메뉴 건너뛰기




Volumn 6, Issue 2, 2007, Pages 711-723

Structural and functional analysis of hypothetical proteins in mouse hippocampus from two-dimensional gel electrophoresis

Author keywords

2D gel electrophoresis; Enzyme activity; Hypothetical proteins; Mass spectrometry; Recovery of enzyme activity

Indexed keywords

GUANIDINE; PHOSPHATASE; PHOSPHATE PHOSPHATASE; PYRIDOXAL PHOSPHATE PHOSPHATASE; PYRIDOXINE DERIVATIVE; PYRIPHOSPHATE PHOSPHATASE; RECOMBINANT PROTEIN; THIOREDOXIN; UNCLASSIFIED DRUG;

EID: 33847420464     PISSN: 15353893     EISSN: None     Source Type: Journal    
DOI: 10.1021/pr060453o     Document Type: Article
Times cited : (9)

References (53)
  • 1
    • 27844598851 scopus 로고    scopus 로고
    • Searching for hypothetical proteins: Theory and practice based upon original data and literature
    • Lubec, G.; Afjehi-Sadat, L.; Yang, J. W.; John, J. P. Searching for hypothetical proteins: theory and practice based upon original data and literature. Prog. Neurobiol. 2005, 77, 90-127.
    • (2005) Prog. Neurobiol , vol.77 , pp. 90-127
    • Lubec, G.1    Afjehi-Sadat, L.2    Yang, J.W.3    John, J.P.4
  • 3
    • 2942729565 scopus 로고    scopus 로고
    • Hypothetical proteins with putative enzyme activity in human amnion, lymphocyte, bronchial epithelial and kidney cell lines
    • Afjehi-Sadat, L.; Krapfenbauer, K.; Slavc, I.; Fountoulakis, M.; Lubec, G. Hypothetical proteins with putative enzyme activity in human amnion, lymphocyte, bronchial epithelial and kidney cell lines. Biochim. Biophys. Acta 2004, 7700, 65-74.
    • (2004) Biochim. Biophys. Acta , vol.7700 , pp. 65-74
    • Afjehi-Sadat, L.1    Krapfenbauer, K.2    Slavc, I.3    Fountoulakis, M.4    Lubec, G.5
  • 4
    • 3042518994 scopus 로고    scopus 로고
    • Altered expression of hypothetical proteins in hippocampus of transgenic mice overexpressing human Cu/Zn-superoxide dismutase 1
    • Shin, J. H.; Yang, J. W.; Le Pecheur, M.; London, J.; Hoeger, H.; Lubec, G. Altered expression of hypothetical proteins in hippocampus of transgenic mice overexpressing human Cu/Zn-superoxide dismutase 1. Proteome Sci. 2004, 2, 2.
    • (2004) Proteome Sci , vol.2 , pp. 2
    • Shin, J.H.1    Yang, J.W.2    Le Pecheur, M.3    London, J.4    Hoeger, H.5    Lubec, G.6
  • 7
    • 2542625285 scopus 로고    scopus 로고
    • Deranged hypothetical proteins Rik protein, Nit protein 2 and mitochondrial inner membrane protein, Mitofilin, in fetal Down syndrome brain
    • Myung, J. K.; Gulesserian, T.; Fountoulakis, M.; Lubec, G. Deranged hypothetical proteins Rik protein, Nit protein 2 and mitochondrial inner membrane protein, Mitofilin, in fetal Down syndrome brain. Cell. Mol. Biol. (Paris) 2003, 49, 739-746.
    • (2003) Cell. Mol. Biol. (Paris) , vol.49 , pp. 739-746
    • Myung, J.K.1    Gulesserian, T.2    Fountoulakis, M.3    Lubec, G.4
  • 8
    • 29144479312 scopus 로고    scopus 로고
    • Detection of hypothetical proteins in human fetal perireticular nucleus
    • Hepner, F.; Myung, J. K.; Ulfig, N.; Pollak, A.; Lubec, G. Detection of hypothetical proteins in human fetal perireticular nucleus. J. Proteome Res. 2005, 4, 2379-2385.
