Human DDX6 Blocking Peptide (CDBP0987) This Product Is for Research Use Only and Is Not Intended for Diagnostic Use

Total Page：16

File Type：pdf, Size：1020Kb

Human DDX6 blocking peptide (CDBP0987) This product is for research use only and is not intended for diagnostic use. PRODUCT INFORMATION Product Overview Blocking/Immunizing peptide for anti-DEAD-box protein 6 antibody Antigen Description This gene encodes a member of the DEAD box protein family. The protein is an RNA helicase found in P-bodies and stress granules, and functions in translation suppression and mRNA degradation. It is required for microRNA-induced gene silencing. Multiple alternatively spliced variants, encoding the same protein, have been identified. Nature Synthetic Expression System N/A Species Human Species Reactivity Human, Mouse, Dog, Rat Conjugate Unconjugated Applications Apuri, BL, ELISA Procedure None Format Lyophilized powder Size 100 μg Preservative None Storage Shipped at ambient temperature, store at -20°C. ANTIGEN GENE INFORMATION Gene Name DDX6 DEAD (Asp-Glu-Ala-Asp) box helicase 6 [ Homo sapiens ] Official Symbol DDX6 Synonyms DDX6; DEAD (Asp-Glu-Ala-Asp) box helicase 6; DEAD (Asp Glu Ala Asp) box polypeptide 6 , DEAD/H (Asp Glu Ala Asp/His) box polypeptide 6 (RNA helicase, 54kD) , HLR2; probable ATP- dependent RNA helicase DDX6; RCK; DEAD box-6; oncogene RCK; DEAD box protein 6; ATP- dependent RNA helicase p54; DEAD (Asp-Glu-Ala-Asp) box polypeptide 6; DEAD/H (Asp-Glu- 45-1 Ramsey Road, Shirley, NY 11967, USA Email: [email protected] Tel: 1-631-624-4882 Fax: 1-631-938-8221 1 © Creative Diagnostics All Rights Reserved Ala-Asp/His) box polypeptide 6 (RNA helicase, 54kD); P54; HLR2; FLJ36338; Entrez Gene ID 1656 mRNA Refseq NM_001257191 Protein Refseq NP_001244120 UniProt ID P26196 Chromosome Location 11q23.3 Pathway Deadenylation-dependent mRNA decay, organism-specific biosystem; Decapping complex, organism-specific biosystem; Decapping complex, conserved biosystem; Gene Expression, organism-specific biosystem; RNA degradation, organism-specific biosystem; RNA degradation, conserved biosystem; mRNA Decay by 5 to 3 Exoribonuclease, organism-specific biosystem; Function ATP binding; ATP-dependent helicase activity; RNA binding; RNA helicase activity; helicase activity; hydrolase activity; nucleic acid binding; nucleotide binding; protein binding; 45-1 Ramsey Road, Shirley, NY 11967, USA Email: [email protected] Tel: 1-631-624-4882 Fax: 1-631-938-8221 2 © Creative Diagnostics All Rights Reserved.

Copy Link

Recommended publications

DEAD-Box RNA Helicases in Cell Cycle Control and Clinical Therapy
cells Review DEAD-Box RNA Helicases in Cell Cycle Control and Clinical Therapy Lu Zhang 1,2 and Xiaogang Li 2,3,* 1 Department of Nephrology, Renmin Hospital of Wuhan University, Wuhan 430060, China; [email protected] 2 Department of Internal Medicine, Mayo Clinic, 200 1st Street, SW, Rochester, MN 55905, USA 3 Department of Biochemistry and Molecular Biology, Mayo Clinic, 200 1st Street, SW, Rochester, MN 55905, USA * Correspondence: [email protected]; Tel.: +1-507-266-0110 Abstract: Cell cycle is regulated through numerous signaling pathways that determine whether cells will proliferate, remain quiescent, arrest, or undergo apoptosis. Abnormal cell cycle regula- tion has been linked to many diseases. Thus, there is an urgent need to understand the diverse molecular mechanisms of how the cell cycle is controlled. RNA helicases constitute a large family of proteins with functions in all aspects of RNA metabolism, including unwinding or annealing of RNA molecules to regulate pre-mRNA, rRNA and miRNA processing, clamping protein complexes on RNA, or remodeling ribonucleoprotein complexes, to regulate gene expression. RNA helicases also regulate the activity of speciﬁc proteins through direct interaction. Abnormal expression of RNA helicases has been associated with different diseases, including cancer, neurological disorders, aging, and autosomal dominant polycystic kidney disease (ADPKD) via regulation of a diverse range of cellular processes such as cell proliferation, cell cycle arrest, and apoptosis. Recent studies showed that RNA helicases participate in the regulation of the cell cycle progression at each cell cycle phase, including G1-S transition, S phase, G2-M transition, mitosis, and cytokinesis.
