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Volumn 56, Issue 3, 2012, Pages 519-530

MS based proteomic approaches for analysis of barley malt

Author keywords

Barley; Malt; Mass spectrometry; Protein content

Indexed keywords

HORDEUM;

EID: 84868208031     PISSN: 07335210     EISSN: 10959963     Source Type: Journal    
DOI: 10.1016/j.jcs.2012.07.013     Document Type: Review
Times cited : (9)

References (130)
  • 1
    • 0031570324 scopus 로고    scopus 로고
    • Characterization of the structural difference between active and inactive forms of the Ras protein by chemical modification followed by mass spectrometric peptide mapping
    • Akashi S., Shirouzu M., Terada T., Ito Y., Yokoyama S., Takio K. Characterization of the structural difference between active and inactive forms of the Ras protein by chemical modification followed by mass spectrometric peptide mapping. Analytical Biochemistry 1997, 248:15-25.
    • (1997) Analytical Biochemistry , vol.248 , pp. 15-25
    • Akashi, S.1    Shirouzu, M.2    Terada, T.3    Ito, Y.4    Yokoyama, S.5    Takio, K.6
  • 3
    • 1542615443 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis pattern (pH 6-11) and identification of water-soluble barley seed and malt proteins by mass spectrometry
    • Bak-Jensen K.S., Laugesen S., Roepstorff P., Svensson B. Two-dimensional gel electrophoresis pattern (pH 6-11) and identification of water-soluble barley seed and malt proteins by mass spectrometry. Proteomics 2004, 4:728-742.
    • (2004) Proteomics , vol.4 , pp. 728-742
    • Bak-Jensen, K.S.1    Laugesen, S.2    Roepstorff, P.3    Svensson, B.4
  • 6
    • 84868212382 scopus 로고    scopus 로고
    • Influence of the brewing process on the barley protein profile
    • Benkovská D., Flodrová D., Psota V., Bobálová J. Influence of the brewing process on the barley protein profile. Kvasny Prumysl 2011, 57:260-265.
    • (2011) Kvasny Prumysl , vol.57 , pp. 260-265
    • Benkovská, D.1    Flodrová, D.2    Psota, V.3    Bobálová, J.4
  • 7
    • 84868207059 scopus 로고    scopus 로고
    • Freeman, W.H. and Company, New York, (Chapter 2) and 3
    • Berg J.M., Tymoczko J.L., Stryer L. Biochemistry 2007, Freeman, W.H. and Company, New York, (Chapter 2) and 3, pp. 25 - 98. sixth ed.
    • (2007) Biochemistry , pp. 25-98
    • Berg, J.M.1    Tymoczko, J.L.2    Stryer, L.3
  • 8
    • 34547849614 scopus 로고    scopus 로고
    • Proteomic identification of technologically modified proteins in malt by combination of protein fractionation using convective interaction media and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • Bobalova J., Chmelik J. Proteomic identification of technologically modified proteins in malt by combination of protein fractionation using convective interaction media and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Journal of Chromatography A 2007, 1163:80-85.
    • (2007) Journal of Chromatography A , vol.1163 , pp. 80-85
    • Bobalova, J.1    Chmelik, J.2
  • 9
    • 43249107424 scopus 로고    scopus 로고
    • Investigation of protein composition of barley by gel electrophoresis and MALDI mass spectrometry with regard to the malting and brewing process
    • Bobalova J., Salplachta J., Chmelik J. Investigation of protein composition of barley by gel electrophoresis and MALDI mass spectrometry with regard to the malting and brewing process. Journal of the Institute of Brewing 2008, 114:22-26.
    • (2008) Journal of the Institute of Brewing , vol.114 , pp. 22-26
    • Bobalova, J.1    Salplachta, J.2    Chmelik, J.3
  • 11
  • 14
    • 33746914723 scopus 로고    scopus 로고
    • The effects of malting and mashing on barley protein extractability
    • Celus I., Brijs K., Delcour J.A. The effects of malting and mashing on barley protein extractability. Journal of Cereal Science 2006, 44:203-211.
    • (2006) Journal of Cereal Science , vol.44 , pp. 203-211
    • Celus, I.1    Brijs, K.2    Delcour, J.A.3
  • 15
    • 33750588336 scopus 로고    scopus 로고
    • Advances in plant proteomics
    • Chen S., Harmon A.C. Advances in plant proteomics. Proteomics 2006, 6:5504-5516.
    • (2006) Proteomics , vol.6 , pp. 5504-5516
    • Chen, S.1    Harmon, A.C.2
  • 17
    • 34848927237 scopus 로고    scopus 로고
    • Novel staining-free proteomic method for simultaneous identification of proteins and determination of their pI values by using low-molecular-mass pI markers
    • Chmelík J., Mazanec K., Šlais K. Novel staining-free proteomic method for simultaneous identification of proteins and determination of their pI values by using low-molecular-mass pI markers. Electrophoresis 2007, 28:3315-3323.
    • (2007) Electrophoresis , vol.28 , pp. 3315-3323
    • Chmelík, J.1    Mazanec, K.2    Šlais, K.3
  • 20
  • 23
    • 0031840467 scopus 로고    scopus 로고
    • Heat-shock proteins in monitoring aging and heat-induced tolerance in germinating wheat and barley embryos
    • Dell'Aquila A., Corona M.G., Di Turi M. Heat-shock proteins in monitoring aging and heat-induced tolerance in germinating wheat and barley embryos. Seed Science Research 1998, 8:91-98.