    • (2005) J. Proteome Res , vol.4 , pp. 2379-2385
    • Hepner, F.1    Myung, J.K.2    Ulfig, N.3    Pollak, A.4    Lubec, G.5
  • 9
    • 33746866302 scopus 로고    scopus 로고
    • Mass spectrometric identification of serine hydrolase OVCA2 in the medulloblastoma cell line DAOY
    • Azizi, A. A.; Gelpi, E.; Yang, J. W.; Rupp, B.; Godwin, A. K.; Slater, C.; Slavc, I.; Lubec, G. Mass spectrometric identification of serine hydrolase OVCA2 in the medulloblastoma cell line DAOY. Cancer Lett. 2006, 241, 235-249.
    • (2006) Cancer Lett , vol.241 , pp. 235-249
    • Azizi, A.A.1    Gelpi, E.2    Yang, J.W.3    Rupp, B.4    Godwin, A.K.5    Slater, C.6    Slavc, I.7    Lubec, G.8
  • 11
    • 33644959879 scopus 로고    scopus 로고
    • Cloning and characterization of CBL-CIPK signalling components from a legume (Pisum sativum)
    • Mahajan, S.; Sopory, S. K.; Tuteja, N. Cloning and characterization of CBL-CIPK signalling components from a legume (Pisum sativum). FEBS J. 2006, 273, 907-925.
    • (2006) FEBS J , vol.273 , pp. 907-925
    • Mahajan, S.1    Sopory, S.K.2    Tuteja, N.3
  • 12
    • 33646933886 scopus 로고    scopus 로고
    • Recombinant expression and biochemical characterization of the unique elongating beta-ketoacyl-acyl carrier protein synthase involved in fatty acid biosynthesis of Plasmodium falciparum using natural and artificial substrates
    • Lack, G.; Homberger-Zizzari, E.; Folkers, G.; Scapozza, L.; Perozzo, R. Recombinant expression and biochemical characterization of the unique elongating beta-ketoacyl-acyl carrier protein synthase involved in fatty acid biosynthesis of Plasmodium falciparum using natural and artificial substrates. J. Biol. Chem. 2006, 281, 9538-9546.
    • (2006) J. Biol. Chem , vol.281 , pp. 9538-9546
    • Lack, G.1    Homberger-Zizzari, E.2    Folkers, G.3    Scapozza, L.4    Perozzo, R.5
  • 14
    • 0019258624 scopus 로고
    • Elution of proteins from sodium dodecyl sulfate-polyacrylamide gels, removal of sodium dodecyl sulfate, and renaturation of enzymatic activity: Results with sigma subunit of Escherichia coli RNA polymerase, wheat germ DNA topoisomerase, and other enzymes
    • Hager, D. A.; Burgess, R. R. Elution of proteins from sodium dodecyl sulfate-polyacrylamide gels, removal of sodium dodecyl sulfate, and renaturation of enzymatic activity: results with sigma subunit of Escherichia coli RNA polymerase, wheat germ DNA topoisomerase, and other enzymes. Anal. Biochem. 1980, 109, 76-86.
    • (1980) Anal. Biochem , vol.109 , pp. 76-86
    • Hager, D.A.1    Burgess, R.R.2
  • 15
    • 33746871457 scopus 로고    scopus 로고
    • Components of the protein quality control system are expressed in a strain-dependent manner in the mouse hippocampus
    • Pollak, D. D.; John, J.; Bubna-Littitz, H.; Schneider, A.; Hoeger, H.; Lubec, G. Components of the protein quality control system are expressed in a strain-dependent manner in the mouse hippocampus. Neurochem. Int. 2006, 49, 500-507.
