コーパス検索結果 (1語後でソート)
通し番号をクリックするとPubMedの該当ページを表示します
1 ry metabolism and metabolic regulation of C. acetobutylicum.
2 cterization of Rex-mediated regulation in C. acetobutylicum.
3 le in the solventogenic shift of Clostridium acetobutylicum.
4 rmation and oxidative stress tolerance in C. acetobutylicum.
5 h from acidogenesis to solventogenesis in C. acetobutylicum.
6 FeFe]-hydrogenase (H(2)ase) from Clostridium acetobutylicum.
7 hogenesis and solventogenesis in Clostridium acetobutylicum.
8 f the TCA cycle and central metabolism of C. acetobutylicum.
9 same as that in B. subtilis and Clostridium acetobutylicum.
10 ydF, and hydG from the bacterium Clostridium acetobutylicum.
11 on of solvent formation genes in Clostridium acetobutylicum.
12 the highest (ca. 200 mM) ever reported in C. acetobutylicum.
13 racis, Staphylococcus aureus and Clostridium acetobutylicum.
14 yrate kinase, respectively, from Clostridium acetobutylicum.
15 operons of Bacillus subtilis and Clostridium acetobutylicum.
16 in reaction mixtures containing Clostridium acetobutylicum 2[4Fe-4S]-ferredoxin and [Fe-Fe]-hydrogen
17 ADHE of Escherichia coli (49%), Clostridium acetobutylicum (44%), and E. histolytica (43%) and lesse
18 Importantly, analysis of the proteome of C. acetobutylicum 824 by electrospray ionization-mass spect
21 ly map the metabolic pathways of Clostridium acetobutylicum, a soil bacterium whose major fermentatio
22 Acetoacetate decarboxylase from Clostridium acetobutylicum (AAD) catalyzes the decarboxylation of ac
23 n vitro gel retardation experiments using C. acetobutylicum adc and C. beijerinckii ptb promoter frag
24 es reveal the first structure of Clostridium acetobutylicum alcohol dehydrogenase (CaADH), a protein
25 ative to the anaerobic bacterium Clostridium acetobutylicum, an organism well-known for its historica
27 tional copies were identified in Clostridium acetobutylicum and Staphylococcus aureus, indicating con
28 arity to a glucanohydrolase from Clostridium acetobutylicum and SusG had high similarity to amylases
32 ryl-CoA dehydrogenase (BCD) from Clostridium acetobutylicum are responsible for the formation of buty
36 the solvent-producing bacterium Clostridium acetobutylicum ATCC 824 has been determined by the shotg
41 lly reproduce ABE fermentations of the WT C. acetobutylicum (ATCC 824), as well as its mutants, using
42 ated endospore-forming bacterium Clostridium acetobutylicum, attesting to their importance in the fun
43 iation of endospore formation in Clostridium acetobutylicum, but genes encoding key phosphorelay comp
46 ty of an [FeFe]-hydrogenase from Clostridium acetobutylicum (CaH2ase) immobilized on single-wall carb
47 dy of an [FeFe]-hydrogenase from Clostridium acetobutylicum (CaHydA), we now report electrochemical a
49 rom Chamydomonas reinhardtii and Clostridium acetobutylicum) can be covalently attached to functional
50 into a clostridial chromosome--here, the C. acetobutylicum chromosome--with the aim of altering cell
51 genesis pathway and of the cellulosome of C. acetobutylicum comprise a new set of metabolic capacitie
52 from the Gram-positive anaerobe Clostridium acetobutylicum confirms key features of its sophisticate
53 ol-ethanol (ABE) fermentation by Clostridium acetobutylicum, during which cells convert carbon source
54 A becomes the fourth most abundant RNA in C. acetobutylicum, excluding ribosomal RNAs and transfer RN
55 es between CdSe nanocrystals and Clostridium acetobutylicum [FeFe] hydrogenase I (CaI) enabled light-
57 mercaptopropionic acid (MPA) and Clostridium acetobutylicum [FeFe]-hydrogenase I (CaI) that photocata
59 ical and genetic approaches, we show that C. acetobutylicum forms Asn and Asn-tRNA(Asn) by tRNA-depen
61 Analysis of the Gram-positive Clostridium acetobutylicum genome reveals an inexplicable level of r
66 e [FeFe] hydrogenase, HydA, from Clostridium acetobutylicum in the non-nitrogen-fixing cyanobacterium
68 est an autostimulatory role for sigmaF in C. acetobutylicum, in contrast to the model organism for en
70 that the five orphan histidine kinases of C. acetobutylicum interact directly with Spo0A to control i
78 PHX genes in all these genomes except for C. acetobutylicum (not PHX), and B. subtilis, and B. halodu
81 om Chlamydomonas reinhardtii and Clostridium acetobutylicum, only one of which has a chain of redox r
82 ntative production of acetone by Clostridium acetobutylicum provided a crucial alternative source of
84 om Chlamydomonas reinhardtii and Clostridium acetobutylicum, react with O2 according to the same mech
90 program of the solvent-tolerant Clostridium acetobutylicum strain 824(pGROE1) and the plasmid contro
92 is of 824(pMSPOA) (a spo0A-overexpressing C. acetobutylicum strain with enhanced sporulation) against
94 e transcriptional program of two Clostridium acetobutylicum strains (SKO1 and M5) relative to that of
95 ry of the development of omics studies of C. acetobutylicum, summarize the recent application of quan
96 nt industrial and model organism Clostridium acetobutylicum, the spoIIE gene was successfully disrupt
99 tion of these proteins can allow Clostridium acetobutylicum to survive and even grow in oxygenated cu
104 rial biofuel-producing bacterium Clostridium acetobutylicum, which previously lacked robust integrati
105 identified in B. subtilis are missing in C. acetobutylicum, which suggests major differences in the