Anti-NDUFA6 Antibody (ARG65567)

Total Page：16

File Type：pdf, Size：1020Kb

Product datasheet [email protected] ARG65567 Package: 100 μl anti-NDUFA6 antibody Store at: -20°C Summary Product Description Rabbit Polyclonal antibody recognizes NDUFA6 Tested Reactivity Hu Tested Application WB Host Rabbit Clonality Polyclonal Isotype IgG Target Name NDUFA6 Antigen Species Human Immunogen Fusion protein of human NDUFA6 Conjugation Un-conjugated Alternate Names NADH-ubiquinone oxidoreductase B14 subunit; Complex I-B14; CI-B14; NADHB14; LYR motif-containing protein 6; B14; LYRM6; NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6 Application Instructions Application table Application Dilution WB 200-1000 Application Note * The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist. Positive Control Human normal kidney tissue Calculated Mw 15 kDa Properties Form Liquid Purification Purified by antigen-affinity chromatography. Buffer 1XPBS (pH 7.4), 0.05% Sodium azide and 40% Glycerol Preservative 0.05% Sodium azide Stabilizer 40% Glycerol Concentration 1.6 mg/ml Storage instruction For continuous use, store undiluted antibody at 2-8°C for up to a week. For long-term storage, aliquot and store at -20°C. Storage in frost free freezers is not recommended. Avoid repeated freeze/thaw cycles. Suggest spin the vial prior to opening. The antibody solution should be gently mixed before use. Note For laboratory research only, not for drug, diagnostic or other use. www.arigobio.com 1/2 Bioinformation Database links GeneID: 4700 Human Swiss-port # P56556 Human Gene Symbol NDUFA6 Gene Full Name NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, 6, 14kDa Background NDUFA6 (NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, 6), also known as LYRM6 (LYR motif- containing protein 6), NADHB14 or B14, is a 128 amino acid protein that localizes to the matrix side of the mitochondrial membrane and belongs to the complex I LYR family. Existing as a subunit of the multi- protein membrane respiratory chain NADH dehydrogenase complex (Complex I), NDUFA6 functions as an accessory protein that facilitates the transfer of electrons from NADH to the respiratory chain. Function Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed to be not involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. [UniProt] Highlight Related products: Anti-Rabbit IgG secondary antibodies; Related poster download: The Structure & Functions of Mitochondria.pdf Research Area Controls and Markers antibody; Metabolism antibody; Signaling Transduction antibody Images ARG65567 anti-NDUFA6 antibody WB image Western blot: 40 μg of Human normal kidney tissue lysate stained with ARG65567 anti-NDUFA6 antibody at 1:250 dilution. Exporsure time: 1 minute. www.arigobio.com 2/2 Powered by TCPDF (www.tcpdf.org).

Copy Link

Recommended publications

Low Abundance of the Matrix Arm of Complex I in Mitochondria Predicts Longevity in Mice
ARTICLE Received 24 Jan 2014 | Accepted 9 Apr 2014 | Published 12 May 2014 DOI: 10.1038/ncomms4837 OPEN Low abundance of the matrix arm of complex I in mitochondria predicts longevity in mice Satomi Miwa1, Howsun Jow2, Karen Baty3, Amy Johnson1, Rafal Czapiewski1, Gabriele Saretzki1, Achim Treumann3 & Thomas von Zglinicki1 Mitochondrial function is an important determinant of the ageing process; however, the mitochondrial properties that enable longevity are not well understood. Here we show that optimal assembly of mitochondrial complex I predicts longevity in mice. Using an unbiased high-coverage high-conﬁdence approach, we demonstrate that electron transport chain proteins, especially the matrix arm subunits of complex I, are decreased in young long-living mice, which is associated with improved complex I assembly, higher complex I-linked state 3 oxygen consumption rates and decreased superoxide production, whereas the opposite is seen in old mice. Disruption of complex I assembly reduces oxidative metabolism with concomitant increase in mitochondrial superoxide production. This is rescued by knockdown of the mitochondrial chaperone, prohibitin. Disrupted complex I assembly causes premature senescence in primary cells. We propose that lower abundance of free catalytic complex I components supports complex I assembly, efﬁcacy of substrate utilization and minimal ROS production, enabling enhanced longevity. 1 Institute for Ageing and Health, Newcastle University, Newcastle upon Tyne NE4 5PL, UK. 2 Centre for Integrated Systems Biology of Ageing and Nutrition, Newcastle University, Newcastle upon Tyne NE4 5PL, UK. 3 Newcastle University Protein and Proteome Analysis, Devonshire Building, Devonshire Terrace, Newcastle upon Tyne NE1 7RU, UK. Correspondence and requests for materials should be addressed to T.v.Z.
