메뉴 건너뛰기




Volumn 3, Issue 12, 2012, Pages 1024-1028

SAR development of lysine-based irreversible inhibitors of transglutaminase 2 for huntington's disease

Author keywords

acrylamides; celiac disease; in vitro ADME; plasma stability; polar surface area

Indexed keywords

ACRYLAMIDE; ENZYME INHIBITOR; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE 2; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE 2 INHIBITOR; UNCLASSIFIED DRUG;

EID: 84871208434     PISSN: None     EISSN: 19485875     Source Type: Journal    
DOI: 10.1021/ml300241m     Document Type: Article
Times cited : (29)

References (25)
  • 1
    • 0026338017 scopus 로고
    • Transglutaminases: Multifunctional cross-linking enzymes that stabilize tissues
    • Greenberg, C. S.; Birckbichler, R. H. Transglutaminases: Multifunctional cross-linking enzymes that stabilize tissues FASEB J. 1991, 5, 3071-3077
    • (1991) FASEB J. , vol.5 , pp. 3071-3077
    • Greenberg, C.S.1    Birckbichler, R.H.2
  • 2
    • 0025010874 scopus 로고
    • A novel guanine nucleotide-binding protein coupled to the α1-Adrenergic receptor
    • Im, M.-J.; Riek, P.; Graham, R. A novel guanine nucleotide-binding protein coupled to the α1-Adrenergic receptor J. Biol. Chem. 1990, 265, 18952-18960
    • (1990) J. Biol. Chem. , vol.265 , pp. 18952-18960
    • Im, M.-J.1    Riek, P.2    Graham, R.3
  • 3
    • 0031890194 scopus 로고    scopus 로고
    • Regulation of human tissue transglutaminase function by magnesium-nucleotide complexes
    • Lai, T.-S.; Slaughter, T.; Peoples, K.; Hettasch, J.; Greenburg, C. Regulation of human tissue transglutaminase function by magnesium-nucleotide complexes J. Biol. Chem. 1998, 273, 1776-1781
    • (1998) J. Biol. Chem. , vol.273 , pp. 1776-1781
    • Lai, T.-S.1    Slaughter, T.2    Peoples, K.3    Hettasch, J.4    Greenburg, C.5
  • 5
    • 38549156658 scopus 로고    scopus 로고
    • Transglutaminase 2 undergoes a large conformational change upon activation
    • Pinkas, D.; Strop, P.; Brunger, A.; Khosla, C. Transglutaminase 2 undergoes a large conformational change upon activation PLOS Biol. 2007, 5, 2788-2796
    • (2007) PLOS Biol. , vol.5 , pp. 2788-2796
    • Pinkas, D.1    Strop, P.2    Brunger, A.3    Khosla, C.4
  • 6
    • 0037022619 scopus 로고    scopus 로고
    • Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity
    • Liu, S.; Cerione, R. A.; Clardy, J. Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity Proc. Natl. Acad. Sci. U.S.A. 2002, 99, 2743-2747
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 2743-2747
    • Liu, S.1    Cerione, R.A.2    Clardy, J.3
  • 8
  • 11
    • 34447286702 scopus 로고    scopus 로고
    • Transglutaminase 2 inhibitors and their therapeutic role in disease states
    • Siegel, M.; Khosla, C. Transglutaminase 2 inhibitors and their therapeutic role in disease states Pharmacol. Ther. 2007, 115, 232-245
    • (2007) Pharmacol. Ther. , vol.115 , pp. 232-245
    • Siegel, M.1    Khosla, C.2
  • 13
    • 79551554590 scopus 로고    scopus 로고
    • The importance of integrating basic and clinical research toward the development of new therapies for Huntington's disease
    • Muñoz-Sanjuan, I.; Bates, G. P. The importance of integrating basic and clinical research toward the development of new therapies for Huntington's disease J. Clin. Invest. 2011, 121, 476-483
