메뉴 건너뛰기




Volumn 77, Issue 11, 2011, Pages 3793-3801

Secretome of the coprophilous fungus Doratomyces stemonitis C8, isolated from koala feces

Author keywords

[No Author keywords available]

Indexed keywords

BIOFUEL PRODUCTION; CELLOBIOHYDROLASES; CROSS-SPECIES; DE NOVO SEQUENCING; DEGRADING ENZYMES; EFFICIENT PLANTS; GLYCOSYL HYDROLASES; HIGH POTENTIAL; INDUSTRIAL PROCESSS; INTEGRAL PART; LC-MS/MS; LIQUID CHROMATOGRAPHY-TANDEM MASS SPECTROMETRY; MALDI-TOF/TOF MS; MATRIX-ASSISTED LASER DESORPTION IONIZATION; PLANT BIOMASS; PROTEOMIC ANALYSIS; QUADRUPOLES; SECRETOME; T. REESEI; TANDEM MASS SPECTROMETRY; TIME OF FLIGHT; TWO-DIMENSIONAL GEL ELECTROPHORESIS; XYLANASES; ZYMOGRAPHY;

EID: 79958286762     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.00252-11     Document Type: Article
Times cited : (34)

References (55)
  • 1
    • 76649123913 scopus 로고    scopus 로고
    • Improving enzymes for biomass conversion: a basic research perspective
    • Banerjee, G., J. S. Scott-Craig, and J. D. Walton. 2010. Improving enzymes for biomass conversion: a basic research perspective. Bioenerg. Res. 3:82-92.
    • (2010) Bioenerg. Res. , vol.3 , pp. 82-92
    • Banerjee, G.1    Scott-Craig, J.S.2    Walton, J.D.3
  • 2
    • 50249096176 scopus 로고    scopus 로고
    • Fungal secretomes-nature's toolbox for white biotechnology
    • Bouws, H., A. Wattenberg, and H. Zorn. 2008. Fungal secretomes-nature's toolbox for white biotechnology. Appl. Microbiol. Biotechnol. 80:381-388.
    • (2008) Appl. Microbiol. Biotechnol. , vol.80 , pp. 381-388
    • Bouws, H.1    Wattenberg, A.2    Zorn, H.3
  • 3
    • 12144282020 scopus 로고    scopus 로고
    • Xylanases, xylanase families and extremophilic xylanases
    • Collins, T., C. Gerday, and G. Feller. 2005. Xylanases, xylanase families and extremophilic xylanases. FEMS Microbiol. Rev. 29:3-23.
    • (2005) FEMS Microbiol. Rev. , vol.29 , pp. 3-23
    • Collins, T.1    Gerday, C.2    Feller, G.3
  • 4
    • 27644525170 scopus 로고    scopus 로고
    • Growth of the plant cell wall
    • Cosgrove, D. J. 2005. Growth of the plant cell wall. Nat. Rev. Mol. Cell Biol. 6:850-861.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 850-861
    • Cosgrove, D.J.1
  • 5
    • 79251613225 scopus 로고    scopus 로고
    • Podospora anserina hemicellulases potentiate the Trichoderma reesei secretome for saccharification of lignocellulosic biomass
    • Couturier, M., et al. 2011. Podospora anserina hemicellulases potentiate the Trichoderma reesei secretome for saccharification of lignocellulosic biomass. Appl. Environ. Microbiol. 77:237-246.
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 237-246
    • Couturier, M.1
  • 6
    • 35549005302 scopus 로고    scopus 로고
    • Crystal structure of glycoside hydrolase family 78 α-L-rhamnosidase from Bacillus sp
    • Cui, Z., Y. Maruyama, B. Mikami, W. Hashimoto, and K. Murata. 2007. Crystal structure of glycoside hydrolase family 78 α-L-rhamnosidase from Bacillus sp. GL1. J. Mol. Biol. 374:384-398.
