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1 an EGase catalytic domain from the bacterium Thermobifida fusca.
2 ed LPMOs based on enzymes from the bacterium Thermobifida fusca.
3 3A) from the aerobic cellulolytic bacterium, Thermobifida fusca.
4 -glucosidase from the thermophilic bacterium Thermobifida fusca and inserted into the tobacco (Nicoti
5 activities of nine thermal stable mutants of Thermobifida fusca BglC were assayed by isothermal titra
6 e cellulolytic enzymes in the model organism Thermobifida fusca, but only Nocardiopsis dassonvillei s
7 nd between an inactive endocellulase mutant (Thermobifida fusca Cel6A D117Acd) and four oligosacchari
9 nserved noncatalytic active site residues of Thermobifida fusca Cel6B were constructed, cloned and ex
11 ribing the steady-state binding of MUS-CB to Thermobifida fusca cellulase Cel6A are similar to those
12 bility of a high-resolution structure of the Thermobifida fusca endocellulase Cel6A catalytic domain
14 lulase, Cel48A, formerly E6, was cloned from Thermobifida fusca into Escherichia coli and Streptomyce
18 ases in the cellulose-degrading actinomycete Thermobifida fusca is controlled by a transcriptional re
20 nced genome of the thermophilic actinomycete Thermobifida fusca revealed an orphan nonribosomal pepti
22 acterized laccase from the aerobic bacterium Thermobifida fusca The resultant chimera exhibited activ
23 Here we present two cryo-EM snapshots of the Thermobifida fusca type I-E Cascade: (1) unwinding 11 bp
25 egrading enzymes from cellulolytic bacterium Thermobifida fusca , we show that the model can be used
26 and characterizing evolution experiments on Thermobifida fusca, we were able to show that evolutiona
27 strains of the cellulolytic actinobacterium, Thermobifida fusca, were generated for two different sce
29 6, Nocardioides sp. strain JS614 TOPRIM, and Thermobifida fusca YX Tfu2914 inteins have a mixture of
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