Probe Set Gene Accession Fold Change Supplemental Table 1
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ASPA Gene Aspartoacylase
ASPA gene aspartoacylase Normal Function The ASPA gene provides instructions for making an enzyme called aspartoacylase. In the brain, this enzyme breaks down a compound called N-acetyl-L-aspartic acid (NAA) into aspartic acid (an amino acid that is a building block of many proteins) and another molecule called acetic acid. The production and breakdown of NAA appears to be critical for maintaining the brain's white matter, which consists of nerve fibers surrounded by a myelin sheath. The myelin sheath is the covering that protects nerve fibers and promotes the efficient transmission of nerve impulses. The precise function of NAA is unclear. Researchers had suspected that it played a role in the production of the myelin sheath, but recent studies suggest that NAA does not have this function. The enzyme may instead be involved in the transport of water molecules out of nerve cells (neurons). Health Conditions Related to Genetic Changes Canavan disease More than 80 mutations in the ASPA gene are known to cause Canavan disease, which is a rare inherited disorder that affects brain development. Researchers have described two major forms of this condition: neonatal/infantile Canavan disease, which is the most common and most severe form, and mild/juvenile Canavan disease. The ASPA gene mutations that cause the neonatal/infantile form severely impair the activity of aspartoacylase, preventing the breakdown of NAA and allowing this substance to build up to high levels in the brain. The mutations that cause the mild/juvenile form have milder effects on the enzyme's activity, leading to less accumulation of NAA. -
Global Histone Modification Fingerprinting in Human Cells Using
OPEN Citation: Cell Death Discovery (2017) 3, 16077; doi:10.1038/cddiscovery.2016.77 Official journal of the Cell Death Differentiation Association www.nature.com/cddiscovery ARTICLE Global histone modification fingerprinting in human cells using epigenetic reverse phase protein array Marina Partolina1,HazelCThoms1, Kenneth G MacLeod2, Giovanny Rodriguez-Blanco1,MatthewNClarke1, Anuroop V Venkatasubramani1,3, Rima Beesoo4, Vladimir Larionov5, Vidushi S Neergheen-Bhujun4, Bryan Serrels2, Hiroshi Kimura6, Neil O Carragher2 and Alexander Kagansky1,7 The balance between acetylation and deacetylation of histone proteins plays a critical role in the regulation of genomic functions. Aberrations in global levels of histone modifications are linked to carcinogenesis and are currently the focus of intense scrutiny and translational research investments to develop new therapies, which can modify complex disease pathophysiology through epigenetic control. However, despite significant progress in our understanding of the molecular mechanisms of epigenetic machinery in various genomic contexts and cell types, the links between epigenetic modifications and cellular phenotypes are far from being clear. For example, enzymes controlling histone modifications utilize key cellular metabolites associated with intra- and extracellular feedback loops, adding a further layer of complexity to this process. Meanwhile, it has become increasingly evident that new assay technologies which provide robust and precise measurement of global histone modifications are required, -
Generated by SRI International Pathway Tools Version 25.0, Authors S
Authors: Pallavi Subhraveti Ron Caspi Quang Ong Peter D Karp An online version of this diagram is available at BioCyc.org. Biosynthetic pathways are positioned in the left of the cytoplasm, degradative pathways on the right, and reactions not assigned to any pathway are in the far right of the cytoplasm. Transporters and membrane proteins are shown on the membrane. Ingrid Keseler Periplasmic (where appropriate) and extracellular reactions and proteins may also be shown. Pathways are colored according to their cellular function. Gcf_000725805Cyc: Streptomyces xanthophaeus Cellular Overview Connections between pathways are omitted for legibility. -