    • (2007) GL1. J. Mol. Biol. , vol.374 , pp. 384-398
    • Cui, Z.1    Maruyama, Y.2    Mikami, B.3    Hashimoto, W.4    Murata, K.5
  • 7
    • 85055213046 scopus 로고    scopus 로고
    • Industrial mycology: past, present and future
    • Z. An (ed.), CRC Press, New York, NY
    • Demain, A. L., J. Velasco, and J. L. Adrio. 2005. Industrial mycology: past, present and future. p. 1-26. In Z. An (ed.), Handbook of industrial mycology. CRC Press, New York, NY.
    • (2005) Handbook of industrial mycology , pp. 1-26
    • Demain, A.L.1    Velasco, J.2    Adrio, J.L.3
  • 8
    • 79958255326 scopus 로고    scopus 로고
    • Modification of plant cell wall polysaccharides using enzymes from Aspergillus
    • K. J. Yarema (ed.), Taylor and Francis, Boca Raton, FL
    • de Vries, R. P., M. C. McCann, and J. Visser. 2005. Modification of plant cell wall polysaccharides using enzymes from Aspergillus, p. 613-644. In K. J. Yarema (ed.), Handbook of carbohydrate engineering. Taylor and Francis, Boca Raton, FL.
    • (2005) Handbook of carbohydrate engineering , pp. 613-644
    • de Vries, R.P.1    McCann, M.C.2    Visser, J.3
  • 10
    • 48949118871 scopus 로고    scopus 로고
    • The genome sequence of the model ascomycete fungus Podospora anserina
    • Espagne, E., et al. 2008. The genome sequence of the model ascomycete fungus Podospora anserina. Genome Biol. 9:R77.
    • (2008) Genome Biol , vol.9
    • Espagne, E.1
  • 11
    • 1542395649 scopus 로고    scopus 로고
    • Fungal proteomics: initial mapping of biological control strain Trichoderma harzianum
    • Grinyer, J., M. McKay, H. Nevalainen, and B. Herbert. 2004. Fungal proteomics: initial mapping of biological control strain Trichoderma harzianum. Curr. Genet. 45:163-169.
    • (2004) Curr. Genet. , vol.45 , pp. 163-169
    • Grinyer, J.1    McKay, M.2    Nevalainen, H.3    Herbert, B.4
  • 12
    • 7944236701 scopus 로고    scopus 로고
    • Specific xyloglucanases as a new class of polysaccharide-degrading enzymes
    • Grishutin, S. G., et al. 2004. Specific xyloglucanases as a new class of polysaccharide-degrading enzymes. Biochim. Biophys. Acta 1674:268-281.
    • (2004) Biochim. Biophys. Acta , vol.1674 , pp. 268-281
    • Grishutin, S.G.1
  • 13
    • 60649098811 scopus 로고    scopus 로고
    • Comparative secretome analyses of two Trichoderma reesei RUT-C30 and CL847 hypersecretory strains
    • Herpoël-Gimbert, I., et al. 2008. Comparative secretome analyses of two Trichoderma reesei RUT-C30 and CL847 hypersecretory strains. Biotechnol. Biofuels 1:18.
    • (2008) Biotechnol. Biofuels , vol.1 , pp. 18
    • Herpoël-Gimbert, I.1
  • 14
    • 77952257725 scopus 로고    scopus 로고
    • Microbial enzyme systems for biomass conversion: emerging paradigms
    • Himmel, M. E., et al. 2010. Microbial enzyme systems for biomass conversion: emerging paradigms. Biofuels 1:323-341.
    • (2010) Biofuels , vol.1 , pp. 323-341
    • Himmel, M.E.1
  • 15
    • 70749131505 scopus 로고    scopus 로고
    • Hemicellulase production in Chrysosporium lucknowense C1
    • Hinz, S. W. A., et al. 2009. Hemicellulase production in Chrysosporium lucknowense C1. J. Cereal Sci. 50:318-323.
    • (2009) J. Cereal Sci. , vol.50 , pp. 318-323
    • Hinz, S.W.A.1
  • 16
    • 64749099325 scopus 로고
    • Microbial fermentation in herbivorous marsupials
    • Hume, I. J. 1984. Microbial fermentation in herbivorous marsupials. Bioscience 34:435-440.
