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1 ation was obtained also for Escherichia coli SecA protein.
2 which led to the overproduction of wild-type SecA protein.
3 he translocation apparatus by binding to the SecA protein.
4 Y, SecE and SecG (SecYEG) and the peripheral SecA protein.
5 ked between amino acid residues 75 and 97 of SecA protein.
6 in in SecA2, unlike in SecA1 or conventional SecA proteins.
7 itates precursor targeting by binding to the SecA protein, a component of the membrane-embedded trans
8 was employed to generate defined peptides of SecA protein after photocross-linking with [alpha-(32)P]
9 location pathway that involves the essential SecA protein and the membrane-bound SecYEG translocon is
10 basal expression, reduced auto-repression by SecA protein, and abolished the responsiveness of secA e
11 e by overproduction of membrane-stuck mutant SecA proteins, and, in one case, a membrane-associated S
12 in translocation ATPase of Escherichia coli, SecA protein, auto-regulates its translation by binding
13 onstrate that the carboxyl-terminal third of SecA protein binds to the amino-terminal 107 amino acid
14 basal expression, reduced auto-repression by SecA protein, but retained a normal pattern of derepress
17 ong with collisional quenchers with a set of SecA proteins containing single tryptophan substitutions
18 sfer methodology with genetically engineered SecA proteins containing unique pairs of tryptophan and
19 sfer methodology with genetically engineered SecA proteins containing unique pairs of tryptophan and
20 mutational alteration, it is suggested that SecA protein contains two distinct RNA-binding sites.
21 ractionation studies which demonstrated that SecA proteins defective in this region were found almost
26 rtance of the early amino-terminal region of SecA protein in the functioning of this domain, and demo
33 translocons are saturated with ribosomes and SecA protein, reflecting the inherent affinity of these
34 acterium tuberculosis is the presence of two SecA proteins: SecA1, the essential "housekeeping" SecA,
35 Biochemical characterization of the mutant SecA proteins showed that Ser226, Val310, Ile789, Glu806
38 t of a small group of bacteria that have two SecA proteins: the canonical SecA (SecA1) and a second,
42 teria, SecA1 is the essential 'housekeeping' SecA protein whereas SecA2 is an accessory secretion fac
43 ively in their integral membrane form, while SecA proteins with defects in the low-affinity ATP-domai
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