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Volumn 8, Issue 1, 2009, Pages 8-14

SNP Analysis and Haplotype Identification in Chymotrypsin Inhibitor-2 (CI-2) Gene of Barley

Author keywords

barley; chymotrypsin inhibitor; haplotype; SNP

Indexed keywords

HORDEUM; HORDEUM VULGARE SUBSP. SPONTANEUM;

EID: 58449119660     PISSN: 16712927     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1671-2927(09)60003-1     Document Type: Article
Times cited : (3)

References (32)
  • 1
    • 85024813985 scopus 로고
    • Inhibitors of chymotrypsin and microbial serine proteases in barley grains
    • Boisen S., Andersen C.T., and Hejgaard J. Inhibitors of chymotrypsin and microbial serine proteases in barley grains. Physiologia Plantarum 52 (1981) 167-176
    • (1981) Physiologia Plantarum , vol.52 , pp. 167-176
    • Boisen, S.1    Andersen, C.T.2    Hejgaard, J.3
  • 2
    • 4344668713 scopus 로고    scopus 로고
    • Single nucleotide polymorphism haplotype diversity and recombination in the isa gene of barley
    • Bundock P., and Henry R.J. Single nucleotide polymorphism haplotype diversity and recombination in the isa gene of barley. Theoretical and Applied Genetics 109 (2004) 543-551
    • (2004) Theoretical and Applied Genetics , vol.109 , pp. 543-551
    • Bundock, P.1    Henry, R.J.2
  • 3
    • 0023398125 scopus 로고
    • The determination of the three-dimensional structure of barley serine proteinase inhibitor 2 by nuclear magnetic resonance, distance geometry and restrained molecular dynamics
    • Clore G.M., Gronenborn A.M., Kjaer M., and Poulsen F. The determination of the three-dimensional structure of barley serine proteinase inhibitor 2 by nuclear magnetic resonance, distance geometry and restrained molecular dynamics. Protein Engineering 1 (1987) 305-311
    • (1987) Protein Engineering , vol.1 , pp. 305-311
    • Clore, G.M.1    Gronenborn, A.M.2    Kjaer, M.3    Poulsen, F.4
  • 4
    • 0025364861 scopus 로고
    • The mutational spectrum of single base-pair substitutions causing human genetic disease: patterns and predictions
    • Cooper D.N., and Krawczak M. The mutational spectrum of single base-pair substitutions causing human genetic disease: patterns and predictions. Human Genetics 85 (1990) 55-74
    • (1990) Human Genetics , vol.85 , pp. 55-74
    • Cooper, D.N.1    Krawczak, M.2
  • 5
    • 0023853921 scopus 로고
    • The CpG dinucleotide and human genetic disease
    • Cooper D.N., and Youssoufian H. The CpG dinucleotide and human genetic disease. Human Genetics 78 (1988) 151-155
    • (1988) Human Genetics , vol.78 , pp. 151-155
    • Cooper, D.N.1    Youssoufian, H.2
  • 8
    • 0019881708 scopus 로고
    • Isoelectric focusing of subtilisin inhibitors: detection and partial characterization of cereal inhibitors of chymotrypsin and microbial proteases
    • Hejgaard J. Isoelectric focusing of subtilisin inhibitors: detection and partial characterization of cereal inhibitors of chymotrypsin and microbial proteases. Analytical Biochemistry 116 (1981) 444-449
    • (1981) Analytical Biochemistry , vol.116 , pp. 444-449
    • Hejgaard, J.1
  • 9
    • 0025369318 scopus 로고
    • Recombinant chymotrypsin inhibitor. 2: Expression, kinetic analysis of inhibition with alpha-chymotrypsin and wild-type and mutant subtilisin BPN', and protein engineering to investigate inhibitory specificity and mechanism
    • Longstaff C., Campbell A.F., and Fersht A.R. Recombinant chymotrypsin inhibitor. 2: Expression, kinetic analysis of inhibition with alpha-chymotrypsin and wild-type and mutant subtilisin BPN', and protein engineering to investigate inhibitory specificity and mechanism. Biochemistry 29 (1990) 7339-7347
