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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
15  to the accessory Sec system is an accessory SecA protein called SecA2.
16                                    Bacterial SecA proteins can be categorized by the presence or abse
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
22              The enzymatic activities of two SecA proteins from the same microorganism have not been
23 teraction with SecA, no reciprocal study for SecA protein has been reported to date.
24 ues to determine the oligomeric structure of SecA protein in solution.
25                      Increasing the level of SecA protein in the cell was found to reverse this slow-
26 rtance of the early amino-terminal region of SecA protein in the functioning of this domain, and demo
27  of this domain in regulating penetration of SecA protein into the inner membrane.
28                                          The SecA protein is present in all bacteria, and it is a cen
29                         We produced a mutant SecA protein lacking residues 2-11, which was found to e
30          Furthermore, a hyperactive Azi-PrlD SecA protein of E. coli had increased PPXD and C-domain
31 eport the three-dimensional structure of the SecA protein of Mycobacterium tuberculosis.
32          The identification of an additional SecA protein, particularly in Gram-positive pathogens, h
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
36                                Azi- and PrlD-SecA proteins that confer azide-resistant and signal seq
37                                              SecA protein, the ATPase promoting translocation of prot
38 t of a small group of bacteria that have two SecA proteins: the canonical SecA (SecA1) and a second,
39                                   Binding of SecA protein to geneX-secA RNA or various mutant derivat
40 rystal structure of the Thermus thermophilus SecA protein (TtSecA).
41                   The level of Azi- and PrlD-SecA protein was also elevated in inverted membrane vesi
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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