    • (1984) Bioscience , vol.34 , pp. 435-440
    • Hume, I.J.1
  • 17
    • 52649091899 scopus 로고    scopus 로고
    • Characterization of an endoglucanase belonging to a new subfamily of glycoside hydrolase family 45 of the basidiomycete Phanerochaete chrysosporium
    • Igarashi, K., T. Ishida, C. Hori, and M. Samejima. 2008. Characterization of an endoglucanase belonging to a new subfamily of glycoside hydrolase family 45 of the basidiomycete Phanerochaete chrysosporium. Appl. Environ. Microbiol. 74:5628-5634.
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 5628-5634
    • Igarashi, K.1    Ishida, T.2    Hori, C.3    Samejima, M.4
  • 19
    • 2242431959 scopus 로고    scopus 로고
    • Posttranslational modification of proteins: tools for functional proteomics. Humana Press, Totowa, NJ
    • Kannicht, C. (ed.). 2002. Methods in molecular biology, vol. 194. Posttranslational modification of proteins: tools for functional proteomics. Humana Press, Totowa, NJ.
    • (2002) Methods in molecular biology , vol.194
    • Kannicht, C.1
  • 20
    • 43849086853 scopus 로고    scopus 로고
    • Revealing the structural and functional diversity of plant cell walls
    • Knox, J. P. 2008. Revealing the structural and functional diversity of plant cell walls. Curr. Opin. Plant Biol. 11:308-313.
    • (2008) Curr. Opin. Plant Biol. , vol.11 , pp. 308-313
    • Knox, J.P.1
  • 22
    • 34547741043 scopus 로고    scopus 로고
    • Identification of genes encoding microbial glucuronoyl esterases
    • Li, X.-L., S. Spániková, R. P. de Vries, and P. Biely. 2007. Identification of genes encoding microbial glucuronoyl esterases. FEBS Lett. 581:4029- 4035.
    • (2007) FEBS Lett , vol.581 , pp. 4029-4035
    • Li, X.-L.1    Spániková, S.2    de Vries, R.P.3    Biely, P.4
  • 23
    • 0037253223 scopus 로고    scopus 로고
    • Expanding the organismal scope of proteomics: cross-species protein identification by mass spectrometry and its implications
    • Liska, A. J., and A. Shevchenko. 2003. Expanding the organismal scope of proteomics: cross-species protein identification by mass spectrometry and its implications. Proteomics 3:19-28.
    • (2003) Proteomics , vol.3 , pp. 19-28
    • Liska, A.J.1    Shevchenko, A.2
  • 24
    • 0036794713 scopus 로고    scopus 로고
    • Pectate lyases, cell wall degradation and fruit softening
    • Marin-Rodriguez, M. C., J. Orchard, and G. B. Seymour. 2002. Pectate lyases, cell wall degradation and fruit softening. J. Exp. Bot. 53:2115-2119.
    • (2002) J. Exp. Bot. , vol.53 , pp. 2115-2119
    • Marin-Rodriguez, M.C.1    Orchard, J.2    Seymour, G.B.3
  • 25
    • 43449098828 scopus 로고    scopus 로고
    • Genome sequencing and analysis of the biomassdegrading fungus Trichoderma reesei (syn. Hypocrea jecorina)
    • Martinez, D., et al. 2008. Genome sequencing and analysis of the biomassdegrading fungus Trichoderma reesei (syn. Hypocrea jecorina). Nat. Biotechnol. 26:553-560.
    • (2008) Nat. Biotechnol. , vol.26 , pp. 553-560
    • Martinez, D.1
  • 26
    • 37049006919 scopus 로고    scopus 로고
    • Comparison of Penicillium echinulatum and Trichoderma reesei cellulases in relation to their activity against various cellulosic substrates
    • Martins, L. F., D. Kolling, M. Camassola, A. J. P. Dillon, and L. P. Ramos. 2008. Comparison of Penicillium echinulatum and Trichoderma reesei cellulases in relation to their activity against various cellulosic substrates. Bioresour. Technol. 99:1417-1424.
    • (2008) Bioresour. Technol. , vol.99 , pp. 1417-1424
    • Martins, L.F.1    Kolling, D.2    Camassola, M.3    Dillon, A.J.P.4    Ramos, L.P.5
  • 27
    • 0036801315 scopus 로고    scopus 로고
    • Secreted proteases from pathogenic fungi
    • Monod, M., et al. 2002. Secreted proteases from pathogenic fungi. Int. J. Med. Microbiol. 292:405-419.
