9,354 research outputs found
MOLPHY
No full textThis is the MOLPHY (ProtML) distribution, version 2.3. Copyright (c) 1992-1996, Jun Adachi & Masami Hasegawa. All rights reserved. MOLPHY is a program package for MOLecular PHYlogenetics.MOLPHY is a free software, and you can use and redistribute it. The programs are written in a standard subset of C with UNIX-like OS. The utilities are written in the "Perl" (Ver.4.036) with UNIX-like OS. MOLPHY has been tested on SUN4\u27s (cc & gcc with SUN-OS 4.1.3) and HP9000/700 (cc, c89 & gcc with HP-UX 9.05). However, MOLPHY has NOT been tested on VAX, IBM-PC, and Macintosh
Proline-rich tyrosine kinase 2 mediates gonadotropin-releasing hormone signaling to a specific extracellularly regulated kinase-sensitive transcriptional locus in the luteinizing hormone beta-subunit gene
No full textG protein-coupled receptor regulation of gene transcription primarily occurs through the phosphorylation of transcription factors by MAPKs. This requires transduction of an activating signal via scaffold proteins that can ultimately determine the outcome by binding signaling kinases and adapter proteins with effects on the target transcription factor and locus of activation. By investigating these mechanisms, we have elucidated how pituitary gonadotrope cells decode an input GnRH signal into coherent transcriptional output from the LH beta-subunit gene promoter. We show that GnRH activates c-Src and multiple members of the MAPK family, c-Jun NH2-terminal kinase 1/2, p38MAPK, and ERK1/2. Using dominant-negative point mutations and chemical inhibitors, we identified that calcium-dependent proline-rich tyrosine kinase 2 specifically acts as a scaffold for a focal adhesion/cytoskeleton-dependent complex comprised of c-Src, Grb2, and mSos that translocates an ERK-activating signal to the nucleus. The locus of action of ERK was specifically mapped to early growth response-1 (Egr-1) DNA binding sites within the LH beta-subunit gene proximal promoter, which was also activated by p38MAPK, but not c-Jun NH2-terminal kinase 1/2. Egr-1 was confirmed as the transcription factor target of ERK and p38MAPK by blockade of protein expression, transcriptional activity, and DNA binding. We have identified a novel GnRH-activated proline-rich tyrosine kinase 2-dependent ERK-mediated signal transduction pathway that specifically regulates Egr-1 activation of the LH beta-subunit proximal gene promoter, and thus provide insight into the molecular mechanisms required for differential regulation of gonadotropin gene expression
C1s and F1s photoelectron angular distribution from oriented CH3F molecules: a combined theoretical TDDFT and experimental study
No full textauthor
No full textauthorIn other places [Old Joe, the trapper] pointed out otter (or, as he pronounced it, "author") slidesPRINTED ITEM G.M.Story April 1959Not UsedNot UsedWithdrawn[see 'otter']Checked by Jordyn Hughes on Thu 09 Jun 201
Jia ru ju he wu dui jun yun tuan liu ji jun yun tuan liu dui liu de ying xiang
No full textWong, Chai Kwok = 加入聚合物對均勻湍流及均勻湍流對流的影響 / 黃濟國.Thesis M.Phil. Chinese University of Hong Kong 2013.Includes bibliographical references (leaves 89-91).Abstracts also in Chinese.Title from PDF title page (viewed on 01, November, 2016).Wong, Chai Kwok = Jia ru ju he wu dui jun yun tuan liu ji jun yun tuan liu dui liu de ying xiang / Huang Jiguo
Author Correction: Manipulating anion intercalation enables a high-voltage aqueous dual ion battery
No full textThe original version of this Article did not acknowledge Prof. Jun Fan as a corresponding author. This has now been corrected in both the PDF and HTML versions of the Article.link_to_subscribed_fulltex
抗線維化薬を志向した選択的TGF-B RII阻害剤の開発
No full text博士論文 要旨Abstract/本文Full以下に掲載：ACS Medicinal Chemistry Letters 12(5) pp.745-751 2021. American Chemical Society. 共著者：Shohei Miwa, Masahiro Yokota, Yoshifumi Ueyama, Katsuya Maeda, Yosuke Ogoshi, Noriyoshi Seki, Naoki Ogawa, Jun Nishihata, Akihiro Nomura, Tsuyoshi Adachi, Yuki Kitao, Keisuke Nozawa, Tomohiro Ishikawa, Yutaka Ukaji, Makoto Shiozak
Data for proteomic analysis of ATP-binding proteins and kinase inhibitor target proteins using an ATP probe
No full textAbstractInteractions between ATP and ATP-binding proteins (ATPome) are common and are required for most cellular processes. Thus, it is clearly important to identify and quantify these interactions for understanding basic cellular mechanisms and the pathogenesis of various diseases. We used an ATP competition assay (competition between ATP and acyl-ATP probes) that enabled us to distinguish specific ATP-binding proteins from non-specific proteins (Adachi et al., 2014) [1]. As a result, we identified 539 proteins, including 178 novel ATP-binding protein candidates. We also established an ATPome selectivity profiling method for kinase inhibitors using our cataloged ATPome list. Normally only kinome selectivity is profiled in selectivity profiling of kinase inhibitors. In this data, we expand the profiled targets from the kinome to the ATPome through performance of ATPome selectivity profiling and obtained target profiles of staurosporine and (S)-crizotinib. The data accompanying the manuscript on this approach (Adachi et al., 2014) [1] have been deposited to the ProteomeXchange with identifier http://www.ebi.ac.uk/pride/archive/projects/PXD001200
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