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Volumn 51, Issue 8, 2012, Pages 1796-1802

Examining protein surface structure in highly conserved sequence variants with mass spectrometry

Author keywords

[No Author keywords available]

Indexed keywords

ACIDIC RESIDUES; BACKBONE STRUCTURES; CYTOCHROME C; ELECTROSTATIC SURFACES; HOMOLOGOUS PROTEINS; HUMAN LYSOZYME; MINIMAL SAMPLE; NATURALLY OCCURRING; NON-COVALENT ADDUCTS; NONCOVALENT; NONCOVALENT ATTACHMENT; POINT MUTATIONS; PROTEIN STRUCTURES; SEQUENCE HOMOLOGY; SEQUENCE VARIANTS; STRUCTURAL STATE; TERTIARY STRUCTURES;

EID: 84857523888     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi2018199     Document Type: Article
Times cited : (6)

References (31)
  • 1
    • 34548184125 scopus 로고    scopus 로고
    • Residual structure, backbone dynamics, and interactions within the synuclein family
    • Sung, Y. H. and Eliezer, D. (2007) Residual structure, backbone dynamics, and interactions within the synuclein family J. Mol. Biol. 372, 689-707
    • (2007) J. Mol. Biol. , vol.372 , pp. 689-707
    • Sung, Y.H.1    Eliezer, D.2
  • 2
    • 0031990490 scopus 로고    scopus 로고
    • Ala30Pro mutation in the gene encoding α-synuclein in Parkinson's disease
    • Kruger, R., Kuhn, W., Muller, T., Woitalla, D., Graeber, M., and Kosel, S. 1998, Ala30Pro mutation in the gene encoding α-synuclein in Parkinson's disease Nat. Genet. 18, 106-108
    • (1998) Nat. Genet. , vol.18 , pp. 106-108
    • Kruger, R.1    Kuhn, W.2    Muller, T.3    Woitalla, D.4    Graeber, M.5    Kosel, S.6
  • 3
    • 0030744876 scopus 로고    scopus 로고
    • Mutation in the α-synuclein gene identified in families with Parkinson's disease
    • Polymeropoulos, M. H., Lavedan, C., Leroy, E., Ide, S. E., Dehejia, A., and Dutra, A. 1997, Mutation in the α-synuclein gene identified in families with Parkinson's disease Science 276, 2045-2047
    • (1997) Science , vol.276 , pp. 2045-2047
    • Polymeropoulos, M.H.1    Lavedan, C.2    Leroy, E.3    Ide, S.E.4    Dehejia, A.5    Dutra, A.6
  • 5
    • 1842337282 scopus 로고
    • Gene mutations in human haemoglobin: Chemical difference between normal and sickle cell haemoglobin
    • Ingram, V. M. (1957) Gene mutations in human haemoglobin: Chemical difference between normal and sickle cell haemoglobin Nature 180, 326-328
    • (1957) Nature , vol.180 , pp. 326-328
    • Ingram, V.M.1
  • 6
    • 0032484104 scopus 로고    scopus 로고
    • Crystal structure of deoxy-human hemoglobin β6 Glu → Trp: Implications for the structure and formation of the sickle cell fiber
    • Harrington, D. J., Adachi, K., and Royer, W. E. (1998) Crystal structure of deoxy-human hemoglobin β6 Glu → Trp: Implications for the structure and formation of the sickle cell fiber J. Biol. Chem. 273, 32690-32696
    • (1998) J. Biol. Chem. , vol.273 , pp. 32690-32696
    • Harrington, D.J.1    Adachi, K.2    Royer, W.E.3
  • 7
    • 0032567404 scopus 로고    scopus 로고
    • The rub family of ubiquitin-like proteins: Crystal structure of Arabidopsis Rub1 and expression of multiple rubs in Arabidopsis
    • Rao-Naik, C., delaCruz, W., Laplaza, J. M., Tan, S., Callis, J., and Fisher, A. J. (1998) The rub family of ubiquitin-like proteins: Crystal structure of Arabidopsis Rub1 and expression of multiple rubs in Arabidopsis J. Biol. Chem. 273, 34976-34982
    • (1998) J. Biol. Chem. , vol.273 , pp. 34976-34982
    • Rao-Naik, C.1    Delacruz, W.2    Laplaza, J.M.3    Tan, S.4    Callis, J.5    Fisher, A.J.6
  • 8
    • 0000857187 scopus 로고
    • The Ubiquitin System: Functions and Mechanisms
    • Finley, D. and Varshavsky, A. (1985) The Ubiquitin System: Functions and Mechanisms Trends Biochem. Sci. 10, 343-347
    • (1985) Trends Biochem. Sci. , vol.10 , pp. 343-347
    • Finley, D.1    Varshavsky, A.2
  • 9
    • 0035903602 scopus 로고    scopus 로고
    • Investigating and engineering enzymes by genetic selection
    • Taylor, S. V., Kast, P., and Hilvert, D. (2001) Investigating and engineering enzymes by genetic selection Angew. Chem., Int. Ed. 40, 3310-3335
    • (2001) Angew. Chem., Int. Ed. , vol.40 , pp. 3310-3335
    • Taylor, S.V.1    Kast, P.2    Hilvert, D.3
  • 10
