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1 orm the protein translocating element of the Tat system.
2 Pmut3* exported to the periplasm through the Tat system.
3 ated that Mycobacterium smegmatis contains a TAT system.
4 but not because of reversion to a functional TAT system.
5 nal recognition particle (SRP), and Delta pH/Tat systems.
6 ly, with 24% dissymmetry in a triazatruxene (TAT) system.
7 s introduce the twin-arginine translocation (Tat) systems.
8                                              Tat systems accomplish this feat with three membrane com
9 cent progress on the characterization of the Tat system and critically discuss the structure and oper
10   The pectin lyase, PnlH, is exported by the Tat system and is somehow targeted to the outer membrane
11  highlight the remarkable flexibility of the Tat system and its potential for studying and engineerin
12                    However, the roles of the Tat system and related substrates in Brucella remain unc
13 upon a functional twin arginine translocase (Tat) system and a Tat signal sequence.
14 ansported to the periplasm of E. coli by the tat system, and the corresponding B polypeptides of CT,
15                 Although the genetics of the Tat system are reasonably well-defined in Escherichia co
16 pan from this Tat(BC) fusion inactivates the Tat system but does not affect assembly of the core comp
17 assembly cycle could explain how the DeltapH/Tat system can assemble translocases to accommodate fold
18               We conclude that, in vivo, the Tat system can reject substrates at a late stage in tran
19 n bacteria, the twin arginine translocation (Tat) system can transport folded proteins.
20 A and tatC encode components of a functional Tat system capable of exporting characteristic Tat subst
21                                          The Tat system catalyzes the transport of folded globular pr
22  not require a twin arginine motif and known Tat system components.
23                                The thylakoid Tat system comprises three membrane components.
24                                         Many Tat systems consist of three essential membrane componen
25           However, it is unknown whether the TAT system contributes in any way to virulence through t
26 strate that the twin arginine translocation (Tat) system contributes to bacterial resistance to catio
27                                The thylakoid Tat system employs three membrane components and the pH
28                                  Because the Tat system exports only folded proteins, this result imp
29 several virulence factors that depend on the TAT system for proper export to the periplasm, outer mem
30                                          The Tat system, found in the cytoplasmic membrane of many ba
31             The twin-arginine translocation (Tat) system, found in prokaryotes, chloroplasts, and som
32                                          The Tat system has been shown to operate in the plasma membr
33 ve important consequences for the use of the Tat system in biotechnology applications where high leve
34                                          The Tat system in Escherichia coli is composed of TatA, TatB
35 atB, and tatC) are required for a functional TAT system in M. smegmatis.
36 between the mechanistically distinct Sec and Tat systems in the assembly of a single integral membran
37 demonstrate the functional activity of these Tat systems in vivo, since expression of the tatABC oper
38 000 is a multifactorial process and that the Tat system is an important virulence determinant of this
39 m of membrane integration of proteins by the Tat system is fundamentally distinct from that employed
40               Targeting of substrates to the Tat system is mediated by the presence of an N-terminal
41  biological membranes, the DeltapH-dependent/Tat system is unusual in its sole reliance upon the tran
42                                          The Tat system is used to transport folded proteins across t
43 richia coli twin-arginine protein transport (Tat) system is a molecular machine dedicated to the tran
44 ylakoid twin arginine protein translocation (Tat) system is thought to have a multivalent receptor co
45 tA, the protein-translocating element of the Tat system, is a small transmembrane protein that assemb
46                                          The Tat system may need to transport flexibly folded protein
47                 Twin-arginine translocation (Tat) systems mediate the transmembrane translocation of
48                         The Escherichia coli Tat system mediates Sec-independent export of protein pr
49 scherichia coli twin arginine translocation (Tat) system mediates Sec-independent export of protein p
50     The twin-arginine protein translocation (Tat) system mediates transport of folded proteins across
51  functioning in alternative respiration, the TAT system of A. tumefaciens is an important virulence d
52                                          The Tat system of Escherichia coli is made up of TatA, TatB,
53 anslocated into the periplasmic space by the Tat system of Escherichia coli.
54 tructural and functional conservation in the Tat systems of these three bacterial species.
55                 Twin arginine translocation (Tat) systems of thylakoid and bacterial membranes transp
56 ylakoid twin arginine protein translocation (Tat) system operates by a cyclical mechanism in which pr
57 plasm using the twin-arginine translocation (Tat) system, or fused to an integral plasma membrane pro
58 e action of the twin-arginine translocation (Tat) system propose that substrates bind initially to th
59                                          The TAT system proved essential for the export of phospholip
60             The twin-arginine translocation (TAT) system secretes fully folded proteins that contain
61                         The Escherichia coli Tat system serves to export folded proteins harbouring a
62             The twin-arginine translocation (Tat) system serves to translocate folded proteins across
63             The twin-arginine translocation (Tat) system targets cofactor-containing proteins across
64 eins), is based on the unique ability of the Tat system to efficiently cotranslocate noncovalent comp
65 we utilized the twin arginine translocation (tat) system to produce fluorescent CT chimeras, as well
66 ribution of the twin-arginine translocation (Tat) system to the physiology of DC3000.
67         The twin arginine protein transport (Tat) system translocates folded proteins across the cyto
68                                              Tat systems transport completely folded proteins across
69                                              Tat systems transport folded proteins across energized m
70                 Twin-arginine translocation (Tat) systems transport folded proteins across cellular m
71                     Twin arginine transport (Tat) systems transport folded proteins using proton-moti
72                 Twin arginine translocation (Tat) systems transport large folded proteins across seal
73                                          The Tat system transports folded proteins across bacterial a
74                                          The Tat system transports folded proteins across bacterial p
75             The twin-arginine translocation (Tat) system transports folded proteins across bacterial
76             The twin-arginine translocation (Tat) system transports folded proteins across bacterial
77             The twin-arginine translocation (Tat) system transports folded proteins across the bacter
78             The twin-arginine translocation (Tat) system transports folded proteins across the bacter
79                 The twin arginine transport (Tat) system transports folded proteins across the prokar
80 hat the thylakoid twin-arginine translocase (Tat) system transports folded proteins in a unidirection
81 scherichia coli twin-arginine translocation (Tat) system transports fully folded and assembled protei
82 he mechanism and capabilities of the E. coli Tat system using green fluorescent protein (GFP) fused t
83 haviour of reporter proteins targeted to the Tat system was analysed in more detail.
84                   To verify that loss of the Tat system was responsible for the various phenotypes ex
85 ins through the twin-arginine translocation (Tat) system, we screened a collection of E. coli mutant
86 y mutations affecting the PrsDE (Type I) and TAT systems were observed to affect the growth phenotype
87        These results imply a novel aspect of Tat systems, whereby multiple precursor-binding sites ca
88 tionally to the twin-arginine translocation (Tat) system which transports folded substrates across th