[Show full text]
The LYR Protein Subunit NB4M/NDUFA6 of Mitochondrial Complex I Anchors an Acyl Carrier Protein and Is Essential for Catalytic Activity
The LYR protein subunit NB4M/NDUFA6 of mitochondrial complex I anchors an acyl carrier protein and is essential for catalytic activity Heike Angerera, Michael Radermacherb, Michalina Mankowska a, Mirco Stegerc, Klaus Zwickerd, Heinrich Heidec, Ilka Wittigc,e, Ulrich Brandte,f, and Volker Zickermanna,e,1 aInstitute of Biochemistry II, Structural Bioenergetics Group, Medical School, Goethe University Frankfurt, 60438 Frankfurt, Germany; bDepartment of Molecular Physiology and Biophysics, College of Medicine, University of Vermont, Burlington, VT 05405; cFunctional Proteomics, SFB 815 Core Unit, and dInstitute of Biochemistry I, Medical School, Goethe University Frankfurt, 60590 Frankfurt, Germany; eCluster of Excellence Macromolecular Complexes, Goethe University Frankfurt, Germany; and fNijmegen Centre for Mitochondrial Disorders, Radboud University Medical Centre, 6525 GA, Nijmegen, The Netherlands Edited by Wolfgang Baumeister, Max Planck Institute of Biochemistry, Martinsried, Germany, and approved February 25, 2014 (received for review December 4, 2013) Mitochondrial complex I is the largest and most complicated enzyme is identical to LYR motif containing protein 6 (LYRM6). Sever- of the oxidative phosphorylation system. It comprises a number al other LYRM proteins were shown to be associated with of so-called accessory subunits of largely unknown structure and the maintenance of mitochondrial homeostasis. LYRM4 (alterna- function. Here we studied subunit NB4M [NDUFA6, LYR motif tive designation ISD11, iron-sulfur protein biogenesis
[Show full text]
THE FUNCTIONAL SIGNIFICANCE of MITOCHONDRIAL SUPERCOMPLEXES in C. ELEGANS by WICHIT SUTHAMMARAK Submitted in Partial Fulfillment
THE FUNCTIONAL SIGNIFICANCE OF MITOCHONDRIAL SUPERCOMPLEXES in C. ELEGANS by WICHIT SUTHAMMARAK Submitted in partial fulfillment of the requirements For the degree of Doctor of Philosophy Dissertation Advisor: Drs. Margaret M. Sedensky & Philip G. Morgan Department of Genetics CASE WESTERN RESERVE UNIVERSITY January, 2011 CASE WESTERN RESERVE UNIVERSITY SCHOOL OF GRADUATE STUDIES We hereby approve the thesis/dissertation of _____________________________________________________ candidate for the ______________________degree *. (signed)_______________________________________________ (chair of the committee) ________________________________________________ ________________________________________________ ________________________________________________ ________________________________________________ ________________________________________________ (date) _______________________ *We also certify that written approval has been obtained for any proprietary material contained therein. Dedicated to my family, my teachers and all of my beloved ones for their love and support ii ACKNOWLEDGEMENTS My advanced academic journey began 5 years ago on the opposite side of the world. I traveled to the United States from Thailand in search of a better understanding of science so that one day I can return to my homeland and apply the knowledge and experience I have gained to improve the lives of those affected by sickness and disease yet unanswered by science. Ultimately, I hoped to make the academic transition into the scholarly community by proving myself through scientific research and understanding so that I can make a meaningful contribution to both the scientific and medical communities. The following dissertation would not have been possible without the help, support, and guidance of a lot of people both near and far. I wish to thank all who have aided me in one way or another on this long yet rewarding journey. My sincerest thanks and appreciation goes to my advisors Philip Morgan and Margaret Sedensky.