Identification of Proteins Differentially Expressed in the Conventional Renal Cell Carcinoma by Proteomic Analysis
J Korean Med Sci 2005; 20: 450-5 Copyright � The Korean Academy ISSN 1011-8934 of Medical Sciences Identification of Proteins Differentially Expressed in the Conventional Renal Cell Carcinoma by Proteomic Analysis Renal cell carcinoma (RCC) is one of the most malignant tumors in urology, and Jeong Seok Hwa, Hyo Jin Park*, due to its insidious onset patients frequently have advanced disease at the time of Jae Hun Jung, Sung Chul Kam, clinical presentation. Thus, early detection is crucial in management of RCC. To Hyung Chul Park, Choong Won Kim*, identify tumor specific proteins of RCC, we employed proteomic analysis. We pre- Kee Ryeon Kang*, Jea Seog Hyun, Ky Hyun Chung pared proteins from conventional RCC and the corresponding normal kidney tis- sues from seven patients with conventional RCC. The expression of proteins was Department of Urology and Biochemistry*, College of determined by silver stain after two-dimensional polyacrylamide gel electrophore- Medicine and Institute of Health Science, sis (2D-PAGE). The overall protein expression patterns in the RCC and the normal Gyeongsang National University, Jinju, Korea kidney tissues were quite similar except some areas. Of 66 differentially expressed Received : 29 December 2004 protein spots (p<0.05 by Student t-test), 8 different proteins from 11 spots were Accepted : 13 January 2005 identified by MALDI-TOF-MS. The expression of the following proteins was repress- ed (p<0.05); aminoacylase-1, enoyl-CoA hydratase, aldehyde reductase, tropo- Address for correspondence myosin -4 chain, agmatinase and ketohexokinase. Two proteins, vimentin and -1 Jeong Seok Hwa, M.D. Department of Urology, College of Medicine, antitrypsin precursor, were dominantly expressed in RCC (p<0.05). -
CUMMINGS-DISSERTATION.Pdf (4.094Mb)
D-AMINOACYLASES AND DIPEPTIDASES WITHIN THE AMIDOHYDROLASE SUPERFAMILY: RELATIONSHIP BETWEEN ENZYME STRUCTURE AND SUBSTRATE SPECIFICITY A Dissertation by JENNIFER ANN CUMMINGS Submitted to the Office of Graduate Studies of Texas A&M University in partial fulfillment of the requirements for the degree of DOCTOR OF PHILOSOPHY December 2010 Major Subject: Chemistry D-AMINOACYLASES AND DIPEPTIDASES WITHIN THE AMIDOHYDROLASE SUPERFAMILY: RELATIONSHIP BETWEEN ENZYME STRUCTURE AND SUBSTRATE SPECIFICITY A Dissertation by JENNIFER ANN CUMMINGS Submitted to the Office of Graduate Studies of Texas A&M University in partial fulfillment of the requirements for the degree of DOCTOR OF PHILOSOPHY Approved by: Chair of Committee, Frank Raushel Committee Members, Paul Lindahl David Barondeau Gregory Reinhart Head of Department, David Russell December 2010 Major Subject: Chemistry iii ABSTRACT D-Aminoacylases and Dipeptidases within the Amidohydrolase Superfamily: Relationship Between Enzyme Structure and Substrate Specificity. (December 2010) Jennifer Ann Cummings, B.S., Southern Oregon University; M.S., Texas A&M University Chair of Advisory Committee: Dr. Frank Raushel Approximately one third of the genes for the completely sequenced bacterial genomes have an unknown, uncertain, or incorrect functional annotation. Approximately 11,000 putative proteins identified from the fully-sequenced microbial genomes are members of the catalytically diverse Amidohydrolase Superfamily. Members of the Amidohydrolase Superfamily separate into 24 Clusters of Orthologous Groups (cogs). Cog3653 includes proteins annotated as N-acyl-D-amino acid deacetylases (DAAs), and proteins within cog2355 are homologues to the human renal dipeptidase. The substrate profiles of three DAAs (Bb3285, Gox1177 and Sco4986) and six microbial dipeptidase (Sco3058, Gox2272, Cc2746, LmoDP, Rsp0802 and Bh2271) were examined with N-acyl-L-, N-acyl-D-, L-Xaa-L-Xaa, L-Xaa-D-Xaa and D-Xaa-L-Xaa substrate libraries. -
WO2019226953A1.Pdf