[Show full text]
Comprehensive Protein Interactome Analysis of a Key RNA Helicase: Detection of Novel Stress Granule Proteins
Biomolecules 2015, 5, 1441-1466; doi:10.3390/biom5031441 OPEN ACCESS biomolecules ISSN 2218-273X www.mdpi.com/journal/biomolecules/ Article Comprehensive Protein Interactome Analysis of a Key RNA Helicase: Detection of Novel Stress Granule Proteins Rebecca Bish 1,†, Nerea Cuevas-Polo 1,†, Zhe Cheng 1, Dolores Hambardzumyan 2, Mathias Munschauer 3, Markus Landthaler 3 and Christine Vogel 1,* 1 Center for Genomics and Systems Biology, Department of Biology, New York University, 12 Waverly Place, New York, NY 10003, USA; E-Mails: [email protected] (R.B.); [email protected] (N.C.-P.); [email protected] (Z.C.) 2 The Cleveland Clinic, Department of Neurosciences, Lerner Research Institute, 9500 Euclid Avenue, Cleveland, OH 44195, USA; E-Mail: [email protected] 3 RNA Biology and Post-Transcriptional Regulation, Max-Delbrück-Center for Molecular Medicine, Berlin-Buch, Robert-Rössle-Str. 10, Berlin 13092, Germany; E-Mails: [email protected] (M.M.); [email protected] (M.L.) † These authors contributed equally to this work. * Author to whom correspondence should be addressed; E-Mail: [email protected]; Tel.: +1-212-998-3976; Fax: +1-212-995-4015. Academic Editor: André P. Gerber Received: 10 May 2015 / Accepted: 15 June 2015 / Published: 15 July 2015 Abstract: DDX6 (p54/RCK) is a human RNA helicase with central roles in mRNA decay and translation repression. To help our understanding of how DDX6 performs these multiple functions, we conducted the first unbiased, large-scale study to map the DDX6-centric protein-protein interactome using immunoprecipitation and mass spectrometry. Using DDX6 as bait, we identify a high-confidence and high-quality set of protein interaction partners which are enriched for functions in RNA metabolism and ribosomal proteins.
[Show full text]
Gene Expression During Normal and FSHD Myogenesis Tsumagari Et Al
Gene expression during normal and FSHD myogenesis Tsumagari et al. Tsumagari et al. BMC Medical Genomics 2011, 4:67 http://www.biomedcentral.com/1755-8794/4/67 (27 September 2011) Tsumagari et al. BMC Medical Genomics 2011, 4:67 http://www.biomedcentral.com/1755-8794/4/67 RESEARCHARTICLE Open Access Gene expression during normal and FSHD myogenesis Koji Tsumagari1, Shao-Chi Chang1, Michelle Lacey2,3, Carl Baribault2,3, Sridar V Chittur4, Janet Sowden5, Rabi Tawil5, Gregory E Crawford6 and Melanie Ehrlich1,3* Abstract Background: Facioscapulohumeral muscular dystrophy (FSHD) is a dominant disease linked to contraction of an array of tandem 3.3-kb repeats (D4Z4) at 4q35. Within each repeat unit is a gene, DUX4, that can encode a protein containing two homeodomains. A DUX4 transcript derived from the last repeat unit in a contracted array is associated with pathogenesis but it is unclear how. Methods: Using exon-based microarrays, the expression profiles of myogenic precursor cells were determined. Both undifferentiated myoblasts and myoblasts differentiated to myotubes derived from FSHD patients and controls were studied after immunocytochemical verification of the quality of the cultures. To further our understanding of FSHD and normal myogenesis, the expression profiles obtained were compared to those of 19 non-muscle cell types analyzed by identical methods. Results: Many of the ~17,000 examined genes were differentially expressed (> 2-fold, p < 0.01) in control myoblasts or myotubes vs. non-muscle cells (2185 and 3006, respectively) or in FSHD vs. control myoblasts or myotubes (295 and 797, respectively). Surprisingly, despite the morphologically normal differentiation of FSHD myoblasts to myotubes, most of the disease-related dysregulation was seen as dampening of normal myogenesis- specific expression changes, including in genes for muscle structure, mitochondrial function, stress responses, and signal transduction.