[Show full text]
Mitochondrial Medicine in the Omics Era
Mitochondrial Medicine in the Omics Era Joyeeta Rahman1 and Shamima Rahman1,2* 1 Mitochondrial Research Group, UCL Great Ormond Street Institute of Child Health and 2 Metabolic Unit, Great Ormond Street Hospital NHS Foundation Trust, London, UK *Correspondence to: Professor Shamima Rahman Mitochondrial Research Group Genetics and Genomic Medicine UCL Great Ormond Street Institute of Child Health London WC1N 1EH, UK. Telephone: +44 (0)2079052608 [email protected] Keywords: Mitochondrial disease, OXPHOS, signalling, omics, genomics, transcriptomics, proteomics, metabolomics, mitochondrial stress response, treatment 1 Abstract Mitochondria are dynamic bioenergetic organelles whose maintenance requires ~1500 proteins from two genomes. Mutations in either the mitochondrial or nuclear genome can disrupt a plethora of cellular metabolic and homeostatic functions. Mitochondrial diseases represent one the most common and severe groups of inherited genetic disorders, characterised by clinical, biochemical, and genetic heterogeneity, diagnostic odysseys, and lack of curative therapies. This review aims to discuss recent advances in mitochondrial biology and medicine arising from widespread utilisation of high-throughput omics technologies, and also includes a broad discussion of emerging therapies for mitochondrial disease. New insights into both bioenergetic and biosynthetic mitochondrial functionalities have expedited the genetic diagnosis of primary mitochondrial disorders, and identified novel mitochondrial pathomechanisms and new targets
[Show full text]
Epigenetic Regulation of Developmental Expression of Cyp2d Genes in Mouse Liver
CORE Metadata, citation and similar papers at core.ac.uk Provided by Elsevier - Publisher Connector Acta Pharmaceutica Sinica B 2012;2(2):146–158 Institute of Materia Medica, Chinese Academy of Medical Sciences Chinese Pharmaceutical Association Acta Pharmaceutica Sinica B www.elsevier.com/locate/apsb www.sciencedirect.com ORIGINAL ARTICLE Epigenetic regulation of developmental expression of Cyp2d genes in mouse liver Ye Lia, Xiao-bo Zhongb,n aDepartment of Pharmacology, School of Chemical Biology and Pharmaceutical Sciences, Capital Medical University, Beijing 100069, China bDepartment of Pharmacology, Toxicology, and Therapeutics, University of Kansas Medical Center, Kansas City, KS 66160, USA Received 28 November 2011; revised 26 December 2011; accepted 10 January 2012 KEY WORDS Abstract CYP2D6 expression in liver is age-dependent. Because epigenetic mechanisms, such as DNA methylation and histone modiﬁcations, modulate age-related gene expression during develop- Cyp2d; ment, and are highly conserved among species, the current study examined the epigenetic regulation of DNA methylation; age-related expression of the Cyp2d genes in mouse liver. DNA methylation (DNAme), histone 3 Histone methylation; lysine 4 dimethylation (H3K4me2), and histone 3 lysine 27 trimethylation (H3K27me3) was Liver development established by ChIP-on-chip tiling microarrays from mouse livers at prenatal, neonatal, and adult stages. Levels of DNAme, H3K4me2, and H3K27me3 were analyzed in a genomic region containing the Cyp2d clustering genes and their surrounding genes. Gradually increased expression levels of the Cyp2d9, Cyp2d10, Cyp2d22,andCyp2d26 genes from prenatal, through neonatal, to adult are associated with gradually increased levels of H3K4me2 in the nucleosomes associated with these genes. Gene expression patterns during liver development in several Cyp2d surrounding genes, such as Srebf2, Sept3, Ndufa6, Tcf2, Nfam1,andCyb5r3, could be also explained by changes of DNA methylation, H3K4me2, or H3K27me3 in those genes.