) ( 2 (51) International Patent Classification: Street, Brookline, MA 02446 (US). WILSON, Christo¬ C12N 9/22 (2006.01) pher, Gerard; 696 Main Street, Apartment 311, Waltham, MA 0245 1(US). DOMAN, Jordan, Leigh; 25 Avon Street, (21) International Application Number: Somverville, MA 02143 (US). PCT/US20 19/033 848 (74) Agent: HEBERT, Alan, M. et al. ;Wolf, Greenfield, Sacks, (22) International Filing Date: P.C., 600 Atlanitc Avenue, Boston, MA 02210-2206 (US). 23 May 2019 (23.05.2019) (81) Designated States (unless otherwise indicated, for every (25) Filing Language: English kind of national protection av ailable) . AE, AG, AL, AM, (26) Publication Language: English AO, AT, AU, AZ, BA, BB, BG, BH, BN, BR, BW, BY, BZ, CA, CH, CL, CN, CO, CR, CU, CZ, DE, DJ, DK, DM, DO, (30) Priority Data: DZ, EC, EE, EG, ES, FI, GB, GD, GE, GH, GM, GT, HN, 62/675,726 23 May 2018 (23.05.2018) US HR, HU, ID, IL, IN, IR, IS, JO, JP, KE, KG, KH, KN, KP, 62/677,658 29 May 2018 (29.05.2018) US KR, KW, KZ, LA, LC, LK, LR, LS, LU, LY, MA, MD, ME, (71) Applicants: THE BROAD INSTITUTE, INC. [US/US]; MG, MK, MN, MW, MX, MY, MZ, NA, NG, NI, NO, NZ, 415 Main Street, Cambridge, MA 02142 (US). PRESI¬ OM, PA, PE, PG, PH, PL, PT, QA, RO, RS, RU, RW, SA, DENT AND FELLOWS OF HARVARD COLLEGE SC, SD, SE, SG, SK, SL, SM, ST, SV, SY, TH, TJ, TM, TN, [US/US]; 17 Quincy Street, Cambridge, MA 02138 (US). -
Inhibition of N-Acetylglutamate Synthase by Various Monocarboxylic and Dicarboxylic Short-Chain Coenzyme a Esters and the Production of Alternative Glutamate Esters☆
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Elsevier - Publisher Connector Biochimica et Biophysica Acta 1842 (2014) 2510–2516 Contents lists available at ScienceDirect Biochimica et Biophysica Acta journal homepage: www.elsevier.com/locate/bbadis Inhibition of N-acetylglutamate synthase by various monocarboxylic and dicarboxylic short-chain coenzyme A esters and the production of alternative glutamate esters☆ M. Dercksen a,b,⁎, L. IJlst a, M. Duran a, L.J. Mienie b, A. van Cruchten a, F.H. van der Westhuizen b, R.J.A. Wanders a a Laboratory Genetic Metabolic Diseases, Departments of Pediatrics and Clinical Chemistry, Academic Medical Centre, University of Amsterdam, Meibergdreef 9, 1105 AZ Amsterdam, The Netherlands b Centre for Human Metabonomics, North-West University (Potchefstroom Campus), Hoffman street 11, Potchefstroom, South Africa, 2520 article info abstract Article history: Hyperammonemia is a frequent finding in various organic acidemias. One possible mechanism involves the Received 11 December 2012 inhibition of the enzyme N-acetylglutamate synthase (NAGS), by short-chain acyl-CoAs which accumulate due Received in revised form 9 April 2013 to defective catabolism of amino acids and/or fatty acids in the cell. The aim of this study was to investigate the Accepted 29 April 2013 effect of various acyl-CoAs on the activity of NAGS in conjunction with the formation of glutamate esters. NAGS Available online 2 May 2013 activity was measured in vitro using a sensitive enzyme assay with ultraperformance liquid chromatography– – Keywords: tandem mass spectrometry (UPLC MS/MS) product analysis. Propionyl-CoA and butyryl-CoA proved to be the N-acetylglutamate synthase most powerful inhibitors of N-acetylglutamate (NAG) formation. -
N-Acetylglutamate Content in Liver and Gut of Normal and Fasted Mice, Normal Human Livers, and Livers of Individuals with Carbam
003 I -3998/90/2704-0408$02.00/0 PEDIATRIC RESEARCH Vol. 27, No. 4, 1990 Copyright O 1990 International Pediatric Research Foundation, Inc Printed in U.S. A. N-Acetylglutamate Content in Liver and Gut of Normal and Fasted Mice, Normal Human Livers, and Livers of Individuals with Carbamyl Phosphate Synthetase or Ornithine Transcarbamylase Deficiency MENDEL TUCHMAN AND ROBERT A. HOLZKNECHT Division ofMetabolism, Depurtmmt.