Risultati della ricerca - Alahuhta, Markus
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High resolution crystal structures of triosephosphate isomerase complexed with its suicide inhibitors: The conformational flexibility of the catalytic glutamate in its closed, liga... di Venkatesan, Rajaram, Alahuhta, Markus, Pihko, Petri M, Wierenga, Rik K
Pubblicazione 2011testo -
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Structure of CBM4 from Clostridium thermocellum cellulase K di Alahuhta, Markus, Luo, Yonghua, Ding, Shi-You, Himmel, Michael E., Lunin, Vladimir V.
Pubblicazione 2011testo -
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Expression of an endoglucanase–cellobiohydrolase fusion protein in Saccharomyces cerevisiae, Yarrowia lipolytica, and Lipomyces starkeyi di Xu, Qi, Alahuhta, Markus, Wei, Hui, Knoshaug, Eric P., Wang, Wei, Baker, John O., Vander Wall, Todd, Himmel, Michael E., Zhang, Min
Pubblicazione 2018testo -
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Engineering towards a complete heterologous cellulase secretome in Yarrowia lipolytica reveals its potential for consolidated bioprocessing di Wei, Hui, Wang, Wei, Alahuhta, Markus, Vander Wall, Todd, Baker, John O, Taylor, Larry E, Decker, Stephen R, Himmel, Michael E, Zhang, Min
Pubblicazione 2014testo -
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The catalytic mechanism and unique low pH optimum of Caldicellulosiruptor bescii family 3 pectate lyase di Alahuhta, Markus, Taylor, Larry E., Brunecky, Roman, Sammond, Deanne W., Michener, William, Adams, Michael W. W., Himmel, Michael E., Bomble, Yannick J., Lunin, Vladimir
Pubblicazione 2015testo -
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Characterization of the Biomass Degrading Enzyme GuxA from Acidothermus cellulolyticus di Hengge, Neal N., Mallinson, Sam J. B., Pason, Patthra, Lunin, Vladimir V., Alahuhta, Markus, Chung, Daehwan, Himmel, Michael E., Westpheling, Janet, Bomble, Yannick J.
Pubblicazione 2022testo -
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Crystal structure and biochemical characterization of Chlamydomonas FDX2 reveal two residues that, when mutated, partially confer FDX2 the redox potential and catalytic properties... di Boehm, Marko, Alahuhta, Markus, Mulder, David W., Peden, Erin A., Long, Hai, Brunecky, Roman, Lunin, Vladimir V., King, Paul W., Ghirardi, Maria L., Dubini, Alexandra
Pubblicazione 2015testo -
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Phylogenetics-based identification and characterization of a superior 2,3-butanediol dehydrogenase for Zymomonas mobilis expression di Subramanian, Venkataramanan, Lunin, Vladimir V., Farmer, Samuel J., Alahuhta, Markus, Moore, Kyle T., Ho, Angela, Chaudhari, Yogesh B., Zhang, Min, Himmel, Michael E., Decker, Stephen R.
Pubblicazione 2020testo -
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Natural diversity of glycoside hydrolase family 48 exoglucanases: insights from structure di Brunecky, Roman, Alahuhta, Markus, Sammond, Deanne W., Xu, Qi, Chen, Mo, Wilson, David B., Brady, John W., Himmel, Michael E., Bomble, Yannick J., Lunin, Vladimir V.
Pubblicazione 2017testo -
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Expression and secretion of fungal endoglucanase II and chimeric cellobiohydrolase I in the oleaginous yeast Lipomyces starkeyi di Xu, Qi, Knoshaug, Eric P., Wang, Wei, Alahuhta, Markus, Baker, John O., Yang, Shihui, Vander Wall, Todd, Decker, Stephen R., Himmel, Michael E., Zhang, Min, Wei, Hui
Pubblicazione 2017testo -
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Comparative Biochemical and Structural Analysis of Novel Cellulose Binding Proteins (Tāpirins) from Extremely Thermophilic Caldicellulosiruptor Species di Lee, Laura L., Hart, William S., Lunin, Vladimir V., Alahuhta, Markus, Bomble, Yannick J., Himmel, Michael E., Blumer-Schuette, Sara E., Adams, Michael W. W., Kelly, Robert M.
Pubblicazione 2019testo -
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An iterative computational design approach to increase the thermal endurance of a mesophilic enzyme di Sammond, Deanne W., Kastelowitz, Noah, Donohoe, Bryon S., Alahuhta, Markus, Lunin, Vladimir V., Chung, Daehwan, Sarai, Nicholas S., Yin, Hang, Mittal, Ashutosh, Himmel, Michael E., Guss, Adam M., Bomble, Yannick J.
Pubblicazione 2018testo -
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Discrete and Structurally Unique Proteins (Tāpirins) Mediate Attachment of Extremely Thermophilic Caldicellulosiruptor Species to Cellulose di Blumer-Schuette, Sara E., Alahuhta, Markus, Conway, Jonathan M., Lee, Laura L., Zurawski, Jeffrey V., Giannone, Richard J., Hettich, Robert L., Lunin, Vladimir V., Himmel, Michael E., Kelly, Robert M.
Pubblicazione 2015testo