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Volumn 493, Issue , 2011, Pages 277-298

Protein Thermal Shifts to Identify Low Molecular Weight Fragments

Author keywords

[No Author keywords available]

Indexed keywords

ACETAZOLAMIDE; BENZENESULFONAMIDE DERIVATIVE; CARBONATE DEHYDRATASE II; CARBONATE DEHYDRATASE INHIBITOR; CHLOROTHIAZIDE; DEATH ASSOCIATED PROTEIN KINASE; DEATH ASSOCIATED PROTEIN KINASE 1; DICLOFENAMIDE; ETHOXZOLAMIDE; FUROSEMIDE; METHAZOLAMIDE; NUCLEOTIDE DERIVATIVE; SULFANILAMIDE; UNCLASSIFIED DRUG;

EID: 79952428084     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-381274-2.00011-X     Document Type: Chapter
Times cited : (99)

References (32)
  • 1
    • 77952087949 scopus 로고    scopus 로고
    • Atomic resolution studies of carbonic anhydrase II
    • C.A. Behnke Atomic resolution studies of carbonic anhydrase II Acta. Crystallogr. D Biol. Crystallogr. 66 2010 616 627
    • (2010) Acta. Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 616-627
    • Behnke, C.A.1
  • 2
    • 33746359639 scopus 로고    scopus 로고
    • The death-associated protein kinases: Structure, function, and beyond
    • DOI 10.1146/annurev.biochem.75.103004.142615
    • S. Bialik, and A. Kimchi The death-associated protein kinases: Structure, function, and beyond Annu. Rev. Biochem. 75 2006 189 210 (Pubitemid 44118031)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 189-210
    • Bialik, S.1    Kimchi, A.2
  • 3
    • 0025281866 scopus 로고
    • Study of strong to ultratight protein interactions using differential scanning calorimetry
    • DOI 10.1021/bi00481a024
    • J.F. Brandts, and L.N. Lin Study of strong to ultratight protein interactions using differential scanning calorimetry Biochemistry 29 1990 6927 6940 (Pubitemid 20225495)
    • (1990) Biochemistry , vol.29 , Issue.29 , pp. 6927-6940
    • Brandts, J.F.1    Lin, L.-N.2
  • 5
    • 56049092342 scopus 로고    scopus 로고
    • A quantitative model of thermal stabilization and destabilization of proteins by ligands
    • P. Cimmperman A quantitative model of thermal stabilization and destabilization of proteins by ligands Biophys. J. 95 2008 3222 3231
    • (2008) Biophys. J. , vol.95 , pp. 3222-3231
    • Cimmperman, P.1
  • 6
    • 0013913906 scopus 로고
    • Cooperative effects in binding by bovine serum albumin. I. The binding of 1-anilino-8-naphthalenesulfonate. Fluorimetric titrations
    • E. Daniel, and G. Weber Cooperative effects in binding by bovine serum albumin. I. The binding of 1-anilino-8-naphthalenesulfonate. Fluorimetric titrations Biochemistry 5 1966 1893 1900
    • (1966) Biochemistry , vol.5 , pp. 1893-1900
    • Daniel, E.1    Weber, G.2
  • 7
    • 0030956737 scopus 로고    scopus 로고
    • Fluorescence methods for studying equilibrium macromolecule-ligand interactions
    • DOI 10.1016/S0076-6879(97)78013-3
    • M.R. Eftink Fluorescence methods for studying equilibrium macromolecule-ligand interactions Methods Enzymol. 278 1997 221 257 (Pubitemid 27229922)
    • (1997) Methods in Enzymology , vol.278 , pp. 221-257
    • Eftink, M.R.1
  • 8
    • 0015119467 scopus 로고
    • Folding of staphylococcal nuclease: Magnetic resonance and fluorescence studies of individual residues
    • H.F. Epstein Folding of staphylococcal nuclease: Magnetic resonance and fluorescence studies of individual residues Proc. Natl. Acad. Sci. USA 68 1971 2042 2046
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 2042-2046
    • Epstein, H.F.1
  • 10
    • 0001255467 scopus 로고
    • Structural Studies of Ribonuclease. V. Reversible Change Configuration
    • J.J. Hermans, and H.A. Scheraga Structural Studies of Ribonuclease. V. Reversible Change Configuration J. Am. Chem. Soc. 83 1961 3283 3292