~ofPediatrics and Laboratory Medicine and Pulhology, Universifyu/ Minnesota, Minneapolis, Minnesota 55455 ABSTRACT. N-acetylglutamate (NAG) content was CPS I, carbamyl phosphate synthetase I measured in homogenates of liver and small intestine ob- OTC, ornithine transcarbamylase tained from normal and 24-h starved syngeneic mice. Sub- GC-MS, gas chromatography-mass spectrometry sequently, NAG was determined in normal, and in car- MSD, mass selective detector bamyl phosphate synthetase I and ornithine transcarbam- SIM, selected ion monitoring ylase enzyme-deficient human liver tissue homogenates. TMS, trimethylsilyl The method used in this study, which is direct and highly specific, used anion exchange extraction, gas chromato- graphic separation, and mass spectrometric detection and quantitation. Hepatic NAG content in the fed animals was In 1953, Grisolia and Cohen (1) discovered that a derivative 94.8 + 19.8 nmoljg tissue or 602.5 + 168.4 nmol/g protein n of L-glutamic acid enhanced the biosynthesis of L-citrulline by (mean + SD, = 5), whereas it was much lower in the preparation of mammalian liver. This naturally occumng com- fasted mice (49.4 + 13.0 nmol/g tissue or 330.1 + 113.9 n pound was isolated and identified as NAG, which is the cofactor nmol/g protein, mean + SD, = 5). -
Global Histone Modification Fingerprinting in Human Cells Using Epigenetic Reverse Phase Protein Array
Edinburgh Research Explorer Global histone modification fingerprinting in human cells using epigenetic reverse phase protein array Citation for published version: Partolina, M, Thoms, HC, Macleod, KG, Rodriguez-blanco, G, Clarke, MN, Venkatasubramani, AV, Beesoo, R, Larionov, V, Neergheen-bhujun, VS, Serrels, B, Kimura, H, Carragher, NO & Kagansky, A 2017, 'Global histone modification fingerprinting in human cells using epigenetic reverse phase protein array', Cell Death Discovery, vol. 3, pp. 16077. https://doi.org/10.1038/cddiscovery.2016.77 Digital Object Identifier (DOI): 10.1038/cddiscovery.2016.77 Link: Link to publication record in Edinburgh Research Explorer Document Version: Publisher's PDF, also known as Version of record Published In: Cell Death Discovery Publisher Rights Statement: This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ General rights Copyright for the publications made accessible via the Edinburgh Research Explorer is retained by the author(s) and / or other copyright owners and it is a condition of accessing these publications that users recognise and abide by the legal requirements associated with these rights. Take down policy The University of Edinburgh has made every reasonable effort to ensure that Edinburgh Research Explorer content complies with UK legislation. -
Biochemical and Proteomic Profiling of Maize Endosperm Texture and Protein Quality Kyla J
University of Nebraska - Lincoln DigitalCommons@University of Nebraska - Lincoln Theses, Dissertations, and Student Research in Agronomy and Horticulture Department Agronomy and Horticulture 7-2015 Biochemical and Proteomic Profiling of Maize Endosperm Texture and Protein Quality Kyla J. Morton University of Nebraska-Lincoln Follow this and additional works at: http://digitalcommons.unl.edu/agronhortdiss Part of the Agricultural Science Commons, Agronomy and Crop Sciences Commons, Plant Biology Commons, and the Plant Breeding and Genetics Commons Morton, Kyla J., "Biochemical and Proteomic Profiling of Maize Endosperm Texture and Protein Quality" (2015). Theses, Dissertations, and Student Research in Agronomy and Horticulture. 88. http://digitalcommons.unl.edu/agronhortdiss/88 This Article is brought to you for free and open access by the Agronomy and Horticulture Department at DigitalCommons@University of Nebraska - Lincoln. It has been accepted for inclusion in Theses, Dissertations, and Student Research in Agronomy and Horticulture by an authorized administrator of DigitalCommons@University of Nebraska - Lincoln. BIOCHEMICAL AND PROTEOMIC PROFILING OF MAIZE ENDOSPERM TEXTURE AND PROTEIN QUALITY by Kyla J. Morton A DISSERTATION Presented to the Faculty of The Graduate College at the University of Nebraska In Partial Fulfillment of Requirements For the Degree of Doctor of Philosophy Major: Agronomy and Horticulture (Plant Breeding and Genetics) Under the Supervision of Professor David R. Holding Lincoln, Nebraska July, 2015 BIOCHEMICAL AND PROTEOMIC ANALYSIS OF MAIZE ENDOSPERM KERNEL TEXTURE AND PROTEIN QUALITY Kyla J. Morton, Ph.D. University of Nebraska, 2015 Advisor: David R. Holding The research described herein, focuses on the biochemical and proteomic analysis of the maize endosperm and what influences kernel texture. -
