7 results on '"Yadav, J.S."'
Search Results
2. Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete chrysosporium provide insight into selective ligninolysis
- Author
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Fernandez-Fueyo, E., Ruiz-Duenas, F.J., Ferreira, P., Floudas, D., Hibbett, D.S., Canessa, P., Larrondo, L.F., James, T.Y., Seelenfreund, D., Lobos, S., Polanco, R., Tello, M., Honda, Y., Watanabe, T., Ryu, J.S., Kubicek, C.P., Schmoll, M., Gaskell, J., Hammel, K.E., St John, F.J., Vanden Wymelenberg, A., Sabat, G., Splinter BonDurant, S., Syed, K., Yadav, J.S., Doddapaneni, H., Subramanian, V., Lavin, J.L., Oguiza, J.A., Perez, G., Pisabarro, A.G., Ramirez, L., Santoyo, F., Master, E., Coutinho, P.M., Henrissat, B., Lombard, V., Magnuson, J.K., Kues, U., Hori, C., Igarashi, K., Samejima, M., Held, B.W., Barry, K.W., LaButti, K.M., Lapidus, A., Lindquist, E.A., Lucas, S.M., Riley, R., Salamov, A.A., Hoffmeister, D., Schwenk, D., Hadar, Y., Yarden, O., de Vries, R.P., Wiebenga, A., Stenlid, J., Eastwood, D., Grigoriev, I.V., Berka, R.M., Blanchette, R.A., Kersten, P., Martinez, A.T., Vicuna, R., Cullen, D., Fernandez-Fueyo, E., Ruiz-Duenas, F.J., Ferreira, P., Floudas, D., Hibbett, D.S., Canessa, P., Larrondo, L.F., James, T.Y., Seelenfreund, D., Lobos, S., Polanco, R., Tello, M., Honda, Y., Watanabe, T., Ryu, J.S., Kubicek, C.P., Schmoll, M., Gaskell, J., Hammel, K.E., St John, F.J., Vanden Wymelenberg, A., Sabat, G., Splinter BonDurant, S., Syed, K., Yadav, J.S., Doddapaneni, H., Subramanian, V., Lavin, J.L., Oguiza, J.A., Perez, G., Pisabarro, A.G., Ramirez, L., Santoyo, F., Master, E., Coutinho, P.M., Henrissat, B., Lombard, V., Magnuson, J.K., Kues, U., Hori, C., Igarashi, K., Samejima, M., Held, B.W., Barry, K.W., LaButti, K.M., Lapidus, A., Lindquist, E.A., Lucas, S.M., Riley, R., Salamov, A.A., Hoffmeister, D., Schwenk, D., Hadar, Y., Yarden, O., de Vries, R.P., Wiebenga, A., Stenlid, J., Eastwood, D., Grigoriev, I.V., Berka, R.M., Blanchette, R.A., Kersten, P., Martinez, A.T., Vicuna, R., and Cullen, D.