    • (1990) Biochemistry , vol.29 , pp. 7339-7347
    • Longstaff, C.1    Campbell, A.F.2    Fersht, A.R.3
  • 11
    • 0036931439 scopus 로고    scopus 로고
    • Characterization of the flanking regions of Zea mays microsatellites reveals a large number of useful sequence polymorphisms
    • Mogg R., Batley J., Hanley S., Edwards D., O'Sullivan H., and Edwards K.J. Characterization of the flanking regions of Zea mays microsatellites reveals a large number of useful sequence polymorphisms. Theoretical and Applied Genetics 105 (2002) 532-543
    • (2002) Theoretical and Applied Genetics , vol.105 , pp. 532-543
    • Mogg, R.1    Batley, J.2    Hanley, S.3    Edwards, D.4    O'Sullivan, H.5    Edwards, K.J.6
  • 12
    • 58449136919 scopus 로고
    • Contribution of residues in the reactive site loop of chymotrypsin inhibitor 2 to protein stability and activity
    • Jackson S.E., and Fersht A.R. Contribution of residues in the reactive site loop of chymotrypsin inhibitor 2 to protein stability and activity. Biochemistry 30 (1994) 10428-10435
    • (1994) Biochemistry , vol.30 , pp. 10428-10435
    • Jackson, S.E.1    Fersht, A.R.2
  • 13
    • 0027384577 scopus 로고
    • Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor 2
    • Jackson S.E., Moracci M., Masry N., Johnson C.M., and Fersht A.R. Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor 2. Biochemistry 32 (1993) 11259-11269
    • (1993) Biochemistry , vol.32 , pp. 11259-11269
    • Jackson, S.E.1    Moracci, M.2    Masry, N.3    Johnson, C.M.4    Fersht, A.R.5
  • 14
    • 0025337398 scopus 로고
    • Role of arginine 67 in the stabilization of chymotrypsin inhibitor 2: Examination of amide proton exchange rates and denaturation thermodynamics of an engineered protein
    • Jandu S.K., Ray S., Brooks L., and Leatherbarrow R.J. Role of arginine 67 in the stabilization of chymotrypsin inhibitor 2: Examination of amide proton exchange rates and denaturation thermodynamics of an engineered protein. Biochemistry 29 (1990) 6264-6269
    • (1990) Biochemistry , vol.29 , pp. 6264-6269
    • Jandu, S.K.1    Ray, S.2    Brooks, L.3    Leatherbarrow, R.J.4
  • 15
    • 0000375324 scopus 로고
    • Identification of the reactive sites in two homologous serine proteinase inhibitors isolated from barley
    • Jonassen I., and Svendsen I. Identification of the reactive sites in two homologous serine proteinase inhibitors isolated from barley. Carlsberg Research Communications 47 (1982) 199-203
    • (1982) Carlsberg Research Communications , vol.47 , pp. 199-203
    • Jonassen, I.1    Svendsen, I.2
  • 16
    • 0031149258 scopus 로고    scopus 로고
    • Expression of de novo high-lysine a-helical coiled-coil proteins may significantly increase the accumulated levels of lysine in mature seeds of transgenic tobacco plants
    • Keeler S.J., Maloney C.L., Webber P.Y., Patterson C., Hirata L.T., Falco S.C., and Rice J.A. Expression of de novo high-lysine a-helical coiled-coil proteins may significantly increase the accumulated levels of lysine in mature seeds of transgenic tobacco plants. Plant Molecular Biology 34 (1997) 15-29
    • (1997) Plant Molecular Biology , vol.34 , pp. 15-29
    • Keeler, S.J.1    Maloney, C.L.2    Webber, P.Y.3    Patterson, C.4    Hirata, L.T.5    Falco, S.C.6    Rice, J.A.7
  • 17
    • 0032736844 scopus 로고    scopus 로고