[Show full text]
WO 2017/070647 Al 27 April 2017 (27.04.2017) P O P C T
(12) INTERNATIONAL APPLICATION PUBLISHED UNDER THE PATENT COOPERATION TREATY (PCT) (19) World Intellectual Property Organization International Bureau (10) International Publication Number (43) International Publication Date WO 2017/070647 Al 27 April 2017 (27.04.2017) P O P C T (51) International Patent Classification: HN, HR, HU, ID, IL, IN, IR, IS, JP, KE, KG, KN, KP, KR, A61K 31/455 (2006.01) C12N 15/86 (2006.01) KW, KZ, LA, LC, LK, LR, LS, LU, LY, MA, MD, ME, A61K 31/465 (2006.01) A61P 27/02 (2006.01) MG, MK, MN, MW, MX, MY, MZ, NA, NG, NI, NO, NZ, A61K 31/19 (2006.01) A61P 27/06 (2006.01) OM, PA, PE, PG, PH, PL, PT, QA, RO, RS, RU, RW, SA, A61K 48/00 (2006.01) A61K 45/06 (2006.01) SC, SD, SE, SG, SK, SL, SM, ST, SV, SY, TH, TJ, TM, TN, TR, TT, TZ, UA, UG, US, UZ, VC, VN, ZA, ZM, (21) International Application Number: ZW. PCT/US2016/058388 (84) Designated States (unless otherwise indicated, for every (22) International Filing Date: kind of regional protection available): ARIPO (BW, GH, 24 October 2016 (24.10.201 6) GM, KE, LR, LS, MW, MZ, NA, RW, SD, SL, ST, SZ, (25) Filing Language: English TZ, UG, ZM, ZW), Eurasian (AM, AZ, BY, KG, KZ, RU, TJ, TM), European (AL, AT, BE, BG, CH, CY, CZ, DE, (26) Publication Language: English DK, EE, ES, FI, FR, GB, GR, HR, HU, IE, IS, IT, LT, LU, (30) Priority Data: LV, MC, MK, MT, NL, NO, PL, PT, RO, RS, SE, SI, SK, 62/245,467 23 October 2015 (23.
[Show full text]
Downloaded Per Proteome Cohort Via the Web- Site Links of Table 1, Also Providing Information on the Deposited Spectral Datasets
www.nature.com/scientificreports OPEN Assessment of a complete and classifed platelet proteome from genome‑wide transcripts of human platelets and megakaryocytes covering platelet functions Jingnan Huang1,2*, Frauke Swieringa1,2,9, Fiorella A. Solari2,9, Isabella Provenzale1, Luigi Grassi3, Ilaria De Simone1, Constance C. F. M. J. Baaten1,4, Rachel Cavill5, Albert Sickmann2,6,7,9, Mattia Frontini3,8,9 & Johan W. M. Heemskerk1,9* Novel platelet and megakaryocyte transcriptome analysis allows prediction of the full or theoretical proteome of a representative human platelet. Here, we integrated the established platelet proteomes from six cohorts of healthy subjects, encompassing 5.2 k proteins, with two novel genome‑wide transcriptomes (57.8 k mRNAs). For 14.8 k protein‑coding transcripts, we assigned the proteins to 21 UniProt‑based classes, based on their preferential intracellular localization and presumed function. This classifed transcriptome‑proteome profle of platelets revealed: (i) Absence of 37.2 k genome‑ wide transcripts. (ii) High quantitative similarity of platelet and megakaryocyte transcriptomes (R = 0.75) for 14.8 k protein‑coding genes, but not for 3.8 k RNA genes or 1.9 k pseudogenes (R = 0.43–0.54), suggesting redistribution of mRNAs upon platelet shedding from megakaryocytes. (iii) Copy numbers of 3.5 k proteins that were restricted in size by the corresponding transcript levels (iv) Near complete coverage of identifed proteins in the relevant transcriptome (log2fpkm > 0.20) except for plasma‑derived secretory proteins, pointing to adhesion and uptake of such proteins. (v) Underrepresentation in the identifed proteome of nuclear‑related, membrane and signaling proteins, as well proteins with low‑level transcripts.
