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1 ectively, and determine the structure of the activated complex.
2 links two Toll receptor molecules to form an activated complex.
3 s of the dimer are farther apart than in the activated complex.
4 these snapshots primarily capture the fully activated complex.
5 e exchange before transitioning to the fully activated complex.
6 -EM, by blocking its transition to the fully activated complex.
7 5 protein were simultaneously present in the activated complexes.
9 ith preexisting CP spots, demonstrating that activated complexes accumulate in previously formed CPs
12 eversible albeit unfavorable formation of an activated complex, and natural-abundance 13C NMR kinetic
13 latter in MeOH occurred via a four-centered activated complex, and subsequent hydrolysis of the resu
14 subtle differences in the SID spectra of the activated complex are also observed as a function of tra
15 However, at high salt, interactions of the activated complex are limited to a more restricted set o
17 bstrate interactions requires the use of the activated complex as the interacting chaperonin species.
18 ition from the precatalytic complex B to the activated complex B(act) and leads to widespread intron
19 o M(+)1(red) during electron transfer in the activated complexes, [BPH(2), M(+)1], contributions of i
20 The rate of formation and breakdown of the activated complex can be determined from an analysis of
21 on the inflammatory response induced by the activated complex composed of the latter coreceptor in t
23 r collect relevant values for all stable and activated complexes defined by the reaction scheme and h
26 ansfer, and as a result, the [Bz(.+)(H2O)n]* activated complexes either undergo dissociative proton t
28 folding rate when, as is often the case, the activated complex exposes more backbone than is exposed
30 u(OTf)(2), which serves as a source of P(IV)-activated complex for nitriles to react under the Ritter
36 olding landscape such that a metastable "pre-activated" complex forms before the thermodynamically mo
37 roteins, clears activators of complement and activated complexes from portal blood without obvious in
38 ibuted to the formation in the plasma of the activated complex H(2)O(2)* followed by its stabilizatio
39 s study presents an approach for probing the activated complex in a reaction by negative ion photodet
40 accelerated rate (8-fold increase) when the activated complex instead of the nucleotide-free complex
42 ition zone, and their energetically distinct activated complexes leading to exchange gives evidence o
43 e charge delocalization stabilization of the activated complex of enediynes containing acceptor subst
44 converge in the nucleus of cells to form an activated complex of transcription factor activator prot
45 lular receptor (JH receptor [JHR]), a ligand-activated complex of transcription factors consisting of
47 We report here that in response to insulin, activated complexes of IRS-1.PI 3-kinase can be immunopr
48 main fragment band, the fully allosterically activated complexes of T127L and CRP show the amino-term
49 nzymes are complementary in structure to the activated complexes of the reactions they catalyze has p
50 ed either in control of translocation of the activated complex or in modulation of its DNA binding pr
52 ic transition state with the assembly of the activated complex requiring an equivalent of water at lo
58 The Arrhenius equation (ln k vs. 1/T) and activated complex theory (ln k/T vs. 1/T) were used to e
60 ed proton transfers in a six-membered cyclic activated complex (TS1), which involves two hydrogen-bon
62 concentration of the T-cell-receptor-ligand-activated complex, which transfers the signal to downstr