    • (1998) Seed Science Research , vol.8 , pp. 91-98
    • Dell'Aquila, A.1    Corona, M.G.2    Di Turi, M.3
  • 24
    • 0026672913 scopus 로고
    • Differences in the thermostabilities of barley (1-3,1-4)- beta-glucanases are only partly determined by N-glycosylation
    • Doan D.N.P., Fincher G.B. Differences in the thermostabilities of barley (1-3,1-4)- beta-glucanases are only partly determined by N-glycosylation. FEBS Letters 1992, 309:265-271.
    • (1992) FEBS Letters , vol.309 , pp. 265-271
    • Doan, D.N.P.1    Fincher, G.B.2
  • 25
    • 0029109382 scopus 로고
    • Tissue-specific expression of germin-like oxalate oxidase during development and fungal infection of barley seedlings
    • Dumas B., Freyssinet G., Pallett K.E. Tissue-specific expression of germin-like oxalate oxidase during development and fungal infection of barley seedlings. Plant Physiology 1995, 107:1091-1096.
    • (1995) Plant Physiology , vol.107 , pp. 1091-1096
    • Dumas, B.1    Freyssinet, G.2    Pallett, K.E.3
  • 26
    • 0035609335 scopus 로고    scopus 로고
    • Hordein polypeptide patterns in relation to malting quality in Brazilian barley varieties
    • Echart-Almeida C., Cavalli-Molina S. Hordein polypeptide patterns in relation to malting quality in Brazilian barley varieties. Pesquisa Agropecuaria Brasileira 2001, 36:211-217.
    • (2001) Pesquisa Agropecuaria Brasileira , vol.36 , pp. 211-217
    • Echart-Almeida, C.1    Cavalli-Molina, S.2
  • 28
    • 0002722711 scopus 로고
    • Mobilization of endospermal reserves during the germination of barley
    • Enari T.M., Sopanen T. Mobilization of endospermal reserves during the germination of barley. Journal of the Institute of Brewing 1986, 92:25-31.
    • (1986) Journal of the Institute of Brewing , vol.92 , pp. 25-31
    • Enari, T.M.1    Sopanen, T.2
  • 29
    • 0000261095 scopus 로고    scopus 로고
    • Measurement of beta-amylase in malting barley (Hordeum vulgare L.). II. The effect of germination and kilning
    • Evans D.E., Wallace W., Lance R.C.M., MacLeod L.C. Measurement of beta-amylase in malting barley (Hordeum vulgare L.). II. The effect of germination and kilning. Journal of Cereal Science 1997, 26:241-250.
    • (1997) Journal of Cereal Science , vol.26 , pp. 241-250
    • Evans, D.E.1    Wallace, W.2    Lance, R.C.M.3    MacLeod, L.C.4
  • 30
    • 0038116819 scopus 로고    scopus 로고
    • Proteomics in 2002: a year of technical development and wide-ranging applications
    • Figeys D. Proteomics in 2002: a year of technical development and wide-ranging applications. Analytical Chemistry 2003, 75:2891-2905.
    • (2003) Analytical Chemistry , vol.75 , pp. 2891-2905
    • Figeys, D.1
  • 31
    • 84868207431 scopus 로고    scopus 로고
    • Biochemistry, physiology and genetics of endosperm mobilization in germinated barley grain
    • Wiley-Blackwell Publishing Ltd., Published online, S.E. Ullrich (Ed.)
    • Finger G.B. Biochemistry, physiology and genetics of endosperm mobilization in germinated barley grain. Barley: Production, Improvement, and Uses 2011, 463-467. Wiley-Blackwell Publishing Ltd., Published online. S.E. Ullrich (Ed.).
    • (2011) Barley: Production, Improvement, and Uses , pp. 463-467
    • Finger, G.B.1
  • 32
    • 0037953141 scopus 로고    scopus 로고
    • Feasibility study of a tissue-specific approach to barley proteome analysis: aleurone layer, endosperm, embryo and single seeds
    • Finnie C., Svensson B. Feasibility study of a tissue-specific approach to barley proteome analysis: aleurone layer, endosperm, embryo and single seeds. Journal of Cereal Science 2003, 38:217-227.
    • (2003) Journal of Cereal Science , vol.38 , pp. 217-227
    • Finnie, C.1    Svensson, B.2
  • 34
    • 32644485468 scopus 로고    scopus 로고
    • Differential appearance of isoforms and cultivar variation in protein temporal profiles revealed in the maturing barley grain proteome
    • Finnie C., Bak-Jensen K.S., Laugesen S., Roepstorff P., Svensson B. Differential appearance of isoforms and cultivar variation in protein temporal profiles revealed in the maturing barley grain proteome. Plant Science 2006, 170:808-821.
    • (2006) Plant Science , vol.170 , pp. 808-821
    • Finnie, C.1    Bak-Jensen, K.S.2    Laugesen, S.3    Roepstorff, P.4    Svensson, B.5
  • 35
    • 0024969741 scopus 로고
    • A method for two-dimensional electrophoresis of proteins from green plant tissues
    • Flengsrud R., Kobro G. A method for two-dimensional electrophoresis of proteins from green plant tissues. Analytical Biochemistry 1989, 177:33-36.
    • (1989) Analytical Biochemistry , vol.177 , pp. 33-36
    • Flengsrud, R.1    Kobro, G.2
  • 36
    • 77958615681 scopus 로고    scopus 로고
    • Development of multidimensional liquid chromatography and application in proteomic analysis
    • Gao M., Qi D., Zhang P., Deng C., Zhang X. Development of multidimensional liquid chromatography and application in proteomic analysis. Expert Review of Proteomics 2010, 7:665-678.
