488 scopus 로고    scopus 로고
    • Structural characterization of transglutaminase-catalyzed cross-linking between glyceraldehyde 3-phosphate dehydrogenase and polyglutamine repeats
    • M. Ruoppolo, S. Orrù, S. Francese, I. Caputo, and C. Esposito Structural characterization of transglutaminase-catalyzed cross-linking between glyceraldehyde 3-phosphate dehydrogenase and polyglutamine repeats Protein Sci. 12 2003 170 179
    • (2003) Protein Sci. , vol.12 , pp. 170-179
    • Ruoppolo, M.1    Orrù, S.2    Francese, S.3    Caputo, I.4    Esposito, C.5
  • 12
    • 12944335007 scopus 로고    scopus 로고
    • Reversal of a full-length mutant huntingtin neuronal cell phenotype by chemical inhibitors of polyglutamine-mediated aggregation
    • J. Wang, S. Gines, M.E. MacDonald, and J.F. Gusella Reversal of a full-length mutant huntingtin neuronal cell phenotype by chemical inhibitors of polyglutamine-mediated aggregation BMC Neurosci. 6 2005
    • (2005) BMC Neurosci. , vol.6
    • Wang, J.1    Gines, S.2    Macdonald, M.E.3    Gusella, J.F.4
  • 13
    • 0033989493 scopus 로고    scopus 로고
    • Reduced apoptosis after nerve growth factor and serum withdrawal: Conversion of tetrameric glyceraldehyde-3-phosphate dehydrogenase to a dimer
    • G.W. Carlile, R.M. Chalmers-Redman, N.A. Tatton, A. Pong, K.E. Borden, and W.G. Tatton Reduced apoptosis after nerve growth factor and serum withdrawal: conversion of tetrameric glyceraldehyde-3-phosphate dehydrogenase to a dimer Mol. Pharmacol. 57 2000 2 12
    • (2000) Mol. Pharmacol. , vol.57 , pp. 2-12
    • Carlile, G.W.1    Chalmers-Redman, R.M.2    Tatton, N.A.3    Pong, A.4    Borden, K.E.5    Tatton, W.G.6
  • 14
    • 0037734329 scopus 로고    scopus 로고
    • Neuroprotection by deprenyl and other propargylamines: Glyceraldehyde-3-phosphate dehydrogenase rather than monoamine oxidase B
    • W. Tatton, R. Chalmers-Redman, and N. Tatton Neuroprotection by deprenyl and other propargylamines: glyceraldehyde-3-phosphate dehydrogenase rather than monoamine oxidase B J. Neural. Transm. 110 2003 509 515
    • (2003) J. Neural. Transm. , vol.110 , pp. 509-515
    • Tatton, W.1    Chalmers-Redman, R.2    Tatton, N.3
  • 15
    • 0027480753 scopus 로고
    • Covalent attachment of 4-hydroxynonenal to glyceraldehyde-3-phosphate dehydrogenase. A possible involvement of intra- and intermolecular cross-linking reaction
    • K. Uchida, and E.R. Stadtman Covalent attachment of 4-hydroxynonenal to glyceraldehyde-3-phosphate dehydrogenase. A possible involvement of intra- and intermolecular cross-linking reaction J. Biol. Chem. 268 1993 6388 6393
    • (1993) J. Biol. Chem. , vol.268 , pp. 6388-6393
    • Uchida, K.1    Stadtman, E.R.2
  • 18
    • 79251555277 scopus 로고    scopus 로고
    • Novel inhibitors of glyceraldehyde-3-phosphate dehydrogenase: Covalent modification of NAD-binding site by aromatic thiols
    • K.A. Chernorizov, J.L. Elkina, P.I. Semenyuk, V.K. Svedas, and V.I. Muronetz Novel inhibitors of glyceraldehyde-3-phosphate dehydrogenase: covalent modification of NAD-binding site by aromatic thiols Biochemistry (Moscow) 75 2010 1444 1449
    • (2010) Biochemistry (Moscow) , vol.75 , pp. 1444-1449
    • Chernorizov, K.A.1    Elkina, J.L.2    Semenyuk, P.I.3    Svedas, V.K.4    Muronetz, V.I.5
  • 19
    • 0020439065 scopus 로고
    • Purification of all glycolytic enzymes from one muscle extract
    • R.K. Scopes, and A. Stoter Purification of all glycolytic enzymes from one muscle extract Methods Enzymol. 90 1982 479 490
    • (1982) Methods Enzymol. , vol.90 , pp. 479-490
    • Scopes, R.K.1    Stoter, A.2
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 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 Differ. 16 2009 1573 1581
    • (2009) Cell Death Differ. , vol.16 , pp. 1573-1581
    • Colell, A.1    Green, D.R.2    Ricci, J.E.3
  • 24
    • 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
  • 28
    • 0037379388 scopus 로고    scopus 로고
    • Molecular basis of enzyme inactivation by an endogenous electrophile 4-hydroxy-2-nonenal: Identification of modification sites in glyceraldehyde-3-phosphate dehydrogenase
    • T. Ishii, E. Tatsuda, S. Kumazawa, T. Nakayama, and K. Uchida Molecular basis of enzyme inactivation by an endogenous electrophile 4-hydroxy-2-nonenal: identification of modification sites in glyceraldehyde-3-phosphate dehydrogenase Biochemistry 42 2003 3474 3480
    • (2003) Biochemistry , vol.42 , pp. 3474-3480
    • Ishii, T.1    Tatsuda, E.2    Kumazawa, S.3    Nakayama, T.4    Uchida, K.5
  • 29
    • 84878229848 scopus 로고    scopus 로고
    • Target identification using drug affinity responsive target stability (DARTS)
    • B. Lomenick, G. Jung, J.A. Wohlschlegel, and J. Huang Target identification using drug affinity responsive target stability (DARTS) Curr. Protoc. Chem. Biol. 3 2011 163 180
    • (2011) Curr. Protoc. Chem. Biol. , vol.3 , pp. 163-180
    • Lomenick, B.1    Jung, G.2    Wohlschlegel, J.A.3    Huang, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.