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Volumn 1838, Issue 1 PARTA, 2014, Pages 34-42

Ligand- and drug-binding studies of membrane proteins revealed through circular dichroism spectroscopy

Author keywords

Circular dichroism (CD) spectroscopy; kd determination; Ligand interactions; Membrane proteins; Synchrotron radiation circular dichroism (SRCD); Two component signal transduction

Indexed keywords

AROMATIC AMINO ACID; CARRIER PROTEIN; MEMBRANE PROTEIN; PHOSPHOLIPASE A2; SUGE PROTEIN; UNCLASSIFIED DRUG;

EID: 84888368393     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2013.06.019     Document Type: Review
Times cited : (59)

References (65)
  • 5
    • 0031795747 scopus 로고    scopus 로고
    • Biomolecules interactions and competitions by non-immobilised ligand interaction assay by circular dichroism
    • G. Siligardi, and R. Hussain Biomolecules interactions and competitions by non-immobilised ligand interaction assay by circular dichroism Enantiomer 3 1998 77 87 (Pubitemid 28499743)
    • (1998) Enantiomer , vol.3 , Issue.2 , pp. 77-87
    • Siligardi, G.1    Hussain, R.2
  • 7
    • 84874839952 scopus 로고    scopus 로고
    • Biophysical Approaches Determining Ligand Binding to Biomolecular Targets, Detection, Measurement and Modelling
    • A. Podjarmy, A. Dejaegere, B. Kieffer, RSC Publishing
    • S.R. Martin, M.J. Schilstra, and G. Siligardi Biophysical Approaches Determining Ligand Binding to Biomolecular Targets, Detection, Measurement and Modelling A. Podjarmy, A. Dejaegere, B. Kieffer, Chapter 7: Circular Dichroism 2011 RSC Publishing 226 246
    • (2011) Chapter 7: Circular Dichroism , pp. 226-246
    • Martin, S.R.1    Schilstra, M.J.2    Siligardi, G.3
  • 8
    • 84882869231 scopus 로고    scopus 로고
    • Applications of Circular Dichroism
    • J. Lindon, G. Tranter, D. Koppenaal, 2nd edition Elsevier Oxford
    • G. Siligardi, and R. Hussain Applications of Circular Dichroism J. Lindon, G. Tranter, D. Koppenaal, Encyclopedia of Spectroscopy and Spectrometry 2nd edition vol. 1 2010 Elsevier Oxford 9 14
    • (2010) Encyclopedia of Spectroscopy and Spectrometry , vol.1 VOL. , pp. 9-14
    • Siligardi, G.1    Hussain, R.2
  • 9
    • 0025301439 scopus 로고
    • Protein secondary structure and circular dichroism: A practical guide
    • W.C. Johnson Protein secondary structure and circular dichroism: a practical guide Proteins Struct. Funct. Genet. 7 1990 205 214
    • (1990) Proteins Struct. Funct. Genet. , vol.7 , pp. 205-214
    • Johnson, W.C.1
  • 11
    • 84255170906 scopus 로고    scopus 로고
    • Circular dichroism beamline B23 at Diamond Light Source
    • R. Hussain, T. Jávorfi, and G. Siligardi Circular dichroism beamline B23 at Diamond Light Source J. Synchrotron Radiat. 19 2010 132 135
    • (2010) J. Synchrotron Radiat. , vol.19 , pp. 132-135
    • Hussain, R.1    Jávorfi, T.2    Siligardi, G.3
  • 12
    • 78349254955 scopus 로고    scopus 로고
    • Measuring circular dichroism in a capillary cell using the B23 synchrotron radiation CD beamline at Diamond Light Source
    • T. Javorfi, R. Hussain, D. Myatt, and G. Siligardi Measuring circular dichroism in a capillary cell using the B23 synchrotron radiation CD beamline at Diamond Light Source Chirality 22 2010 E149 E153
    • (2010) Chirality , vol.22
    • Javorfi, T.1    Hussain, R.2    Myatt, D.3    Siligardi, G.4
  • 13
    • 84873372650 scopus 로고    scopus 로고