- Abstract
Efficient lignin depolymerization is unique to the wood decay basidiomycetes, collectively referred to as white rot fungi. Phanerochaete chrysosporium simultaneously degrades lignin and cellulose, whereas the closely related species, Ceriporiopsis subvermispora, also depolymerizes lignin but may do so with relatively little cellulose degradation. To investigate the basis for selective ligninolysis, we conducted comparative genome analysis of C. subvermispora and P. chrysosporium. Genes encoding manganese peroxidase numbered 13 and five in C. subvermispora and P. chrysosporium, respectively. In addition, the C. subvermispora genome contains at least seven genes predicted to encode laccases, whereas the P. chrysosporium genome contains none. We also observed expansion of the number of C. subvermispora desaturase-encoding genes putatively involved in lipid metabolism. Microarray-based transcriptome analysis showed substantial up-regulation of several desaturase and MnP genes in wood-containing medium. MS identified MnP proteins in C. subvermispora culture filtrates, but none in P. chrysosporium cultures. These results support the importance of MnP and a lignin degradation mechanism whereby cleavage of the dominant nonphenolic structures is mediated by lipid peroxidation products. Two C. subvermispora genes were predicted to encode peroxidases structurally similar to P. chrysosporium lignin peroxidase and, following heterologous expression in Escherichia coli, the enzymes were shown to oxidize high redox potential substrates, but not Mn2+. Apart from oxidative lignin degradation, we also examined cellulolytic and hemicellulolytic systems in both fungi. In summary, the C. subvermispora genetic inventory and expression patterns exhibit increased oxidoreductase potential and diminished cellulolytic capability relative to P. chrysosporium., Efficient lignin depolymerization is unique to the wood decay basidiomycetes, collectively referred to as white rot fungi. Phanerochaete chrysosporium simultaneously degrades lignin and cellulose, whereas the closely related species, Ceriporiopsis subvermispora, also depolymerizes lignin but may do so with relatively little cellulose degradation. To investigate the basis for selective ligninolysis, we conducted comparative genome analysis of C. subvermispora and P. chrysosporium. Genes encoding manganese peroxidase numbered 13 and five in C. subvermispora and P. chrysosporium, respectively. In addition, the C. subvermispora genome contains at least seven genes predicted to encode laccases, whereas the P. chrysosporium genome contains none. We also observed expansion of the number of C. subvermispora desaturase-encoding genes putatively involved in lipid metabolism. Microarray-based transcriptome analysis showed substantial up-regulation of several desaturase and MnP genes in wood-containing medium. MS identified MnP proteins in C. subvermispora culture filtrates, but none in P. chrysosporium cultures. These results support the importance of MnP and a lignin degradation mechanism whereby cleavage of the dominant nonphenolic structures is mediated by lipid peroxidation products. Two C. subvermispora genes were predicted to encode peroxidases structurally similar to P. chrysosporium lignin peroxidase and, following heterologous expression in Escherichia coli, the enzymes were shown to oxidize high redox potential substrates, but not Mn2+. Apart from oxidative lignin degradation, we also examined cellulolytic and hemicellulolytic systems in both fungi. In summary, the C. subvermispora genetic inventory and expression patterns exhibit increased oxidoreductase potential and diminished cellulolytic capability relative to P. chrysosporium.
- Published
- 2012
3. Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P. chrysosporium, to elucidate the genetic basis of the distinct wood types they colonize
- Author
-
Suzuki, H., Macdonald, J., Syed, K., Salamov, A., Hori, C., Aerts, A., Henrissat, B., Wiebenga, A., vanKuyk, P.A., Barry, K., Lindquist, E., LaButti, K., Lapidus, A., Lucas, S., Coutinho, P., Gong, Y., Samejima, M., Mahadevan, R., Abou-Zaid, M., de Vries, R.P., Igarashi, K., Yadav, J.S., Grigoriev, I.V., Master, E.R., Suzuki, H., Macdonald, J., Syed, K., Salamov, A., Hori, C., Aerts, A., Henrissat, B., Wiebenga, A., vanKuyk, P.A., Barry, K., Lindquist, E., LaButti, K., Lapidus, A., Lucas, S., Coutinho, P., Gong, Y., Samejima, M., Mahadevan, R., Abou-Zaid, M., de Vries, R.P., Igarashi, K., Yadav, J.S., Grigoriev, I.V., and Master, E.R.