    • (2002) Int. J. Med. Microbiol. , vol.292 , pp. 405-419
    • Monod, M.1
  • 28
    • 47249105555 scopus 로고    scopus 로고
    • The secretome of the maize pathogen Ustilago maydis
    • Mueller, O., et al. 2008. The secretome of the maize pathogen Ustilago maydis. Fungal Genet. Biol. 45:S63-S70.
    • (2008) Fungal Genet. Biol. , vol.45
    • Mueller, O.1
  • 29
    • 64049118903 scopus 로고    scopus 로고
    • Reduced genomic potential for secreted plant cell-wall-degrading enzymes in the ectomycorrhizal fungus Amanita bisporigera, based on the secretome of Trichoderma reesei
    • Nagendran, S., H. E. Hallen-Adams, J. M. Paper, N. Aslam, and J. D. Walton. 2009. Reduced genomic potential for secreted plant cell-wall-degrading enzymes in the ectomycorrhizal fungus Amanita bisporigera, based on the secretome of Trichoderma reesei. Fungal Genet. Biol. 46:427-435.
    • (2009) Fungal Genet. Biol. , vol.46 , pp. 427-435
    • Nagendran, S.1    Hallen-Adams, H.E.2    Paper, J.M.3    Aslam, N.4    Walton, J.D.5
  • 31
    • 33646570211 scopus 로고    scopus 로고
    • Proteomic analysis of extracellular proteins from Aspergillus oryzae grown under submerged and solid-state culture conditions
    • Oda, K., et al. 2006. Proteomic analysis of extracellular proteins from Aspergillus oryzae grown under submerged and solid-state culture conditions. Appl. Environ. Microbiol. 72:3448-3457.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 3448-3457
    • Oda, K.1
  • 32
    • 0026279667 scopus 로고
    • An investigation of streptococcal flora in feces of koalas
    • Osawa, R. 1991. An investigation of streptococcal flora in feces of koalas. J. Wildl. Manage. 55:623-627.
    • (1991) J. Wildl. Manage. , vol.55 , pp. 623-627
    • Osawa, R.1
  • 34
    • 47549110973 scopus 로고    scopus 로고
    • Genomic adaptation: a fungal perspective
    • Pain, A., and C. Hertz-Fowler. 2008. Genomic adaptation: a fungal perspective. Nat. Rev. Microbiol. 6:572-573.
    • (2008) Nat. Rev. Microbiol. , vol.6 , pp. 572-573
    • Pain, A.1    Hertz-Fowler, C.2
  • 35
    • 34748923122 scopus 로고    scopus 로고
    • Comparative proteomics of extracellular proteins in vitro and in planta from the pathogenic fungus Fusarium graminearum
    • Paper, J. M., J. S. Scott-Craig, N. D. Adhikari, C. A. Cuomo, and J. D. Walton. 2007. Comparative proteomics of extracellular proteins in vitro and in planta from the pathogenic fungus Fusarium graminearum. Proteomics 7:3171-3183.
    • (2007) Proteomics , vol.7 , pp. 3171-3183
    • Paper, J.M.1    Scott-Craig, J.S.2    Adhikari, N.D.3    Cuomo, C.A.4    Walton, J.D.5
  • 36
    • 34249935468 scopus 로고    scopus 로고
    • New insights into pectin methylesterase structure and function
    • Pelloux, J., C. Rustérucci, and E. J. Mellerowicz. 2007. New insights into pectin methylesterase structure and function. Trends Plant Sci. 12:267-277.
    • (2007) Trends Plant Sci , vol.12 , pp. 267-277
    • Pelloux, J.1    Rustérucci, C.2    Mellerowicz, E.J.3
  • 37
    • 0023553310 scopus 로고
    • A versatile transformation system for the cellulolytic filamentous fungus Trichoderma reesei
    • Penttilä, M., H. Nevalainen, M. Rättö, E. Salminen, and J. Knowles. 1987. A versatile transformation system for the cellulolytic filamentous fungus Trichoderma reesei. Gene 61:155-164.