    • (2010) Expert Review of Proteomics , vol.7 , pp. 665-678
    • Gao, M.1    Qi, D.2    Zhang, P.3    Deng, C.4    Zhang, X.5
  • 39
    • 0024119482 scopus 로고
    • Two-dimensional electrophoresis with immobilized pH gradients of leaf proteins from barley (Hordeum vulgare): method, reproducibility and genetic aspects
    • Görg A., Postel W., Domscheit A., Günther S. Two-dimensional electrophoresis with immobilized pH gradients of leaf proteins from barley (Hordeum vulgare): method, reproducibility and genetic aspects. Electrophoresis 1988, 9:681-692.
    • (1988) Electrophoresis , vol.9 , pp. 681-692
    • Görg, A.1    Postel, W.2    Domscheit, A.3    Günther, S.4
  • 40
    • 0026519178 scopus 로고
    • Two-dimensional polyacrylamide gel electrophoresis, with immobilized pH gradients in the first dimension, of barley seed proteins: discrimination of cultivars with different malting grades
    • Görg A., Postel W., Baumer M., Weiss W. Two-dimensional polyacrylamide gel electrophoresis, with immobilized pH gradients in the first dimension, of barley seed proteins: discrimination of cultivars with different malting grades. Electrophoresis 1992, 13:192-203.
    • (1992) Electrophoresis , vol.13 , pp. 192-203
    • Görg, A.1    Postel, W.2    Baumer, M.3    Weiss, W.4
  • 41
    • 0026497929 scopus 로고
    • Detection of polypeptides and amylase isoenzyme modifications related to malting quality during malting process of barley by two- dimensional electrophoresis and isoelectric focusing with immobilized pH gradients
    • Görg A., Postel W., Weiss W. Detection of polypeptides and amylase isoenzyme modifications related to malting quality during malting process of barley by two- dimensional electrophoresis and isoelectric focusing with immobilized pH gradients. Electrophoresis 1992, 13:759-770.
    • (1992) Electrophoresis , vol.13 , pp. 759-770
    • Görg, A.1    Postel, W.2    Weiss, W.3
  • 42
    • 38949103034 scopus 로고    scopus 로고
    • Barley grain non-specific lipid-transfer proteins (ns-LTPs) in beer production and quality
    • Gorjanović S. Barley grain non-specific lipid-transfer proteins (ns-LTPs) in beer production and quality. Journal of the Institute of Brewing 2007, 113:310-324.
    • (2007) Journal of the Institute of Brewing , vol.113 , pp. 310-324
    • Gorjanović, S.1
  • 43
    • 76349093176 scopus 로고    scopus 로고
    • A review: biological and technological functions of barley seed pathogenesis-related proteins (PRs)
    • Gorjanović S. A review: biological and technological functions of barley seed pathogenesis-related proteins (PRs). Journal of the Institute of Brewing 2009, 115:334-360.
    • (2009) Journal of the Institute of Brewing , vol.115 , pp. 334-360
    • Gorjanović, S.1
  • 44
    • 77956287355 scopus 로고    scopus 로고
    • A review: the role of barley seed pathogenesis-related proteins (PRs) in beer production
    • Gorjanović S. A review: the role of barley seed pathogenesis-related proteins (PRs) in beer production. Journal of the Institute of Brewing 2010, 116:111-124.
    • (2010) Journal of the Institute of Brewing , vol.116 , pp. 111-124
    • Gorjanović, S.1
  • 48
    • 26444456180 scopus 로고    scopus 로고
    • Application of mass spectrometry in proteomics
    • Guerrera I.C., Kleiner O. Application of mass spectrometry in proteomics. Bioscience Reports 2005, 25:71-93.
    • (2005) Bioscience Reports , vol.25 , pp. 71-93
    • Guerrera, I.C.1    Kleiner, O.2
  • 49
    • 34250169808 scopus 로고    scopus 로고
    • Genomics and proteomics in process development: opportunities and challenges
    • Gupta P., Lee K.H. Genomics and proteomics in process development: opportunities and challenges. Trends in Biotechnology 2007, 25:324-330.
    • (2007) Trends in Biotechnology , vol.25 , pp. 324-330
    • Gupta, P.1    Lee, K.H.2
  • 50
  • 51
    • 33746636784 scopus 로고    scopus 로고
    • Identification of the major proteins in beer foam by mass spectrometry following sodium dodecyl sulfate- polyacrylamide gel electrophoresis
    • Hao J., Li Q., Dong J.J., Yu J.J., Gu G.X., Fan W., Chen J. Identification of the major proteins in beer foam by mass spectrometry following sodium dodecyl sulfate- polyacrylamide gel electrophoresis. Journal of the American Society of Brewing Chemists 2006, 64:166-174.
    • (2006) Journal of the American Society of Brewing Chemists , vol.64 , pp. 166-174
    • Hao, J.1    Li, Q.2    Dong, J.J.3    Yu, J.J.4    Gu, G.X.5    Fan, W.6    Chen, J.7
  • 52
    • 0029106550 scopus 로고
    • Analysis of glycan structures of barley (1-3,1-4)-beta-d- glucan 4-glucanohydrolase isoenzyme EII
    • Harthill J.E., Thomsen K.K. Analysis of glycan structures of barley (1-3,1-4)-beta-d- glucan 4-glucanohydrolase isoenzyme EII. Plant Physiology and Biochemistry 1995, 33:9-18.