    • (2011) J. Clin. Invest. , vol.121 , pp. 476-483
    • Muñoz-Sanjuan, I.1    Bates, G.P.2
  • 16
    • 13244279859 scopus 로고    scopus 로고
    • Tissue transglutaminase contributes to disease progression in the R6/2 Huntington's disease mouse model via aggregate-independent mechanisms
    • Bailey, C.; Johnson, G. Tissue transglutaminase contributes to disease progression in the R6/2 Huntington's disease mouse model via aggregate-independent mechanisms J. Neurochem. 2005, 92, 83-92
    • (2005) J. Neurochem. , vol.92 , pp. 83-92
    • Bailey, C.1    Johnson, G.2
  • 17
    • 0034990512 scopus 로고    scopus 로고
    • Tissue transglutaminase selectively modifies proteins associated with truncated mutant huntingtin in intact cells
    • Chun, W.; Lesort, M.; Tucholski, J.; Faber, P. W.; MacDonald, M. E.; Ross, C. A.; Johnson, G. V. W. Tissue transglutaminase selectively modifies proteins associated with truncated mutant huntingtin in intact cells Neurobiol. Dis. 2001, 8, 391-404
    • (2001) Neurobiol. Dis. , vol.8 , pp. 391-404
    • Chun, W.1    Lesort, M.2    Tucholski, J.3    Faber, P.W.4    MacDonald, M.E.5    Ross, C.A.6    Johnson, G.V.W.7
  • 18
    • 34250174215 scopus 로고    scopus 로고
    • Type 2 transglutaminase differentially modulates striatal cell death in the presence of wild type or mutant huntingtin
    • Ruan, Q.; Quintanilla, R. A.; Johnson, G. V. Type 2 transglutaminase differentially modulates striatal cell death in the presence of wild type or mutant huntingtin J. Neurochem. 2007, 102, 25-36
    • (2007) J. Neurochem. , vol.102 , pp. 25-36
    • Ruan, Q.1    Quintanilla, R.A.2    Johnson, G.V.3
  • 19
    • 84863839736 scopus 로고    scopus 로고
    • Tissue transglutaminase overexpression does not modify the disease phenotype of the R6/2 mouse model of Huntington's disease
    • Kumar, A.; Kneynsberg, A.; Tucholski, J.; Perry, G.; van Groen, T.; Detloff, P. J.; Lesort, M. Tissue transglutaminase overexpression does not modify the disease phenotype of the R6/2 mouse model of Huntington's disease Exp. Neurol. 2012, 237, 78-89
    • (2012) Exp. Neurol. , vol.237 , pp. 78-89
    • Kumar, A.1    Kneynsberg, A.2    Tucholski, J.3    Perry, G.4    Van Groen, T.5    Detloff, P.J.6    Lesort, M.7
  • 23
    • 0034951866 scopus 로고    scopus 로고
    • Evaluation of novel dipeptide-bound α,β-unsaturated amides and epoxides as irreversible inhibitors of guinea pig liver transglutaminase
    • Marrano, C.; de Macédo, P.; Keillor, J. W. Evaluation of novel dipeptide-bound α,β-unsaturated amides and epoxides as irreversible inhibitors of guinea pig liver transglutaminase Bioorg. Med. Chem. 2001, 9, 1923-1928
    • (2001) Bioorg. Med. Chem. , vol.9 , pp. 1923-1928
    • Marrano, C.1    De MacÉdo, P.2    Keillor, J.W.3
  • 24
  • 25
    • 59849088616 scopus 로고    scopus 로고
    • A simple in vitro assay for assessing the reactivity of nitrile containing compounds
    • MacFaul, P. A.; Morley, A. D.; Crawford, J. J. A simple in vitro assay for assessing the reactivity of nitrile containing compounds Bioorg. Med. Chem. Lett. 2009, 19, 1136-1138
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 1136-1138
    • MacFaul, P.A.1    Morley, A.D.2    Crawford, J.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.