- Abstract
Background Softwood is the predominant form of land plant biomass in the Northern hemisphere, and is among the most recalcitrant biomass resources to bioprocess technologies. The white rot fungus, Phanerochaete carnosa, has been isolated almost exclusively from softwoods, while most other known white-rot species, including Phanerochaete chrysosporium, were mainly isolated from hardwoods. Accordingly, it is anticipated that P. carnosa encodes a distinct set of enzymes and proteins that promote softwood decomposition. To elucidate the genetic basis of softwood bioconversion by a white-rot fungus, the present study reports the P. carnosa genome sequence and its comparative analysis with the previously reported P. chrysosporium genome. Results P. carnosa encodes a complete set of lignocellulose-active enzymes. Comparative genomic analysis revealed that P. carnosa is enriched with genes encoding manganese peroxidase, and that the most divergent glycoside hydrolase families were predicted to encode hemicellulases and glycoprotein degrading enzymes. Most remarkably, P. carnosa possesses one of the largest P450 contingents (266 P450s) among the sequenced and annotated wood-rotting basidiomycetes, nearly double that of P. chrysosporium. Along with metabolic pathway modeling, comparative growth studies on model compounds and chemical analyses of decomposed wood components showed greater tolerance of P. carnosa to various substrates including coniferous heartwood. Conclusions The P. carnosa genome is enriched with genes that encode P450 monooxygenases that can participate in extractives degradation, and manganese peroxidases involved in lignin degradation. The significant expansion of P450s in P. carnosa, along with differences in carbohydrate- and lignin-degrading enzymes, could be correlated to the utilization of heartwood and sapwood preparations from both coniferous and hardwood species. Keywords: Phanerochaete carnosa; Comparative genomics; Phanerochaete chrysosporium; So, Background Softwood is the predominant form of land plant biomass in the Northern hemisphere, and is among the most recalcitrant biomass resources to bioprocess technologies. The white rot fungus, Phanerochaete carnosa, has been isolated almost exclusively from softwoods, while most other known white-rot species, including Phanerochaete chrysosporium, were mainly isolated from hardwoods. Accordingly, it is anticipated that P. carnosa encodes a distinct set of enzymes and proteins that promote softwood decomposition. To elucidate the genetic basis of softwood bioconversion by a white-rot fungus, the present study reports the P. carnosa genome sequence and its comparative analysis with the previously reported P. chrysosporium genome. Results P. carnosa encodes a complete set of lignocellulose-active enzymes. Comparative genomic analysis revealed that P. carnosa is enriched with genes encoding manganese peroxidase, and that the most divergent glycoside hydrolase families were predicted to encode hemicellulases and glycoprotein degrading enzymes. Most remarkably, P. carnosa possesses one of the largest P450 contingents (266 P450s) among the sequenced and annotated wood-rotting basidiomycetes, nearly double that of P. chrysosporium. Along with metabolic pathway modeling, comparative growth studies on model compounds and chemical analyses of decomposed wood components showed greater tolerance of P. carnosa to various substrates including coniferous heartwood. Conclusions The P. carnosa genome is enriched with genes that encode P450 monooxygenases that can participate in extractives degradation, and manganese peroxidases involved in lignin degradation. The significant expansion of P450s in P. carnosa, along with differences in carbohydrate- and lignin-degrading enzymes, could be correlated to the utilization of heartwood and sapwood preparations from both coniferous and hardwood species. Keywords: Phanerochaete carnosa; Comparative genomics; Phanerochaete chrysosporium; So