    • (1995) Plant Physiology and Biochemistry , vol.33 , pp. 9-18
    • Harthill, J.E.1    Thomsen, K.K.2
  • 53
    • 0033218504 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization mass spectrometry of carbohydrates
    • Harvey D.J. Matrix-assisted laser desorption/ionization mass spectrometry of carbohydrates. Mass Spectrometry Reviews 1999, 18:349-450.
    • (1999) Mass Spectrometry Reviews , vol.18 , pp. 349-450
    • Harvey, D.J.1
  • 54
    • 34447098784 scopus 로고    scopus 로고
    • Patterns of beauty-omics meets plant development
    • Hennig L. Patterns of beauty-omics meets plant development. Trends in Plant Science 2007, 12:287-293.
    • (2007) Trends in Plant Science , vol.12 , pp. 287-293
    • Hennig, L.1
  • 55
    • 84855523412 scopus 로고    scopus 로고
    • Plant cell organelle proteomics in response to abiotic stress
    • Hossain Z., Nouri M.Z., Komatsu S. Plant cell organelle proteomics in response to abiotic stress. Journal of Proteome Research 2012, 11:37-48.
    • (2012) Journal of Proteome Research , vol.11 , pp. 37-48
    • Hossain, Z.1    Nouri, M.Z.2    Komatsu, S.3
  • 56
    • 34548129610 scopus 로고    scopus 로고
    • Advances in hyphenated analytical techniques for shotgun proteome and peptidome analysis-A review
    • Hu L., Ye M., Jiang X., Feng S., Zou H. Advances in hyphenated analytical techniques for shotgun proteome and peptidome analysis-A review. Analytica Chimica Acta 2007, 598:193-204.
    • (2007) Analytica Chimica Acta , vol.598 , pp. 193-204
    • Hu, L.1    Ye, M.2    Jiang, X.3    Feng, S.4    Zou, H.5
  • 57
    • 77952789560 scopus 로고    scopus 로고
    • Studies on the influence of germination conditions on protein breakdown in buckwheat and oats
    • Hübner F., Arendt E.K. Studies on the influence of germination conditions on protein breakdown in buckwheat and oats. Journal of the Institute of Brewing 2010, 116:3-13.
    • (2010) Journal of the Institute of Brewing , vol.116 , pp. 3-13
    • Hübner, F.1    Arendt, E.K.2
  • 58
    • 33750973618 scopus 로고    scopus 로고
    • Enrichment and identification of integral membrane proteins from barley aleurone layers by reversed- phase chromatography, SDS-PAGE, and LC-MS/MS
    • Hynek R., Svensson B., Jensen O.N., Barkholt V., Finnie C. Enrichment and identification of integral membrane proteins from barley aleurone layers by reversed- phase chromatography, SDS-PAGE, and LC-MS/MS. Journal of Proteome Research 2006, 5:3105-3113.
    • (2006) Journal of Proteome Research , vol.5 , pp. 3105-3113
    • Hynek, R.1    Svensson, B.2    Jensen, O.N.3    Barkholt, V.4    Finnie, C.5
  • 63
    • 0011166861 scopus 로고    scopus 로고
    • Mass spectrometry and the proteome
    • Springer-Verlag, Berlin Heidelberg, New York, P. James (Ed.)
    • James P. Mass spectrometry and the proteome. Proteome Research: Mass Spectrometry 2001, 1-8. Springer-Verlag, Berlin Heidelberg, New York. P. James (Ed.).
    • (2001) Proteome Research: Mass Spectrometry , pp. 1-8
    • James, P.1
  • 66
  • 67
    • 0025784036 scopus 로고
    • Regulation of synthesis and transport of secreted proteins in cereal aleurone
    • Jones R.L., Jacobsen J.V. Regulation of synthesis and transport of secreted proteins in cereal aleurone. International Review of Cytology 1991, 126:49-88.
    • (1991) International Review of Cytology , vol.126 , pp. 49-88
    • Jones, R.L.1    Jacobsen, J.V.2
  • 69
    • 77952065511 scopus 로고    scopus 로고
    • Proteome and flavonoid analysis reveals distinct responses of epidermal tissue and whole leaves upon UV-B radiation of barley (Hordeum vulgare L.) seedlings
    • Kaspar S., Matros A., Mock H.P. Proteome and flavonoid analysis reveals distinct responses of epidermal tissue and whole leaves upon UV-B radiation of barley (Hordeum vulgare L.) seedlings. Journal of Proteomic Research 2010, 9:2402-2411.
    • (2010) Journal of Proteomic Research , vol.9 , pp. 2402-2411
    • Kaspar, S.1    Matros, A.2    Mock, H.P.3
  • 71
    • 84855521319 scopus 로고    scopus 로고
    • Proteomics techniques for the development of flood tolerant crops
    • Komatsu S., Hiraga S., Yanagawa Y. Proteomics techniques for the development of flood tolerant crops. Journal of Proteome Research 2012, 11:68-78.
    • (2012) Journal of Proteome Research , vol.11 , pp. 68-78
    • Komatsu, S.1    Hiraga, S.2    Yanagawa, Y.3
  • 72
    • 79960971804 scopus 로고    scopus 로고
    • Plant proteome changes under abiotic stress-Contribution of proteomics studies to understanding plant stress response
    • Kosová K., Vítámvás P., Prášil I.T., Renaut J. Plant proteome changes under abiotic stress-Contribution of proteomics studies to understanding plant stress response. Journal of Proteomics 2011, 74:1301-1322.