    • Conformation and stability of barley chymotrypsin inhibitor-2 (CI-2) mutants containing multiple lysine substitutions
    • Keith R.R., and Rao A.G. Conformation and stability of barley chymotrypsin inhibitor-2 (CI-2) mutants containing multiple lysine substitutions. Protein Engineering 12 (1999) 967-973
    • (1999) Protein Engineering , vol.12 , pp. 967-973
    • Keith, R.R.1    Rao, A.G.2
  • 18
    • 3242810318 scopus 로고    scopus 로고
    • MEGA3: integrated software for molecular evolutionary genetics analysis and sequence alignment
    • Kumar S., Tamura K., and Nei M. MEGA3: integrated software for molecular evolutionary genetics analysis and sequence alignment. Brief Bioinformatics 5 (2004) 150-163
    • (2004) Brief Bioinformatics , vol.5 , pp. 150-163
    • Kumar, S.1    Tamura, K.2    Nei, M.3
  • 19
    • 0031576337 scopus 로고    scopus 로고
    • Glutamine, alanine or glycine repeats inserted into the loop of a protein have minimal effects on stability and folding rates
    • Ladurner A.G., and Fersht A.R. Glutamine, alanine or glycine repeats inserted into the loop of a protein have minimal effects on stability and folding rates. Journal of Molecular Biology 273 (1997) 330-337
    • (1997) Journal of Molecular Biology , vol.273 , pp. 330-337
    • Ladurner, A.G.1    Fersht, A.R.2
  • 20
    • 0026346980 scopus 로고
    • Refinement of the three-dimensional solution structure of barley serine proteinase inhibitor 2 and comparison with the structures in crystals
    • Ludvigsen S., Shen H., Kjaer M., Madsen J.C., and Poulsen F.M. Refinement of the three-dimensional solution structure of barley serine proteinase inhibitor 2 and comparison with the structures in crystals. Journal of Molecular Biology 222 (1991) 621-635
    • (1991) Journal of Molecular Biology , vol.222 , pp. 621-635
    • Ludvigsen, S.1    Shen, H.2    Kjaer, M.3    Madsen, J.C.4    Poulsen, F.M.5
  • 21
    • 0033009569 scopus 로고    scopus 로고
    • Analysis of protein-protein interactions by mutagenesis: direct versus indirect effects
    • Otzen D.E., and Fersht A.R. Analysis of protein-protein interactions by mutagenesis: direct versus indirect effects. Protein Engineering 12 (1999) 41-45
    • (1999) Protein Engineering , vol.12 , pp. 41-45
    • Otzen, D.E.1    Fersht, A.R.2
  • 22
    • 0028865428 scopus 로고
    • Structure factors contributing to the hydrophobic effect: The partly exposed hydrophobic minicore in chymotrypsin inhibitor 2
    • Otzen D.E., Rheinnecker M., and Fersht A.R. Structure factors contributing to the hydrophobic effect: The partly exposed hydrophobic minicore in chymotrypsin inhibitor 2. Biochemistry 34 (1995) 13051-13058
    • (1995) Biochemistry , vol.34 , pp. 13051-13058
    • Otzen, D.E.1    Rheinnecker, M.2    Fersht, A.R.3
  • 23
    • 0001635560 scopus 로고
    • Nucleotide sequence of a chymotrypsin inhibitor-2 gene of barley (Hordeum vulgare L.)
    • Peterson D.M., Forde J., Williamson M., Rohde W., and Kreis M. Nucleotide sequence of a chymotrypsin inhibitor-2 gene of barley (Hordeum vulgare L.). Plant Physiology 96 (1991) 1389-1390
    • (1991) Plant Physiology , vol.96 , pp. 1389-1390
    • Peterson, D.M.1    Forde, J.2    Williamson, M.3    Rohde, W.4    Kreis, M.5
  • 24
    • 0028595683 scopus 로고
    • Structure-function validation of high lysine analogs of [.alpha]-hordothionin designed by protein modeling
    • Rao A.G., Hassan M., and Hemple J.C. Structure-function validation of high lysine analogs of [.alpha]-hordothionin designed by protein modeling. Protein Engineering 7 (1994) 1485-1493
