메뉴 건너뛰기




Volumn 80, Issue 4, 2008, Pages 719-733

Secretome analysis of Phanerochaete chrysosporium strain CIRM-BRFM41 grown on softwood

Author keywords

Chemical pulping; Phanerochaete chrysosporium; Secretome; Softwood

Indexed keywords

BIOPULPING; DESORPTION; ELECTROPHORESIS; ENZYMES; MASS SPECTROMETRY; PLANTS (BOTANY); PULP; SOFTWOODS;

EID: 50849138842     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-008-1596-x     Document Type: Article
Times cited : (75)

References (62)
  • 1
    • 11244354522 scopus 로고    scopus 로고
    • Fungal degradation of wood: Initial proteomic analysis of extracellular proteins of Phanerochaete chrysosporium grown on oak substrate
    • A Abbas H Koc F Liu M Tien 2005 Fungal degradation of wood: initial proteomic analysis of extracellular proteins of Phanerochaete chrysosporium grown on oak substrate Curr Genet 47 49 56
    • (2005) Curr Genet , vol.47 , pp. 49-56
    • Abbas, A.1    Koc, H.2    Liu, F.3    Tien, M.4
  • 4
    • 23744496272 scopus 로고    scopus 로고
    • Transcriptional regulation of plant cell wall degradation by filamentous fungi
    • N Aro T Pakula M Penttilä 2005 Transcriptional regulation of plant cell wall degradation by filamentous fungi FEMS Microbiol Rev 29 719 739
    • (2005) FEMS Microbiol Rev , vol.29 , pp. 719-739
    • Aro, N.1    Pakula, T.2    Penttilä, M.3
  • 5
    • 33746598622 scopus 로고    scopus 로고
    • Impact of xylanase pre-treatment on peroxide bleaching stage of biokraft pulp
    • C Atik S Imamoglu H Bermek 2006 Impact of xylanase pre-treatment on peroxide bleaching stage of biokraft pulp Int Biodeterior Biodegrad 58 22 26
    • (2006) Int Biodeterior Biodegrad , vol.58 , pp. 22-26
    • Atik, C.1    Imamoglu, S.2    Bermek, H.3
  • 6
    • 2542640024 scopus 로고    scopus 로고
    • Protein identification by mass spectrometry: Issues to be considered
    • MA Baldwin 2004 Protein identification by mass spectrometry: issues to be considered Mol Cell Proteomics 3 1 9
    • (2004) Mol Cell Proteomics , vol.3 , pp. 1-9
    • Baldwin, M.A.1
  • 7
    • 0027305189 scopus 로고
    • Influence of primary and secondary proteases produced by free and immobilized cells of the white-rot fungus Phanerochaete chrysosporium on lignin peroxidase activity
    • P Bonnarme M Asther Ma Asther 1993 Influence of primary and secondary proteases produced by free and immobilized cells of the white-rot fungus Phanerochaete chrysosporium on lignin peroxidase activity J Biotechnol 30 271 282
    • (1993) J Biotechnol , vol.30 , pp. 271-282
    • Bonnarme, P.1    Asther, M.2    Ma, A.3
  • 9
    • 0033118394 scopus 로고    scopus 로고
    • Lignocellulose degradation by Phanerochaete chrysosporium: Purification and characterization of the main α-galactosidase
    • H Brumer 3rd PF Sims ML Sinnott 1999 Lignocellulose degradation by Phanerochaete chrysosporium: purification and characterization of the main α-galactosidase Biochem J 339 43 53
    • (1999) Biochem J , vol.339 , pp. 43-53
    • Brumer III, H.1    Sims, P.F.2    Sinnott, M.L.3
  • 10
    • 0027973851 scopus 로고
    • Preferential degradation of phenolic lignin units by two white rot fungi
    • S Camarero GC Galletti AT Martinez 1994 Preferential degradation of phenolic lignin units by two white rot fungi Appl Environ Microbiol 60 4509 4516
    • (1994) Appl Environ Microbiol , vol.60 , pp. 4509-4516
    • Camarero, S.1    Galletti, G.C.2    Martinez, A.T.3
  • 11
    • 0030909542 scopus 로고    scopus 로고
    • Demonstration of in situ oxidative degradation of lignin side chains by two white-rot fungi using analytical pyrolysis of methylated wheat straw