    • (2011) Journal of Proteomics , vol.74 , pp. 1301-1322
    • Kosová, K.1    Vítámvás, P.2    Prášil, I.T.3    Renaut, J.4
  • 73
    • 84868203657 scopus 로고    scopus 로고
    • Barley, malt, and malting
    • The Master Brewers Association of the Americas, St. Paul, Minnesota
    • Kramer P. Barley, malt, and malting. Raw Materials and Brewhouse Operations 2006, vol. 1:15-54. The Master Brewers Association of the Americas, St. Paul, Minnesota.
    • (2006) Raw Materials and Brewhouse Operations , vol.1 , pp. 15-54
    • Kramer, P.1
  • 74
    • 35748942555 scopus 로고    scopus 로고
    • Barley peroxidase isozymes-expression and post-translational modification in mature seeds as identified by two-dimensional gel electrophoresis and mass spectrometry
    • Laugesen S., Bak-Jensen K.S., Hägglund P., Henriksen A., Finnie C., Svensson B., Roepstorff P. Barley peroxidase isozymes-expression and post-translational modification in mature seeds as identified by two-dimensional gel electrophoresis and mass spectrometry. International Journal of Mass Spectrometry 2007, 268:244-253.
    • (2007) International Journal of Mass Spectrometry , vol.268 , pp. 244-253
    • Laugesen, S.1    Bak-Jensen, K.S.2    Hägglund, P.3    Henriksen, A.4    Finnie, C.5    Svensson, B.6    Roepstorff, P.7
  • 75
    • 79751519808 scopus 로고    scopus 로고
    • Utilization of the linear mode of MALDI-TOF mass spectrometry in the study of glycation during the malting process
    • Laštovičková M., Mazanec K., Benkovská D., Bobálová J. Utilization of the linear mode of MALDI-TOF mass spectrometry in the study of glycation during the malting process. Journal of the Institute of Brewing 2010, 116:245-250.
    • (2010) Journal of the Institute of Brewing , vol.116 , pp. 245-250
    • Laštovičková, M.1    Mazanec, K.2    Benkovská, D.3    Bobálová, J.4
  • 76
    • 79958282304 scopus 로고    scopus 로고
    • The combination of lectin affinity chromatography, gel electrophoresis and mass spectrometry in the study of plant glycoproteome: preliminary insights
    • Laštovičková M., Smětalová D., Bobalova J. The combination of lectin affinity chromatography, gel electrophoresis and mass spectrometry in the study of plant glycoproteome: preliminary insights. Chromatographia 2011, 73:S113-S122.
    • (2011) Chromatographia , vol.73
    • Laštovičková, M.1    Smětalová, D.2    Bobalova, J.3
  • 77
    • 0038386063 scopus 로고    scopus 로고
    • Beer polypeptides and silica gel-Part I. Polypeptides involved in haze formation
    • Leiper K.A., Stewart G.G., McKeown I.P. Beer polypeptides and silica gel-Part I. Polypeptides involved in haze formation. Journal of the Institute of Brewing 2003, 109:57-72.
    • (2003) Journal of the Institute of Brewing , vol.109 , pp. 57-72
    • Leiper, K.A.1    Stewart, G.G.2    McKeown, I.P.3
  • 78
    • 0038047702 scopus 로고    scopus 로고
    • Beer polypeptides and silica gel-Part II. Polypeptides involved in foam formation
    • Leiper K.A., Stewart G.G., McKeown I.P. Beer polypeptides and silica gel-Part II. Polypeptides involved in foam formation. Journal of the Institute of Brewing 2003, 109:73-79.
    • (2003) Journal of the Institute of Brewing , vol.109 , pp. 73-79
    • Leiper, K.A.1    Stewart, G.G.2    McKeown, I.P.3
  • 79
    • 0036468595 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis: recent advances in sample preparation, detection and quantitation
    • Lilley K.S., Razzaq A., Dupree P. Two-dimensional gel electrophoresis: recent advances in sample preparation, detection and quantitation. Current Opinion in Chemical Biology 2002, 6:46-50.
    • (2002) Current Opinion in Chemical Biology , vol.6 , pp. 46-50
    • Lilley, K.S.1    Razzaq, A.2    Dupree, P.3
  • 80
    • 0036219327 scopus 로고    scopus 로고
    • Multidimensional separations for protein/peptide analysis in the post-genomic era
    • Liu H., Lin D., Yates J.R. Multidimensional separations for protein/peptide analysis in the post-genomic era. Biotechniques 2002, 32:898-911.
    • (2002) Biotechniques , vol.32 , pp. 898-911
    • Liu, H.1    Lin, D.2    Yates, J.R.3
  • 81
    • 66149118996 scopus 로고    scopus 로고
    • Divergent flow isoelectric focusing: fast and efficient method for protein sample preparation for mass spectrometry
    • Mazanec K., Bobalova J., Šlais K. Divergent flow isoelectric focusing: fast and efficient method for protein sample preparation for mass spectrometry. Analytical and Bioanalytical Chemistry 2009, 393:1769-1778.
    • (2009) Analytical and Bioanalytical Chemistry , vol.393 , pp. 1769-1778
    • Mazanec, K.1    Bobalova, J.2    Šlais, K.3
  • 82
    • 12344330739 scopus 로고    scopus 로고
    • Role of chromatographic techniques in proteomic analysis
    • Neverova I., Van Eyk J.E. Role of chromatographic techniques in proteomic analysis. Journal of Chromatography B 2005, 815:51-63.