- Published
- 2012
4. The Paleozoic origin of enzymatic lignin decomposition reconstructed from 31 fungal genomes
- Author
-
Floudas, D., Binder, M., Riley, R., Barry, K., Blanchette, R.A., Henrissat, B., Martinez, A.T., Otillar, R., Spatafora, J.W., Yadav, J.S., Aerts, A., Benoit, I., Boyd, A., Carlson, A., Copeland, A., Coutinho, P.M., de Vries, R.P., Ferreira, P., Findley, K., Foster, B., Gaskell, J., Glotzer, D., Gorecki, P., Heitman, J., Hesse, C., Hori, C., Igarashi, K., Jurgens, J.A., Kallen, N., Kersten, P., Kohler, A., Kues, U., Kumar, T.K., Kuo, A., LaButti, K., Larrondo, L.F., Lindquist, E., Ling, A., Lombard, V., Lucas, S., Lundell, T., Martin, R., McLaughlin, D.J., Morgenstern, I., Morin, E., Murat, C., Nagy, L.G., Nolan, M., Ohm, R.A., Patyshakuliyeva, A, Rokas, A., Ruiz-Duenas, F.J., Sabat, G., Salamov, A., Samejima, M., Schmutz, J., Slot, J.C., St John, F., Stenlid, J., Sun, H., Sun, S., Syed, K., Tsang, A., Wiebenga, A., Young, D., Pisabarro, A., Eastwood, D.C., Martin, F., Cullen, D., Grigoriev, I.V., Hibbett, D.S., Floudas, D., Binder, M., Riley, R., Barry, K., Blanchette, R.A., Henrissat, B., Martinez, A.T., Otillar, R., Spatafora, J.W., Yadav, J.S., Aerts, A., Benoit, I., Boyd, A., Carlson, A., Copeland, A., Coutinho, P.M., de Vries, R.P., Ferreira, P., Findley, K., Foster, B., Gaskell, J., Glotzer, D., Gorecki, P., Heitman, J., Hesse, C., Hori, C., Igarashi, K., Jurgens, J.A., Kallen, N., Kersten, P., Kohler, A., Kues, U., Kumar, T.K., Kuo, A., LaButti, K., Larrondo, L.F., Lindquist, E., Ling, A., Lombard, V., Lucas, S., Lundell, T., Martin, R., McLaughlin, D.J., Morgenstern, I., Morin, E., Murat, C., Nagy, L.G., Nolan, M., Ohm, R.A., Patyshakuliyeva, A, Rokas, A., Ruiz-Duenas, F.J., Sabat, G., Salamov, A., Samejima, M., Schmutz, J., Slot, J.C., St John, F., Stenlid, J., Sun, H., Sun, S., Syed, K., Tsang, A., Wiebenga, A., Young, D., Pisabarro, A., Eastwood, D.C., Martin, F., Cullen, D., Grigoriev, I.V., and Hibbett, D.S.
- Published
- 2012
5. Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete chrysosporium provide insight into selective ligninolysis
- Author
-
Fernandez-Fueyo, E., Ruiz-Duenas, F.J., Ferreira, P., Floudas, D., Hibbett, D.S., Canessa, P., Larrondo, L.F., James, T.Y., Seelenfreund, D., Lobos, S., Polanco, R., Tello, M., Honda, Y., Watanabe, T., Ryu, J.S., Kubicek, C.P., Schmoll, M., Gaskell, J., Hammel, K.E., St John, F.J., Vanden Wymelenberg, A., Sabat, G., Splinter BonDurant, S., Syed, K., Yadav, J.S., Doddapaneni, H., Subramanian, V., Lavin, J.L., Oguiza, J.A., Perez, G., Pisabarro, A.G., Ramirez, L., Santoyo, F., Master, E., Coutinho, P.M., Henrissat, B., Lombard, V., Magnuson, J.K., Kues, U., Hori, C., Igarashi, K., Samejima, M., Held, B.W., Barry, K.W., LaButti, K.M., Lapidus, A., Lindquist, E.A., Lucas, S.M., Riley, R., Salamov, A.A., Hoffmeister, D., Schwenk, D., Hadar, Y., Yarden, O., de Vries, R.P., Wiebenga, A., Stenlid, J., Eastwood, D., Grigoriev, I.V., Berka, R.M., Blanchette, R.A., Kersten, P., Martinez, A.T., Vicuna, R., Cullen, D., Fernandez-Fueyo, E., Ruiz-Duenas, F.J., Ferreira, P., Floudas, D., Hibbett, D.S., Canessa, P., Larrondo, L.F., James, T.Y., Seelenfreund, D., Lobos, S., Polanco, R., Tello, M., Honda, Y., Watanabe, T., Ryu, J.S., Kubicek, C.P., Schmoll, M., Gaskell, J., Hammel, K.E., St John, F.J., Vanden Wymelenberg, A., Sabat, G., Splinter BonDurant, S., Syed, K., Yadav, J.S., Doddapaneni, H., Subramanian, V., Lavin, J.L., Oguiza, J.A., Perez, G., Pisabarro, A.G., Ramirez, L., Santoyo, F., Master, E., Coutinho, P.M., Henrissat, B., Lombard, V., Magnuson, J.K., Kues, U., Hori, C., Igarashi, K., Samejima, M., Held, B.W., Barry, K.W., LaButti, K.M., Lapidus, A., Lindquist, E.A., Lucas, S.M., Riley, R., Salamov, A.A., Hoffmeister, D., Schwenk, D., Hadar, Y., Yarden, O., de Vries, R.P., Wiebenga, A., Stenlid, J., Eastwood, D., Grigoriev, I.V., Berka, R.M., Blanchette, R.A., Kersten, P., Martinez, A.T., Vicuna, R., and Cullen, D.