    • (1961) J. Am. Chem. Soc. , vol.83 , pp. 3283-3292
    • Hermans, J.J.1    Scheraga, H.A.2
  • 12
    • 33745170360 scopus 로고    scopus 로고
    • Inhibition of carbonic anhydrase-II by sulfamate and sulfamide groups: An investigation involving direct thermodynamic binding measurements
    • DOI 10.1021/jm058279n
    • A.L. Klinger Inhibition of carbonic anhydrase-II by sulfamate and sulfamide groups: An investigation involving direct thermodynamic binding measurements J. Med. Chem. 49 2006 3496 3500 (Pubitemid 43902456)
    • (2006) Journal of Medicinal Chemistry , vol.49 , Issue.12 , pp. 3496-3500
    • Klinger, A.L.1    McComsey, D.F.2    Smith-Swintosky, V.3    Shank, R.P.4    Maryanoff, B.E.5
  • 13
    • 0001858251 scopus 로고
    • Application of a theory of enzyme specificity to protein synthesis
    • D.E. Koshland Application of a theory of enzyme specificity to protein synthesis Proc. Natl. Acad. Sci. USA 44 1958 98 104
    • (1958) Proc. Natl. Acad. Sci. USA , vol.44 , pp. 98-104
    • Koshland, D.E.1
  • 14
    • 0000013948 scopus 로고
    • Protein structure and enzyme activity
    • K. Linderstrøm-Lang, and J.A. Schellman Protein structure and enzyme activity P.D. Boyer, H. Lardy, K. Myrbk, The Enzymes", Vol. 1 2nd Edn. 1959 Academic Press New York 443 510
    • (1959) The Enzymes", Vol. 1 , pp. 443-510
    • Linderstrøm-Lang, K.1    Schellman, J.A.2
  • 15
    • 4143121255 scopus 로고    scopus 로고
    • Evaluation of fluorescence-based thermal shift assays for hit identification in drug discovery
    • M.C. Lo Evaluation of fluorescence-based thermal shift assays for hit identification in drug discovery Anal. Biochem. 332 2004 153 159
    • (2004) Anal. Biochem. , vol.332 , pp. 153-159
    • Lo, M.C.1
  • 16
    • 16344382388 scopus 로고    scopus 로고
    • Thermodynamic stability of carbonic anhydrase: Measurements of binding affinity and stoichiometry using thermofluor
    • DOI 10.1021/bi048135v
    • D. Matulis Thermodynamic stability of carbonic anhydrase: Measurements of binding affinity and stoichiometry using ThermoFluor Biochemistry 44 2005 5258 5266 (Pubitemid 40471238)
    • (2005) Biochemistry , vol.44 , Issue.13 , pp. 5258-5266
    • Matulis, D.1    Kranz, J.K.2    Salemme, F.R.3    Todd, M.J.4
  • 17
    • 0013915140 scopus 로고
    • Fluorescent probes for conformational states of proteins. I. Mechanism of fluorescence of 2-p-toluidinylnaphthalene-6-sulfonate, a hydrophobic probe
    • W.O. McClure, and G.M. Edelman Fluorescent probes for conformational states of proteins. I. Mechanism of fluorescence of 2-p-toluidinylnaphthalene-6- sulfonate, a hydrophobic probe Biochemistry 5 1966 1908 1919
    • (1966) Biochemistry , vol.5 , pp. 1908-1919
    • McClure, W.O.1    Edelman, G.M.2
  • 19
    • 0026344361 scopus 로고
    • Solid model compounds and the thermodynamics of protein unfolding
    • K.P. Murphy, and S.J. Gill Solid model compounds and the thermodynamics of protein unfolding J. Mol. Biol. 222 1991 699 709
    • (1991) J. Mol. Biol. , vol.222 , pp. 699-709
    • Murphy, K.P.1    Gill, S.J.2
  • 20
    • 2542474493 scopus 로고    scopus 로고
    • Analysis of small-molecule interactions using Biacore S51 technology
    • DOI 10.1016/j.ab.2004.03.028, PII S000326970400260X
    • D.G. Myszka Analysis of small-molecule interactions using Biacore S51 technology Anal. Biochem. 329 2004 316 323 (Pubitemid 38680515)
    • (2004) Analytical Biochemistry , vol.329 , Issue.2 , pp. 316-323
    • Myszka, D.G.1
  • 21
    • 37249005205 scopus 로고    scopus 로고
    • The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability
    • DOI 10.1038/nprot.2007.321, PII NPROT.2007.321
