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Volumn 9, Issue 42, 2007, Pages 5704-5711

Erratum: Second-harmonic generation for studying structural motion of biological molecules in real time and space (Physical Chemistry Chemical Physics (2007) 9, DOI: 10.1039/b710505c);Second-harmonic generation for studying structural motion of biological molecules in real time and space

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EID: 35448970955     PISSN: 14639076     EISSN: None     Source Type: Journal    
DOI: 10.1039/b716874h     Document Type: Erratum
Times cited : (39)

References (44)
  • 2
    • 0000833201 scopus 로고
    • Optical second harmonic-generation at interfaces
    • Y. R. Shen Optical second harmonic-generation at interfaces Annu. Rev. Phys. Chem. 1989 40 327 350
    • (1989) Annu. Rev. Phys. Chem. , vol.40 , pp. 327-350
    • Shen, Y.R.1
  • 3
    • 0042709672 scopus 로고    scopus 로고
    • Liquid interfaces probed by second-harmonic and sum-frequency spectroscopy
    • K. B. Eisenthal Liquid interfaces probed by second-harmonic and sum-frequency spectroscopy Chem. Rev. 1996 96 1343 1360
    • (1996) Chem. Rev. , vol.96 , pp. 1343-1360
    • Eisenthal, K.B.1
  • 4
    • 0001149541 scopus 로고
    • Determination of molecular-orientation of monolayer adsorbates by optical second-harmonic generation
    • T. F. Heinz H. W. K. Tom Y. R. Shen Determination of molecular- orientation of monolayer adsorbates by optical second-harmonic generation Phys. Rev. A: At., Mol., Opt. Phys. 1983 28 1883 1885
    • (1983) Phys. Rev. A: At., Mol., Opt. Phys. , vol.28 , pp. 1883-1885
    • Heinz, T.F.1    Tom, H.W.K.2    Shen, Y.R.3
  • 5
    • 0000947862 scopus 로고
    • Investigation of surface-induced alignment of liquid-crystal molecules by optical second-harmonic generation
    • M. B. Feller W. Chen Y. R. Shen Investigation of surface-induced alignment of liquid-crystal molecules by optical second-harmonic generation Phys. Rev. A: At., Mol., Opt. Phys. 1991 43 6778 6792
    • (1991) Phys. Rev. A: At., Mol., Opt. Phys. , vol.43 , pp. 6778-6792
    • Feller, M.B.1    Chen, W.2    Shen, Y.R.3
  • 7
    • 0001411019 scopus 로고
    • The phase of second-harmonic light generated at an interface and its relation to absolute molecular-orientation
    • K. Kemnitz K. Bhattacharyya J. M. Hicks G. R. Pinto K. B. Eisenthal T. F. Heinz The phase of second-harmonic light generated at an interface and its relation to absolute molecular-orientation Chem. Phys. Lett. 1986 131 285 290
    • (1986) Chem. Phys. Lett. , vol.131 , pp. 285-290
    • Kemnitz, K.1    Bhattacharyya, K.2    Hicks, J.M.3    Pinto, G.R.4    Eisenthal, K.B.5    Heinz, T.F.6
  • 8
    • 0000991558 scopus 로고
    • Surface polar ordering in a liquid-crystal observed by optical second-harmonic generation
    • P. Guyotsionnest H. Hsiung Y. R. Shen Surface polar ordering in a liquid-crystal observed by optical second-harmonic generation Phys. Rev. Lett. 1986 57 2963 2966
    • (1986) Phys. Rev. Lett. , vol.57 , pp. 2963-2966
    • Guyotsionnest, P.1    Hsiung, H.2    Shen, Y.R.3
  • 9
    • 6444232536 scopus 로고
    • Polarization of water molecules at a charged interface - Second harmonic studies of the silica- water interface
    • S. W. Ong X. L. Zhao K. B. Eisenthal Polarization of water molecules at a charged interface - second harmonic studies of the silica- water interface Chem. Phys. Lett. 1992 191 327 335
    • (1992) Chem. Phys. Lett. , vol.191 , pp. 327-335
    • Ong, S.W.1    Zhao, X.L.2    Eisenthal, K.B.3
  • 10
    • 0242385409 scopus 로고    scopus 로고
    • Second-harmonic imaging microscopy for visualizing biomolecular arrays in cells, tissues and organisms
    • P. J. Campagnola L. M. Loew Second-harmonic imaging microscopy for visualizing biomolecular arrays in cells, tissues and organisms Nat. Biotechnol. 2003 21 1356 1360