    • (2006) Neurochem. Int , vol.49 , pp. 500-507
    • Pollak, D.D.1    John, J.2    Bubna-Littitz, H.3    Schneider, A.4    Hoeger, H.5    Lubec, G.6
  • 16
    • 33644761190 scopus 로고    scopus 로고
    • Strain-dependent regulation of neurotransmission and actin-remodelling proteins in the mouse hippocampus
    • Pollak, D. D.; John, J.; Scharl, T.; Leisch, F.; Schneider, A.; Hoeger, H.; Lubec, G. Strain-dependent regulation of neurotransmission and actin-remodelling proteins in the mouse hippocampus. Genes, Brain Behav. 2006, 5, 200-204.
    • (2006) Genes, Brain Behav , vol.5 , pp. 200-204
    • Pollak, D.D.1    John, J.2    Scharl, T.3    Leisch, F.4    Schneider, A.5    Hoeger, H.6    Lubec, G.7
  • 17
    • 30744441654 scopus 로고    scopus 로고
    • Protein dysregulation in mouse hippocampus polytransgenic for chromosome 21 structures in the Down Syndrome Critical Region
    • Shin, J. H.; Gulesserian, T.; Verger, E.; Delabar, J. M.; Lubec, G. Protein dysregulation in mouse hippocampus polytransgenic for chromosome 21 structures in the Down Syndrome Critical Region. J. Proteome Res. 2006, 5, 44-53.
    • (2006) J. Proteome Res , vol.5 , pp. 44-53
    • Shin, J.H.1    Gulesserian, T.2    Verger, E.3    Delabar, J.M.4    Lubec, G.5
  • 18
    • 32344446003 scopus 로고    scopus 로고
    • Strain-dependent expression of signaling proteins in the mouse hippocampus
    • Pollak, D. D.; John, J.; Schneider, A.; Hoeger, H.; Lubec, G. Strain-dependent expression of signaling proteins in the mouse hippocampus. Neuroscience 2006, 138, 149-158.
    • (2006) Neuroscience , vol.138 , pp. 149-158
    • Pollak, D.D.1    John, J.2    Schneider, A.3    Hoeger, H.4    Lubec, G.5
  • 20
    • 18144388978 scopus 로고    scopus 로고
    • Proteome analysis in hippocampus of mice overexpressing human Cu/Zn-superoxide dismutase 1
    • Shin, J. H.; London, J.; Le Pecheur, M.; Weitzdoerfer, R.; Hoeger, H.; Lubec, G. Proteome analysis in hippocampus of mice overexpressing human Cu/Zn-superoxide dismutase 1. Neurochem. Int. 2005, 46, 641-653.
    • (2005) Neurochem. Int , vol.46 , pp. 641-653
    • Shin, J.H.1    London, J.2    Le Pecheur, M.3    Weitzdoerfer, R.4    Hoeger, H.5    Lubec, G.6
  • 21
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72, 248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 22
    • 0036288814 scopus 로고    scopus 로고
    • Reduction of actin-related protein complex 2/3 in fetal Down syndrome brain
    • Weitzdoerfer, R.; Fountoulakis, M.; Lubec, G. Reduction of actin-related protein complex 2/3 in fetal Down syndrome brain. Biochem. Biophys. Res. Commun. 2002, 293, 836-841.
    • (2002) Biochem. Biophys. Res. Commun , vol.293 , pp. 836-841
    • Weitzdoerfer, R.1    Fountoulakis, M.2    Lubec, G.3
  • 23
    • 20844436280 scopus 로고    scopus 로고
    • Proteome analysis of primary neurons and astrocytes from rat cerebellum
    • Yang, J. W.; Rodrigo, R.; Felipo, V.; Lubec, G. Proteome analysis of primary neurons and astrocytes from rat cerebellum. J. Proteome Res. 2005, 4, 768-788.