[Show full text]
POGLUT1, the Putative Effector Gene Driven by Rs2293370 in Primary
www.nature.com/scientificreports OPEN POGLUT1, the putative efector gene driven by rs2293370 in primary biliary cholangitis susceptibility Received: 6 June 2018 Accepted: 13 November 2018 locus chromosome 3q13.33 Published: xx xx xxxx Yuki Hitomi 1, Kazuko Ueno2,3, Yosuke Kawai1, Nao Nishida4, Kaname Kojima2,3, Minae Kawashima5, Yoshihiro Aiba6, Hitomi Nakamura6, Hiroshi Kouno7, Hirotaka Kouno7, Hajime Ohta7, Kazuhiro Sugi7, Toshiki Nikami7, Tsutomu Yamashita7, Shinji Katsushima 7, Toshiki Komeda7, Keisuke Ario7, Atsushi Naganuma7, Masaaki Shimada7, Noboru Hirashima7, Kaname Yoshizawa7, Fujio Makita7, Kiyoshi Furuta7, Masahiro Kikuchi7, Noriaki Naeshiro7, Hironao Takahashi7, Yutaka Mano7, Haruhiro Yamashita7, Kouki Matsushita7, Seiji Tsunematsu7, Iwao Yabuuchi7, Hideo Nishimura7, Yusuke Shimada7, Kazuhiko Yamauchi7, Tatsuji Komatsu7, Rie Sugimoto7, Hironori Sakai7, Eiji Mita7, Masaharu Koda7, Yoko Nakamura7, Hiroshi Kamitsukasa7, Takeaki Sato7, Makoto Nakamuta7, Naohiko Masaki 7, Hajime Takikawa8, Atsushi Tanaka 8, Hiromasa Ohira9, Mikio Zeniya10, Masanori Abe11, Shuichi Kaneko12, Masao Honda12, Kuniaki Arai12, Teruko Arinaga-Hino13, Etsuko Hashimoto14, Makiko Taniai14, Takeji Umemura 15, Satoru Joshita 15, Kazuhiko Nakao16, Tatsuki Ichikawa16, Hidetaka Shibata16, Akinobu Takaki17, Satoshi Yamagiwa18, Masataka Seike19, Shotaro Sakisaka20, Yasuaki Takeyama 20, Masaru Harada21, Michio Senju21, Osamu Yokosuka22, Tatsuo Kanda 22, Yoshiyuki Ueno 23, Hirotoshi Ebinuma24, Takashi Himoto25, Kazumoto Murata4, Shinji Shimoda26, Shinya Nagaoka6, Seigo Abiru6, Atsumasa Komori6,27, Kiyoshi Migita6,27, Masahiro Ito6,27, Hiroshi Yatsuhashi6,27, Yoshihiko Maehara28, Shinji Uemoto29, Norihiro Kokudo30, Masao Nagasaki2,3,31, Katsushi Tokunaga1 & Minoru Nakamura6,7,27,32 Primary biliary cholangitis (PBC) is a chronic and cholestatic autoimmune liver disease caused by the destruction of intrahepatic small bile ducts. Our previous genome-wide association study (GWAS) identifed six susceptibility loci for PBC.