    • (2005) Journal of Chromatography B , vol.815 , pp. 51-63
    • Neverova, I.1    Van Eyk, J.E.2
  • 83
    • 0004332561 scopus 로고
    • Barley: taxanomy, origin, distribution, production, genetics, and breeding
    • American Association of Cereal Chemists, St. Paul, MN, A.W. MacGregor, R.S. Bhatty (Eds.)
    • Nilan R.A., Ullrich S.E. Barley: taxanomy, origin, distribution, production, genetics, and breeding. Barley: Chemistry and Technology 1993, 1-30. American Association of Cereal Chemists, St. Paul, MN. A.W. MacGregor, R.S. Bhatty (Eds.).
    • (1993) Barley: Chemistry and Technology , pp. 1-30
    • Nilan, R.A.1    Ullrich, S.E.2
  • 84
    • 0034792093 scopus 로고    scopus 로고
    • The role of mass spectrometry in proteome studies
    • Nyman T.A. The role of mass spectrometry in proteome studies. Biomolecular Engineering 2001, 18:221-227.
    • (2001) Biomolecular Engineering , vol.18 , pp. 221-227
    • Nyman, T.A.1
  • 87
    • 3543141896 scopus 로고    scopus 로고
    • Proteome analysis of barley seeds: identification of major proteins from two-dimensional gels (pI 4-7)
    • Østergaard O., Finnie C., Laugesen S., Roepstorff P., Svensson B. Proteome analysis of barley seeds: identification of major proteins from two-dimensional gels (pI 4-7). Proteomics 2004, 4:2437-2447.
    • (2004) Proteomics , vol.4 , pp. 2437-2447
    • Østergaard, O.1    Finnie, C.2    Laugesen, S.3    Roepstorff, P.4    Svensson, B.5
  • 88
    • 23044462504 scopus 로고    scopus 로고
    • Probing heat-stable water-soluble proteins from barley to malt and beer
    • Perrocheau L., Rogniaux H., Boivin P., Marion D. Probing heat-stable water-soluble proteins from barley to malt and beer. Proteomics 2005, 5:2849-2858.
    • (2005) Proteomics , vol.5 , pp. 2849-2858
    • Perrocheau, L.1    Rogniaux, H.2    Boivin, P.3    Marion, D.4
  • 89
    • 33646508515 scopus 로고    scopus 로고
    • Stability of barley and malt lipid transfer protein 1 (LTP1) toward heating and reducing agents: relationships with the brewing process
    • Perrocheau L., Bakan B., Boivin P., Marion D. Stability of barley and malt lipid transfer protein 1 (LTP1) toward heating and reducing agents: relationships with the brewing process. Journal of Agricultural and Food Chemistry 2006, 54:3108-3113.
    • (2006) Journal of Agricultural and Food Chemistry , vol.54 , pp. 3108-3113
    • Perrocheau, L.1    Bakan, B.2    Boivin, P.3    Marion, D.4
  • 90
    • 0003780536 scopus 로고
    • Whole-crop utilization of barley, including potential new uses
    • American Association of Cereal Chemists, St. Paul, MN, A.W. MacGregor, R.S. Bhatty (Eds.)
    • Petersen P.B., Munck L. Whole-crop utilization of barley, including potential new uses. Barley: Chemistry and Technology 1993, 437-474. American Association of Cereal Chemists, St. Paul, MN. A.W. MacGregor, R.S. Bhatty (Eds.).
    • (1993) Barley: Chemistry and Technology , pp. 437-474
    • Petersen, P.B.1    Munck, L.2
  • 92
    • 0033214111 scopus 로고    scopus 로고
    • Barley (Hordeum vulgare) oxalate oxidase is a manganese-containing enzyme
    • Requena L., Bornemann S. Barley (Hordeum vulgare) oxalate oxidase is a manganese-containing enzyme. Biochemical Journal 1999, 343:185-190.
    • (1999) Biochemical Journal , vol.343 , pp. 185-190
    • Requena, L.1    Bornemann, S.2
  • 94
    • 11244296896 scopus 로고    scopus 로고
    • The influence of nonspecific cleavage sites on identification of low molecular mass proteins by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry with seamless post-source decay fragment ion analysis
    • Řehulka P., Chmelík P., Allmaier G. The influence of nonspecific cleavage sites on identification of low molecular mass proteins by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry with seamless post-source decay fragment ion analysis. Rapid Communication in Mass Spectrometry 2005, 19:79-82.
    • (2005) Rapid Communication in Mass Spectrometry , vol.19 , pp. 79-82
    • Řehulka, P.1    Chmelík, P.2    Allmaier, G.3
  • 96
    • 0036839991 scopus 로고    scopus 로고
    • Determination of molecular weights of c hordeins by matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS)
    • Savage A.W.J., Saletti R., Foti S., Shewry P.R., Tatham A.S. Determination of molecular weights of c hordeins by matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS). Cereal Chemistry 2002, 79:768-770.
    • (2002) Cereal Chemistry , vol.79 , pp. 768-770
    • Savage, A.W.J.1    Saletti, R.2    Foti, S.3    Shewry, P.R.4    Tatham, A.S.5
  • 97
    • 60349130052 scopus 로고    scopus 로고
    • A brief summary of the different types of mass spectrometers used in proteomics
    • Humana Press Inc., Totowa, J.D. Thompson, C. Schaeffer-Reiss, M. Ueffing (Eds.)
    • Schaeffer-Reiss C. A brief summary of the different types of mass spectrometers used in proteomics. Functional Proteomics: Methods and Protocols. Book Series: Methods in Molecular Biology 2008, 3-16. Humana Press Inc., Totowa. J.D. Thompson, C. Schaeffer-Reiss, M. Ueffing (Eds.).