    • Automated circular dichroism spectroscopy for medium-throughput analysis of protein conformation
    • S. Fiedler, L. Cole, and S. Keller Automated circular dichroism spectroscopy for medium-throughput analysis of protein conformation Anal. Chem. 85 2013 1868 1872
    • (2013) Anal. Chem. , vol.85 , pp. 1868-1872
    • Fiedler, S.1    Cole, L.2    Keller, S.3
  • 14
    • 0036296323 scopus 로고    scopus 로고
    • Expression, purification and characterisation of full-length histidine protein kinase RegB from Rhodobacter sphaeroides
    • DOI 10.1016/S0022-2836(02)00424-2
    • C.A. Potter, A. Ward, C. Laguri, M.P. Williamson, P.J.F. Henderson, and M.K. Phillips-Jones Expression, purification and characterisation of full-length heterologously expressed histidine protein kinase RegB from Rhodobacter sphaeroides J. Mol. Biol. 320 2002 201 213 (Pubitemid 34722212)
    • (2002) Journal of Molecular Biology , vol.320 , Issue.2 , pp. 201-213
    • Potter, C.A.1    Ward, A.2    Laguri, C.3    Williamson, M.P.4    Henderson, P.J.F.5    Phillips-Jones, M.K.6
  • 15
    • 74249091562 scopus 로고    scopus 로고
    • Structural characterisation of the intra-membrane histidine kinase YbdK from Bacillus subtilis in DPC micelles
    • Y.P. Kim, K.J. Yeo, M.H. Kim, Y.-C. Kim, and Y.H. Jeon Structural characterisation of the intra-membrane histidine kinase YbdK from Bacillus subtilis in DPC micelles Biochem. Biophys. Res. Commun. 391 2010 1506 1511
    • (2010) Biochem. Biophys. Res. Commun. , vol.391 , pp. 1506-1511
    • Kim, Y.P.1    Yeo, K.J.2    Kim, M.H.3    Kim, Y.-C.4    Jeon, Y.H.5
  • 16
    • 78149448781 scopus 로고    scopus 로고
    • Discovery of biphasic thermal unfolding of OmpC with implications for surface loop stability
    • N. Keegan, H. Ridley, and J.H. Lakey Discovery of biphasic thermal unfolding of OmpC with implications for surface loop stability Biochemistry 49 2010 9715 9721
    • (2010) Biochemistry , vol.49 , pp. 9715-9721
    • Keegan, N.1    Ridley, H.2    Lakey, J.H.3
  • 17
    • 53149107441 scopus 로고    scopus 로고
    • Expression and characterisation of the integral membrane domain of bacterial histidine kinase SCO3062 for structural studies
    • K.J. Yeo, S.-N. Kwak, H.J. Kim, C. Cheong, M.H. Kim, and Y.H. Jeon Expression and characterisation of the integral membrane domain of bacterial histidine kinase SCO3062 for structural studies Biochem. Biophys. Res. Commun. 376 2008 409 413
    • (2008) Biochem. Biophys. Res. Commun. , vol.376 , pp. 409-413
    • Yeo, K.J.1    Kwak, S.-N.2    Kim, H.J.3    Cheong, C.4    Kim, M.H.5    Jeon, Y.H.6
  • 19
    • 77956294944 scopus 로고    scopus 로고
    • Synchrotron radiation circular dichroism spectroscopy-defined structure of the C-terminal domain of NaChBac and its role in channel assembly
    • A.M. Powl, A.O. O'Reilly, A.J. Miles, and B.A. Wallace Synchrotron radiation circular dichroism spectroscopy-defined structure of the C-terminal domain of NaChBac and its role in channel assembly Proc. Natl. Acad. Sci. U. S. A. 107 2010 14064 14069
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 14064-14069
    • Powl, A.M.1    O'Reilly, A.O.2    Miles, A.J.3    Wallace, B.A.4
  • 20
    • 0347994116 scopus 로고    scopus 로고
    • On the analysis of membrane protein circular dichroism spectra
    • DOI 10.1110/ps.03258404
    • N. Sreerama, and R.W. Woody On the analysis of membrane protein circular dichroism spectra Protein Sci. 13 2004 100 112 (Pubitemid 38021145)
