戻る
「早戻しボタン」を押すと検索画面に戻ります。 [閉じる]

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 changes in solvent-accessible surface areas (SASA).
2 us proteins, including KaiA, KaiB, KaiC, and SasA.
3 40H) x Ade(a) and E(40H) x Ade(s), have zero SASA.
4                                              SasA, a circadian clock-output protein, binds to the CI
5                                 We find that SasA, a circadian sensor histidine kinase associated wit
6                                              SasA, a clock-associated histidine kinase, is necessary
7                                              SasA acts as a kinase toward RpaA, whereas CikA, previou
8                                            N-SasA adopts a canonical thioredoxin fold but lacks the c
9             Because the clock output protein SasA also binds to CI and competes with KaiB for binding
10       Using solvent-accessible surface area (SASA) analysis, we identify key cysteine residues suscep
11 lated by two antagonistic histidine kinases, SasA and CikA, which are sequentially activated at disti
12 eins and a set of output signaling proteins, SasA and CikA, which transduce this rhythm to control ge
13 he mutually antagonistic signaling proteins, SasA and CikA.
14 Its advantage is that the footprint reflects SASA and hydrogen bonding, whereas one drawback is the l
15 ts that the structural differences between N-SasA and KaiB are the result of only a few critical amin
16 e no clear details to suggest competition of SasA and KaiB for KaiC binding.
17                                            N-SasA and KaiB share significant sequence similarity and,
18       Here, we report the NMR structure of N-SasA and show it to be different from that of KaiB.
19  stability, solvent-accessible surface area (SASA), and ionic, aromatic, and van der Waals interactio
20 ve time, communicate temporal information to SasA, and may control access to promoter elements by imp
21 mponents and associated regulators (CikA and SasA) buffers stochastic variations in protein levels.
22             Solvent accessible surface area (SASA) calculations on all the five MD structures shows t
23  output-independent pathway, suggesting that SasA can influence entrainment through direct interactio
24 lfactory epithelium (SORB, SORF, all SVR and Sasa CaSR sequences), testis (SORB, SORD and Sasa CaSR)
25 Sasa CaSR sequences), testis (SORB, SORD and Sasa CaSR) and/or anterior kidney (SORB and Sasa CaSR).
26  Sasa CaSR) and/or anterior kidney (SORB and Sasa CaSR).
27                       A family of sequences (Sasa CaSR1-6), isolated using the same degenerate primer
28 iate global transcription via output factors SasA, CikA, LabA, RpaA, and RpaB.
29  show that KaiB and the clock-output protein SasA compete for overlapping binding sites, which includ
30  have an alternating pattern of high and low SASA consistent with a beta strand structure.
31                                     CikA and SasA cooperate to generate an oscillation of RpaA activi
32                          In 2001, Hatano and Sasa derived a testable prediction of this theory.
33  mutation in the central circadian regulator sasA disrupted both the phase and amplitude of the circa
34 query according to amino acids, buried area (SASA), energy or keywords related to indication areas, e
35 al (p)ppGpp synthetase in Bacillus subtilis, sasA, exhibits high levels of extrinsic noise in express
36 rs; rare cells with unusually high levels of sasA expression, having increased antibiotic tolerance.
37 urviving antibiotic treatment increases with sasA expression.
38    We suggest that this surface is used by N-SasA for protein-protein interactions.
39 (beta), and solvent accessible surface area (SASA, gamma) terms.
40 hose in the previously reported trees of the sasA gene and the kaiBC operon, two other elements of th
41 (PCC 7942) the kai genes A, B, and C and the sasA gene encode the functional protein core of the timi
42 ions in the Synechococcus adaptive sensor A (sasA) gene that produce nearly WT rhythms of gene expres
43                              The ability of <SASA&gt; data from HR-HRPF to differentiate molecular model
44 ality was found to be comparable to that of <SASA&gt; data obtained from X-ray crystal structures, indic
45 oreover, we demonstrated the ability to use <SASA&gt; measurements from HR-HRPF to differentiate molecul
46               The accuracy of the resulting <SASA&gt; measurements was tested by using well-characterize
47 te average solvent accessible surface area (<SASA&gt;) of amino acid side chains.
48 ns, analyzing parameters such as RMSD, RMSF, SASA, H-bond, and RoG profiles.
49 ctions as the sensory domain controlling the SasA histidine kinase activity.
50  and stable Solvent Accessible Surface Area (SASA), indicating robust ligand-receptor binding.
51             The N-terminal domain of SasA (N-SasA) interacts directly with KaiC and likely functions
52 tral timing mechanism, and the sensor kinase SasA is a primary transducer of temporal information.
53                                 We find that sasA is regulated by multisite phosphorylation of the tr
54                                     Although sasA is required for global gene expression rhythmicity,
55 shares a sequence-homologous domain with the SasA kinase.
56                             Mutations in the sasA locus cause defective fruiting body formation, redu
57                                The wild-type sasA locus has been located on a 14-kb cloned fragment o
58                                  A wild-type sasA locus is critical for Myxococcus xanthus multicellu
59                 These data indicate that the sasA locus is required for the biosynthesis of O-antigen
60 s genes are similar to those of the original sasA locus mutants.
61 nce of a 7-kb region containing the complete sasA locus was determined.
62 and sporulation result from mutations in the sasA locus, which encodes the wzm wzt wbgA (formerly rfb
63                  Mutants carrying these same sasA mutations are defective in social motility and form
64                     The N-terminal domain of SasA (N-SasA) interacts directly with KaiC and likely fu
65 ibited a degree of correlation with the mean SASA of whole residues within each peptide segment, HDX
66 uantify the solvent accessible surface area (SASA) of beta1 strand residues in the GABAA beta3 homope
67  "mark" the solvent accessible surface area (SASA) of proteins to reflect protein HOS.
68 ctions, the solvent accessible surface area (SASA) of the ligands, and stabilization of key structura
69         The solvent accessible surface area (SASA) of the polypeptide chain plays a key role in prote
70 s and both solvent-accessible surface areas (SASAs) of methionine residues (Pearson's r = 0.78, p < 0
71 ly more active than expected from either the SASA or hydrogen bonding status of the exchangeable amid
72 esidues (Pearson's r = 0.78, p < 0.0001) and SASAs per residue in methionine-lacking peptides (Pearso
73 by the Kai proteins on the rate at which the SasA protein autophosphorylates.
74 nmentally sensitive NblS-RpaB system and the SasA-RpaA clock output system integrate relevant extra-
75                                          The SasA-RpaA two-component system constitutes a key output
76 onequilibrium systems, supporting Hatano and Sasa's proposed extension of thermodynamics to arbitrary
77 assembly sites (S. aureus surface protein A (SasA), SasD, SasF and SasK) do not.
78 ividuals revealed eight more genes including sasA/sraP, darA/pstA, and rsbU with signals of adaptive
79 inning of rfbA, produced less O-antigen than sasA+ strains.
80                                              SasA uses structural mimicry to cooperatively recruit th
81 Furthermore, the expression of both fdgA and sasA was partially dependent on the C-signal.
82 required for the developmental expression of sasA, which is also involved in the biosynthesis of the