    • (1987) Gene , vol.61 , pp. 155-164
    • Penttilä, M.1    Nevalainen, H.2    Rättö, M.3    Salminen, E.4    Knowles, J.5
  • 38
    • 58449095185 scopus 로고    scopus 로고
    • Fungi from koala (Phascolarctos cinereus) faeces exhibit a broad range of enzyme activities against recalcitrant substrates
    • Peterson, R. A., J. R. Bradner, T. H. Roberts, and K. M. H. Nevalainen. 2009. Fungi from koala (Phascolarctos cinereus) faeces exhibit a broad range of enzyme activities against recalcitrant substrates. Lett. Appl. Microbiol. 48: 218-225.
    • (2009) Lett. Appl. Microbiol. , vol.48 , pp. 218-225
    • Peterson, R.A.1    Bradner, J.R.2    Roberts, T.H.3    Nevalainen, K.M.H.4
  • 39
    • 70449522158 scopus 로고    scopus 로고
    • Fungal proteins with mannanase activity identified directly from a Congo Red stained zymogram by mass spectrometry
    • Peterson, R., J. Grinyer, J. Joss, A. Khan, and H. Nevalainen. 2009. Fungal proteins with mannanase activity identified directly from a Congo Red stained zymogram by mass spectrometry. J. Microbiol. Methods 79:374-377.
    • (2009) J. Microbiol. Methods , vol.79 , pp. 374-377
    • Peterson, R.1    Grinyer, J.2    Joss, J.3    Khan, A.4    Nevalainen, H.5
  • 40
    • 79953785804 scopus 로고    scopus 로고
    • Extracellular hydrolase profiles of fungi isolated from koala faeces invite biotechnological interest
    • Peterson, R., J. Grinyer, and H. Nevalainen. 2011. Extracellular hydrolase profiles of fungi isolated from koala faeces invite biotechnological interest. Mycol. Prog. 10:207-218.
    • (2011) Mycol. Prog. , vol.10 , pp. 207-218
    • Peterson, R.1    Grinyer, J.2    Nevalainen, H.3
  • 41
    • 0034253281 scopus 로고    scopus 로고
    • α-L-arabinofuranosidases: biochemistry, molecular biology and application in biotechnology
    • Saha, B. C. 2000. α-L-arabinofuranosidases: biochemistry, molecular biology and application in biotechnology. Biotechnol. Adv. 18:403-423.
    • (2000) Biotechnol. Adv. , vol.18 , pp. 403-423
    • Saha, B.C.1
  • 42
    • 34948842973 scopus 로고    scopus 로고
    • Expression analysis of extracellular proteins from Phanerochaete chrysosporium grown on different liquid and solid substrates
    • Sato, S., F. Liu, H. Koc, and 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
  • 43
    • 65249115871 scopus 로고    scopus 로고
    • Comparative proteomic analysis of Botrytis cinerea secretome
    • Shah, P., et al. 2009. Comparative proteomic analysis of Botrytis cinerea secretome. J. Proteome Res. 8:1123-1130.
    • (2009) J. Proteome Res. , vol.8 , pp. 1123-1130
    • Shah, P.1
  • 44
    • 33750462747 scopus 로고    scopus 로고
    • Amino acid regions of family 45 endoglucanases involved in cotton defibrillation and in resistance to anionic surfactants and oxidizing agents
    • Shimonaka, A., et al. 2006. Amino acid regions of family 45 endoglucanases involved in cotton defibrillation and in resistance to anionic surfactants and oxidizing agents. Biosci. Biotechnol. Biochem. 70:2460-2466.
    • (2006) Biosci. Biotechnol. Biochem. , vol.70 , pp. 2460-2466
    • Shimonaka, A.1
  • 45
    • 0032782326 scopus 로고    scopus 로고
    • Hydroxyl radical generation by an extracellular low-molecular-weight substance and phenol oxidase activity during wood degradation by the white-rot basidiomycete Trametes versicolor
    • Tanaka, H., S. Itakura, and A. Enoki. 1999. Hydroxyl radical generation by an extracellular low-molecular-weight substance and phenol oxidase activity during wood degradation by the white-rot basidiomycete Trametes versicolor. J. Biotechnol. 75:57-70.