[Show full text]
Genomic Approach in Idiopathic Intellectual Disability Maria De Fátima E Costa Torres
ESTUDOS DE 8 01 PDPGM 2 CICLO Genomic approach in idiopathic intellectual disability Maria de Fátima e Costa Torres D Autor. Maria de Fátima e Costa Torres D.ICBAS 2018 Genomic approach in idiopathic intellectual disability Genomic approach in idiopathic intellectual disability Maria de Fátima e Costa Torres SEDE ADMINISTRATIVA INSTITUTO DE CIÊNCIAS BIOMÉDICAS ABEL SALAZAR FACULDADE DE MEDICINA MARIA DE FÁTIMA E COSTA TORRES GENOMIC APPROACH IN IDIOPATHIC INTELLECTUAL DISABILITY Tese de Candidatura ao grau de Doutor em Patologia e Genética Molecular, submetida ao Instituto de Ciências Biomédicas Abel Salazar da Universidade do Porto Orientadora – Doutora Patrícia Espinheira de Sá Maciel Categoria – Professora Associada Afiliação – Escola de Medicina e Ciências da Saúde da Universidade do Minho Coorientadora – Doutora Maria da Purificação Valenzuela Sampaio Tavares Categoria – Professora Catedrática Afiliação – Faculdade de Medicina Dentária da Universidade do Porto Coorientadora – Doutora Filipa Abreu Gomes de Carvalho Categoria – Professora Auxiliar com Agregação Afiliação – Faculdade de Medicina da Universidade do Porto DECLARAÇÃO Dissertação/Tese Identificação do autor Nome completo _Maria de Fátima e Costa Torres_ N.º de identificação civil _07718822 N.º de estudante __ 198600524___ Email institucional [email protected] OU: [email protected] _ Email alternativo [email protected] _ Tlf/Tlm _918197020_ Ciclo de estudos (Mestrado/Doutoramento) _Patologia e Genética Molecular__ Faculdade/Instituto _Instituto de Ciências
[Show full text]
Instability in NAD Metabolism Leads to Impaired Cardiac Mitochondrial
RESEARCH ARTICLE Instability in NAD+ metabolism leads to impaired cardiac mitochondrial function and communication Knut H Lauritzen1*, Maria Belland Olsen1, Mohammed Shakil Ahmed2, Kuan Yang1, Johanne Egge Rinholm3, Linda H Bergersen4,5, Qin Ying Esbensen6, Lars Jansen Sverkeli7, Mathias Ziegler7, Ha˚ vard Attramadal2, Bente Halvorsen1,8, Pa˚ l Aukrust1,8,9, Arne Yndestad1,8 1Research Institute of Internal Medicine, Oslo University Hospital, Rikshospitalet and University of Oslo, Oslo, Norway; 2Institute for Surgical Research, Oslo University Hospital and University of Oslo, Oslo, Norway; 3Department of Microbiology, Oslo University Hospital, Oslo, Norway; 4Department of Oral Biology, University of Oslo, Oslo, Norway; 5Department of Neuroscience and Pharmacology, Center for Healthy Aging, University of Copenhagen, Copenhagen, Denmark; 6Department of Clinical Molecular Biology, University of Oslo and Akershus University Hospital, Nordbyhagen, Norway; 7Department of Biomedicine, University of Bergen, Bergen, Norway; 8Institute of Clinical Medicine, University of Oslo, Faculty of