    • (2004) Protein Science , vol.13 , Issue.1 , pp. 100-112
    • Sreerama, N.1    Woody, R.W.2
  • 22
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • DOI 10.1006/abio.2000.4880
    • N. Sreerama, and R.W. Woody Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON and CDSSTR methods with an expanded reference set Anal. Biochem. 287 2000 252 260 (Pubitemid 32006234)
    • (2000) Analytical Biochemistry , vol.287 , Issue.2 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 23
    • 0019873820 scopus 로고
    • Estimation of globular protein secondary structure from circular dichroism
    • S.W. Provencher, and J. Glockner Estimation of globular protein secondary structure from circular dichroism Biochemistry 20 1981 33 37
    • (1981) Biochemistry , vol.20 , pp. 33-37
    • Provencher, S.W.1    Glockner, J.2
  • 24
    • 84859903462 scopus 로고    scopus 로고
    • Interactions of the intact FsrC membrane histidine kinase with its pheromone ligand GBAP revealed through synchrotron radiation circular dichroism
    • S.G. Patching, S. Edara, P. Ma, J. Nakayama, R. Hussain, G. Siligardi, and M.K. Phillips-Jones Interactions of the intact FsrC membrane histidine kinase with its pheromone ligand GBAP revealed through synchrotron radiation circular dichroism Biochim. Biophys. Acta Biomembr. 1818 2012 1595 1602
    • (2012) Biochim. Biophys. Acta Biomembr. , vol.1818 , pp. 1595-1602
    • Patching, S.G.1    Edara, S.2    Ma, P.3    Nakayama, J.4    Hussain, R.5    Siligardi, G.6    Phillips-Jones, M.K.7
  • 25
    • 84870895754 scopus 로고    scopus 로고
    • Interactions of the intact FsrC membrane histidine kinase with the tricyclic peptide siamycin i revealed through synchrotron radiation circular dichroism
    • M.K. Phillips-Jones, S.G. Patching, S. Edara, J. Nakayama, R. Hussain, and G. Siligardi Interactions of the intact FsrC membrane histidine kinase with the tricyclic peptide siamycin I revealed through synchrotron radiation circular dichroism Phys. Chem. Chem. Phys. 15 2013 444 447
    • (2013) Phys. Chem. Chem. Phys. , vol.15 , pp. 444-447
    • Phillips-Jones, M.K.1    Patching, S.G.2    Edara, S.3    Nakayama, J.4    Hussain, R.5    Siligardi, G.6
  • 26
    • 79957795877 scopus 로고    scopus 로고
    • Changes in PLA2 activity after interacting with anti-inflammatory drugs and model membranes: Evidence for the involvement of tryptophan residues
    • D. Gaspar, M. Lúcio, S. Rocha, J.L.F. Costa Lima, and S. Reis Changes in PLA2 activity after interacting with anti-inflammatory drugs and model membranes: evidence for the involvement of tryptophan residues Chem. Phys. Lipids 164 2011 292 299
    • (2011) Chem. Phys. Lipids , vol.164 , pp. 292-299
    • Gaspar, D.1    Lúcio, M.2    Rocha, S.3    Costa Lima, J.L.F.4    Reis, S.5
  • 27
    • 79959922924 scopus 로고    scopus 로고
    • Spectroscopic analysis of the intrinsic chromophores within small multidrug resistance protein SugE
    • D.C. Bay, and R.J. Turner Spectroscopic analysis of the intrinsic chromophores within small multidrug resistance protein SugE Biochim. Biophys. Acta Biomembr. 1808 2011 2233 2244
    • (2011) Biochim. Biophys. Acta Biomembr. , vol.1808 , pp. 2233-2244
    • Bay, D.C.1    Turner, R.J.2
  • 30
    • 80054687050 scopus 로고    scopus 로고