[Show full text]
The RNA Helicase DDX6 Controls Cellular Plasticity by Modulating P-Body Homeostasis
Article The RNA Helicase DDX6 Controls Cellular Plasticity by Modulating P-Body Homeostasis Graphical Abstract Authors Bruno Di Stefano, En-Ching Luo, Chuck Haggerty, ..., Alexander Meissner, Gene W. Yeo, Konrad Hochedlinger Correspondence [email protected] (G.W.Y.), [email protected] (K.H.) In Brief P-bodies are cytoplasmic RNP granules whose role in stem cells remains largely elusive. Di Stefano et al. show that the disruption of P-bodies upon loss of DDX6 perturbs the self-renewal and differentiation of various stem cell populations through translational upregulation of cell fate regulators and profound rewiring of chromatin landscapes. Highlights d DDX6-depleted PSCs lose P-bodies and cannot exit pluripotency d DDX6 depletion perturbs adult stem potency in a context- dependent manner d DDX6 suppresses the translation of P-body enriched TFs and chromatin regulators d P-body loss profoundly alters chromatin organization in stem cells Di Stefano et al., 2019, Cell Stem Cell 25, 1–17 November 7, 2019 ª 2019 Elsevier Inc. https://doi.org/10.1016/j.stem.2019.08.018 Please cite this article in press as: Di Stefano et al., The RNA Helicase DDX6 Controls Cellular Plasticity by Modulating P-Body Homeostasis, Cell Stem Cell (2019), https://doi.org/10.1016/j.stem.2019.08.018 Cell Stem Cell Article The RNA Helicase DDX6 Controls Cellular Plasticity by Modulating P-Body Homeostasis Bruno Di Stefano,1,2,3,4,5,12 En-Ching Luo,6,7,8,12 Chuck Haggerty,9 Stefan Aigner,6,7,8 Jocelyn Charlton,9 Justin Brumbaugh,1,2,3,4,5 Fei Ji,1 Ine´ s Rabano Jime´ nez,6,7,8 Katie J.
[Show full text]
HNRNPK Maintains Epidermal Progenitor Function Through Transcription of Proliferation Genes and Degrading Differentiation Promoting Mrnas
ARTICLE https://doi.org/10.1038/s41467-019-12238-x OPEN HNRNPK maintains epidermal progenitor function through transcription of proliferation genes and degrading differentiation promoting mRNAs Jingting Li 1, Yifang Chen1, Xiaojun Xu2, Jackson Jones1, Manisha Tiwari1, Ji Ling1, Ying Wang1, Olivier Harismendy 2,3 & George L. Sen1 1234567890():,; Maintenance of high-turnover tissues such as the epidermis requires a balance between stem cell proliferation and differentiation. The molecular mechanisms governing this process are an area of investigation. Here we show that HNRNPK, a multifunctional protein, is necessary to prevent premature differentiation and sustains the proliferative capacity of epidermal stem and progenitor cells. To prevent premature differentiation of progenitor cells, HNRNPK is necessary for DDX6 to bind a subset of mRNAs that code for transcription factors that promote differentiation. Upon binding, these mRNAs such as GRHL3, KLF4, and ZNF750 are degraded through the mRNA degradation pathway, which prevents premature differentiation. To sustain the proliferative capacity of the epidermis, HNRNPK is necessary for RNA Poly- merase II binding to proliferation/self-renewal genes such as MYC, CYR61, FGFBP1, EGFR, and cyclins to promote their expression. Our study establishes a prominent role for HNRNPK in maintaining adult tissue self-renewal through both transcriptional and post-transcriptional mechanisms. 1 Department of Dermatology, Department of Cellular and Molecular Medicine, UCSD Stem Cell Program, University of California, San Diego, La Jolla, CA 92093, USA. 2 Moores Cancer Center, University of California, San Diego, La Jolla, CA 92093, USA. 3 Department of Biomedical Informatics, University of California, San Diego, La Jolla, CA 92093, USA. Correspondence and requests for materials should be addressed to G.L.S.
