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Volumn 7, Issue 9, 2015, Pages 831-834

Looking for protein stabilizing drugs with thermal shift assay

Author keywords

Pharmacological chaperones; Rare disease; Thermal shift assay

Indexed keywords

DIAGNOSIS; PROTEINS;

EID: 84940956600     PISSN: 19427603     EISSN: 19427611     Source Type: Journal    
DOI: 10.1002/dta.1798     Document Type: Note
Times cited : (50)

References (19)
  • 1
    • 25144523127 scopus 로고    scopus 로고
    • Loss of protein structure stability as a major causative factor in monogenic disease
    • P. Yue, Z. Li, J. Moult. Loss of protein structure stability as a major causative factor in monogenic disease. J. Mol. Biol. 2005, 353, 459.
    • (2005) J. Mol. Biol. , vol.353 , pp. 459
    • Yue, P.1    Li, Z.2    Moult, J.3
  • 2
    • 77449098166 scopus 로고    scopus 로고
    • Treating lysosomal storage diseases with pharmacological chaperones: From concept to clinics
    • G. Parenti. Treating lysosomal storage diseases with pharmacological chaperones: From concept to clinics. EMBO Mol. Med. 2009, 1, 268.
    • (2009) EMBO Mol. Med. , vol.1 , pp. 268
    • Parenti, G.1
  • 3
    • 84880366642 scopus 로고    scopus 로고
    • Fabry_CEP: A tool to identify Fabry mutations responsive to pharmacological chaperones
    • M. Cammisa, A. Correra, G. Andreotti, M. V. Cubellis. Fabry_CEP: A tool to identify Fabry mutations responsive to pharmacological chaperones. Orphanet J. Rare Dis. 2013, 8, 111.
    • (2013) Orphanet J. Rare Dis. , vol.8 , pp. 111
    • Cammisa, M.1    Correra, A.2    Andreotti, G.3    Cubellis, M.V.4
  • 5
    • 85017330275 scopus 로고    scopus 로고
    • Analysis of protein stability and ligand interactions by thermal shift assay
    • K. Huynh, C. L. Partch. Analysis of protein stability and ligand interactions by thermal shift assay. Curr. Protoc. Protein Sci. 2015, 79, 28.
    • (2015) Curr. Protoc. Protein Sci. , vol.79 , pp. 28
    • Huynh, K.1    Partch, C.L.2
  • 7
    • 4143121255 scopus 로고    scopus 로고
    • Evaluation of fluorescence-based thermal shift assays for hit identification in drug discovery
    • M. C. Lo, A. Aulabaugh, G. Jin, R. Cowling, J. Bard, M. Malamas, G. Ellestad. Evaluation of fluorescence-based thermal shift assays for hit identification in drug discovery. Anal. Biochem. 2004, 332, 153.
    • (2004) Anal. Biochem. , vol.332 , pp. 153
    • Lo, M.C.1    Aulabaugh, A.2    Jin, G.3    Cowling, R.4    Bard, J.5    Malamas, M.6    Ellestad, G.7
  • 8
    • 33748929006 scopus 로고    scopus 로고
    • Thermofluor-based high-throughput stability optimization of proteins for structural studies
    • U. B. Ericsson, B. M. Hallberg, G. T. Detitta, N. Dekker, P. Nordlund. Thermofluor-based high-throughput stability optimization of proteins for structural studies. Anal. Biochem. 2006, 357, 289.
    • (2006) Anal. Biochem. , vol.357 , pp. 289
    • Ericsson, U.B.1    Hallberg, B.M.2    Detitta, G.T.3    Dekker, N.4    Nordlund, P.5
  • 10
    • 16344382388 scopus 로고    scopus 로고
    • Thermodynamic stability of carbonic anhydrase: Measurements of binding affinity and stoichiometry using ThermoFluor
    • D. Matulis, J. K. Kranz, F. R. Salemme, M. J. Todd. Thermodynamic stability of carbonic anhydrase: Measurements of binding affinity and stoichiometry using ThermoFluor. Biochemistry. 2005, 44, 5258.
    • (2005) Biochemistry , vol.44 , pp. 5258
    • Matulis, D.1    Kranz, J.K.2    Salemme, F.R.3    Todd, M.J.4
  • 11
    • 84870011168 scopus 로고    scopus 로고
    • 2-(3-Oxo-1,3-diphenylpropyl)malonic acids as potent allosteric ligands of the PIF pocket of phosphoinositide-dependent kinase-1: Development and prodrug concept