- Abstract
Efficient lignin depolymerization is unique to the wood decay basidiomycetes, collectively referred to as white rot fungi. Phanerochaete chrysosporium simultaneously degrades lignin and cellulose, whereas the closely related species, Ceriporiopsis subvermispora, also depolymerizes lignin but may do so with relatively little cellulose degradation. To investigate the basis for selective ligninolysis, we conducted comparative genome analysis of C. subvermispora and P. chrysosporium. Genes encoding manganese peroxidase numbered 13 and five in C. subvermispora and P. chrysosporium, respectively. In addition, the C. subvermispora genome contains at least seven genes predicted to encode laccases, whereas the P. chrysosporium genome contains none. We also observed expansion of the number of C. subvermispora desaturase-encoding genes putatively involved in lipid metabolism. Microarray-based transcriptome analysis showed substantial up-regulation of several desaturase and MnP genes in wood-containing medium. MS identified MnP proteins in C. subvermispora culture filtrates, but none in P. chrysosporium cultures. These results support the importance of MnP and a lignin degradation mechanism whereby cleavage of the dominant nonphenolic structures is mediated by lipid peroxidation products. Two C. subvermispora genes were predicted to encode peroxidases structurally similar to P. chrysosporium lignin peroxidase and, following heterologous expression in Escherichia coli, the enzymes were shown to oxidize high redox potential substrates, but not Mn2+. Apart from oxidative lignin degradation, we also examined cellulolytic and hemicellulolytic systems in both fungi. In summary, the C. subvermispora genetic inventory and expression patterns exhibit increased oxidoreductase potential and diminished cellulolytic capability relative to P. chrysosporium., Efficient lignin depolymerization is unique to the wood decay basidiomycetes, collectively referred to as white rot fungi. Phanerochaete chrysosporium simultaneously degrades lignin and cellulose, whereas the closely related species, Ceriporiopsis subvermispora, also depolymerizes lignin but may do so with relatively little cellulose degradation. To investigate the basis for selective ligninolysis, we conducted comparative genome analysis of C. subvermispora and P. chrysosporium. Genes encoding manganese peroxidase numbered 13 and five in C. subvermispora and P. chrysosporium, respectively. In addition, the C. subvermispora genome contains at least seven genes predicted to encode laccases, whereas the P. chrysosporium genome contains none. We also observed expansion of the number of C. subvermispora desaturase-encoding genes putatively involved in lipid metabolism. Microarray-based transcriptome analysis showed substantial up-regulation of several desaturase and MnP genes in wood-containing medium. MS identified MnP proteins in C. subvermispora culture filtrates, but none in P. chrysosporium cultures. These results support the importance of MnP and a lignin degradation mechanism whereby cleavage of the dominant nonphenolic structures is mediated by lipid peroxidation products. Two C. subvermispora genes were predicted to encode peroxidases structurally similar to P. chrysosporium lignin peroxidase and, following heterologous expression in Escherichia coli, the enzymes were shown to oxidize high redox potential substrates, but not Mn2+. Apart from oxidative lignin degradation, we also examined cellulolytic and hemicellulolytic systems in both fungi. In summary, the C. subvermispora genetic inventory and expression patterns exhibit increased oxidoreductase potential and diminished cellulolytic capability relative to P. chrysosporium.
