Measurement of the e+e-→D(*)+D(*)- cross sections

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Chromatin structure and binding proteins can affect transcription through multiple avenues.

<p>Chemical additions can be made to histones by chromatin-modifying enzymes such as Set1, which adds methyl groups to a specific place on the histone (1); many of these chemical modifications can be removed by other proteins (2). Some proteins bind to specific modifications on histones that have been added (3). Nucleosome spacing (4) can be altered by chromatin remodelers that use the power of ATP to drive movement and histone chaperones (5) can remove and replace histones on DNA. All of these factors can control access of the DNA and chromatin to other factors, such as transcription factors that may need to bind open pieces of DNA (6). This is a dynamic process requiring many proteins to act in concert as appropriate.</p

Cellular responses to stress and environmental factors.

<p>Stresses such as heat shock are sensed by factors located inside of or outside of the cell (1). In the case of HSF1, it relays the message to the nucleus (2) to strongly increase the transcription of genes involved in fixing protein shape (3). RNA stability (4) and protein production levels (5) are also important factors determining the response to stress. Protein activity (6), such as the chaperones induced by heat shock, is critical in mediating the response. In higher eukaryotes, cells may send signals (7) to neighboring cells to assist in mounting a larger stress response encompassing many cells and tissues.</p

Identification and conservation of a NRF-2/GABP binding site in the 5′-UTR of

<p><b>Copyright information:</b></p><p>Taken from "The gene encoding the fragile X RNA-binding protein is controlled by nuclear respiratory factor 2 and the CREB family of transcription factors"</p><p>Nucleic Acids Research 2006;34(4):1205-1215.</p><p>Published online 25 Feb 2006</p><p>PMCID:PMC1383620.</p><p>© The Author 2006. Published by Oxford University Press. All rights reserved</p> () Sequence alignment of homologs from several species showing a newly identified binding site for NRF-2. GenBank accession nos are as follows: (), (), (), (), (), (), (), () and (). The major transcription start site as identified in humans is shown and numbering is based on the human sequence (). Nucleotides conserved in all nine species are indicated with an asterisk. The underlined bases in the NRF-2 human sequence represent those changed for mutational analysis and the changes are shown in italics above the site. () Identification of the zebrafish promoter (GenBank accession no. ) and alignment with the human promoter (accession no. ). Boxes represent protein binding sites known to operate in humans that are conserved in zebrafish. Underlined sites represent potential positional differences between the two species for these factors. Conserved nucleotides are denoted with an asterisk

固有振動問題における領域最適化解析 (質量最小化問題)

We present a practical method of numerical analysis for oprimization problems of domains in which natural vibration problems of linear elastic bodies are defined. In this paper, we apply the traction method that was proposed as a solution to the domain optimization problems to elliptic boundary value problems. The problems treated are those which determine the domain that minimizes a mass under constraints in specified vibration eigenvalues. Using the Lagrange multiplier method, we obtain the shape gradient functions for these domain optimization problems from the optimality criteria. A numerical analysis technique for the multiconstraint problems is also presented. We show the successful resolution of the problems of beamlike plates clamped at both ends.journal articl