메뉴 건너뛰기




Volumn 47, Issue 12, 2012, Pages 2284-2290

Towards alpha-glucosidase folding induced by trifluoroethanol: Kinetics and computational prediction

Author keywords

Alpha glucosidase; Docking simulation; Molecular dynamics; Trifluoroethanol; Unfolding

Indexed keywords

ALPHA-GLUCOSIDASE; BINDING MECHANISMS; COMPUTATIONAL PREDICTIONS; COMPUTATIONAL SIMULATION; COSOLVENTS; DIABETES MELLITUS; DOCKING SIMULATIONS; DOSE-DEPENDENT MANNER; ENZYME STRUCTURES; FERMENTABLE SUGARS; FOLDING BEHAVIOR; MOLECULAR DYNAMICS SIMULATIONS; STRUCTURAL CHANGE; STRUCTURAL SIMULATIONS; TRIFLUOROETHANOL; UNFOLDING;

EID: 84870792838     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2012.09.005     Document Type: Article
Times cited : (14)

References (26)
  • 1
    • 0022815673 scopus 로고
    • Structural and functional analysis of the MAL1 locus of Saccharomyces cerevisiae
    • M.J. Charron, R.A. Dubin, and C.A. Michels Structural and functional analysis of the MAL1 locus of Saccharomyces cerevisiae Mol Cell Biol 6 1986 3891 3899
    • (1986) Mol Cell Biol , vol.6 , pp. 3891-3899
    • Charron, M.J.1    Dubin, R.A.2    Michels, C.A.3
  • 2
    • 0038185186 scopus 로고    scopus 로고
    • Is there a role for alpha-glucosidase inhibitors in the prevention of type 2 diabetes mellitus
    • A.J. Scheen Is there a role for alpha-glucosidase inhibitors in the prevention of type 2 diabetes mellitus Drugs 63 2003 933 951
    • (2003) Drugs , vol.63 , pp. 933-951
    • Scheen, A.J.1
  • 3
    • 1542299147 scopus 로고    scopus 로고
    • Biotechnology and molecular biology of the a-glucosidase inhibitor acarbose
    • U. Wehmeier, and W. Piepersberg Biotechnology and molecular biology of the a-glucosidase inhibitor acarbose Appl Microbiol Biotechnol 63 2004 613 625
    • (2004) Appl Microbiol Biotechnol , vol.63 , pp. 613-625
    • Wehmeier, U.1    Piepersberg, W.2
  • 4
    • 36749059401 scopus 로고    scopus 로고
    • Who should benefit from the use of alpha-glucosidase inhibitors
    • A. Godbout, and J.L. Chiasson Who should benefit from the use of alpha-glucosidase inhibitors Curr Diab Rep 7 2007 333 339
    • (2007) Curr Diab Rep , vol.7 , pp. 333-339
    • Godbout, A.1    Chiasson, J.L.2
  • 5
    • 72549111666 scopus 로고    scopus 로고
    • Inhibition kinetics and the aggregation of alpha-glucosidase by different denaturants
    • X.Q. Wu, H. Xu, H. Yue, K.Q. Liu, and X.Y. Wang Inhibition kinetics and the aggregation of alpha-glucosidase by different denaturants Protein J 28 2009 448 456
    • (2009) Protein J , vol.28 , pp. 448-456
    • Wu, X.Q.1    Xu, H.2    Yue, H.3    Liu, K.Q.4    Wang, X.Y.5
  • 6
    • 77949293261 scopus 로고    scopus 로고
    • Alpha-glucosidase folding during urea denaturation: Enzyme kinetics and computational prediction
    • X.Q. Wu, J. Wang, Z.R. Lü, H.M. Tang, D. Park, and S.H. Oh Alpha-glucosidase folding during urea denaturation: enzyme kinetics and computational prediction Appl Biochem Biotechnol 160 2010 1341 1355
    • (2010) Appl Biochem Biotechnol , vol.160 , pp. 1341-1355
    • Wu, X.Q.1    Wang, J.2    Lü, Z.R.3    Tang, H.M.4    Park, D.5    Oh, S.H.6
  • 8
    • 35348925111 scopus 로고    scopus 로고
    • Effect of polyamines on the structure, thermal stability and 2,2,2-trifluoroethanol-induced aggregation of [alpha]-chymotrypsin
    • N. Rezaei-Ghaleh, A. Ebrahim-Habibi, A.A. Moosavi-Movahedi, and M. Nemat-Gorgani Effect of polyamines on the structure, thermal stability and 2,2,2-trifluoroethanol-induced aggregation of [alpha]-chymotrypsin Int J Biol Macromol 41 2007 597 604
    • (2007) Int J Biol Macromol , vol.41 , pp. 597-604
    • Rezaei-Ghaleh, N.1    Ebrahim-Habibi, A.2    Moosavi-Movahedi, A.A.3    Nemat-Gorgani, M.4