- Published
- 2012
6. Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P. chrysosporium, to elucidate the genetic basis of the distinct wood types they colonize
- Author
-
Suzuki, H., Macdonald, J., Syed, K., Salamov, A., Hori, C., Aerts, A., Henrissat, B., Wiebenga, A., vanKuyk, P.A., Barry, K., Lindquist, E., LaButti, K., Lapidus, A., Lucas, S., Coutinho, P., Gong, Y., Samejima, M., Mahadevan, R., Abou-Zaid, M., de Vries, R.P., Igarashi, K., Yadav, J.S., Grigoriev, I.V., Master, E.R., Suzuki, H., Macdonald, J., Syed, K., Salamov, A., Hori, C., Aerts, A., Henrissat, B., Wiebenga, A., vanKuyk, P.A., Barry, K., Lindquist, E., LaButti, K., Lapidus, A., Lucas, S., Coutinho, P., Gong, Y., Samejima, M., Mahadevan, R., Abou-Zaid, M., de Vries, R.P., Igarashi, K., Yadav, J.S., Grigoriev, I.V., and Master, E.R.
- Abstract
Background Softwood is the predominant form of land plant biomass in the Northern hemisphere, and is among the most recalcitrant biomass resources to bioprocess technologies. The white rot fungus, Phanerochaete carnosa, has been isolated almost exclusively from softwoods, while most other known white-rot species, including Phanerochaete chrysosporium, were mainly isolated from hardwoods. Accordingly, it is anticipated that P. carnosa encodes a distinct set of enzymes and proteins that promote softwood decomposition. To elucidate the genetic basis of softwood bioconversion by a white-rot fungus, the present study reports the P. carnosa genome sequence and its comparative analysis with the previously reported P. chrysosporium genome. Results P. carnosa encodes a complete set of lignocellulose-active enzymes. Comparative genomic analysis revealed that P. carnosa is enriched with genes encoding manganese peroxidase, and that the most divergent glycoside hydrolase families were predicted to encode hemicellulases and glycoprotein degrading enzymes. Most remarkably, P. carnosa possesses one of the largest P450 contingents (266 P450s) among the sequenced and annotated wood-rotting basidiomycetes, nearly double that of P. chrysosporium. Along with metabolic pathway modeling, comparative growth studies on model compounds and chemical analyses of decomposed wood components showed greater tolerance of P. carnosa to various substrates including coniferous heartwood. Conclusions The P. carnosa genome is enriched with genes that encode P450 monooxygenases that can participate in extractives degradation, and manganese peroxidases involved in lignin degradation. The significant expansion of P450s in P. carnosa, along with differences in carbohydrate- and lignin-degrading enzymes, could be correlated to the utilization of heartwood and sapwood preparations from both coniferous and hardwood species. Keywords: Phanerochaete carnosa; Comparative genomics; Phanerochaete chrysosporium; So, Background Softwood is the predominant form of land plant biomass in the Northern hemisphere, and is among the most recalcitrant biomass resources to bioprocess technologies. The white rot fungus, Phanerochaete carnosa, has been isolated almost exclusively from softwoods, while most other known white-rot species, including Phanerochaete chrysosporium, were mainly isolated from hardwoods. Accordingly, it is anticipated that P. carnosa encodes a distinct set of enzymes and proteins that promote softwood decomposition. To elucidate the genetic basis of softwood bioconversion by a white-rot fungus, the