Year |
Citation |
Score |
2016 |
Xu Q, Resch MG, Podkaminer K, Yang S, Baker JO, Donohoe BS, Wilson C, Klingeman DM, Olson DG, Decker SR, Giannone RJ, Hettich RL, Brown SD, Lynd LR, Bayer EA, et al. Dramatic performance of Clostridium thermocellum explained by its wide range of cellulase modalities. Science Advances. 2: e1501254. PMID 26989779 DOI: 10.1126/Sciadv.1501254 |
0.31 |
|
2016 |
Salvachúa D, Katahira R, Cleveland NS, Khanna P, Resch MG, Black BA, Purvine SO, Zink EM, Prieto A, Martínez MJ, Martínez AT, Simmons BA, Gladden JM, Beckham GT. Lignin depolymerization by fungal secretomes and a microbial sink Green Chemistry. 18: 6046-6062. DOI: 10.1039/C6Gc01531J |
0.321 |
|
2015 |
Donohoe BS, Resch MG. Mechanisms employed by cellulase systems to gain access through the complex architecture of lignocellulosic substrates. Current Opinion in Chemical Biology. 29: 100-7. PMID 26529490 DOI: 10.1016/J.Cbpa.2015.08.014 |
0.335 |
|
2015 |
Happs RM, Guan X, Resch MG, Davis MF, Beckham GT, Tan Z, Crowley MF. O-glycosylation effects on family 1 carbohydrate-binding module solution structures. The Febs Journal. PMID 26307003 DOI: 10.1111/Febs.13500 |
0.337 |
|
2014 |
Sammond DW, Yarbrough JM, Mansfield E, Bomble YJ, Hobdey SE, Decker SR, Taylor LE, Resch MG, Bozell JJ, Himmel ME, Vinzant TB, Crowley MF. Predicting enzyme adsorption to lignin films by calculating enzyme surface hydrophobicity. The Journal of Biological Chemistry. 289: 20960-9. PMID 24876380 DOI: 10.1074/Jbc.M114.573642 |
0.307 |
|
2014 |
Resch MG, Donohoe BS, Ciesielski PN, Nill JE, Magnusson L, Himmel ME, Mittal A, Katahira R, Biddy MJ, Beckham GT. Clean Fractionation Pretreatment Reduces Enzyme Loadings for Biomass Saccharification and Reveals the Mechanism of Free and Cellulosomal Enzyme Synergy Acs Sustainable Chemistry & Engineering. 2: 1377-1387. DOI: 10.1021/Sc500210W |
0.364 |
|
2013 |
Brunecky R, Alahuhta M, Xu Q, Donohoe BS, Crowley MF, Kataeva IA, Yang SJ, Resch MG, Adams MW, Lunin VV, Himmel ME, Bomble YJ. Revealing nature's cellulase diversity: the digestion mechanism of Caldicellulosiruptor bescii CelA. Science (New York, N.Y.). 342: 1513-6. PMID 24357319 DOI: 10.1126/Science.1244273 |
0.374 |
|
2013 |
Payne CM, Resch MG, Chen L, Crowley MF, Himmel ME, Taylor LE, Sandgren M, Ståhlberg J, Stals I, Tan Z, Beckham GT. Glycosylated linkers in multimodular lignocellulose-degrading enzymes dynamically bind to cellulose. Proceedings of the National Academy of Sciences of the United States of America. 110: 14646-51. PMID 23959893 DOI: 10.1073/Pnas.1309106110 |
0.356 |
|
2013 |
Resch MG, Donohoe BS, Baker JO, Decker SR, Bayer EA, Beckham GT, Himmel ME. Fungal cellulases and complexed cellulosomal enzymes exhibit synergistic mechanisms in cellulose deconstruction Energy and Environmental Science. 6: 1858-1867. DOI: 10.1039/C3Ee00019B |
0.351 |
|
2011 |
Panchenko T, Sorensen TC, Woodcock CL, Kan ZY, Wood S, Resch MG, Luger K, Englander SW, Hansen JC, Black BE. Replacement of histone H3 with CENP-A directs global nucleosome array condensation and loosening of nucleosome superhelical termini. Proceedings of the National Academy of Sciences of the United States of America. 108: 16588-93. PMID 21949362 DOI: 10.1073/Pnas.1113621108 |
0.585 |
|
2010 |
Beckham GT, Bomble YJ, Matthews JF, Taylor CB, Resch MG, Yarbrough JM, Decker SR, Bu L, Zhao X, McCabe C, Wohlert J, Bergenstråhle M, Brady JW, Adney WS, Himmel ME, et al. The O-glycosylated linker from the Trichoderma reesei Family 7 cellulase is a flexible, disordered protein. Biophysical Journal. 99: 3773-81. PMID 21112302 DOI: 10.1016/J.Bpj.2010.10.032 |
0.335 |
|
2010 |
Watanabe S, Resch M, Lilyestrom W, Clark N, Hansen JC, Peterson C, Luger K. Structural characterization of H3K56Q nucleosomes and nucleosomal arrays. Biochimica Et Biophysica Acta. 1799: 480-6. PMID 20100606 DOI: 10.1016/J.Bbagrm.2010.01.009 |
0.575 |
|
2009 |
McBryant SJ, Klonoski J, Sorensen TC, Norskog SS, Williams S, Resch MG, Toombs JA, Hobdey SE, Hansen JC. Determinants of histone H4 N-terminal domain function during nucleosomal array oligomerization: roles of amino acid sequence, domain length, and charge density. The Journal of Biological Chemistry. 284: 16716-22. PMID 19395382 DOI: 10.1074/Jbc.M109.011288 |
0.577 |
|
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