    • (2005) J. Proteome Res , vol.4 , pp. 768-788
    • Yang, J.W.1    Rodrigo, R.2    Felipo, V.3    Lubec, G.4
  • 25
    • 0029894369 scopus 로고    scopus 로고
    • Human brain GABA transaminase is immunologically distinct from those of other mammalian brains
    • Choi, E. Y.; Jang, S. H.; Choi, S. Y. Human brain GABA transaminase is immunologically distinct from those of other mammalian brains. Neurochem. Int. 1996, 28, 597-600.
    • (1996) Neurochem. Int , vol.28 , pp. 597-600
    • Choi, E.Y.1    Jang, S.H.2    Choi, S.Y.3
  • 27
    • 33747197197 scopus 로고    scopus 로고
    • Predicting eukaryotic protein subcellular location by fusing optimized evidence-theoretic K-nearest neighbor classifiers
    • Chou, K. C.; Shen, H. B. Predicting eukaryotic protein subcellular location by fusing optimized evidence-theoretic K-nearest neighbor classifiers. J. Proteome Res. 2006, 5, 1888-1897.
    • (2006) J. Proteome Res , vol.5 , pp. 1888-1897
    • Chou, K.C.1    Shen, H.B.2
  • 28
    • 0031573401 scopus 로고    scopus 로고
    • A stable nonfluorescent derivative of resorufin for the fluorometric determination of trace hydrogen peroxide: Applications in detecting the activity of phagocyte NADPH oxidase and other oxidases
    • Zhou, M.; Diwu, Z.; Panchuk-Voloshina, N.; Haugland, R. P. A stable nonfluorescent derivative of resorufin for the fluorometric determination of trace hydrogen peroxide: applications in detecting the activity of phagocyte NADPH oxidase and other oxidases. Anal. Biochem. 1997, 253, 162-168.
    • (1997) Anal. Biochem , vol.253 , pp. 162-168
    • Zhou, M.1    Diwu, Z.2    Panchuk-Voloshina, N.3    Haugland, R.P.4
  • 29
    • 3342901640 scopus 로고    scopus 로고
    • A new automated method for the determination of the Total Antioxidant Capacity (TAC) of human plasma, based on the crocin bleaching assay
    • Kampa, M.; Nistikaki, A.; Tsaousis, V.; Maliaraki, N.; Notas, G.; Castanas, E. A new automated method for the determination of the Total Antioxidant Capacity (TAC) of human plasma, based on the crocin bleaching assay. BMC Clin. Pathol. 2002, 2, 3.
    • (2002) BMC Clin. Pathol , vol.2 , pp. 3
    • Kampa, M.1    Nistikaki, A.2    Tsaousis, V.3    Maliaraki, N.4    Notas, G.5    Castanas, E.6
  • 30
    • 0030586361 scopus 로고    scopus 로고
    • The ferric reducing ability of plasma (FRAP) as a measure of "antioxidant power": The FRAP assay
    • Benzie, I. F.; Strain, J. J. The ferric reducing ability of plasma (FRAP) as a measure of "antioxidant power": the FRAP assay. Anal. Biochem. 1996, 239, 70-76.
    • (1996) Anal. Biochem , vol.239 , pp. 70-76
    • Benzie, I.F.1    Strain, J.J.2
  • 31
    • 0020529907 scopus 로고
    • Radioenzymatic assay for direct measurement of plasma pyridoxal 5′-phosphate
    • Camp, V. M.; Chipponi, J.; Faraj, B. A. Radioenzymatic assay for direct measurement of plasma pyridoxal 5′-phosphate. Clin. Chem. 1983, 29, 642-644.
    • (1983) Clin. Chem , vol.29 , pp. 642-644
    • Camp, V.M.1    Chipponi, J.2    Faraj, B.A.3
  • 32
    • 0028116826 scopus 로고
    • Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approach to database search
    • Koonin, E. V.; Tatusov, R. L. Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approach to database search. J. Mol. Biol. 1994, 244, 125-132.