[Show full text]
DCP1 Forms Asymmetric Trimers to Assemble Into Active Mrna Decapping Complexes in Metazoa
DCP1 forms asymmetric trimers to assemble into active mRNA decapping complexes in metazoa Felix Tritschler1, Joerg E. Braun1, Carina Motz, Catia Igreja, Gabrielle Haas, Vincent Truffault, Elisa Izaurralde2, and Oliver Weichenrieder2 Department of Biochemistry, Max Planck Institute for Developmental Biology, Spemannstrasse 35, D-72076 Tu¨bingen, Germany Edited by James E. Dahlberg, University of Wisconsin Medical School, Madison, WI, and approved October 29, 2009 (received for review August 28, 2009) DCP1 stimulates the decapping enzyme DCP2, which removes the DCP1a in mRNA decapping we expressed the domain in E. coli -mRNA 5؅ cap structure committing mRNAs to degradation. In (DCP1a residues S539 to L582). Using static light scattering mea multicellular eukaryotes, DCP1-DCP2 interaction is stabilized by surements coupled with size exclusion chromatography, we found additional proteins, including EDC4. However, most information unexpectedly that the purified domain forms stable trimers in on DCP2 activation stems from studies in S. cerevisiae, which lacks solution (Table S1). We have termed this domain the DCP1- EDC4. Furthermore, DCP1 orthologs from multicellular eukaryotes trimerization domain (DCP1-TD). Furthermore, although the re- have a C-terminal extension, absent in fungi. Here, we show that in combinant polypeptide contains 51 residues per monomer (i.e., 44 metazoa, a conserved DCP1 C-terminal domain drives DCP1 trim- from DCP1a-TD and seven from the expression vector), NMR erization. Crystal structures of the DCP1-trimerization domain re- spectroscopy yields Ͼ115 peaks in the 15N-HSQC spectrum (Fig. veal an antiparallel assembly comprised of three kinked ␣-helices. S2), suggesting that in solution the trimers are asymmetric (assum- Trimerization is required for DCP1 to be incorporated into active ing a single trimeric assembly).
[Show full text]
UNIVERSITY of CALIFORNIA, SAN DIEGO Measuring
UNIVERSITY OF CALIFORNIA, SAN DIEGO Measuring and Correlating Blood and Brain Gene Expression Levels: Assays, Inbred Mouse Strain Comparisons, and Applications to Human Disease Assessment A dissertation submitted in partial satisfaction of the requirements for the degree of Doctor of Philosophy in Biomedical Sciences by Mary Elizabeth Winn Committee in charge: Professor Nicholas J Schork, Chair Professor Gene Yeo, Co-Chair Professor Eric Courchesne Professor Ron Kuczenski Professor Sanford Shattil 2011 Copyright Mary Elizabeth Winn, 2011 All rights reserved. 2 The dissertation of Mary Elizabeth Winn is approved, and it is acceptable in quality and form for publication on microfilm and electronically: Co-Chair Chair University of California, San Diego 2011 iii DEDICATION To my parents, Dennis E. Winn II and Ann M. Winn, to my siblings, Jessica A. Winn and Stephen J. Winn, and to all who have supported me throughout this journey. iv TABLE OF CONTENTS Signature Page iii Dedication iv Table of Contents v List of Figures viii List of Tables x Acknowledgements xiii Vita xvi Abstract of Dissertation xix Chapter 1 Introduction and Background 1 INTRODUCTION 2 Translational Genomics, Genome-wide Expression Analysis, and Biomarker Discovery 2 Neuropsychiatric Diseases, Tissue Accessibility and Blood-based Gene Expression 4 Mouse Models of Human Disease 5 Microarray Gene Expression Profiling and Globin Reduction 7 Finding and Accessible Surrogate Tissue for Neural Tissue 9 Genetic Background Effect Analysis 11 SPECIFIC AIMS 12 ENUMERATION OF CHAPTERS
[Show full text]
