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1 correlated with the methylation of FrzCD (a methyl-accepting chemotaxis protein).
2 omain has high homology with the eubacterial methyl-accepting chemotaxis protein.
3 main that controls input-output signaling in methyl-accepting chemotaxis proteins.
4 is bioinformatically indistinguishable from methyl-accepting chemotaxis proteins.
5 ses, cyclic-di-GMP synthases/hydrolases, and methyl-accepting chemotaxis proteins.
6 eptad stutter adjacent to the HAMP domain in methyl-accepting chemotaxis proteins.
7 e residues within the cytoplasmic domains of methyl-accepting chemotaxis proteins.
8 fused through a membrane-spanning region to methyl-accepting chemotaxis proteins.
9 ethylation changes, methylation enzymes, and methyl-accepting chemotaxis proteins.
10 s well as two genes, mcpA and mcpB, encoding methyl-accepting chemotaxis proteins.
11 lassical two-component histidine kinases and methyl-accepting chemotaxis proteins.
12 o contains a homolog of E. coli Trg or other methyl-accepting chemotaxis proteins.
13 ylated FrzCD protein, the Frz homolog of the methyl-accepting chemotaxis proteins.
14 ts with defects in any one of the four known methyl-accepting chemotaxis proteins also retained the a
15 rane signal transduction proteins, including methyl-accepting chemotaxis proteins and histidine kinas
16 ignal-transducing regulatory systems include methyl-accepting chemotaxis proteins and membrane-bound,
17 n inosine/xanthosine triphosphatase, GidA, a methyl-accepting chemotaxis protein, and a PIN domain pr
18 equires the activity of FrzCD, a cytoplasmic methyl-accepting chemotaxis protein, and FrzF, a methylt
19 HAMP (histidine kinase, adenylyl cyclase, methyl-accepting chemotaxis protein, and phosphatase) li
20 c HAMP (histidine kinase, adenylyl cyclases, methyl-accepting chemotaxis proteins, and phosphatases)
21 ied in histidine kinases, adenylyl cyclases, methyl-accepting chemotaxis proteins, and phosphatases,
22 ing in histidine kinases, adenylyl cyclases, methyl-accepting chemotaxis proteins, and some phosphata
24 nisms, such as sensory histidine kinases and methyl-accepting chemotaxis proteins, are molecular devi
25 gutted" mutant that was deleted for all four methyl-accepting chemotaxis proteins, as well as for Che
26 ent signal transduction pathway proteins and methyl-accepting chemotaxis proteins, but will be expand
28 brane proteins (PilQ, MshO, MshP, and CapK), methyl-accepting chemotaxis proteins, chemotaxis and mot
29 s of the bacterial chemotaxis proteins MCPs (methyl-accepting chemotaxis proteins), CheW, CheY and Ch
30 and difE, encoding respective homologs of a methyl-accepting chemotaxis protein, CheW, and CheA, are
33 eR (DeltacheR(3)), CheA (DeltacheA(3)) and a methyl-accepting chemotaxis protein (Deltamcp(3)) are de
36 a mutant strain of F1 in which the putative methyl-accepting chemotaxis protein-encoding gene Pput_0
39 ant, hyper-reversal mutant in the M. xanthus methyl accepting chemotaxis protein homolog, frzCD224, f
42 omal or a plasmid-encoded allele displayed a methyl-accepting chemotaxis protein localization pattern
43 therefore be considered a marker for general methyl-accepting chemotaxis protein (MCP) clustering.
46 8 amino acids of Tar4 (TtTar4H), a predicted methyl-accepting chemotaxis protein (MCP) from the stric
49 eric bacteria shuttles between transmembrane methyl-accepting chemotaxis protein (MCP) receptor compl
50 nd severely reduced in mutants with impaired methyl-accepting chemotaxis protein (MCP) signaling acti
51 pG, we examined the targeting of this single methyl-accepting chemotaxis protein (MCP) under differen
52 fied were two adjacent genes, one encoding a methyl-accepting chemotaxis protein (MCP), presumably re
54 rom CNB-1 and genetic complementation of the methyl-accepting chemotaxis protein (MCP)-null mutant CN
58 It was demonstrated previously that DifA (methyl-accepting chemotaxis protein [MCP]-like), DifC (C
60 of which encodes modular cyanobacteriochrome-methyl-accepting chemotaxis proteins (MCPs) and other pr
62 lis CheR-mediated methylation of B. subtilis methyl-accepting chemotaxis proteins (MCPs) but not of E
64 important model for transmembrane signaling, methyl-accepting chemotaxis proteins (MCPs) have been ex
66 , the che3 cluster, encoding homologs to two methyl-accepting chemotaxis proteins (MCPs), a CheW, a h
67 manner similar to that observed earlier for methyl-accepting chemotaxis proteins (MCPs), but only if
68 in product shows strong sequence identity to methyl-accepting chemotaxis proteins (MCPs), followed by
69 ng one of the genes encoding the 18 putative methyl-accepting chemotaxis proteins (MCPs), revealed th
70 Transmembrane chemoreceptors, also known as methyl-accepting chemotaxis proteins (MCPs), translate e
71 f closely resembles the signaling domains of methyl-accepting chemotaxis proteins (MCPs), which under
78 ins a conserved C-terminal module present in methyl-accepting chemotaxis proteins (MCPs); but, in con
79 In bacterial chemotaxis, the chemoreceptors [methyl-accepting chemotaxis proteins (MCPs)] transduce c
81 poly-HAMP (histidine kinase-adenylyl cyclase-methyl-accepting chemotaxis protein-phosphatase) domain
82 of two components of the CheIV cluster, the methyl-accepting chemotaxis protein PilJ and the PilJ de
83 portant role in chemotaxis by deamidation of methyl-accepting chemotaxis protein receptors (MCPs) and
84 tic analysis of the HAMP domain from the Tsr methyl-accepting chemotaxis protein resulted in a distin
85 w, potential flagellar genes, three putative methyl-accepting chemotaxis proteins, STM3138 (McpA), ST
86 ically similar sensory proteins, such as the methyl-accepting chemotaxis proteins, the transmembrane
87 element observed in many sensor kinases and methyl-accepting chemotaxis proteins, transmits signals
88 4 operon, which encodes homologues to a MCP (methyl-accepting chemotaxis protein), two CheWs, a hybri
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