    • A. Wilhelm, L. A. Lopez-Garcia, K. Busschots, W. Frohner, F. Maurer, S. Boettcher, H. Zhang, J. O. Schulze, R. M. Biondi, M. Engel. 2-(3-Oxo-1, 3-diphenylpropyl)malonic acids as potent allosteric ligands of the PIF pocket of phosphoinositide-dependent kinase-1: Development and prodrug concept. J. Med. Chem. 2012, 55, 9817.
    • (2012) J. Med. Chem. , vol.55 , pp. 9817
    • Wilhelm, A.1    Lopez-Garcia, L.A.2    Busschots, K.3    Frohner, W.4    Maurer, F.5    Boettcher, S.6    Zhang, H.7    Schulze, J.O.8    Biondi, R.M.9    Engel, M.10
  • 12
    • 84908398480 scopus 로고    scopus 로고
    • Biochemical phenotype of a common disease-causing mutation and a possible therapeutic approach for the phosphomannomutase 2-associated disorder of glycosylation
    • G. Andreotti, E. Pedone, A. Giordano, M. V. Cubellis. Biochemical phenotype of a common disease-causing mutation and a possible therapeutic approach for the phosphomannomutase 2-associated disorder of glycosylation. Mol. Genet. Genomic. Med. 2013, 1, 32.
    • (2013) Mol. Genet. Genomic. Med. , vol.1 , pp. 32
    • Andreotti, G.1    Pedone, E.2    Giordano, A.3    Cubellis, M.V.4
  • 13
    • 84918564491 scopus 로고    scopus 로고
    • Conformational response to ligand binding in phosphomannomutase2: insights into inborn glycosylation disorder
    • G. Andreotti, I. Cabeza de Vaca, A. Poziello, M. C. Monti, V. Guallar, M. V. Cubellis. Conformational response to ligand binding in phosphomannomutase2: insights into inborn glycosylation disorder. J. Biol. Chem. 2014, 289, 34900.
    • (2014) J. Biol. Chem. , vol.289 , pp. 34900
    • Andreotti, G.1    Cabeza de Vaca, I.2    Poziello, A.3    Monti, M.C.4    Guallar, V.5    Cubellis, M.V.6
  • 15
    • 66649137718 scopus 로고    scopus 로고
    • Effects of pH and iminosugar pharmacological chaperones on lysosomal glycosidase structure and stability
    • R. L. Lieberman, J. A. D'Aquino, D. Ringe, G. A. Petsko. Effects of pH and iminosugar pharmacological chaperones on lysosomal glycosidase structure and stability. Biochemistry. 2009, 48, 4816.
    • (2009) Biochemistry , vol.48 , pp. 4816
    • Lieberman, R.L.1    D'Aquino, J.A.2    Ringe, D.3    Petsko, G.A.4
  • 16
    • 84555202420 scopus 로고    scopus 로고
    • The molecular basis of pharmacological chaperoning in human alpha-galactosidase
    • A. I. Guce, N. E. Clark, J. J. Rogich, S. C. Garman. The molecular basis of pharmacological chaperoning in human alpha-galactosidase. Chem. Biol. 2011, 18, 1521.
    • (2011) Chem. Biol. , vol.18 , pp. 1521
    • Guce, A.I.1    Clark, N.E.2    Rogich, J.J.3    Garman, S.C.4
  • 18
    • 61849099371 scopus 로고    scopus 로고
    • Molecular interaction of imino sugars with human alpha-galactosidase: Insight into the mechanism of complex formation and pharmacological chaperone action in Fabry disease
    • K. Sugawara, Y. Tajima, I. Kawashima, T. Tsukimura, S. Saito, K. Ohno, K. Iwamoto, T. Kobayashi, K. Itoh, H. Sakuraba. Molecular interaction of imino sugars with human alpha-galactosidase: Insight into the mechanism of complex formation and pharmacological chaperone action in Fabry disease. Mol. Genet. Metab. 2009, 96, 233.
    • (2009) Mol. Genet. Metab. , vol.96 , pp. 233
    • Sugawara, K.1    Tajima, Y.2    Kawashima, I.3    Tsukimura, T.4    Saito, S.5    Ohno, K.6    Iwamoto, K.7    Kobayashi, T.8    Itoh, K.9    Sakuraba, H.10
  • 19
    • 84891868024 scopus 로고    scopus 로고
    • A thermodynamic assay to test pharmacological chaperones for Fabry disease
    • G. Andreotti, V. Citro, A. Correra, M. V. Cubellis. A thermodynamic assay to test pharmacological chaperones for Fabry disease. Biochim. Biophys. Acta. 2014, 1840, 1214.
    • (2014) Biochim. Biophys. Acta , vol.1840 , pp. 1214
    • Andreotti, G.1    Citro, V.2    Correra, A.3    Cubellis, M.V.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.