    • (1994) J. Mol. Biol , vol.244 , pp. 125-132
    • Koonin, E.V.1    Tatusov, R.L.2
  • 33
    • 0034730072 scopus 로고    scopus 로고
    • The crystal structure of Bacillus cereus phosphonoacetaldehyde hydrolase: Insight into catalysis of phosphorus bond cleavage and catalytic diversification within the HAD enzyme superfamily
    • Morais, M. C.; Zhang, W.; Baker, A. S.; Zhang, G.; Dunaway-Mariano, D.; Allen, K. N. The crystal structure of Bacillus cereus phosphonoacetaldehyde hydrolase: insight into catalysis of phosphorus bond cleavage and catalytic diversification within the HAD enzyme superfamily. Biochemistry 2000, 39, 10385-10396.
    • (2000) Biochemistry , vol.39 , pp. 10385-10396
    • Morais, M.C.1    Zhang, W.2    Baker, A.S.3    Zhang, G.4    Dunaway-Mariano, D.5    Allen, K.N.6
  • 34
    • 4944254297 scopus 로고    scopus 로고
    • X-ray crystal structure of the hypothetical phosphotyrosine phosphatase MDP-1 of the haloacid dehalogenase superfamily
    • Peisach, E.; Selengut, J. D.; Dunaway-Mariano, D.; Allen, K. N. X-ray crystal structure of the hypothetical phosphotyrosine phosphatase MDP-1 of the haloacid dehalogenase superfamily. Biochemistry 2004, 43, 12770-12779.
    • (2004) Biochemistry , vol.43 , pp. 12770-12779
    • Peisach, E.1    Selengut, J.D.2    Dunaway-Mariano, D.3    Allen, K.N.4
  • 35
    • 1542267779 scopus 로고    scopus 로고
    • Analysis of the substrate specificity loop of the HAD superfamily cap domain
    • Lahiri, S. D.; Zhang, G.; Dai, J.; Dunaway-Mariano, D.; Allen, K. N. Analysis of the substrate specificity loop of the HAD superfamily cap domain. Biochemistry 2004, 43, 2812-2820.
    • (2004) Biochemistry , vol.43 , pp. 2812-2820
    • Lahiri, S.D.1    Zhang, G.2    Dai, J.3    Dunaway-Mariano, D.4    Allen, K.N.5
  • 36
    • 0032724654 scopus 로고    scopus 로고
    • Crystal structures of intermediates in the dehalogenation of haloalkanoates by L-2-haloacid dehalogenase
    • Ridder, I. S.; Rozeboom, H. J.; Kalk, K. H.; Dijkstra, B. W. Crystal structures of intermediates in the dehalogenation of haloalkanoates by L-2-haloacid dehalogenase. J. Biol. Chem. 1999, 274, 30672-30678.
    • (1999) J. Biol. Chem , vol.274 , pp. 30672-30678
    • Ridder, I.S.1    Rozeboom, H.J.2    Kalk, K.H.3    Dijkstra, B.W.4
  • 37
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • Schwede, T.; Kopp, J.; Guex, N.; Peitsch, M. C. SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res. 2003, 31, 3381-3385.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 39
    • 0022457811 scopus 로고
    • The role of thioredoxin reductase in the reduction of free radicals at the surface of the epidermis
    • Schallreuter, K. U.; Wood, J. M. The role of thioredoxin reductase in the reduction of free radicals at the surface of the epidermis. Biochem. Biophys. Res. Commun. 1986, 136, 630-637.