    • S Camarero GC Galletti AT Martínez 1997 Demonstration of in situ oxidative degradation of lignin side chains by two white-rot fungi using analytical pyrolysis of methylated wheat straw Rapid Commun Mass Spectrom 11 331 334
    • (1997) Rapid Commun Mass Spectrom , vol.11 , pp. 331-334
    • Camarero, S.1    Galletti, G.C.2    Martínez, A.T.3
  • 12
    • 0028973385 scopus 로고
    • D-Xylan-degrading enzyme system from the fungus Phanerochaete chrysosporium: Isolation and partial characterisation of an α-(4-O-methyl) -d-glucuronidase
    • A Castanares AJ Hay AH Gordon SI McCrae TM Wood 1995 D-Xylan-degrading enzyme system from the fungus Phanerochaete chrysosporium: isolation and partial characterisation of an α-(4-O-methyl)-d-glucuronidase J Biotechnol 43 183 194
    • (1995) J Biotechnol , vol.43 , pp. 183-194
    • Castanares, A.1    Hay, A.J.2    Gordon, A.H.3    McCrae, S.I.4    Wood, T.M.5
  • 13
    • 13444257870 scopus 로고    scopus 로고
    • Proteomic analysis of secreted proteins from Arabidopsis thaliana seedlings: Improved recovery following removal of phenolic compounds
    • S Charmont E Jamet R Pont-Lezica H Canut 2005 Proteomic analysis of secreted proteins from Arabidopsis thaliana seedlings: improved recovery following removal of phenolic compounds Phytochemistry 66 453 461
    • (2005) Phytochemistry , vol.66 , pp. 453-461
    • Charmont, S.1    Jamet, E.2    Pont-Lezica, R.3    Canut, H.4
  • 18
    • 0028595597 scopus 로고
    • Establishment of genetic linkage by allele-specific polymerase chain reaction: Application to the lignin peroxidase gene family of Phanerochaete chrysosporium
    • J Gaskell P Stewart PJ Kersten SF Covert J Reiser D Cullen 1994 Establishment of genetic linkage by allele-specific polymerase chain reaction: application to the lignin peroxidase gene family of Phanerochaete chrysosporium Biotechnology 12 1372 1375
    • (1994) Biotechnology , vol.12 , pp. 1372-1375
    • Gaskell, J.1    Stewart, P.2    Kersten, P.J.3    Covert, S.F.4    Reiser, J.5    Cullen, D.6
  • 19
    • 0032961627 scopus 로고    scopus 로고
    • Mass spectrometric identification of proteins from silver-stained polyacrylamide gel: A method for the removal of silver ions to enhance sensitivity
    • F Gharahdaghi CR Weinberg DA Meagher BS Imai SM Mische 1999 Mass spectrometric identification of proteins from silver-stained polyacrylamide gel: a method for the removal of silver ions to enhance sensitivity Electrophoresis 20 601 605
    • (1999) Electrophoresis , vol.20 , pp. 601-605
    • Gharahdaghi, F.1    Weinberg, C.R.2    Meagher, D.A.3    Imai, B.S.4    Mische, S.M.5
  • 20
    • 0027180067 scopus 로고
    • Molecular biology of the lignin-degrading basidiomycete Phanerochaete chrysosporium
    • MH Gold M Alic 1993 Molecular biology of the lignin-degrading basidiomycete Phanerochaete chrysosporium Microbiol Rev 57 605 622
    • (1993) Microbiol Rev , vol.57 , pp. 605-622
    • Gold, M.H.1    Alic, M.2
  • 21
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino-acid sequence similarities
    • B Henrissat 1991 A classification of glycosyl hydrolases based on amino-acid sequence similarities Biochem J 280 309 316
    • (1991) Biochem J , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 22
    • 0033589832 scopus 로고    scopus 로고
    • Design and scale up of a process for manganese peroxidase production using the hypersecretory strain Phanerochaete chrysosporium I-1512
    • I Herpoël M Asther JC Sigoillot 1999 Design and scale up of a process for manganese peroxidase production using the hypersecretory strain Phanerochaete chrysosporium I-1512 Biotechnol Bioeng 65 468 473
    • (1999) Biotechnol Bioeng , vol.65 , pp. 468-473
    • Herpoël, I.1    Asther, M.2    Sigoillot, J.C.3
  • 23