    • Toward rational design of protein detergent complexes: Determinants of mixed micelles that are critical for the in vitro stabilisation of a G-protein coupled receptor
    • M.A. O'Malley, M.E. Helgeson, N.J. Wagner, and A.S. Robinson Toward rational design of protein detergent complexes: determinants of mixed micelles that are critical for the in vitro stabilisation of a G-protein coupled receptor Biophys. J. 101 2011 1938 1948
    • (2011) Biophys. J. , vol.101 , pp. 1938-1948
    • O'Malley, M.A.1    Helgeson, M.E.2    Wagner, N.J.3    Robinson, A.S.4
  • 31
    • 70349481163 scopus 로고    scopus 로고
    • Structure analysis of the membrane protein TatCd from the Tat system of B. Subtilis by circular dichroism
    • O.V. Nolandt, T.H. Walther, S. Roth, J. Bürck, and A.S. Ulrich Structure analysis of the membrane protein TatCd from the Tat system of B. subtilis by circular dichroism Biochim. Biophys. Acta Biomembr. 1788 2009 2238 2244
    • (2009) Biochim. Biophys. Acta Biomembr. , vol.1788 , pp. 2238-2244
    • Nolandt, O.V.1    Walther, T.H.2    Roth, S.3    Bürck, J.4    Ulrich, A.S.5
  • 32
    • 52049091255 scopus 로고    scopus 로고
    • The effect of lipids on the structure of eukaryotic cytolysin equinatoxin II: A synchrotron radiation circular dichroism spectroscopic study
    • A.J. Miles, A. Drechsler, K. Kristan, G. Anderluh, R.S. Norton, B.A. Wallace, and F. Separovic The effect of lipids on the structure of eukaryotic cytolysin equinatoxin II: a synchrotron radiation circular dichroism spectroscopic study Biochim. Biophys. Acta Biomembr. 1778 2008 2091 2096
    • (2008) Biochim. Biophys. Acta Biomembr. , vol.1778 , pp. 2091-2096
    • Miles, A.J.1    Drechsler, A.2    Kristan, K.3    Anderluh, G.4    Norton, R.S.5    Wallace, B.A.6    Separovic, F.7
  • 33
    • 80051784870 scopus 로고    scopus 로고
    • Correlation of structural and functional thermal stability of the integral membrane protein Na, K-ATPase
    • A.J. Miles, B.A. Wallace, and M. Esmann Correlation of structural and functional thermal stability of the integral membrane protein Na, K-ATPase Biochim. Biophys. Acta Biomembr. 1808 2011 2573 2580
    • (2011) Biochim. Biophys. Acta Biomembr. , vol.1808 , pp. 2573-2580
    • Miles, A.J.1    Wallace, B.A.2    Esmann, M.3
  • 34
    • 0034847257 scopus 로고    scopus 로고
    • Calcium-induced conformational changes in Leishmania infantum kinetoplastid membrane protein-11
    • DOI 10.1007/s007750000175
    • M.A. Fuertes, J.M. Pérez, M. Soto, M.C. López, and C. Alonso Calcium-induced conformational changes in Leishmania infantum kinetoplastid membrane protein-11 J. Biol. Inorg. Chem. 6 2001 107 117 (Pubitemid 32822160)
    • (2001) Journal of Biological Inorganic Chemistry , vol.6 , Issue.1 , pp. 107-117
    • Fuertes, M.A.1    Perez, J.M.2    Soto, M.3    Lopez, M.C.4    Alonso, C.5
  • 35
    • 0027506131 scopus 로고
    • Circular dichroism analysis of ligand-induced conformational changes in protein kinase C
    • L. Boscá, and F. Morán Circular dichroism analysis of ligand-induced conformational changes in protein kinase C Biochem. J. 290 1993 827 832
    • (1993) Biochem. J. , vol.290 , pp. 827-832
    • Boscá, L.1    Morán, F.2
  • 37
    • 33846587373 scopus 로고    scopus 로고
    • Consecutive Binding of Chlorophylls a and b During the Assembly in Vitro of Light-harvesting Chlorophyll-a/b Protein (LHCIIb)
    • DOI 10.1016/j.jmb.2006.11.069, PII S0022283606016287