    • (1986) Biochem. Biophys. Res. Commun , vol.136 , pp. 630-637
    • Schallreuter, K.U.1    Wood, J.M.2
  • 40
    • 0028106431 scopus 로고
    • Adult T cell leukemia-derived factor/human thioredoxin protects endothelial F-2 cell injury caused by activated neutrophils or hydrogen peroxide
    • Nakamura, H.; Matsuda, M.; Furuke, K.; Kitaoka, Y.; Iwata, S.; Toda, K.; Inamoto, T.; Yamaoka, Y.; Ozawa, K.; Yodoi, J. Adult T cell leukemia-derived factor/human thioredoxin protects endothelial F-2 cell injury caused by activated neutrophils or hydrogen peroxide. Immunol. Lett. 1994, 42, 75-80.
    • (1994) Immunol. Lett , vol.42 , pp. 75-80
    • Nakamura, H.1    Matsuda, M.2    Furuke, K.3    Kitaoka, Y.4    Iwata, S.5    Toda, K.6    Inamoto, T.7    Yamaoka, Y.8    Ozawa, K.9    Yodoi, J.10
  • 41
    • 0024461420 scopus 로고
    • ATL-derived factor (ADF), an IL-2 receptor/Tac inducer homologous to thioredoxin; possible involvement of dithiol-reduction in the IL-2 receptor induction
    • Tagaya, Y.; Maeda, Y.; Mitsui, A.; Kondo, N.; Matsui, H.; Hamuro, J.; Brown, N.; Arai, K.; Yokota, T.; Wakasugi, H.; et al. ATL-derived factor (ADF), an IL-2 receptor/Tac inducer homologous to thioredoxin; possible involvement of dithiol-reduction in the IL-2 receptor induction. EMBO J. 1989, 8, 757-764.
    • (1989) EMBO J , vol.8 , pp. 757-764
    • Tagaya, Y.1    Maeda, Y.2    Mitsui, A.3    Kondo, N.4    Matsui, H.5    Hamuro, J.6    Brown, N.7    Arai, K.8    Yokota, T.9    Wakasugi, H.10
  • 42
    • 0028298235 scopus 로고
    • Opposing regulatory effects of thioredoxin and eosinophil cytotoxicity-enhancing factor on the development of human immunodeficiency virus 1
    • Newman, G. W.; Balcewicz-Sablinska, M. K.; Guarnaccia, J. R.; Remold, H. G.; Silberstein, D. S. Opposing regulatory effects of thioredoxin and eosinophil cytotoxicity-enhancing factor on the development of human immunodeficiency virus 1. J. Exp. Med. 1994, 180, 359-363.
    • (1994) J. Exp. Med , vol.180 , pp. 359-363
    • Newman, G.W.1    Balcewicz-Sablinska, M.K.2    Guarnaccia, J.R.3    Remold, H.G.4    Silberstein, D.S.5
  • 43
    • 0027270735 scopus 로고
    • Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase
    • Weissman, J. S.; Kim, P. S. Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase. Nature 1993, 365, 185-188.
    • (1993) Nature , vol.365 , pp. 185-188
    • Weissman, J.S.1    Kim, P.S.2
  • 44
    • 15244344816 scopus 로고    scopus 로고
    • Solution structure of At3g04780.1-des15, an Arabidopsis thaliana ortholog of the C-terminal domain of human thioredoxin-like protein
    • Song, J.; Tyler, R. C.; Wrobel, R. L.; Frederick, R. O.; Vojtek, F. C.; Jeon, W. B.; Lee, M. S.; Markley, J. L. Solution structure of At3g04780.1-des15, an Arabidopsis thaliana ortholog of the C-terminal domain of human thioredoxin-like protein. Protein Sci. 2005, 14, 1059-1063.
    • (2005) Protein Sci , vol.14 , pp. 1059-1063
    • Song, J.1    Tyler, R.C.2    Wrobel, R.L.3    Frederick, R.O.4    Vojtek, F.C.5    Jeon, W.B.6    Lee, M.S.7    Markley, J.L.8
  • 45
    • 0030902648 scopus 로고    scopus 로고
    • Factors influencing the antioxidant activity determined by the ABTS.+ radical cation assay
    • Miller, N. J.; Rice-Evans, C. A. Factors influencing the antioxidant activity determined by the ABTS.+ radical cation assay. Free Radical Res. 1997, 26, 195-199.