    • 0038344488 scopus 로고    scopus 로고
    • Family 3 β-glucosidase from cellulose-degrading culture of the white-rot fungus Phanerochaete chrysosporium is a glucan 1,3-β-glucosidase
    • K Igarashi T Tani K Rie S Masahiro 2003 Family 3 β-glucosidase from cellulose-degrading culture of the white-rot fungus Phanerochaete chrysosporium is a glucan 1,3-β-glucosidase J Biosci Bioeng 95 572 576
    • (2003) J Biosci Bioeng , vol.95 , pp. 572-576
    • Igarashi, K.1    Tani, T.2    Rie, K.3    Masahiro, S.4
  • 24
    • 35448971054 scopus 로고    scopus 로고
    • Substrate recognition by glycoside hydrolase family 74 xyloglucanase from the basidiomycete Phanerochaete chrysosporium
    • T Ishida K Yaoi A Hiyoshi K Igarashi M Samejima 2007 Substrate recognition by glycoside hydrolase family 74 xyloglucanase from the basidiomycete Phanerochaete chrysosporium FEBS J 274 5727 5736
    • (2007) FEBS J , vol.274 , pp. 5727-5736
    • Ishida, T.1    Yaoi, K.2    Hiyoshi, A.3    Igarashi, K.4    Samejima, M.5
  • 25
    • 33646033148 scopus 로고    scopus 로고
    • Substrate recognition by unsaturated glucuronyl hydrolase from Bacillus sp. GL1
    • T Itoh W Hashimoto B Mikami K Murata 2006 Substrate recognition by unsaturated glucuronyl hydrolase from Bacillus sp. GL1 Biochem Biophys Res Comm 344 253 262
    • (2006) Biochem Biophys Res Comm , vol.344 , pp. 253-262
    • Itoh, T.1    Hashimoto, W.2    Mikami, B.3    Murata, K.4
  • 27
    • 0242667124 scopus 로고    scopus 로고
    • Biopulping of hybrid poplar improves chemical and energy savings during kraft pulping
    • KY Kang BM Jo JS Oh SD Mansfield 2003 Biopulping of hybrid poplar improves chemical and energy savings during kraft pulping Wood Fiber Sci 35 594 600
    • (2003) Wood Fiber Sci , vol.35 , pp. 594-600
    • Kang, K.Y.1    Jo, B.M.2    Oh, J.S.3    Mansfield, S.D.4
  • 28
    • 1842739371 scopus 로고    scopus 로고
    • Xylanase and mannanase enzymes from Streptomyces galbus NR and their use in biobleaching of softwood kraft pulp
    • AL Kansoh ZA Nagieb 2004 Xylanase and mannanase enzymes from Streptomyces galbus NR and their use in biobleaching of softwood kraft pulp Antonie Van Leeuwenhoek 85 103 114
    • (2004) Antonie Van Leeuwenhoek , vol.85 , pp. 103-114
    • Kansoh, A.L.1    Nagieb, Z.A.2
  • 29
    • 0025246775 scopus 로고
    • Glyoxal oxidase of Phanerochaete chrysosporium: Its characterization and activation by lignin peroxidase
    • PJ Kersten 1990 Glyoxal oxidase of Phanerochaete chrysosporium: its characterization and activation by lignin peroxidase Proc Natl Acad Sci U S A 87 2936 2940
    • (1990) Proc Natl Acad Sci U S a , vol.87 , pp. 2936-2940
    • Kersten, P.J.1
  • 30
    • 0023264566 scopus 로고
    • 2 production by Phanerochaete chrysosporium
    • 2 production by Phanerochaete chrysosporium J Bacteriol 169 2195 2201
    • (1987) J Bacteriol , vol.169 , pp. 2195-2201
    • Kersten, P.J.1    Kirk, T.K.2
  • 31
    • 33845956242 scopus 로고    scopus 로고
    • Extracellular oxidative systems of the lignin-degrading basidiomycete Phanerochaete chrysosporium
    • P Kersten D Cullen 2007 Extracellular oxidative systems of the lignin-degrading basidiomycete Phanerochaete chrysosporium Fungal Genet Biol 44 77 87
    • (2007) Fungal Genet Biol , vol.44 , pp. 77-87
    • Kersten, P.1    Cullen, D.2
  • 33
    • 0001967057 scopus 로고
    • Thioacidolysis of pre-methylated lignin samples from pine compression and poplar woods
    • C Lapierre C Rolando 1988 Thioacidolysis of pre-methylated lignin samples from pine compression and poplar woods Holzforschung 42 1 4
    • (1988) Holzforschung , vol.42 , pp. 1-4
    • Lapierre, C.1    Rolando, C.2
  • 36
    • 0031841226 scopus 로고    scopus 로고