present study reports the P. carnosa genome sequence and its comparative analysis with the previously reported P. chrysosporium genome. Results P. carnosa encodes a complete set of lignocellulose-active enzymes. Comparative genomic analysis revealed that P. carnosa is enriched with genes encoding manganese peroxidase, and that the most divergent glycoside hydrolase families were predicted to encode hemicellulases and glycoprotein degrading enzymes. Most remarkably, P. carnosa possesses one of the largest P450 contingents (266 P450s) among the sequenced and annotated wood-rotting basidiomycetes, nearly double that of P. chrysosporium. Along with metabolic pathway modeling, comparative growth studies on model compounds and chemical analyses of decomposed wood components showed greater tolerance of P. carnosa to various substrates including coniferous heartwood. Conclusions The P. carnosa genome is enriched with genes that encode P450 monooxygenases that can participate in extractives degradation, and manganese peroxidases involved in lignin degradation. The significant expansion of P450s in P. carnosa, along with differences in carbohydrate- and lignin-degrading enzymes, could be correlated to the utilization of heartwood and sapwood preparations from both coniferous and hardwood species. Keywords: Phanerochaete carnosa; Comparative genomics; Phanerochaete chrysosporium; So
- Published
- 2012
7. The Paleozoic origin of enzymatic lignin decomposition reconstructed from 31 fungal genomes
- Author
-
Floudas, D., Binder, M., Riley, R., Barry, K., Blanchette, R.A., Henrissat, B., Martinez, A.T., Otillar, R., Spatafora, J.W., Yadav, J.S., Aerts, A., Benoit, I., Boyd, A., Carlson, A., Copeland, A., Coutinho, P.M., de Vries, R.P., Ferreira, P., Findley, K., Foster, B., Gaskell, J., Glotzer, D., Gorecki, P., Heitman, J., Hesse, C., Hori, C., Igarashi, K., Jurgens, J.A., Kallen, N., Kersten, P., Kohler, A., Kues, U., Kumar, T.K., Kuo, A., LaButti, K., Larrondo, L.F., Lindquist, E., Ling, A., Lombard, V., Lucas, S., Lundell, T., Martin, R., McLaughlin, D.J., Morgenstern, I., Morin, E., Murat, C., Nagy, L.G., Nolan, M., Ohm, R.A., Patyshakuliyeva, A, Rokas, A., Ruiz-Duenas, F.J., Sabat, G., Salamov, A., Samejima, M., Schmutz, J., Slot, J.C., St John, F., Stenlid, J., Sun, H., Sun, S., Syed, K., Tsang, A., Wiebenga, A., Young, D., Pisabarro, A., Eastwood, D.C., Martin, F., Cullen, D., Grigoriev, I.V., Hibbett, D.S., Floudas, D., Binder, M., Riley, R., Barry, K., Blanchette, R.A., Henrissat, B., Martinez, A.T., Otillar, R., Spatafora, J.W., Yadav, J.S., Aerts, A., Benoit, I., Boyd, A., Carlson, A., Copeland, A., Coutinho, P.M., de Vries, R.P., Ferreira, P., Findley, K., Foster, B., Gaskell, J., Glotzer, D., Gorecki, P., Heitman, J., Hesse, C., Hori, C., Igarashi, K., Jurgens, J.A., Kallen, N., Kersten, P., Kohler, A., Kues, U., Kumar, T.K., Kuo, A., LaButti, K., Larrondo, L.F., Lindquist, E., Ling, A., Lombard, V., Lucas, S., Lundell, T., Martin, R., McLaughlin, D.J., Morgenstern, I., Morin, E., Murat, C., Nagy, L.G., Nolan, M., Ohm, R.A., Patyshakuliyeva, A, Rokas, A., Ruiz-Duenas, F.J., Sabat, G., Salamov, A., Samejima, M., Schmutz, J., Slot, J.C., St John, F., Stenlid, J., Sun, H., Sun, S., Syed, K., Tsang, A., Wiebenga, A., Young, D., Pisabarro, A., Eastwood, D.C., Martin, F., Cullen, D., Grigoriev, I.V., and Hibbett, D.S.
- Published
- 2012
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