    • R. Horn, G. Grundmann, and H. Paulsen Consecutive binding of chlorophylls a and b during the assembly in vitro of light-harvesting chlorophyll a/b protein (LHCIIb) J. Mol. Biol. 366 2007 1045 1054 (Pubitemid 46175873)
    • (2007) Journal of Molecular Biology , vol.366 , Issue.3 , pp. 1045-1054
    • Horn, R.1    Grundmann, G.2    Paulsen, H.3
  • 38
    • 84873727690 scopus 로고    scopus 로고
    • Spectroscopic analysis: Synchrotron radiation circular dichroism
    • Separations and Analysis
    • R. Hussain, T. Jávorfi, and G. Siligardi Spectroscopic analysis: synchrotron radiation circular dichroism Comprehensive Chirality Separations and Analysis 8 2012 438 448
    • (2012) Comprehensive Chirality , vol.8 , pp. 438-448
    • Hussain, R.1    Jávorfi, T.2    Siligardi, G.3
  • 39
    • 84255170906 scopus 로고    scopus 로고
    • Circular dichroism beamline B23 at the Diamond Light Source
    • R. Hussain, T. Jávorfi, and G. Siligardi Circular dichroism beamline B23 at the Diamond Light Source J. Synchrotron Radiat. 19 2012 132 135
    • (2012) J. Synchrotron Radiat. , vol.19 , pp. 132-135
    • Hussain, R.1    Jávorfi, T.2    Siligardi, G.3
  • 40
    • 0032911313 scopus 로고    scopus 로고
    • Two-component signal transduction in Bacillus subtilis: How one organism sees its world
    • C. Fabret, V.A. Feher, and J.A. Hoch Two-component signal transduction in Bacillus subtilis: how one organism sees its world J. Bacteriol. 181 1999 1975 1983 (Pubitemid 29164948)
    • (1999) Journal of Bacteriology , vol.181 , Issue.7 , pp. 1975-1983
    • Fabret, C.1    Feher, V.A.2    Hoch, J.A.3
  • 41
    • 0036837964 scopus 로고    scopus 로고
    • Two-component signal transduction in Enterococcus faecalis
    • DOI 10.1128/JB.184.21.5819-5825.2002
    • L.E. Hancock, and M. Perego Two-component signal transduction in Enterococcus faecalis J. Bacteriol. 184 2002 5819 5825 (Pubitemid 35168228)
    • (2002) Journal of Bacteriology , vol.184 , Issue.21 , pp. 5819-5825
    • Hancock, L.1    Perego, M.2
  • 42
    • 0034946367 scopus 로고    scopus 로고
    • Gelatinase biosynthesis-activating pheromone: A peptide lactone that mediates a quorum sensing in Enterococcus faecalis
    • DOI 10.1046/j.1365-2958.2001.02486.x
    • J. Nakayama, Y. Cao, T. Horii, S. Sakuda, A.D.L. Akkermans, W. de Vos, and H. Nagasawa Gelatinase biosynthesis-activating pheromone: a peptide lactone that mediates quorum sensing in Enterococcus faecalis Mol. Microbiol. 41 2001 145 154 (Pubitemid 32660990)
    • (2001) Molecular Microbiology , vol.41 , Issue.1 , pp. 145-154
    • Nakayama, J.1    Cao, Y.2    Horii, T.3    Sakuda, S.4    Akkermans, A.D.L.5    De Vos, W.M.6    Nagasawa, H.7
  • 43
    • 0035038936 scopus 로고    scopus 로고
    • Characterization of fsr, a regulator controlling expression of gelatinase and serine protease in Enterococcus faecalis OG1RF
    • DOI 10.1128/JB.183.11.3372-3382.2001
    • X. Qin, K.V. Singh, G.M. Weinstock, and B.E. Murray Characterisation of fsr, a regulator controlling expression of gelatinase and serine protease in Enterococcus faecalis OG1RF J. Bacteriol. 183 2001 3372 3382 (Pubitemid 32448601)
    • (2001) Journal of Bacteriology , vol.183 , Issue.11 , pp. 3372-3382
    • Qin, X.1    Singh, K.V.2    Weinstock, G.M.3    Murray, B.E.4
  • 47
    • 33947172767 scopus 로고    scopus 로고
    • Detergents for the stabilization and crystallization of membrane proteins