    • Gene cloning and characterization of a novel cellulose-binding β-glucosidase from Phanerochaete chrysosporium
    • B Li V Renganathan 1998 Gene cloning and characterization of a novel cellulose-binding β-glucosidase from Phanerochaete chrysosporium Appl Environ Microbiol 64 2748 2754
    • (1998) Appl Environ Microbiol , vol.64 , pp. 2748-2754
    • Li, B.1    Renganathan, V.2
  • 37
    • 0034682041 scopus 로고    scopus 로고
    • Cloning, sequencing, and characterization of the bifunctional xylosidase-arabinosidase from the anaerobic thermophile Thermoanaerobacter ethanolicus
    • V Mai J Wiegel WW Lorenz 2000 Cloning, sequencing, and characterization of the bifunctional xylosidase-arabinosidase from the anaerobic thermophile Thermoanaerobacter ethanolicus Gene 247 137 143
    • (2000) Gene , vol.247 , pp. 137-143
    • Mai, V.1    Wiegel, J.2    Lorenz, W.W.3
  • 40
    • 0028762328 scopus 로고
    • A 1,2-α-d-mannosidase from a Bacillus sp.: Purification, characterization, and mode of action
    • Y Maruyama T Nakajima E Ichishima 1994 A 1,2-α-d-mannosidase from a Bacillus sp.: purification, characterization, and mode of action Carbohydr Res 251 89 98
    • (1994) Carbohydr Res , vol.251 , pp. 89-98
    • Maruyama, Y.1    Nakajima, T.2    Ichishima, E.3
  • 41
    • 0035861979 scopus 로고    scopus 로고
    • Family 7 cellobiohydrolases from Phanerochaete chrysosporium: Crystal structure of the catalytic module of Cel7D (CBH58) at 1.32 Å resolution and homology models of the isozymes
    • IG Muñoz W Ubhayasekera H Henriksson I Szabó G Pettersson G Johansson SL Mowbray J Ståhlberg 2001 Family 7 cellobiohydrolases from Phanerochaete chrysosporium: crystal structure of the catalytic module of Cel7D (CBH58) at 1.32 Å resolution and homology models of the isozymes J Mol Biol 314 1097 1111
    • (2001) J Mol Biol , vol.314 , pp. 1097-1111
    • Muñoz, I.G.1    Ubhayasekera, W.2    Henriksson, H.3    Szabó, I.4    Pettersson, G.5    Johansson, G.6    Mowbray, S.L.7    Ståhlberg, J.8
  • 42
    • 0037062622 scopus 로고    scopus 로고
    • Molecular cloning of the heparin/heparan sulfate delta 4,5 unsaturated glycuronidase from Flavobacterium heparinum, its recombinant expression in Escherichia coli, and biochemical determination of its unique substrate specificity
    • JR Myette Z Shriver T Kiziltepe MW McLean G Venkataraman R Sasisekharan 2002 Molecular cloning of the heparin/heparan sulfate delta 4,5 unsaturated glycuronidase from Flavobacterium heparinum, its recombinant expression in Escherichia coli, and biochemical determination of its unique substrate specificity Biochemistry 41 7424 7434
    • (2002) Biochemistry , vol.41 , pp. 7424-7434
    • Myette, J.R.1    Shriver, Z.2    Kiziltepe, T.3    McLean, M.W.4    Venkataraman, G.5    Sasisekharan, R.6
  • 43
    • 0032975847 scopus 로고    scopus 로고
    • Microbial system for polysaccharide depolymerization: Enzymatic route for xanthan depolymerization by Bacillus sp. strain GL1
    • H Nankai W Hashimoto H Miki S Kawai K Murata 1999 Microbial system for polysaccharide depolymerization: enzymatic route for xanthan depolymerization by Bacillus sp. strain GL1 Appl Environ Microbiol 65 2520 2526
    • (1999) Appl Environ Microbiol , vol.65 , pp. 2520-2526
    • Nankai, H.1    Hashimoto, W.2    Miki, H.3    Kawai, S.4    Murata, K.5
  • 44
    • 15044352160 scopus 로고    scopus 로고
    • Acid trehalase in yeasts and filamentous fungi: Localization, regulation and physiological function
    • JL Parrou M Jules G Beltran J François 2005 Acid trehalase in yeasts and filamentous fungi: localization, regulation and physiological function FEMS Yeast Res 5 503 511
    • (2005) FEMS Yeast Res , vol.5 , pp. 503-511