    • (2003) Nat. Biotechnol. , vol.21 , pp. 1356-1360
    • Campagnola, P.J.1    Loew, L.M.2
  • 12
    • 85066919432 scopus 로고    scopus 로고
    • Imaging of second harmonic generation by endogenous protein arrays in living cells and tissues
    • W. A. Mohler P. J. Campagnola P. E. Hoppe C. J. Malone Imaging of second harmonic generation by endogenous protein arrays in living cells and tissues Mol. Biol. Cell 2001 12 260A 260A
    • (2001) Mol. Biol. Cell , vol.12
    • Mohler, W.A.1    Campagnola, P.J.2    Hoppe, P.E.3    Malone, C.J.4
  • 13
    • 0036213717 scopus 로고    scopus 로고
    • Three-dimensional high-resolution second-harmonic generation imaging of endogenous structural proteins in biological tissues
    • P. J. Campagnola A. C. Millard M. Terasaki P. E. Hoppe C. J. Malone W. A. Mohler Three-dimensional high-resolution second-harmonic generation imaging of endogenous structural proteins in biological tissues Biophys. J. 2002 82 493 508
    • (2002) Biophys. J. , vol.82 , pp. 493-508
    • Campagnola, P.J.1    Millard, A.C.2    Terasaki, M.3    Hoppe, P.E.4    Malone, C.J.5    Mohler, W.A.6
  • 14
    • 33644749237 scopus 로고    scopus 로고
    • Overcoming photodamage in second-harmonic generation microscopy: Real-time optical recording of neuronal action potentials
    • L. Sacconi D. A. Dombeck W. W. Webb Overcoming photodamage in second-harmonic generation microscopy: Real-time optical recording of neuronal action potentials Proc. Natl. Acad. Sci. U. S. A. 2006 103 3124 3129
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 3124-3129
    • Sacconi, L.1    Dombeck, D.A.2    Webb, W.W.3
  • 15
    • 0041808913 scopus 로고    scopus 로고
    • Direct measurement of the voltage sensitivity of second-harmonic generation from a membrane dye in patch-clamped cells
    • A. C. Millard L. Jin A. Lewis L. M. Loew Direct measurement of the voltage sensitivity of second-harmonic generation from a membrane dye in patch-clamped cells Opt. Lett. 2003 28 1221 1223
    • (2003) Opt. Lett. , vol.28 , pp. 1221-1223
    • Millard, A.C.1    Jin, L.2    Lewis, A.3    Loew, L.M.4
  • 16
    • 0038014315 scopus 로고    scopus 로고
    • 'SHG-labels' for detection of molecules by second harmonic generation
    • J. S. Salafsky 'SHG-labels' for detection of molecules by second harmonic generation Chem. Phys. Lett. 2001 342 485 491
    • (2001) Chem. Phys. Lett. , vol.342 , pp. 485-491
    • Salafsky, J.S.1
  • 17
    • 0242475366 scopus 로고    scopus 로고
    • Second-harmonic generation as a probe of conformational change in molecules
    • J. S. Salafsky Second-harmonic generation as a probe of conformational change in molecules Chem. Phys. Lett. 2003 381 705 709
    • (2003) Chem. Phys. Lett. , vol.381 , pp. 705-709
    • Salafsky, J.S.1
  • 18
    • 33747597796 scopus 로고    scopus 로고
    • Detection of protein conformational change by optical second-harmonic generation
    • J. S. Salafsky Detection of protein conformational change by optical second-harmonic generation J. Chem. Phys. 2006 125 074701
    • (2006) J. Chem. Phys. , vol.125 , pp. 074701
    • Salafsky, J.S.1
  • 19
    • 0029871765 scopus 로고    scopus 로고
    • Substrate binding causes movement in the ATP binding domain of Escherichia coli adenylate kinase
    • T. Bilderback T. Fulmer W. W. Mantulin M. Glaser Substrate binding causes movement in the ATP binding domain of Escherichia coli adenylate kinase Biochemistry 1996 35 6100 6106
    • (1996) Biochemistry , vol.35 , pp. 6100-6106
    • Bilderback, T.1    Fulmer, T.2    Mantulin, W.W.3    Glaser, M.4
  • 20
    • 33144487234 scopus 로고    scopus 로고
    • Roles of static and dynamic domains in stability and catalysis of adenylate kinase
    • E. Bae G. N. Phillips Roles of static and dynamic domains in stability and catalysis of adenylate kinase Proc. Natl. Acad. Sci. U. S. A. 2006 103 2132 2137