    • DOI 10.1016/j.ymeth.2007.01.007, PII S1046202307000102
    • G.G. Privé Detergents for the stabilization and crystallization of membrane proteins Methods 41 2007 388 397 (Pubitemid 46400529)
    • (2007) Methods , vol.41 , Issue.4 , pp. 388-397
    • Prive, G.G.1
  • 48
    • 77950496251 scopus 로고    scopus 로고
    • Practical considerations of membrane protein instability during purification and crystallisation
    • C.G. Tate Practical considerations of membrane protein instability during purification and crystallisation Methods Mol. Biol. 601 2010 187 203
    • (2010) Methods Mol. Biol. , vol.601 , pp. 187-203
    • Tate, C.G.1
  • 49
    • 80051996587 scopus 로고    scopus 로고
    • NMR structures of polytopic integral membrane proteins
    • S.G. Patching NMR structures of polytopic integral membrane proteins Mol. Membr. Biol. 28 2011 370 397
    • (2011) Mol. Membr. Biol. , vol.28 , pp. 370-397
    • Patching, S.G.1
  • 50
    • 33749238054 scopus 로고    scopus 로고
    • Direct analysis of a GPCR-agonist interaction by surface plasmon resonance
    • DOI 10.1007/s00249-006-0070-x
    • P.J. Harding, T.C. Hadingham, J.M. McDonnell, and A. Watts Direct analysis of a GPCR-agonist interaction by surface plasmon resonance Eur. Biophys. J. 35 2006 709 712 (Pubitemid 44484423)
    • (2006) European Biophysics Journal , vol.35 , Issue.8 , pp. 709-712
    • Harding, P.J.1    Hadingham, T.C.2    McDonnell, J.M.3    Watts, A.4
  • 52
    • 84859418071 scopus 로고    scopus 로고
    • Detection of membrane-binding proteins by surface plasmon resonance with an all-aqueous amplification scheme
    • Y. Liu, and Q. Cheng Detection of membrane-binding proteins by surface plasmon resonance with an all-aqueous amplification scheme Anal. Chem. 84 2012 3179 3186
    • (2012) Anal. Chem. , vol.84 , pp. 3179-3186
    • Liu, Y.1    Cheng, Q.2
  • 53
    • 11244254913 scopus 로고    scopus 로고
    • Investigation of ligand binding to the multidrug resistance protein EmrE by isothermal titration calorimetry
    • DOI 10.1529/biophysj.104.049247
    • C.W. Sikora, and R.J. Turner Investigation of ligand binding to the multidrug resistance protein EmrE by isothermal titration calorimetry Biophys. J. 88 2005 475 482 (Pubitemid 40070693)
    • (2005) Biophysical Journal , vol.88 , Issue.1 , pp. 475-482
    • Sikora, C.W.1    Turner, R.J.2
  • 55
    • 51849124172 scopus 로고    scopus 로고
    • A homogeneous G protein-coupled receptor ligand binding assay based on time-resolved fluorescence resonance energy transfer
    • H. La, T. Zhou, B.D. Hamman, and Q. Lin A homogeneous G protein-coupled receptor ligand binding assay based on time-resolved fluorescence resonance energy transfer Assay Drug Dev. Technol. 6 2008 543 550
    • (2008) Assay Drug Dev. Technol. , vol.6 , pp. 543-550
    • La, H.1    Zhou, T.2    Hamman, B.D.3    Lin, Q.4
  • 56
    • 84873205676 scopus 로고    scopus 로고
    • Contributions of fluorescence techniques to understanding G protein-coupled receptor dimerization
    • A.D. Goddard, and A. Watts Contributions of fluorescence techniques to understanding G protein-coupled receptor dimerization Biophys. Rev. 4 2012 291 298
    • (2012) Biophys. Rev. , vol.4 , pp. 291-298
    • Goddard, A.D.1    Watts, A.2
  • 57
    • 0026602584 scopus 로고
    • Conformational analysis of the melanin concentrating hormone (MCM) by CD spectroscopy: Disulphide bridge and aromatic tyrosyl contribution