    • (1999) J. Biotechnol. , vol.75 , pp. 57-70
    • Tanaka, H.1    Itakura, S.2    Enoki, A.3
  • 46
    • 33646762158 scopus 로고    scopus 로고
    • Improving cellulose hydrolysis with new cellulase compositions
    • Cincinnati, OH
    • Teter, S. A., and J. R. Cherry. 2005. Improving cellulose hydrolysis with new cellulase compositions, p. 12027-12033. In AIChE Annual Meeting Conference Proceedings, Cincinnati, OH.
    • (2005) AIChE Annual Meeting Conference Proceedings , pp. 12027-12033
    • Teter, S.A.1    Cherry, J.R.2
  • 47
    • 67650621098 scopus 로고    scopus 로고
    • Analytical and computational approaches to define the Aspergillus niger secretome
    • Tsang, A., G. Butler, J. Powlowski, E. A. Panisko, and S. E. Baker. 2009. Analytical and computational approaches to define the Aspergillus niger secretome. Fungal Genet. Biol. 46:S153-S160.
    • (2009) Fungal Genet. Biol. , vol.46
    • Tsang, A.1    Butler, G.2    Powlowski, J.3    Panisko, E.A.4    Baker, S.E.5
  • 49
    • 84970601695 scopus 로고
    • Eucalyptus digestibility and digestible energy requirements of adult male koalas, Phascolarctos cinereus (Marsupialia)
    • Ulrey, D. E., P. T. Robinson, and P. A. Whetter. 1981. Eucalyptus digestibility and digestible energy requirements of adult male koalas, Phascolarctos cinereus (Marsupialia). Aust. J. Zool. 29:847-852.
    • (1981) Aust. J. Zool. , vol.29 , pp. 847-852
    • Ulrey, D.E.1    Robinson, P.T.2    Whetter, P.A.3
  • 50
    • 77953074402 scopus 로고    scopus 로고
    • Comparative transcriptome and secretome analysis of wood decay fungi Postia placenta and Phanerochaete chrysosporium
    • Vanden Wymelenberg, A., et al. 2010. Comparative transcriptome and secretome analysis of wood decay fungi Postia placenta and Phanerochaete chrysosporium. Appl. Environ. Microbiol. 76:3599-3610.
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 3599-3610
    • Vanden Wymelenberg, A.1
  • 51
    • 0035030366 scopus 로고    scopus 로고
    • Fingerprinting Trichoderma reesei hydrolases in a commercial cellulase preparation
    • Vinzant, T. B., et al. 2001. Fingerprinting Trichoderma reesei hydrolases in a commercial cellulase preparation. Appl. Biochem. Biotechnol. 91-93:99- 107.
    • (2001) Appl. Biochem. Biotechnol. , vol.91-93 , pp. 99-107
    • Vinzant, T.B.1
  • 52
    • 64149097809 scopus 로고    scopus 로고
    • Pectin, a versatile polysaccharide present in plant cell walls
    • Voragen, A., G.-J. Coenen, R. Verhoef, and H. Schols. 2009. Pectin, a versatile polysaccharide present in plant cell walls. Struct. Chem. 20:263- 275.
    • (2009) Struct. Chem. , vol.20 , pp. 263-275
    • Voragen, A.1    Coenen, G.-J.2    Verhoef, R.3    Schols, H.4
  • 54
    • 67649807807 scopus 로고    scopus 로고
    • Natural paradigms of plant cell wall degradation
    • Wei, H., et al. 2009. Natural paradigms of plant cell wall degradation. Curr. Opin. Biotechnol. 20:330-338.
    • (2009) Curr. Opin. Biotechnol. , vol.20 , pp. 330-338
    • Wei, H.1
  • 55
    • 41949086296 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction analysis of the glucuronoyl esterase catalytic domain from Hypocrea jecorina
    • Wood, S. J., et al. 2008. Crystallization and preliminary X-ray diffraction analysis of the glucuronoyl esterase catalytic domain from Hypocrea jecorina. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 64:255-257.
    • (2008) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. , vol.64 , pp. 255-257
    • Wood, S.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.