نتایج جستجو برای: α2
تعداد نتایج: 4557 فیلتر نتایج به سال:
Many neuroimaging studies have demonstrated the different functional contributions of spatially distinct brain areas to working memory (WM) subsystems in cognitive tasks that demand both local information processing and interregional coordination. In WM cognitive task paradigms employing electroencephalography (EEG), brain rhythms such as θ and α have been linked to specific functional roles ov...
The sulphhydryl environment in various mixed-metal hybrid hemoglobins, viz. α2(Cu)β2(FeCO), α2(FeCO)-β2(Cu), α2(Cu)-β2(Ni), α2(Ni)-β2(Cu), was studied by reacting them with the sulphhydryl reagent, 4,4′-dithiodipyridine (4-PDS). The reactivity was compared with that of HbCO, NiHb and CuHb. It is found that there exists a correlation between conformational change and metal ion environment, not o...
These studies examined the effects of α1- and α2-adrenoreceptor blockade in the anteroventral portion of the third cerebral ventricle (AV3V) on modification of baroreflex-induced changes in heart rate and renal sympathetic nerve activity (RSNA) induced by hyperosmolality. Local administration of hypertonic artificial cerebrospinal fluid (aCSF) in the AV3V significantly increased baroreflex-indu...
OBJECTIVE Alpha thalassemia syndromes are caused by mutations on one or more of the four α-globin genes. Mutations could be either more commonly deletional or non-deletional. As some deletions (3.7 and 4.2) cause α+-thalassemia, some cause (-20.5, MED, THAI, FIL) α0 -thalassemia. The aim of this study was to determine alpha thalassemia mutations in patients with unsolved hypochromic microcytic ...
Death receptor activation triggers recruitment of FADD, which via its death effector domain (DED) engages the DEDs of procaspase 8 and its inhibitor FLIP to form death-inducing signalling complexes (DISCs). The DEDs of FADD, FLIP and procaspase 8 interact with one another using two binding surfaces defined by α1/α4 and α2/α5 helices, respectively. Here we report that FLIP has preferential affin...
(a) D: α0 = 1, α1 = 1, α2 = 1. χ(D ) = 1. (b) S: α0 = 1, α1 = 0, α2 = 1. χ(S ) = 2. (c) Möbius band: α0 = 1, α1 = 2, α2 = 1. χ(M) = 0. (d) Mg of genus g: α0 = 1, α1 = 2g, α2 = 1. χ(Mg) = 2− 2g. 6. RP n = (R − {0})/{z ∼ λz} = S/{z ∼ −z} = S/Z2 RP n = σ ∪ RP n−1 implies RP n = σ ∪ σn−1 ∪ · · · ∪ σ χ(RP ) = 1 for n even and 0 for n odd. 7. CP n = (C − {0})/{z ∼ λz} = S/{z ∼ λz||λ| = 1} CP n = σ ∪ ...
We present a preliminary measurement of the electron angular distribution parameter α2 in W → eν events using data collected by the DØ detector during the 1994–1995 Tevatron run. We compare our results with next-toleading order perturbative QCD, which predicts an angular distribution of (1±α1 cosθ∗+α2 cosθ), where θ∗ is the angle between the charged lepton and the antiproton in the Collins-Sope...
Although it is generally recognized that certain α-subunits of γ-aminobutyric acid type A receptors (GABAARs) form enriched clusters on the axonal initial segment (AIS), the degree to which these clusters vary in different brain areas is not well known. In the current study, we quantified the density, size, and enrichment ratio of fluorescently labeled α1-, α2-, or α3-subunits aggregates co-loc...
Escherichia coli ribonucleotide reductase is an α2β2 complex that catalyzes the conversion of nucleotides to deoxynucleotides using a diferric-tyrosyl radical (Y122•) cofactor in β2 to initiate catalysis in α2. Each turnover requires reversible long-range proton-coupled electron transfer (PCET) over 35 Å between the two subunits by a specific pathway (Y122• ⇆ [W48?] ⇆ Y356 within β to Y731 ⇆ Y7...
Escherichia coli class I ribonucleotide reductase (RNR) catalyzes the conversion of nucleotides to deoxynucleotides and is composed of two subunits: α2 and β2. β2 contains a stable di-iron tyrosyl radical (Y(122)(•)) cofactor required to generate a thiyl radical (C(439)(•)) in α2 over a distance of 35 Å, which in turn initiates the chemistry of the reduction process. The radical transfer proce...
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