    • (2008) Functional Proteomics: Methods and Protocols. Book Series: Methods in Molecular Biology , pp. 3-16
    • Schaeffer-Reiss, C.1
  • 99
    • 79952791695 scopus 로고    scopus 로고
    • Plant biotic stress and proteomics
    • Sergeant K., Renaut J. Plant biotic stress and proteomics. Current Proteomics 2010, 7:275-297.
    • (2010) Current Proteomics , vol.7 , pp. 275-297
    • Sergeant, K.1    Renaut, J.2
  • 100
    • 84868194080 scopus 로고    scopus 로고
    • De novo peptide sequencing by nanoelectrospray tandem mass spectrometry using triple quadrupole and quadrupole/time-of-flight instruments
    • Humana Press, Totowa, NJ, F.E. Chapman (Ed.)
    • Shevchenko A., Chernushevich I., Wilm M., Mann M. De novo peptide sequencing by nanoelectrospray tandem mass spectrometry using triple quadrupole and quadrupole/time-of-flight instruments. Methods in Molecular Biology: Protein and Peptide Analysis by Mass Spectrometry 1996, 1-16. Humana Press, Totowa, NJ. F.E. Chapman (Ed.).
    • (1996) Methods in Molecular Biology: Protein and Peptide Analysis by Mass Spectrometry , pp. 1-16
    • Shevchenko, A.1    Chernushevich, I.2    Wilm, M.3    Mann, M.4
  • 101
    • 0002427947 scopus 로고
    • Barley seed proteins
    • American Association of Cereal Chemists, St. Paul, MN, A.W. MacGregor, R.S. Bhatty (Eds.)
    • Shewry P.R. Barley seed proteins. Barley: Chemistry and Technology 1993, 131-197. American Association of Cereal Chemists, St. Paul, MN. A.W. MacGregor, R.S. Bhatty (Eds.).
    • (1993) Barley: Chemistry and Technology , pp. 131-197
    • Shewry, P.R.1
  • 102
    • 34548299548 scopus 로고    scopus 로고
    • Electrophoretic and HPLC methods for comparative study of the protein fractions of malts, worts and beers produced from Scarlett and Prestige barley (Hordeum vulgare L.) varieties
    • Silva F., Nogueira L.C., Gonçalves C., Ferreira A.A., Ferreira I.M.P.L.V.O., Teixeira N. Electrophoretic and HPLC methods for comparative study of the protein fractions of malts, worts and beers produced from Scarlett and Prestige barley (Hordeum vulgare L.) varieties. Food Chemistry 2008, 106:820-829.
    • (2008) Food Chemistry , vol.106 , pp. 820-829
    • Silva, F.1    Nogueira, L.C.2    Gonçalves, C.3    Ferreira, A.A.4    Ferreira, I.M.P.L.V.O.5    Teixeira, N.6
  • 104
    • 84867526641 scopus 로고    scopus 로고
    • Understanding protein interaction and their representation in the gas phase of the mass spectrometer
    • John Wiley and Sons, New York, J. Laskin, C. Lifshitz (Eds.)
    • Sobott F., Robinson C. Understanding protein interaction and their representation in the gas phase of the mass spectrometer. Principles of Mass Spectrometry Applied to Biomolecules 2006, 147-176. John Wiley and Sons, New York. J. Laskin, C. Lifshitz (Eds.).
    • (2006) Principles of Mass Spectrometry Applied to Biomolecules , pp. 147-176
    • Sobott, F.1    Robinson, C.2
  • 105
    • 0002908012 scopus 로고    scopus 로고
    • The basics of matrix-assisted laser desorption, ionisation time-of-flight mass spectrometry and post-source decay analysis
    • Springer-Verlag, Berlin Heidelberg, New York, P. James (Ed.)
    • Spengler B. The basics of matrix-assisted laser desorption, ionisation time-of-flight mass spectrometry and post-source decay analysis. Proteome Research: Mass Spectrometry 2001, 33-51. Springer-Verlag, Berlin Heidelberg, New York. P. James (Ed.).
    • (2001) Proteome Research: Mass Spectrometry , pp. 33-51
    • Spengler, B.1
  • 106
    • 59249085652 scopus 로고    scopus 로고
    • Single-input divergent flow IEF for preparative analysis of proteins
    • Stastna M., Slais K. Single-input divergent flow IEF for preparative analysis of proteins. Electrophoresis 2008, 29:4503-4507.
    • (2008) Electrophoresis , vol.29 , pp. 4503-4507
    • Stastna, M.1    Slais, K.2
  • 107
    • 78751641737 scopus 로고    scopus 로고
    • Protein changes during malting and brewing with focus on haze and foam formation: a review
    • Steiner E., Gastl M., Becker T. Protein changes during malting and brewing with focus on haze and foam formation: a review. European Food Research and Technology 2011, 232:191-204.
    • (2011) European Food Research and Technology , vol.232 , pp. 191-204
    • Steiner, E.1    Gastl, M.2    Becker, T.3
  • 108
  • 109
    • 0017838999 scopus 로고
    • Inheritance of tolerance to low soil pH in barley
    • Stølen O., Andersen S. Inheritance of tolerance to low soil pH in barley. Hereditas 1978, 88:101-105.
    • (1978) Hereditas , vol.88 , pp. 101-105
    • Stølen, O.1    Andersen, S.2
  • 110
    • 74349083387 scopus 로고    scopus 로고
    • Proteomic analysis of specific proteins in the root of salt- tolerant barley
    • Sugimoto M., Takeda K. Proteomic analysis of specific proteins in the root of salt- tolerant barley. Bioscience, Biotechnology and Biochemistry 2009, 73:2762-2765.