Medicine, Oslo, Norway; 9Section of Clinical Immunology and Infectious Diseases, Oslo University Hospital Rikshospitalet, Oslo, Norway Abstract Poly(ADP-ribose) polymerase (PARP) enzymes initiate (mt)DNA repair mechanisms and use nicotinamide adenine dinucleotide (NAD+) as energy source. Prolonged PARP activity can drain cellular NAD+ reserves, leading to de-regulation of important molecular processes. Here, we provide evidence of a pathophysiological mechanism that connects mtDNA damage to cardiac *For correspondence: dysfunction via reduced NAD+ levels and loss of mitochondrial function and communication. Using Knut.Huso.Lauritzen@rr-research. a transgenic model, we demonstrate that high levels of mice cardiomyocyte mtDNA damage cause no a reduction in NAD+ levels due to extreme DNA repair activity, causing impaired activation of Competing interests: The NAD+-dependent SIRT3.
[Show full text]
Bayesian Hidden Markov Tree Models for Clustering Genes with Shared Evolutionary History
Submitted to the Annals of Applied Statistics arXiv: arXiv:0000.0000 BAYESIAN HIDDEN MARKOV TREE MODELS FOR CLUSTERING GENES WITH SHARED EVOLUTIONARY HISTORY By Yang Liy,{,∗, Shaoyang Ningy,∗, Sarah E. Calvoz,x,{, Vamsi K. Moothak,z,x,{ and Jun S. Liuy Harvard Universityy, Broad Institutez, Harvard Medical Schoolx, Massachusetts General Hospital{, and Howard Hughes Medical Institutek Determination of functions for poorly characterized genes is cru- cial for understanding biological processes and studying human dis- eases. Functionally associated genes are often gained and lost together through evolution. Therefore identifying co-evolution of genes can predict functional gene-gene associations. We describe here the full statistical model and computational strategies underlying the orig- inal algorithm CLustering by Inferred Models of Evolution (CLIME 1.0) recently reported by us [Li et al., 2014]. CLIME 1.0 employs a mixture of tree-structured hidden Markov models for gene evolution process, and a Bayesian model-based clustering algorithm to detect gene modules with shared evolutionary histories (termed evolutionary conserved modules, or ECMs). A Dirichlet process prior was adopted for estimating the number of gene clusters and a Gibbs sampler was developed for posterior sampling. We further developed an extended version, CLIME 1.1, to incorporate the uncertainty on the evolution- ary tree structure. By simulation studies and benchmarks on real data sets, we show that CLIME 1.0 and CLIME 1.1 outperform traditional methods that use simple metrics (e.g., the Hamming distance or Pear- son correlation) to measure co-evolution between pairs of genes. 1. Introduction. The human genome encodes more than 20,000 protein- coding genes, of which a large fraction do not have annotated function to date [Galperin and Koonin, 2010].