General and Target-Specific Dexd/H RNA Helicases in Eukaryotic Translation Initiation
International Journal of Molecular Sciences Review General and Target-Speciﬁc DExD/H RNA Helicases in Eukaryotic Translation Initiation Leo Shen 1 and Jerry Pelletier 1,2,3,* 1 Department of Biochemistry, McGill University, Montreal, QC H3G 1Y6, Canada; [email protected] 2 Department of Oncology, McGill University, Montreal, QC H4A 3T2, Canada 3 Rosalind and Morris Goodman Cancer Research Center, McGill University, Montreal, QC H3A 1A3, Canada * Correspondence: [email protected]; Tel.: +1-514-398-2323 Received: 5 June 2020; Accepted: 18 June 2020; Published: 20 June 2020 Abstract: DExD (DDX)- and DExH (DHX)-box RNA helicases, named after their Asp-Glu-x-Asp/His motifs, are integral to almost all RNA metabolic processes in eukaryotic cells. They play myriad roles in processes ranging from transcription and mRNA-protein complex remodeling, to RNA decay and translation. This last facet, translation, is an intricate process that involves DDX/DHX helicases and presents a regulatory node that is highly targetable. Studies aimed at better understanding this family of conserved proteins have revealed insights into their structures, catalytic mechanisms, and biological roles. They have also led to the development of chemical modulators that seek to exploit their essential roles in diseases. Herein, we review the most recent insights on several general and target-speciﬁc DDX/DHX helicases in eukaryotic translation initiation. Keywords: helicase; translation; initiation; DDX; DHX; eIF4A1; DDX3X; DHX9; DHX29; DHX36 1. Introduction RNA helicases play a role in all facets of RNA metabolism, ranging from transcription and translation, to processing and decay. These highly conserved enzymes use ATP to bind, unwind, and disrupt RNA structures and RNA-protein complexes [1].
[Show full text]
Genomics of Asthma, Allergy and Chronic Rhinosinusitis
Laulajainen‑Hongisto et al. Clin Transl Allergy (2020) 10:45 https://doi.org/10.1186/s13601‑020‑00347‑6 Clinical and Translational Allergy REVIEW Open Access Genomics of asthma, allergy and chronic rhinosinusitis: novel concepts and relevance in airway mucosa Anu Laulajainen‑Hongisto1,2†, Annina Lyly1,3*† , Tanzeela Hanif4, Kishor Dhaygude4, Matti Kankainen5,6,7, Risto Renkonen4,5, Kati Donner6, Pirkko Mattila4,6, Tuomas Jartti8, Jean Bousquet9,10,11, Paula Kauppi3† and Sanna Toppila‑Salmi3,4† Abstract Genome wide association studies (GWASs) have revealed several airway disease‑associated risk loci. Their role in the onset of asthma, allergic rhinitis (AR) or chronic rhinosinusitis (CRS), however, is not yet fully understood. The aim of this review is to evaluate the airway relevance of loci and genes identifed in GWAS studies. GWASs were searched from databases, and a list of loci associating signifcantly (p < 10–8) with asthma, AR and CRS was created. This yielded a total of 267 signifcantly asthma/AR–associated loci from 31 GWASs. No signifcant CRS ‑associated loci were found in this search. A total of 170 protein coding genes were connected to these loci. Of these, 76/170 (44%) showed bronchial epithelial protein expression in stained microscopic fgures of Human Protein Atlas (HPA), and 61/170 (36%) had a literature report of having airway epithelial function. Gene ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) annotation analyses were performed, and 19 functional protein categories were found as signif‑ cantly (p < 0.05) enriched among these genes. These were related to cytokine production, cell activation and adaptive immune response, and all were strongly connected in network analysis.