    • (2009) Bioscience, Biotechnology and Biochemistry , vol.73 , pp. 2762-2765
    • Sugimoto, M.1    Takeda, K.2
  • 111
  • 112
    • 46249123929 scopus 로고    scopus 로고
    • Divergent flow isoelectric focusing
    • Šlais K. Divergent flow isoelectric focusing. Electrophoresis 2008, 29:2451-2457.
    • (2008) Electrophoresis , vol.29 , pp. 2451-2457
    • Šlais, K.1
  • 113
  • 114
  • 115
    • 84857030978 scopus 로고    scopus 로고
    • The S-poor prolamins of wheat, barley and rye: revisited
    • Tatham A.S., Shewry P.R. The S-poor prolamins of wheat, barley and rye: revisited. Journal of Cereal Science 2012, 55:79-99.
    • (2012) Journal of Cereal Science , vol.55 , pp. 79-99
    • Tatham, A.S.1    Shewry, P.R.2
  • 116
    • 51649117559 scopus 로고    scopus 로고
    • Proteomics applied on plant abiotic stresses: role of heat shock proteins (HSP)
    • Timperio A.M., Egidi M.G., Zolla L. Proteomics applied on plant abiotic stresses: role of heat shock proteins (HSP). Journal of Proteomics 2008, 71:391-411.
    • (2008) Journal of Proteomics , vol.71 , pp. 391-411
    • Timperio, A.M.1    Egidi, M.G.2    Zolla, L.3
  • 117
    • 0037434980 scopus 로고    scopus 로고
    • From genomics to proteomic
    • Tyers M., Mann M. From genomics to proteomic. Nature 2003, 422:193-197.
    • (2003) Nature , vol.422 , pp. 193-197
    • Tyers, M.1    Mann, M.2
  • 119
    • 0026454690 scopus 로고
    • Qualitative and quantitative changes in barley seed protein patterns during the malting process analyzed by sodium dodecyl sulfate- polyacrylamide gel electrophoresis with respect to malting quality
    • Weiss W., Postel W., Görg A. Qualitative and quantitative changes in barley seed protein patterns during the malting process analyzed by sodium dodecyl sulfate- polyacrylamide gel electrophoresis with respect to malting quality. Electrophoresis 1992, 13:787-797.
    • (1992) Electrophoresis , vol.13 , pp. 787-797
    • Weiss, W.1    Postel, W.2    Görg, A.3
  • 120
    • 30144438909 scopus 로고    scopus 로고
    • Collision-induced dissociation (CID) of peptides and proteins
    • Wells J.M., McLuckey S.A. Collision-induced dissociation (CID) of peptides and proteins. Methods in Enzymology 2005, 402:148-185.
    • (2005) Methods in Enzymology , vol.402 , pp. 148-185
    • Wells, J.M.1    McLuckey, S.A.2
  • 122
    • 0032538528 scopus 로고    scopus 로고
    • Barley oxalate oxidase is a hexameric protein related to seed storage proteins: evidence from X-ray crystallography
    • Woo E.J., Dunwell J.M., Goodenough P.W., Pickersgill R.W. Barley oxalate oxidase is a hexameric protein related to seed storage proteins: evidence from X-ray crystallography. FEBS Letters 1998, 437:87-90.
    • (1998) FEBS Letters , vol.437 , pp. 87-90
    • Woo, E.J.1    Dunwell, J.M.2    Goodenough, P.W.3    Pickersgill, R.W.4
  • 123
    • 0020023025 scopus 로고
    • Purification and chemical properties of two 1,3;1,4- beta-glucan endohydrolases from germinating barley
    • Woodward J.R., Fincher G.B. Purification and chemical properties of two 1,3;1,4- beta-glucan endohydrolases from germinating barley. European Journal of Biochemistry 1982, 121:663-669.
    • (1982) European Journal of Biochemistry , vol.121 , pp. 663-669
    • Woodward, J.R.1    Fincher, G.B.2
  • 126
    • 84868209813 scopus 로고    scopus 로고
    • Southern Illinois University, College of Science, Ethnobotanical Leaflets
    • Young B. Barley; the Versatile Crop 2001, Southern Illinois University, College of Science, Ethnobotanical Leaflets.
    • (2001) Barley; the Versatile Crop
    • Young, B.1
  • 127
    • 0347172922 scopus 로고    scopus 로고
    • Characterization of biomacromolecules using mass spectrometry
    • Zdráhal Z., Plocek J., Konečný P., Chmelík J. Characterization of biomacromolecules using mass spectrometry. Chemické Listy 1997, 91:811-818.
    • (1997) Chemické Listy , vol.91 , pp. 811-818
    • Zdráhal, Z.1    Plocek, J.2    Konečný, P.3    Chmelík, J.4
  • 128
    • 0028854951 scopus 로고
    • Germin-like oxalate oxidase, a H2O2-producing enzyme, accumulates in barley attacked by the powdery mildew fungus
    • Zhang Z., Collinge D.B., Thordal-Christensen H. Germin-like oxalate oxidase, a H2O2-producing enzyme, accumulates in barley attacked by the powdery mildew fungus. Plant Journal 1995, 8:139-145.
    • (1995) Plant Journal , vol.8 , pp. 139-145
    • Zhang, Z.1    Collinge, D.B.2    Thordal-Christensen, H.3


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