[Show full text]
A Framework to Identify Contributing Genes in Patients with Phelan-Mcdermid Syndrome
www.nature.com/npjgenmed Corrected: Author Correction ARTICLE OPEN A framework to identify contributing genes in patients with Phelan-McDermid syndrome Anne-Claude Tabet 1,2,3,4, Thomas Rolland2,3,4, Marie Ducloy2,3,4, Jonathan Lévy1, Julien Buratti2,3,4, Alexandre Mathieu2,3,4, Damien Haye1, Laurence Perrin1, Céline Dupont 1, Sandrine Passemard1, Yline Capri1, Alain Verloes1, Séverine Drunat1, Boris Keren5, Cyril Mignot6, Isabelle Marey7, Aurélia Jacquette7, Sandra Whalen7, Eva Pipiras8, Brigitte Benzacken8, Sandra Chantot-Bastaraud9, Alexandra Afenjar10, Delphine Héron10, Cédric Le Caignec11, Claire Beneteau11, Olivier Pichon11, Bertrand Isidor11, Albert David11, Laila El Khattabi12, Stephan Kemeny13, Laetitia Gouas13, Philippe Vago13, Anne-Laure Mosca-Boidron14, Laurence Faivre15, Chantal Missirian16, Nicole Philip16, Damien Sanlaville17, Patrick Edery18, Véronique Satre19, Charles Coutton19, Françoise Devillard19, Klaus Dieterich20, Marie-Laure Vuillaume21, Caroline Rooryck21, Didier Lacombe21, Lucile Pinson22, Vincent Gatinois22, Jacques Puechberty22, Jean Chiesa23, James Lespinasse24, Christèle Dubourg25, Chloé Quelin25, Mélanie Fradin25, Hubert Journel26, Annick Toutain27, Dominique Martin28, Abdelamdjid Benmansour1, Claire S. Leblond2,3,4, Roberto Toro2,3,4, Frédérique Amsellem29, Richard Delorme2,3,4,29 and Thomas Bourgeron2,3,4 Phelan-McDermid syndrome (PMS) is characterized by a variety of clinical symptoms with heterogeneous degrees of severity, including intellectual disability (ID), absent or delayed speech, and autism spectrum disorders (ASD). It results from a deletion of the distal part of chromosome 22q13 that in most cases includes the SHANK3 gene. SHANK3 is considered a major gene for PMS, but the factors that modulate the severity of the syndrome remain largely unknown. In this study, we investigated 85 patients with different 22q13 rearrangements (78 deletions and 7 duplications).
[Show full text]
Diagnóstico Molecular Do Transtorno Do Espectro Autista Através Do Sequenciamento Completo De Exoma Molecular Diagnosis Of
Universidade de São Paulo Tatiana Ferreira de Almeida Diagnóstico molecular do transtorno do espectro autista através do sequenciamento completo de exoma Molecular diagnosis of autism spectrum disorder through whole exome sequencing São Paulo 2018 Universidade de São Paulo Tatiana Ferreira de Almeida Diagnóstico molecular do transtorno do espectro autista através do sequenciamento completo de exoma Molecular diagnosis of autism spectrum disorder through whole exome sequencing Tese apresentada ao Instituto de Biociências da Universidade de São Paulo, para a obtenção de Título de Doutor em Ciências, na Área de Biologia/Genética. Versão corrigida. Orientador(a): Maria Rita dos Santos Passos-Bueno São Paulo ii 2018 Dedico esta tese à ciência, e a todos os seus amantes. O, reason not the need! Our basest beggars Are in the poorest thing superfluous. Allow not nature more than nature needs, Man’s life is cheap as beast’s. Thou art a lady: If only to go warm were gorgeous, Why, nature needs not what thou gorgeous wear’st Which scarcely keeps thee warm. But, for true need- You heavens, give me that patience, patience I need! You see me here, you gods, a poor old man, As full of grief as age; wretched in both.” iii King Lear, William Shakespeare, 1608 Agradecimentos Agradeço em primeiro lugar ao meu grande amor Danilo, sem ele, há 11 anos, essa jornada não teria começado, a vida não teria me surpreendido e eu estaria de volta em casa, com todos os peixinhos do mar, e infeliz pelo resto da minha vida. Agradeço minha família, principalmente minha mãe Flávia e meu pai Airton por sacrificarem com mínimos protestos, as melhores horas que passaríamos juntos para que eu cumprisse meu trabalho.
[Show full text]