    • G. Siligardi, M.M. Campbell, W.A. Gibbons, and A.F. Drake Conformational analysis of the melanin concentrating hormone (MCM) by CD spectroscopy: disulphide bridge and aromatic tyrosyl contribution Eur. J. Biochem. 206 1991 23 29
    • (1991) Eur. J. Biochem. , vol.206 , pp. 23-29
    • Siligardi, G.1    Campbell, M.M.2    Gibbons, W.A.3    Drake, A.F.4
  • 59
    • 80052263187 scopus 로고    scopus 로고
    • Anti-HIV siamycin i directly inhibits autophosphorylation activity of the bacterial FsrC quorum sensor and other ATP-dependent enzyme activities
    • P. Ma, K. Nishiguchi, H.M. Yuille, L.M. Davis, J. Nakayama, and M.K. Phillips-Jones Anti-HIV siamycin I directly inhibits autophosphorylation activity of the bacterial FsrC quorum sensor and other ATP-dependent enzyme activities FEBS Lett. 585 2011 2660 2664
    • (2011) FEBS Lett. , vol.585 , pp. 2660-2664
    • Ma, P.1    Nishiguchi, K.2    Yuille, H.M.3    Davis, L.M.4    Nakayama, J.5    Phillips-Jones, M.K.6
  • 60
    • 84879314421 scopus 로고    scopus 로고
    • A systematic approach to the amplified expression, functional characterization and purification of inositol transporters from Bacillus subtilis
    • K.E. Bettaney, P. Sukumar, R. Hussain, G. Siligardi, P.J.F. Henderson, and S.G. Patching A systematic approach to the amplified expression, functional characterization and purification of inositol transporters from Bacillus subtilis Mol. Membr. Biol. 30 2013 3 14
    • (2013) Mol. Membr. Biol. , vol.30 , pp. 3-14
    • Bettaney, K.E.1    Sukumar, P.2    Hussain, R.3    Siligardi, G.4    Henderson, P.J.F.5    Patching, S.G.6
  • 61
    • 33847317012 scopus 로고    scopus 로고
    • Sequence and structural features of carbohydrate binding in proteins and assessment of predictability using a neural network
    • A. Malik, and S. Ahmad Sequence and structural features of carbohydrate binding in proteins and assessment of predictability using a neural network BMC Struct. Biol. 7 2007 1 14
    • (2007) BMC Struct. Biol. , vol.7 , pp. 1-14
    • Malik, A.1    Ahmad, S.2
  • 62
    • 7044269246 scopus 로고    scopus 로고
    • 2 determines productive-mode orientation of the enzyme at the membrane surface
    • DOI 10.1016/j.jmb.2004.09.034, PII S0022283604011775
    • 2 determines productive-mode orientation of the enzyme at the membrane surface J. Mol. Biol. 344 2004 71 89 (Pubitemid 39422375)
    • (2004) Journal of Molecular Biology , vol.344 , Issue.1 , pp. 71-89
    • Qin, S.1    Pande, A.H.2    Nemec, K.N.3    Tatulian, S.A.4
  • 64
    • 2542478140 scopus 로고    scopus 로고
    • Stability-indicating chromatographic methods for the determination of some oxicams
    • E.A. Taha, N.N. Salama, and L.S.A. Fattah Stability-indicating chromatographic methods for the determination of some oxicams J. AOAC Int. 87 2004 366 373
    • (2004) J. AOAC Int. , vol.87 , pp. 366-373
    • Taha, E.A.1    Salama, N.N.2    Fattah, L.S.A.3
  • 65
    • 11144259675 scopus 로고    scopus 로고
    • Simultaneous spectrophotometric estimation of chlorzoxazone and nimesulide from combined dosage form
    • U.N. Kale, K.R. Naidu, and M.S. Shingare Simultaneous spectrophotometric estimation of chlorzoxazone and nimesulide from combined dosage form Indian J. Pharm. Sci. 64 2002 168 169
    • (2002) Indian J. Pharm. Sci. , vol.64 , pp. 168-169
    • Kale, U.N.1    Naidu, K.R.2    Shingare, M.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.