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1 links two Toll receptor molecules to form an activated complex.
2 s of the dimer are farther apart than in the activated complex.
3 ectively, and determine the structure of the activated complex.
4 5 protein were simultaneously present in the activated complexes.
6 ith preexisting CP spots, demonstrating that activated complexes accumulate in previously formed CPs
9 eversible albeit unfavorable formation of an activated complex, and natural-abundance 13C NMR kinetic
10 latter in MeOH occurred via a four-centered activated complex, and subsequent hydrolysis of the resu
11 subtle differences in the SID spectra of the activated complex are also observed as a function of tra
12 However, at high salt, interactions of the activated complex are limited to a more restricted set o
13 bstrate interactions requires the use of the activated complex as the interacting chaperonin species.
14 o M(+)1(red) during electron transfer in the activated complexes, [BPH(2), M(+)1], contributions of i
15 The rate of formation and breakdown of the activated complex can be determined from an analysis of
17 r collect relevant values for all stable and activated complexes defined by the reaction scheme and h
19 ansfer, and as a result, the [Bz(.+)(H2O)n]* activated complexes either undergo dissociative proton t
21 folding rate when, as is often the case, the activated complex exposes more backbone than is exposed
23 olding landscape such that a metastable "pre-activated" complex forms before the thermodynamically mo
24 roteins, clears activators of complement and activated complexes from portal blood without obvious in
25 accelerated rate (8-fold increase) when the activated complex instead of the nucleotide-free complex
27 ition zone, and their energetically distinct activated complexes leading to exchange gives evidence o
28 converge in the nucleus of cells to form an activated complex of transcription factor activator prot
30 We report here that in response to insulin, activated complexes of IRS-1.PI 3-kinase can be immunopr
31 main fragment band, the fully allosterically activated complexes of T127L and CRP show the amino-term
32 nzymes are complementary in structure to the activated complexes of the reactions they catalyze has p
33 ed either in control of translocation of the activated complex or in modulation of its DNA binding pr
34 ic transition state with the assembly of the activated complex requiring an equivalent of water at lo
39 ed proton transfers in a six-membered cyclic activated complex (TS1), which involves two hydrogen-bon
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