    • 37349082255 scopus 로고    scopus 로고
    • High resolution X-ray crystallographic structure of bovine heart cytochrome c and its application to the design of an electron transfer biosensor
    • Mirkin, N., Jaconcic, J., Stojanoff, V., and Moreno, A. (2008) High resolution X-ray crystallographic structure of bovine heart cytochrome c and its application to the design of an electron transfer biosensor Proteins 70, 83-92
    • (2008) Proteins , vol.70 , pp. 83-92
    • Mirkin, N.1    Jaconcic, J.2    Stojanoff, V.3    Moreno, A.4
  • 11
    • 0033794003 scopus 로고    scopus 로고
    • NMR spectroscopy: A multifaceted approach to macromolecular structure
    • Ferentz, A. E. and Wagner, G. (2000) NMR spectroscopy: A multifaceted approach to macromolecular structure Q. Rev. Biophys. 33, 29-65
    • (2000) Q. Rev. Biophys. , vol.33 , pp. 29-65
    • Ferentz, A.E.1    Wagner, G.2
  • 12
    • 0025674590 scopus 로고
    • Probing Conformational Changes in Proteins by Mass Spectrometry
    • Chowdhury, S. K., Katta, V., and Chait, B. T. (1990) Probing Conformational Changes in Proteins by Mass Spectrometry J. Am. Chem. Soc. 112, 9012-9013
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 9012-9013
    • Chowdhury, S.K.1    Katta, V.2    Chait, B.T.3
  • 13
    • 0037258408 scopus 로고    scopus 로고
    • Origin of the conformation dependence of protein charge-state distributions in electrospray ionization mass spectrometry
    • Grandori, R. (2003) Origin of the conformation dependence of protein charge-state distributions in electrospray ionization mass spectrometry J. Mass Spectrom. 38, 11-15
    • (2003) J. Mass Spectrom. , vol.38 , pp. 11-15
    • Grandori, R.1
  • 14
    • 23744516059 scopus 로고    scopus 로고
    • Estimates of protein surface areas in solution by electrospray ionization mass spectrometry
    • Kaltashov, I. A. and Mohimen, A. (2005) Estimates of protein surface areas in solution by electrospray ionization mass spectrometry Anal. Chem. 77, 5370-5379
    • (2005) Anal. Chem. , vol.77 , pp. 5370-5379
    • Kaltashov, I.A.1    Mohimen, A.2
  • 15
    • 33644761306 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry for the analysis of protein dynamics
    • Wales, T. E. and Engen, J. R. (2006) Hydrogen exchange mass spectrometry for the analysis of protein dynamics Mass Spectrom. Rev. 25, 158-170
    • (2006) Mass Spectrom. Rev. , vol.25 , pp. 158-170
    • Wales, T.E.1    Engen, J.R.2
  • 16
    • 42349091083 scopus 로고    scopus 로고
    • Protein surface mapping using diethylpyrocarbonate with mass spectrometric detection
    • Mendoza, V. L. and Vachet, R. W. (2008) Protein surface mapping using diethylpyrocarbonate with mass spectrometric detection Anal. Chem. 80, 2895-2904
    • (2008) Anal. Chem. , vol.80 , pp. 2895-2904
    • Mendoza, V.L.1    Vachet, R.W.2
  • 17
    • 33745742438 scopus 로고    scopus 로고
    • Chemical cross-linking and mass spectrometry to map three-dimensional protein structures and protein-protein interactions
    • Sinz, A. (2006) Chemical cross-linking and mass spectrometry to map three-dimensional protein structures and protein-protein interactions Mass Spectrom. Rev. 25, 663-682
    • (2006) Mass Spectrom. Rev. , vol.25 , pp. 663-682
    • Sinz, A.1
  • 18
    • 33747882757 scopus 로고    scopus 로고
    • Using ESI-MS to probe protein structure by site-specific noncovalent attachment of 18-crown-6
    • Ly, T. and Julian, R. R. (2006) Using ESI-MS to probe protein structure by site-specific noncovalent attachment of 18-crown-6 J. Am. Soc. Mass Spectrom. 17, 1209-1215
    • (2006) J. Am. Soc. Mass Spectrom. , vol.17 , pp. 1209-1215
    • Ly, T.1    Julian, R.R.2
  • 19
    • 43949144960 scopus 로고    scopus 로고
    • Exploring the mechanism of selective noncovalent adduct protein probing mass spectrometry utilizing site-directed mutagenesis to examine ubiquitin
    • Liu, Z. J., Cheng, S. J., Gailie, D. R., and Julian, R. R. (2008) Exploring the mechanism of selective noncovalent adduct protein probing mass spectrometry utilizing site-directed mutagenesis to examine ubiquitin Anal. Chem. 80, 3846-3852
    • (2008) Anal. Chem. , vol.80 , pp. 3846-3852