    • Parrou, J.L.1    Jules, M.2    Beltran, G.3    François, J.4
  • 45
    • 0022490037 scopus 로고
    • Comparison of ligninase-I and peroxidase-M2 from the white-rot fungus Phanerochaete chrysosporium
    • A Paszczynski VB Huynh R Crawford 1986 Comparison of ligninase-I and peroxidase-M2 from the white-rot fungus Phanerochaete chrysosporium Arch Biochem Biophys 244 750 765
    • (1986) Arch Biochem Biophys , vol.244 , pp. 750-765
    • Paszczynski, A.1    Huynh, V.B.2    Crawford, R.3
  • 47
    • 0023878613 scopus 로고
    • Improvement and simplification of low-background silver staining of proteins by using sodium dithionite
    • T Rabilloud G Carpentier P Tarroux 1988 Improvement and simplification of low-background silver staining of proteins by using sodium dithionite Electrophoresis 9 288 291
    • (1988) Electrophoresis , vol.9 , pp. 288-291
    • Rabilloud, T.1    Carpentier, G.2    Tarroux, P.3
  • 48
    • 0032101526 scopus 로고    scopus 로고
    • Fate of residual lignin during delignification of kraft pulp by Trametes versicolor
    • ID Reid 1998 Fate of residual lignin during delignification of kraft pulp by Trametes versicolor Appl Environ Microbiol 64 2117 2125
    • (1998) Appl Environ Microbiol , vol.64 , pp. 2117-2125
    • Reid, I.D.1
  • 49
    • 0031912926 scopus 로고    scopus 로고
    • Induction of mannanase, xylanase, and endoglucanase activities in Sclerotium rolfsii
    • A Sachslehner B Nidetzky KD Kulbe D Haltrich 1998 Induction of mannanase, xylanase, and endoglucanase activities in Sclerotium rolfsii Appl Environ Microbiol 64 594 600
    • (1998) Appl Environ Microbiol , vol.64 , pp. 594-600
    • Sachslehner, A.1    Nidetzky, B.2    Kulbe, K.D.3    Haltrich, D.4
  • 50
  • 51
    • 34948842973 scopus 로고    scopus 로고
    • Expression analysis of extracellular proteins from Phanerochaete chrysosporium grown on different liquid and solid substrates
    • S Sato F Liu H Koc M Tien 2007 Expression analysis of extracellular proteins from Phanerochaete chrysosporium grown on different liquid and solid substrates Microbiology 153 3023 3033
    • (2007) Microbiology , vol.153 , pp. 3023-3033
    • Sato, S.1    Liu, F.2    Koc, H.3    Tien, M.4
  • 52
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometry sequencing of proteins from silver-stained polyacrylamide gels
    • A Shevchenko M Wilm O Vorm M Mann 1996 Mass spectrometry sequencing of proteins from silver-stained polyacrylamide gels Anal Chem 68 850 858
    • (1996) Anal Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 53
    • 1942486976 scopus 로고    scopus 로고
    • Factors influencing glycosylation of Trichoderma reesei cellulases. I: Post-secretorial changes of the O- and N-glycosylation pattern of Cel7A
    • I Stals K Sandra S Geysens R Contreras J Van Beeumen M Claeyssens 2004 Factors influencing glycosylation of Trichoderma reesei cellulases. I: Post-secretorial changes of the O- and N-glycosylation pattern of Cel7A Glycobiology 14 713 724
    • (2004) Glycobiology , vol.14 , pp. 713-724
    • Stals, I.1    Sandra, K.2    Geysens, S.3    Contreras, R.4    Van Beeumen, J.5    Claeyssens, M.6
  • 54
    • 0033003023 scopus 로고    scopus 로고
    • Organization and differential regulation of a cluster of lignin peroxidase genes of Phanerochaete chrysosporium
    • P Stewart D Cullen 1999 Organization and differential regulation of a cluster of lignin peroxidase genes of Phanerochaete chrysosporium J Bacteriol 181 3427 3432
    • (1999) J Bacteriol , vol.181 , pp. 3427-3432
    • Stewart, P.1    Cullen, D.2
  • 55
    • 0024959332 scopus 로고
    • Cleavages of aromatic ring and β-O-4 bond of synthetic lignin (DHP) by lignin peroxidase