    • (1994) Protein Engineering , vol.7 , pp. 1485-1493
    • Rao, A.G.1    Hassan, M.2    Hemple, J.C.3
  • 25
    • 0024290472 scopus 로고
    • Amino acid preferences for specific locations at the ends of alpha helices
    • Richardson J.S., and Richardson D.C. Amino acid preferences for specific locations at the ends of alpha helices. Science 240 (1988) 1648-1652
    • (1988) Science , vol.240 , pp. 1648-1652
    • Richardson, J.S.1    Richardson, D.C.2
  • 26
    • 0026516310 scopus 로고
    • Effect of alanine versus glycine in a-helices on protein stability
    • Serrano L., Neira J.L., Sancho J., and Fersht A.R. Effect of alanine versus glycine in a-helices on protein stability. Nature 356 (1992) 453-455
    • (1992) Nature , vol.356 , pp. 453-455
    • Serrano, L.1    Neira, J.L.2    Sancho, J.3    Fersht, A.R.4
  • 28
    • 1642559189 scopus 로고    scopus 로고
    • Efficient validation of single nucleotide polymorphisms in plants by allele-specific PCR, with an example from barley
    • Solemimani V.D., Baum B.R., and Johnson D.A. Efficient validation of single nucleotide polymorphisms in plants by allele-specific PCR, with an example from barley. Plant Molecular Biology Reporter 21 (2003) 281-288
    • (2003) Plant Molecular Biology Reporter , vol.21 , pp. 281-288
    • Solemimani, V.D.1    Baum, B.R.2    Johnson, D.A.3
  • 29
    • 19744373238 scopus 로고    scopus 로고
    • Detection of single nucleotide polymorphisms in 24 kDa dimeric a-amylase inhibitors from cultivated wheat and its diploid putative progenitors
    • Wang J.R., Wei Y.M., Yan Z.H., and Zheng Y.L. Detection of single nucleotide polymorphisms in 24 kDa dimeric a-amylase inhibitors from cultivated wheat and its diploid putative progenitors. Biochimica et Biophysica Acta 1723 (2005) 309-320
    • (2005) Biochimica et Biophysica Acta , vol.1723 , pp. 309-320
    • Wang, J.R.1    Wei, Y.M.2    Yan, Z.H.3    Zheng, Y.L.4
  • 30
    • 0023654716 scopus 로고
    • Nucleotide sequence of barley chymotrypsin inhibitor-2 (CI-2) and its expression in normal and high lysine barley
    • Williamson M.S., Forde J., Buxton B., and Kreis M. Nucleotide sequence of barley chymotrypsin inhibitor-2 (CI-2) and its expression in normal and high lysine barley. European Journal of Biochemistry 165 (1987) 99-106
    • (1987) European Journal of Biochemistry , vol.165 , pp. 99-106
    • Williamson, M.S.1    Forde, J.2    Buxton, B.3    Kreis, M.4
  • 31
    • 0000824271 scopus 로고
    • Molecular cloning of two isoinhibitor forms of chymotrypsin inhibitor 1 (CI-1) from barley endosperm and their expression in normal and mutant barleys
    • Williamson M.S., Forde J., and Kreis M. Molecular cloning of two isoinhibitor forms of chymotrypsin inhibitor 1 (CI-1) from barley endosperm and their expression in normal and mutant barleys. Plant Molecular Biology 10 (1988) 521-535
    • (1988) Plant Molecular Biology , vol.10 , pp. 521-535
    • Williamson, M.S.1    Forde, J.2    Kreis, M.3
  • 32
    • 0036093533 scopus 로고    scopus 로고
    • Identification of a novel HMW glutenin subunit and comparison of its amino acid sequence with those of homologous subunits
    • Yan Z., Wan Y., Liu K., Zheng Y.L., and Wang D.W. Identification of a novel HMW glutenin subunit and comparison of its amino acid sequence with those of homologous subunits. Chinese Science Bulletin 47 (2002) 220-225
    • (2002) Chinese Science Bulletin , vol.47 , pp. 220-225
    • Yan, Z.1    Wan, Y.2    Liu, K.3    Zheng, Y.L.4    Wang, D.W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.