  • 9
    • 77949914143 scopus 로고    scopus 로고
    • The effect of trifluoroethanol on tyrosinase activity and conformation: Inhibition kinetics and computational simulations
    • Z.R. Lü, L. Shi, J. Wang, D. Park, J. Bhak, and J.M. Yang The effect of trifluoroethanol on tyrosinase activity and conformation: inhibition kinetics and computational simulations Appl Biochem Biotechnol 160 2010 1896 1908
    • (2010) Appl Biochem Biotechnol , vol.160 , pp. 1896-1908
    • Lü, Z.R.1    Shi, L.2    Wang, J.3    Park, D.4    Bhak, J.5    Yang, J.M.6
  • 10
    • 79955749680 scopus 로고    scopus 로고
    • Trifluoroethanol-induced activity and structural changes in bos taurus copper- and zinc-containing superoxide dismutase
    • L. Shi, Y. Xia, M. Zhang, S.J. Yin, Y.X. Si, and G.Y. Qian Trifluoroethanol-induced activity and structural changes in bos taurus copper- and zinc-containing superoxide dismutase Protein Pept Lett 18 2011 726 732
    • (2011) Protein Pept Lett , vol.18 , pp. 726-732
    • Shi, L.1    Xia, Y.2    Zhang, M.3    Yin, S.J.4    Si, Y.X.5    Qian, G.Y.6
  • 11
    • 84856301518 scopus 로고    scopus 로고
    • Trifluoroethanol-induced changes in activity and conformation of manganese-containing superoxide dismutase
    • S.J. Yin, Z.R. Lü, D. Park, H.Y. Chung, J.M. Yang, and H.M. Zhou Trifluoroethanol-induced changes in activity and conformation of manganese-containing superoxide dismutase Appl Biochem Biotechnol 166 2012 276 288
    • (2012) Appl Biochem Biotechnol , vol.166 , pp. 276-288
    • Yin, S.J.1    Lü, Z.R.2    Park, D.3    Chung, H.Y.4    Yang, J.M.5    Zhou, H.M.6
  • 12
    • 0037025817 scopus 로고    scopus 로고
    • Structural transformation and aggregation of human alpha-synuclein in trifluoroethanol: Non-amyloid component sequence is essential and beta-sheet formation is prerequisite to aggregation
    • H.T. Li, H.N. Du, L. Tang, J. Hu, and H.Y. Hu Structural transformation and aggregation of human alpha-synuclein in trifluoroethanol: non-amyloid component sequence is essential and beta-sheet formation is prerequisite to aggregation Biopolymers 64 2002 221 226
    • (2002) Biopolymers , vol.64 , pp. 221-226
    • Li, H.T.1    Du, H.N.2    Tang, L.3    Hu, J.4    Hu, H.Y.5
  • 13
    • 78650505110 scopus 로고    scopus 로고
    • Identification of a helical intermediate in trifluoroethanol-induced alpha-synuclein aggregation
    • V.L. Anderson, T.F. Ramlall, C.C. Rospigliosi, W.W. Webb, and D. Eliezer Identification of a helical intermediate in trifluoroethanol-induced alpha-synuclein aggregation Proc Natl Acad Sci U S A 107 2010 18850 18855
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 18850-18855
    • Anderson, V.L.1    Ramlall, T.F.2    Rospigliosi, C.C.3    Webb, W.W.4    Eliezer, D.5
  • 14
    • 84857351291 scopus 로고    scopus 로고
    • A Desolvation model for trifluoroethanol-induced aggregation of enhanced green fluorescent protein
    • V.L. Anderson, and W.W. Webb A Desolvation model for trifluoroethanol- induced aggregation of enhanced green fluorescent protein Biophys J 102 2012 897 906
    • (2012) Biophys J , vol.102 , pp. 897-906
    • Anderson, V.L.1    Webb, W.W.2
  • 16
    • 0346101566 scopus 로고    scopus 로고
    • Effect of thiohydroxyl compounds on tyrosinase: Inactivation and reactivation study
    • Y.D. Park, S.J. Lee, K.H. Park, S. Kim, M.J. Hahn, and J.M. Yang Effect of thiohydroxyl compounds on tyrosinase: inactivation and reactivation study J Protein Chem 22 2003 613 623
    • (2003) J Protein Chem , vol.22 , pp. 613-623
    • Park, Y.D.1    Lee, S.J.2    Park, K.H.3    Kim, S.4    Hahn, M.J.5    Yang, J.M.6