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 2132-2137
    • Bae, E.1    Phillips, G.N.2
  • 22
    • 24644483073 scopus 로고    scopus 로고
    • Large amplitude conformational change in proteins explored with a plastic network model: Adenylate kinase
    • P. Maragakis M. Karplus Large amplitude conformational change in proteins explored with a plastic network model: Adenylate kinase J. Mol. Biol. 2005 352 807 822
    • (2005) J. Mol. Biol. , vol.352 , pp. 807-822
    • Maragakis, P.1    Karplus, M.2
  • 23
    • 0026544877 scopus 로고
    • Structure of the complex between adenylate kinase from Escherichia-Coli and the inhibitor Ap5a refined at 1.9 Å resolution - A model for a catalytic transition-state
    • C. W. Muller G. E. Schulz Structure of the complex between adenylate kinase from Escherichia-Coli and the inhibitor Ap5a refined at 1.9 Å resolution - a model for a catalytic transition-state J. Mol. Biol. 1992 224 159 177
    • (1992) J. Mol. Biol. , vol.224 , pp. 159-177
    • Muller, C.W.1    Schulz, G.E.2
  • 25
    • 0028338283 scopus 로고
    • The closed conformation of a highly flexible protein - The structure of Escherichia coli adenylate kinase with bound Amp and Amppnp
    • M. B. Berry B. Meador T. Bilderback P. Liang M. Glaser G. N. Phillips The closed conformation of a highly flexible protein - the structure of Escherichia coli adenylate kinase with bound Amp and Amppnp Proteins: Struct., Funct., Genet. 1994 19 183 198
    • (1994) Proteins: Struct., Funct., Genet. , vol.19 , pp. 183-198
    • Berry, M.B.1    Meador, B.2    Bilderback, T.3    Liang, P.4    Glaser, M.5    Phillips, G.N.6
  • 26
    • 0034250113 scopus 로고    scopus 로고
    • Protein adsorption at interfaces detected by second harmonic generation
    • J. S. Salafsky K. B. Eisenthal Protein adsorption at interfaces detected by second harmonic generation J. Phys. Chem. B 2000 104 7752 7755
    • (2000) J. Phys. Chem. B , vol.104 , pp. 7752-7755
    • Salafsky, J.S.1    Eisenthal, K.B.2
  • 27
    • 0017690217 scopus 로고
    • Asymmetric binding of inhibitor di(adenosine-5′) pentaphosphate (Ap5a) to adenylate kinase
    • B. D. N. Rao M. Cohn Asymmetric binding of inhibitor di(adenosine- 5′) pentaphosphate (Ap5a) to adenylate kinase Proc. Natl. Acad. Sci. U. S. A. 1977 74 5355 5357
    • (1977) Proc. Natl. Acad. Sci. U. S. A. , vol.74 , pp. 5355-5357
    • Rao, B.D.N.1    Cohn, M.2
  • 28
    • 0015829675 scopus 로고
    • Magnetic-resonance studies of substrate and inhibitor binding to porcine muscle adenylate kinase
    • N. C. Price G. H. Reed M. Cohn Magnetic-resonance studies of substrate and inhibitor binding to porcine muscle adenylate kinase Biochemistry 1973 12 3322 3327
    • (1973) Biochemistry , vol.12 , pp. 3322-3327
    • Price, N.C.1    Reed, G.H.2    Cohn, M.3
  • 29
    • 21344484226 scopus 로고
    • Optical second-harmonic generation from adsorbate layers in total-reflection geometry
    • B. U. Felderhof A. Bratz G. Marowsky O. Roders F. Sieverdes Optical second-harmonic generation from adsorbate layers in total-reflection geometry J. Opt. Soc. Am. B 1993 10 1824 1833
    • (1993) J. Opt. Soc. Am. B , vol.10 , pp. 1824-1833
    • Felderhof, B.U.1    Bratz, A.2    Marowsky, G.3    Roders, O.4    Sieverdes, F.5
  • 30
    • 35448965307 scopus 로고
    • Y. R. Shen, in Molecular nonlinear optics: materials, physics and devices (Quantum electronics principles and application series), ed. J. Zyss, Academic Press, New York
    • Quadratic Molecular Nonlinearities at the Air/Water Interface, ed., Y. R. Shen,, in Molecular nonlinear optics: materials, physics and devices (Quantum electronics principles and application series), ed., J. Zyss,, Academic Press, New York, 1993
    • (1993) Quadratic Molecular Nonlinearities at the Air/Water Interface, Ed.