    • (1997) Free Radical Res , vol.26 , pp. 195-199
    • Miller, N.J.1    Rice-Evans, C.A.2
  • 46
    • 0346118933 scopus 로고    scopus 로고
    • Human pyridoxal phosphatase. Molecular cloning, functional expression, and tissue distribution
    • Jang, Y. M.; Kim, D. W.; Kang, T. C.; Won, M. H.; Baek, N. I.; Moon, B. J.; Choi, S. Y.; Kwon, O. S. Human pyridoxal phosphatase. Molecular cloning, functional expression, and tissue distribution. J. Biol Chem. 2003, 278, 50040-50046.
    • (2003) J. Biol Chem , vol.278 , pp. 50040-50046
    • Jang, Y.M.1    Kim, D.W.2    Kang, T.C.3    Won, M.H.4    Baek, N.I.5    Moon, B.J.6    Choi, S.Y.7    Kwon, O.S.8
  • 47
  • 48
    • 3242792729 scopus 로고    scopus 로고
    • Structural bioinformatics and its impact to biomedical science
    • Chou, K. C. Structural bioinformatics and its impact to biomedical science. Curr. Med. Chem. 2004, 11, 2105-2134.
    • (2004) Curr. Med. Chem , vol.11 , pp. 2105-2134
    • Chou, K.C.1
  • 49
    • 0019332167 scopus 로고
    • How different amino acid sequences determine similar protein structures: The structure and evolutionary dynamics of the globins
    • Lesk, A. M.; Chothia, C. How different amino acid sequences determine similar protein structures: the structure and evolutionary dynamics of the globins. J. Mol. Biol. 1980, 136, 225-270.
    • (1980) J. Mol. Biol , vol.136 , pp. 225-270
    • Lesk, A.M.1    Chothia, C.2
  • 50
    • 0022797368 scopus 로고
    • Alignment of the amino acid sequences of distantly related proteins using variable gap penalties
    • Lesk, A. M.; Levitt, M.; Chothia, C. Alignment of the amino acid sequences of distantly related proteins using variable gap penalties. Protein Eng. 1986, 1, 77-78.
    • (1986) Protein Eng , vol.1 , pp. 77-78
    • Lesk, A.M.1    Levitt, M.2    Chothia, C.3
  • 51
    • 0036968784 scopus 로고    scopus 로고
    • Sequence conservation in families whose members have little or no sequence similarity: The four-helical cytokines and cytochromes
    • Hill, E. E.; Morea, V.; Chothia, C. Sequence conservation in families whose members have little or no sequence similarity: the four-helical cytokines and cytochromes. J. Mol. Biol. 2002, 322, 205-233.
    • (2002) J. Mol. Biol , vol.322 , pp. 205-233
    • Hill, E.E.1    Morea, V.2    Chothia, C.3
  • 52
    • 0036142325 scopus 로고    scopus 로고
    • A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p
    • Gross, E.; Sevier, C. S.; Vala, A.; Kaiser, C. A.; Fass, D. A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p. Nat. Struct. Biol. 2002, 9, 61-67.
    • (2002) Nat. Struct. Biol , vol.9 , pp. 61-67
    • Gross, E.1    Sevier, C.S.2    Vala, A.3    Kaiser, C.A.4    Fass, D.5
  • 53
    • 33747880465 scopus 로고    scopus 로고
    • Ensemble classifier for protein fold pattern recognition
    • Shen, H. B.; Chou, K. C. Ensemble classifier for protein fold pattern recognition. Bioinformatics 2006, 22, 1717-1722.
    • (2006) Bioinformatics , vol.22 , pp. 1717-1722
    • Shen, H.B.1    Chou, K.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.