[Show full text]
The DEAD-Box RNA-Binding Protein DDX6 Regulates Parental RNA Decay for Cellular Reprogramming to Pluripotency
RESEARCH ARTICLE The DEAD-box RNA-binding protein DDX6 regulates parental RNA decay for cellular reprogramming to pluripotency Daisuke Kami1, Tomoya Kitani2, Akihiro Nakamura3, Naoki Wakui4, Rena Mizutani5, Masahito Ohue4, Fuyuki Kametani6, Nobuyoshi Akimitsu5, Satoshi Gojo1* 1 Department of Regenerative Medicine, Graduate School of Medical Science, Kyoto Prefectural University of Medicine, Kyoto, Japan, 2 Department of Cardiovascular Medicine, Graduate School of Medical Science, Kyoto Prefectural University of Medicine, Kyoto, Japan, 3 Department of Pediatric Cardiology and Nephrology, Graduate School of Medical Science, Kyoto Prefectural University of Medicine, Kyoto, Japan, a1111111111 4 Department of Computer Science, School of Computing, Tokyo Institute of Technology, Tokyo, Japan, a1111111111 5 Radioisotope Center, The University of Tokyo, Tokyo, Japan, 6 Department of Dementia and Higher Brain a1111111111 Function, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan a1111111111 a1111111111 * [email protected] Abstract OPEN ACCESS Cellular transitions and differentiation processes require mRNAs supporting the new pheno- Citation: Kami D, Kitani T, Nakamura A, Wakui N, type but also the clearance of existing mRNAs for the parental phenotype. Cellular repro- Mizutani R, Ohue M, et al. (2018) The DEAD- gramming from fibroblasts to induced pluripotent stem cells (iPSCs) occurs at the early box RNA-binding protein DDX6 regulates parental stage of mesenchymal epithelial transition (MET) and involves drastic morphological RNA decay for cellular reprogramming to pluripotency. PLoS ONE 13(10): e0203708. https:// changes. We examined the molecular mechanism for MET, focusing on RNA metabolism. doi.org/10.1371/journal.pone.0203708 DDX6, an RNA helicase, was indispensable for iPSC formation, in addition to RO60 and Editor: Yoon Ki Kim, Korea University, REPUBLIC RNY1, a non-coding RNA, which form complexes involved in intracellular nucleotide sens- OF KOREA ing.
[Show full text]
Druggable Vitiligo Genome: a Fast Track Approach to Take the Genome Wide Association to the Clinic
MOJ Proteomics & Bioinformatics Research Article Open Access Druggable vitiligo genome: a fast track approach to take the genome wide association to the clinic Abstract Volume 2 Issue 3 - 2015 Vitiligo, a skin depigmentation disorder, affects 0.5 to 1% of the population Ramaswamy Narayanan around the globe. While not life threatening, the disorder is associated with serious Department of Biological Sciences, Charles E. Schmidt College psychological trauma. Currently no known cure is available and the precise etiology of Science, Florida Atlantic University, USA is unknown. Genome-Wide Association Studies (GWAS) may provide clues to better understanding the disorder for the development of novel therapeutics. Mining Correspondence: Ramaswamy Narayanan, Department of the GWAS databases resulted in the identification of 51 Vitiligo-associated genes Biological Sciences, Charles E. Schmidt College of Science, (VAG) encompassing protein-coding sequences, noncoding RNAs and pseudogenes. Florida Atlantic University, 777 Glades Road, Boca Raton, FL A druggable class of proteins including enzymes, transporters, transcription factors 33431, USA, Tel +15612972247, Fax +15612973859, and secretome products was part of the VAG. The VAG were also genetically linked Email [email protected] to autoimmune, cancer, cardiovascular, inflammation, infections and neurological diseases. Two genes, Interleukin 2 receptor alpha (IL2RA) and Tyrosinase (TYR) are Received: May 28, 2015 | Published: July 24, 2015 FDA approved targets. Unique population-specific genes were identified in the GWAS databases. Chemogenomics approaches identified 246 compounds targeting the VAG. Key pathways involving the VAG’s mechanism included apoptosis, endocrine, immune, infection, metabolic, neuronal and transcription factor signaling. Five lead targets, four enzymes and one transporter, emerged from this study with bioactive drug-like compounds (<100nM).
[Show full text]