  • 31
    • 0000667455 scopus 로고
    • Excited-state dipole-moments from an efficient analysis of solvatochromic Stokes shift data
    • M. Ravi A. Samanta T. P. Radhakrishnan Excited-state dipole-moments from an efficient analysis of solvatochromic Stokes shift data J. Phys. Chem. 1994 98 9133 9136
    • (1994) J. Phys. Chem. , vol.98 , pp. 9133-9136
    • Ravi, M.1    Samanta, A.2    Radhakrishnan, T.P.3
  • 32
    • 0001425768 scopus 로고
    • Investigation of anisotropic molecular orientational distributions of liquid-crystal monolayers by optical second-harmonic generation
    • W. Chen M. B. Feller Y. R. Shen Investigation of anisotropic molecular orientational distributions of liquid-crystal monolayers by optical second-harmonic generation Phys. Rev. Lett. 1989 63 2665 2668
    • (1989) Phys. Rev. Lett. , vol.63 , pp. 2665-2668
    • Chen, W.1    Feller, M.B.2    Shen, Y.R.3
  • 33
    • 0031886683 scopus 로고    scopus 로고
    • Specific interaction and two-dimensional crystallization of histidine tagged yeast RNA polymerase I on nickel-chelating lipids
    • N. Bischler F. Balavoine P. Milkereit H. Tschochner C. Mioskowski P. Schultz Specific interaction and two-dimensional crystallization of histidine tagged yeast RNA polymerase I on nickel-chelating lipids Biophys. J. 1998 74 1522 1532
    • (1998) Biophys. J. , vol.74 , pp. 1522-1532
    • Bischler, N.1    Balavoine, F.2    Milkereit, P.3    Tschochner, H.4    Mioskowski, C.5    Schultz, P.6
  • 34
    • 0037184061 scopus 로고    scopus 로고
    • Specific orientation and two-dimensional crystallization of the proteasome at metal-chelating lipid interfaces
    • A. Thess S. Hutschenreiter M. Hofmann R. Tampe W. Baumeister R. Guckenberger Specific orientation and two-dimensional crystallization of the proteasome at metal-chelating lipid interfaces J. Biol. Chem. 2002 277 36321 36328
    • (2002) J. Biol. Chem. , vol.277 , pp. 36321-36328
    • Thess, A.1    Hutschenreiter, S.2    Hofmann, M.3    Tampe, R.4    Baumeister, W.5    Guckenberger, R.6
  • 35
    • 24744472221 scopus 로고    scopus 로고
    • High-affinity chelator thiols for switchable and oriented immobilization of histidine-tagged proteins: A generic platform for protein chip technologies
    • A. Tinazli J. L. Tang R. Valiokas S. Picuric S. Lata J. Piehler B. Liedberg R. Tampe High-affinity chelator thiols for switchable and oriented immobilization of histidine-tagged proteins: A generic platform for protein chip technologies Chem.-Eur. J. 2005 11 5249 5259
    • (2005) Chem.-Eur. J. , vol.11 , pp. 5249-5259
    • Tinazli, A.1    Tang, J.L.2    Valiokas, R.3    Picuric, S.4    Lata, S.5    Piehler, J.6    Liedberg, B.7    Tampe, R.8
  • 36
    • 10344265554 scopus 로고    scopus 로고
    • Oriented attachment and membrane reconstitution of his-tagged cytochrome c oxidase to a gold electrode: In situ monitoring by surface-enhanced infrared absorption spectroscopy
    • K. Ataka F. Giess W. Knoll R. Naumann S. Haber-Pohlmeier B. Richter J. Heberle Oriented attachment and membrane reconstitution of his-tagged cytochrome c oxidase to a gold electrode: In situ monitoring by surface-enhanced infrared absorption spectroscopy J. Am. Chem. Soc. 2004 126 16199 16206
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 16199-16206