    • F.H. Niesen The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability Nat. Protoc. 2 2007 2212 2221 (Pubitemid 351565860)
    • (2007) Nature Protocols , vol.2 , Issue.9 , pp. 2212-2221
    • Niesen, F.H.1    Berglund, H.2    Vedadi, M.3
  • 23
    • 0018588511 scopus 로고
    • Stability of proteins: Small globular proteins
    • P.L. Privalov Stability of proteins: Small globular proteins Adv. Protein Chem. 33 1979 167 241
    • (1979) Adv. Protein Chem. , vol.33 , pp. 167-241
    • Privalov, P.L.1
  • 24
    • 0028013609 scopus 로고
    • A multidimensional spectrophotometer for monitoring thermal unfolding transitions of macromolecules
    • G. Ramsay, and M.R. Eftink A multidimensional spectrophotometer for monitoring thermal unfolding transitions of macromolecules Biophys. J. 66 1994 516 523 (Pubitemid 24058470)
    • (1994) Biophysical Journal , vol.66 , Issue.2 , pp. 516-523
    • Ramsay, G.1    Eftink, M.R.2
  • 25
    • 0026908614 scopus 로고
    • Origins and consequences of ligand-induced multiphasic thermal protein denaturation
    • A. Shrake, and P.D. Ross Origins and consequences of ligand-induced multiphasic thermal protein denaturation Biopolymers 32 1992 925 940
    • (1992) Biopolymers , vol.32 , pp. 925-940
    • Shrake, A.1    Ross, P.D.2
  • 26
    • 0020480481 scopus 로고
    • Anilinonaphthalene sulfonate as a probe of membrane composition and function
    • J. Slavik Anilinonaphthalene sulfonate as a probe of membrane composition and function Biochim. Biophys. Acta 694 1982 1 25
    • (1982) Biochim. Biophys. Acta , vol.694 , pp. 1-25
    • Slavik, J.1
  • 27
    • 0013800421 scopus 로고
    • The interaction of a naphthalene dye with apomyoglobin and apohemoglobin. A fluorescent probe non-polar binding sites
    • L. Stryer The interaction of a naphthalene dye with apomyoglobin and apohemoglobin. A fluorescent probe non-polar binding sites J. Mol. Biol. 13 1965 482 495
    • (1965) J. Mol. Biol. , vol.13 , pp. 482-495
    • Stryer, L.1
  • 28
    • 0016662196 scopus 로고
    • The mechanism of stabilization of the structure of nuclease-T by binding of ligands
    • H. Taniuchi, and J.L. Bohnert The mechanism of stabilization of the structure of nuclease-T by binding of ligands J. Biol. Chem. 250 1975 2388 2394
    • (1975) J. Biol. Chem. , vol.250 , pp. 2388-2394
    • Taniuchi, H.1    Bohnert, J.L.2
  • 29
    • 0035914415 scopus 로고    scopus 로고
    • A protein kinase associated with apoptosis and tumor suppression: Structure, activity, and discovery of peptide substrates
    • A.V. Velentza A protein kinase associated with apoptosis and tumor suppression: Structure, activity, and discovery of peptide substrates J. Biol. Chem. 276 2001 38956 38965
    • (2001) J. Biol. Chem. , vol.276 , pp. 38956-38965
    • Velentza, A.V.1
  • 30
    • 17644435744 scopus 로고    scopus 로고
    • Nucleoside monophosphate kinases: Structure, mechanism, and substrate specificity
    • H. Yan, and M.D. Tsai Nucleoside monophosphate kinases: Structure, mechanism, and substrate specificity Adv. Enzymol. Relat. Areas Mol. Biol. 73 1999 103 134 x
    • (1999) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.73 , pp. 103-134
    • Yan, H.1    Tsai, M.D.2
  • 32
    • 67649644363 scopus 로고    scopus 로고
    • Measurement of nanomolar dissociation constants by titration calorimetry and thermal shift assayRadicicol binding to Hsp90 and ethoxzolamide binding to CAII
    • A. Zubriene Measurement of nanomolar dissociation constants by titration calorimetry and thermal shift assayRadicicol binding to Hsp90 and ethoxzolamide binding to CAII Int. J. Mol. Sci. 10 2009 2662 2680
    • (2009) Int. J. Mol. Sci. , vol.10 , pp. 2662-2680
    • Zubriene, A.1


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