  • 17
    • 16344373015 scopus 로고    scopus 로고
    • Protein homology detection by HMM-HMM comparison
    • J. Söding Protein homology detection by HMM-HMM comparison Bioinformatics 21 2005 951 960
    • (2005) Bioinformatics , vol.21 , pp. 951-960
    • Söding, J.1
  • 18
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: A novel method for fast and accurate multiple sequence alignment
    • C. Notredame, D.G. Higgins, and J. Heringa T-Coffee: a novel method for fast and accurate multiple sequence alignment J Mol Biol 302 2000 205 218
    • (2000) J Mol Biol , vol.302 , pp. 205-218
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 19
    • 84864648555 scopus 로고    scopus 로고
    • A simplified homology-model builder toward highly protein-like structures: An inspection of restraining potentials
    • 10.1002/jcc.23024
    • T.R. Kim, S. Oh, J.S.W. Yang, S. Lee, S. Shin, and J. Lee A simplified homology-model builder toward highly protein-like structures: an inspection of restraining potentials J Comput Chem 2012 10.1002/jcc.23024
    • (2012) J Comput Chem
    • Kim, T.R.1    Oh, S.2    Yang, J.S.W.3    Lee, S.4    Shin, S.5    Lee, J.6
  • 20
    • 76149120388 scopus 로고    scopus 로고
    • AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading
    • O. Trott, and A.J. Olson AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading J Comput Chem 31 2010 455 461
    • (2010) J Comput Chem , vol.31 , pp. 455-461
    • Trott, O.1    Olson, A.J.2
  • 22
    • 47149096704 scopus 로고    scopus 로고
    • CHARMM-GUI. A web-based graphical user interface for CHARMM
    • S. Jo, T. Kim, V.G. Iyer, and W. Im CHARMM-GUI. A web-based graphical user interface for CHARMM J Comput Chem 29 2008 1859 1865
    • (2008) J Comput Chem , vol.29 , pp. 1859-1865
    • Jo, S.1    Kim, T.2    Iyer, V.G.3    Im, W.4
  • 23
    • 0141956090 scopus 로고    scopus 로고
    • Brooks III CL. Generalized born model with a simple smoothing function
    • W. Im, and M.S. Lee Brooks III CL. Generalized born model with a simple smoothing function J Comput Chem 24 2003 1691 1702
    • (2003) J Comput Chem , vol.24 , pp. 1691-1702
    • Im, W.1    Lee, M.S.2
  • 24
    • 0034255229 scopus 로고    scopus 로고
    • Conformational changes and inactivation of calf intestinal alkaline phosphatase in trifluoroethanol solutions
    • Y.X. Zhang, Y. Zhu, and H.M. Zhou Conformational changes and inactivation of calf intestinal alkaline phosphatase in trifluoroethanol solutions Int J Biochem Cell Biol 32 2000 887 894
    • (2000) Int J Biochem Cell Biol , vol.32 , pp. 887-894
    • Zhang, Y.X.1    Zhu, Y.2    Zhou, H.M.3
  • 25
    • 33646166939 scopus 로고    scopus 로고
    • Conformational changes and inactivation of bovine carbonic anhydrase II in 2,2,2-trifluoroethanol solutions
    • X. Wei, S. Ding, Y. Jiang, X.G. Zeng, and H.M. Zhou Conformational changes and inactivation of bovine carbonic anhydrase II in 2,2,2- trifluoroethanol solutions Biochemistry (Mosc) 71 Suppl. 1 2006 S77 S82
    • (2006) Biochemistry (Mosc) , vol.71 , Issue.SUPPL. 1
    • Wei, X.1    Ding, S.2    Jiang, Y.3    Zeng, X.G.4    Zhou, H.M.5
  • 26
    • 34548835242 scopus 로고    scopus 로고
    • Effect of Cl- on tyrosinase: Complex inhibition kinetics and biochemical implication
    • H.Y. Han, J.R. Lee, W.A. Xu, M.J. Hahn, J.M. Yang, and Y.D. Park Effect of Cl- on tyrosinase: complex inhibition kinetics and biochemical implication J Biomol Struct Dyn 25 2007 165 171
    • (2007) J Biomol Struct Dyn , vol.25 , pp. 165-171
    • Han, H.Y.1    Lee, J.R.2    Xu, W.A.3    Hahn, M.J.4    Yang, J.M.5    Park, Y.D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.