    • Liu, Z.J.1    Cheng, S.J.2    Gailie, D.R.3    Julian, R.R.4
  • 20
    • 55149085458 scopus 로고    scopus 로고
    • Protein-Metal Interactions of Calmodulin and α-Synuclein Monitored by Selective Noncovalent Adduct Protein Probing Mass Spectrometry
    • Ly, T. and Julian, R. R. (2008) Protein-Metal Interactions of Calmodulin and α-Synuclein Monitored by Selective Noncovalent Adduct Protein Probing Mass Spectrometry J. Am. Soc. Mass Spectrom. 19, 1663-1672
    • (2008) J. Am. Soc. Mass Spectrom. , vol.19 , pp. 1663-1672
    • Ly, T.1    Julian, R.R.2
  • 21
    • 79951915697 scopus 로고    scopus 로고
    • Dynamic Interchanging Native States of Lymphotactin Examined by SNAPP-MS
    • Sun, Q. Y., Tyler, R. C., Volkman, B. F., and Julian, R. R. (2011) Dynamic Interchanging Native States of Lymphotactin Examined by SNAPP-MS J. Am. Soc. Mass Spectrom. 22, 399-407
    • (2011) J. Am. Soc. Mass Spectrom. , vol.22 , pp. 399-407
    • Sun, Q.Y.1    Tyler, R.C.2    Volkman, B.F.3    Julian, R.R.4
  • 22
    • 84856137749 scopus 로고    scopus 로고
    • Reflections on Charge State Distributions, Protein Structure, and the Mystical Mechanism of Electrospray Ionization
    • Hamdy, O. and Julian, R. R. (2012) Reflections on Charge State Distributions, Protein Structure, and the Mystical Mechanism of Electrospray Ionization J. Am. Soc. Mass Spectrom. 23, 1-6
    • (2012) J. Am. Soc. Mass Spectrom. , vol.23 , pp. 1-6
    • Hamdy, O.1    Julian, R.R.2
  • 24
  • 25
    • 0026522022 scopus 로고
    • Monovalent Cation Binding to Cubic Insulin Crystals
    • Gursky, O., Li, Y. L., Badger, J., and Caspar, D. L. D. (1992) Monovalent Cation Binding to Cubic Insulin Crystals Biophys. J. 61, 604-611
    • (1992) Biophys. J. , vol.61 , pp. 604-611
    • Gursky, O.1    Li, Y.L.2    Badger, J.3    Caspar, D.L.D.4
  • 27
    • 0035984339 scopus 로고    scopus 로고
    • Studies of biomolecular conformations and conformational dynamics by mass spectrometry
    • Kaltashov, I. A. and Eyles, S. J. (2002) Studies of biomolecular conformations and conformational dynamics by mass spectrometry Mass Spectrom. Rev. 21, 37-71
    • (2002) Mass Spectrom. Rev. , vol.21 , pp. 37-71
    • Kaltashov, I.A.1    Eyles, S.J.2
  • 28
    • 0015919686 scopus 로고
    • Role of heme in formation of structure of cytochrome-c
    • Fisher, W. R., Taniuchi, H., and Anfinsen, C. B. (1973) Role of heme in formation of structure of cytochrome-c J. Biol. Chem. 248, 3188-3195
    • (1973) J. Biol. Chem. , vol.248 , pp. 3188-3195
    • Fisher, W.R.1    Taniuchi, H.2    Anfinsen, C.B.3
  • 29
    • 0029893286 scopus 로고    scopus 로고
    • The methanol-induced globular and expanded denatured states of cytochrome c: A study by CD fluorescence, NMR and small-angle X-ray scattering
    • Kamatari, Y. O., Konno, T., Kataoka, M., and Akasaka, K. (1996) The methanol-induced globular and expanded denatured states of cytochrome c: A study by CD fluorescence, NMR and small-angle X-ray scattering J. Mol. Biol. 259, 512-523
    • (1996) J. Mol. Biol. , vol.259 , pp. 512-523
    • Kamatari, Y.O.1    Konno, T.2    Kataoka, M.3    Akasaka, K.4
  • 30
    • 0030827122 scopus 로고    scopus 로고
    • Acid-induced unfolding of cytochrome c at different methanol concentrations: Electrospray ionization mass spectrometry specifically monitors changes in the tertiary structure
    • Konermann, L. and Douglas, D. J. (1997) Acid-induced unfolding of cytochrome c at different methanol concentrations: Electrospray ionization mass spectrometry specifically monitors changes in the tertiary structure Biochemistry 36, 12296-12302
    • (1997) Biochemistry , vol.36 , pp. 12296-12302
    • Konermann, L.1    Douglas, D.J.2
  • 31
    • 33748349224 scopus 로고    scopus 로고
    • The role of hydrophobic interactions in initiation and propagation of protein folding
    • Dyson, H. J., Wright, P. E., and Scheraga, H. A. (2006) The role of hydrophobic interactions in initiation and propagation of protein folding Proc. Natl. Acad. Sci. U.S.A. 103, 13057-13061
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 13057-13061
    • Dyson, H.J.1    Wright, P.E.2    Scheraga, H.A.3


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