PHARMACOLOGY REVIEW(S) Comments on N 22-562 Carbaglu Carglumic Acid from Abby Jacobs, AD Date: 3/15/10
CENTER FOR DRUG EVALUATION AND RESEARCH APPLICATION NUMBER: 22-562 PHARMACOLOGY REVIEW(S) Comments on N 22-562 Carbaglu carglumic acid From Abby Jacobs, AD Date: 3/15/10 1. I concur that there are no pharm/tox issues with approval and the labeling of pharm/tox portions is acceptable, with the changes suggested by the reviewer. 2. I do not concur with the postmarketing requests a. There is no need for a chronic study in nonrodents in addition to the rodent chronic study -The number of animals per group will be small -There are human data sufficient for approval. -The animals tested will not have the condition of hyperammonemia, and thus adverse effects observed at high doses may not be relevant to the patient population -the drug is lifesaving - the number of persons having this condition is rather small b. There is no need for a carcinogenicity study The animals tested will not have the condition of hyperammonemia, and thus adverse effects observed at high doses may not be relevant to the patient population -the drug is lifesaving and - the number of persons having this condition is rather small Application Submission Type/Number Type/Number Submitter Name Product Name -------------------- -------------------- -------------------- ------------------------------------------ NDA-22562 ORIG-1 ORPHAN EUROPE CARBAGLU (CARGLUMIC ACID) --------------------------------------------------------------------------------------------------------- This is a representation of an electronic record that was signed electronically and this page is the manifestation of the electronic signature. --------------------------------------------------------------------------------------------------------- /s/ ---------------------------------------------------- ABIGAIL ABBY C C JACOBS 03/15/2010 MEMORANDUM DEPARTMENT OF HEALTH AND HUMAN SERVICES PUBLIC HEALTH SERVICE FOOD AND DRUG ADMINISTRATION CENTER FOR DRUG EVALUATION AND RESEARCH FROM: David B. -
The Use of Immobilized Enzymes in the Food Industry: a Review
C R C Critical Reviews in Food Science and Nutrition ISSN: 0099-0248 (Print) (Online) Journal homepage: http://www.tandfonline.com/loi/bfsn19 The use of immobilized enzymes in the food industry: A review Arun Kilara , Khem M. Shahani & Triveni P. Shukla To cite this article: Arun Kilara , Khem M. Shahani & Triveni P. Shukla (1979) The use of immobilized enzymes in the food industry: A review, C R C Critical Reviews in Food Science and Nutrition, 12:2, 161-198, DOI: 10.1080/10408397909527276 To link to this article: https://doi.org/10.1080/10408397909527276 Published online: 29 Sep 2009. Submit your article to this journal Article views: 73 View related articles Citing articles: 24 View citing articles Full Terms & Conditions of access and use can be found at http://www.tandfonline.com/action/journalInformation?journalCode=bfsn19 Download by: [Texas A&M University Libraries] Date: 09 January 2018, At: 11:05 December 1979 161 THE USE OF IMMOBILIZED ENZYMES IN THE FOOD INDUSTRY: A REVIEW* Authors: ArunKilara** Khem M. Shahani Department of Food Science and Technology University of Nebraska Lincoln, Nebraska Referee: Triveni P. Shukla Krause Milling Company Milwaukee, Wisconsin INTRODUCTION Enzymes are organic substances produced by living cells which catalyze physiologi- cally significant reactions. Enzymes often are defined as biocatalysts, and they possess greater catalytic activity than chemical catalysts. All known enzymes are protein in nature and are generally colloidal, thermolabile, have relatively high molecular weights, exhibit high degrees of stereochemical and substrate specificities, and can usu- ally be isolated from the living cell. There are a wide variety of enzymes which contrib- ute, in part, to the biological diversity observed in nature.