    • Ataka, K.1    Giess, F.2    Knoll, W.3    Naumann, R.4    Haber-Pohlmeier, S.5    Richter, B.6    Heberle, J.7
  • 37
    • 0030459599 scopus 로고    scopus 로고
    • Architecture and function of membrane proteins in planar supported bilayers: A study with photosynthetic reaction centers
    • J. Salafsky J. T. Groves S. G. Boxer Architecture and function of membrane proteins in planar supported bilayers: A study with photosynthetic reaction centers Biochemistry 1996 35 14773 14781
    • (1996) Biochemistry , vol.35 , pp. 14773-14781
    • Salafsky, J.1    Groves, J.T.2    Boxer, S.G.3
  • 38
    • 33749019097 scopus 로고    scopus 로고
    • Innovation: A chemical toolkit for proteins - An expanded genetic code
    • J. M. Xie P. G. Schultz Innovation: A chemical toolkit for proteins - an expanded genetic code Nat. Rev. Mol. Cell Biol. 2006 7 775 782
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 775-782
    • Xie, J.M.1    Schultz, P.G.2
  • 40
    • 33745015242 scopus 로고    scopus 로고
    • In vivo incorporation of multiple unnatural amino acids through nonsense and frameshift suppression
    • E. A. Rodriguez H. A. Lester D. A. Dougherty In vivo incorporation of multiple unnatural amino acids through nonsense and frameshift suppression Proc. Natl. Acad. Sci. U. S. A. 2006 103 8650 8655
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 8650-8655
    • Rodriguez, E.A.1    Lester, H.A.2    Dougherty, D.A.3
  • 41
    • 4644252142 scopus 로고    scopus 로고
    • Unnatural amino acid mutagenesis: A precise tool for probing protein structure and function
    • P. M. England Unnatural amino acid mutagenesis: A precise tool for probing protein structure and function Biochemistry 2004 43 11623 11629
    • (2004) Biochemistry , vol.43 , pp. 11623-11629
    • England, P.M.1
  • 42
    • 35448944935 scopus 로고    scopus 로고
    • Aladan, an alanine derivative of DAN, 6-methylamino-2-acyl-naphthalene is a second-harmonic-active unnatural amino acid (J. S. Salafsky and B.E. Cohen, manuscript in preparation)
    • Aladan, an alanine derivative of DAN, 6-methylamino-2-acyl-naphthalene is a second-harmonic-active unnatural amino acid (J. S. Salafsky and B.E. Cohen, manuscript in preparation)
  • 43
    • 0036682301 scopus 로고    scopus 로고
    • Crystal structures of the kinase domain of c-Abl in complex with the small molecule inhibitors PD173955 and imatinib (STI-571)
    • B. Nagar W. G. Bornmann P. Pellicena T. Schindler D. R. Veach W. T. Miller B. Clarkson J. Kuriyan Crystal structures of the kinase domain of c-Abl in complex with the small molecule inhibitors PD173955 and imatinib (STI-571) Cancer Res. 2002 62 4236 4243
    • (2002) Cancer Res. , vol.62 , pp. 4236-4243
    • Nagar, B.1    Bornmann, W.G.2    Pellicena, P.3    Schindler, T.4    Veach, D.R.5    Miller, W.T.6    Clarkson, B.7    Kuriyan, J.8
  • 44
    • 0037031906 scopus 로고    scopus 로고
    • Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling.
    • J. Takagi B. M. Petre T. Walz T. A. Springer Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling. Cell 110 599 611
    • Cell , vol.110 , pp. 599-611
    • Takagi, J.1    Petre, B.M.2    Walz, T.3    Springer, T.A.4


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