    • U Toshiaki T Higuchi 1989 Cleavages of aromatic ring and β-O-4 bond of synthetic lignin (DHP) by lignin peroxidase FEBS Lett 242 325 329
    • (1989) FEBS Lett , vol.242 , pp. 325-329
    • Toshiaki, U.1    Higuchi, T.2
  • 56
    • 0025865864 scopus 로고
    • The 1,4-β-d-glucan cellobiohydrolases from Phanerochaete chrysosporium. I. a system of synergistically acting enzymes homologous to Trichoderma reesei
    • E Uzcategui A Ruiz R Montesino G Johansson G Pettersson 1991 The 1,4-β-d-glucan cellobiohydrolases from Phanerochaete chrysosporium. I. A system of synergistically acting enzymes homologous to Trichoderma reesei J Biotechnol 19 271 285
    • (1991) J Biotechnol , vol.19 , pp. 271-285
    • Uzcategui, E.1    Ruiz, A.2    Montesino, R.3    Johansson, G.4    Pettersson, G.5
  • 57
    • 0027449290 scopus 로고
    • Identification of the gene encoding the major cellobiohydrolase of the white rot fungus Phanerochaete chrysosporium
    • A Vanden Wymelenberg S Covert D Cullen 1993 Identification of the gene encoding the major cellobiohydrolase of the white rot fungus Phanerochaete chrysosporium Appl Environ Microbiol 59 3492 3494
    • (1993) Appl Environ Microbiol , vol.59 , pp. 3492-3494
    • Vanden Wymelenberg, A.1    Covert, S.2    Cullen, D.3
  • 58
    • 20444468865 scopus 로고    scopus 로고
    • The Phanerochaete chrysosporium secretome: Database predictions and initial mass spectrometry peptide identifications in cellulose-grown medium
    • A Vanden Wymelenberg G Sabat D Martinez AS Rajangam TT Teeri J Gaskell PJ Kersten D Cullen 2005 The Phanerochaete chrysosporium secretome: database predictions and initial mass spectrometry peptide identifications in cellulose-grown medium J Biotechnol 118 17 34
    • (2005) J Biotechnol , vol.118 , pp. 17-34
    • Vanden Wymelenberg, A.1    Sabat, G.2    Martinez, D.3    Rajangam, A.S.4    Teeri, T.T.5    Gaskell, J.6    Kersten, P.J.7    Cullen, D.8
  • 60
    • 33746040871 scopus 로고    scopus 로고
    • Structure, organization, and transcriptional regulation of a family of copper radical oxidase genes in the lignin-degrading basidiomycete Phanerochaete chrysosporium
    • A Vanden Wymelenberg G Sabat M Mozuch PJ Kersten D Cullen RA Blanchette 2006 Structure, organization, and transcriptional regulation of a family of copper radical oxidase genes in the lignin-degrading basidiomycete Phanerochaete chrysosporium Appl Environ Microbiol 72 4871 4877
    • (2006) Appl Environ Microbiol , vol.72 , pp. 4871-4877
    • Vanden Wymelenberg, A.1    Sabat, G.2    Mozuch, M.3    Kersten, P.J.4    Cullen, D.5    Blanchette, R.A.6
  • 61
    • 0036636707 scopus 로고    scopus 로고
    • Sequence dependent fragmentation of peptides generated by MALDI quadrupole time-of-flight (MALDI Q-TOF) mass spectrometry and its implications for protein identification
    • A Wattenberg AJ Organ K Schneider R Tyldesley R Bordoli RH Bateman 2002 Sequence dependent fragmentation of peptides generated by MALDI quadrupole time-of-flight (MALDI Q-TOF) mass spectrometry and its implications for protein identification J Am Soc Mass Spectrom 13 772 783
    • (2002) J Am Soc Mass Spectrom , vol.13 , pp. 772-783
    • Wattenberg, A.1    Organ, A.J.2    Schneider, K.3    Tyldesley, R.4    Bordoli, R.5    Bateman, R.H.6
  • 62
    • 0027477863 scopus 로고
    • 1,2-α-d-Mannosidase from Penicillium citrinum: Molecular and enzymic properties of two isoenzymes
    • T Yoshida T Inoue E Ichishima 1993 1,2-α-d-Mannosidase from Penicillium citrinum: molecular and enzymic properties of two isoenzymes Biochem J 290 349 354
    • (1993) Biochem J , vol.290 , pp. 349-354
    • Yoshida, T.1    Inoue, T.2    Ichishima, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.