DOCSLIB.ORG

Localization Developmental Process Response to Stimulus Signaling

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text

Load more

male germ-line positive a regulation of type antigen processing adult somatic relaxation of stem cell regulation of beak entry into III interferon stabilization of CRD-mediated mRNA and presentation of beak development muscle skeletal muscle population systemic arterial morphogenesis diapause production membrane potential stabilization exogenous peptide monocyte activation development maintenance blood pressure flight forward locomotion antigen via MHC class Regulation of I, TAP-dependent Developmental process biological quality negative Immune system Locomotion sensory organ positive regulation of branched duct hatching secondary neural regulation of precursor cell endoplasmic reticulum oenocyte leading edge cell epithelial cell fate leading edge cell tube formation transmission of process division calcium ion concentration differentiation fate commitment determination, open differentiation nerve impulse hemocyte development regulation of toll-like tracheal system multivesicular body receptor 5 Multicellular organismal process size involved in actin inductive cell endosome transport signaling polymerization-dependent cell motility migration amnioserosa regulation of pathway presynaptic corticotropin regulation of neutrophil angiogenesis formation collateral cellular pH reduction membrane assembly hormone differentiation oenocyte tendon cell involved in proepicardium sprouting of secreting cell development differentiation coronary vascular development injured axon differentiation morphogenesis post-embryonic zygotic specification endodermal-mesodermal positive regulation basolateral protein localization limb morphogenesis of dorsal/ventral axis cell signaling of photoreceptor cell glucose 1-phosphate UDP-glucuronate positive intermediate hermaphrodite metabolic process metabolic process nurse cell nucleus labial disc differentiation microtubule-based regulation of Wnt mesoderm genitalia anchoring development Localization peroxisome Signaling signaling pathway development development localization by BMP signaling transmembrane pathway positive regulation of receptor protein histone H2A-K15 nuclear-transcribed mRNA sialic acid transport spermine catabolic process Metabolic process tyrosine phosphatase ubiquitination catabolic process, nonsense-mediated decay signaling pathway detection of 3’-phosphoadenosine detection of virus response to cobalt ion UDP-glucuronate 5’-phosphosulfate glycerol biosynthetic muscle stretch Catabolism biosynthetic process biosynthetic process process from pyruvate maternal ribonucleoside negative regulation protein deubiquitination aggressive vulval location Cellular involved in ubiquitin-dependent triphosphate of histone H3-K36 behavior cell cycle phase Response to stimulus protein catabolic process catabolic process methylation biosythetic Reproductive regulation of cellular process response to response to corticosterone regulation of prostaglandin response to drug nuclear matrix zonula adherens process selenium ion biosynthetic process organization maintenance fusome organization dosage compensation negative regulation positive regulation of B by hypoactivation of transposition, cell apoptotic process of X chromosome RNA-mediated Cellular component constitutive protein negative ectodomain proteolysis reorganization negative regulation regulation of regulation of macrophage of ligase activity phospholipase establishment of regulation of Rap Regulation of biological process proteinase colony-stimulating actin filament telomere C activity proximal/distal protein signal cell polarity cellular response to activated factor signaling reorganization maintenance via caloric restriction transduction positive regulation of negative regulation of positive regulation of Negative receptor activity pathway involved in semi-conservative neurotransmitter protein geranylgeranylation cholesterol efflux glutamate secretion cell cycle replication regulation of receptor metabolism catalytic activity b negative regulation basolateral protein response to DNA damage urate transport directional locomotion inductive cell migration of RNA polymerase I response to histone H3-K18 localization regulation of silicon dioxide induced protein regulatory region L-ascorbic acid acetylation ligase activity phosphorylation sequence-specific DNA binding Locomotion Regulation of acetylcholine transport actin-myosin molecular function Response to stimulus acetate ester forward locomotion filament sliding response to transport positive regulation of ligase activity methylmercury protein O-linked netrin-activated fucosylation regulation of signaling Localization integrin activation pathway negative erythrophore differentiation diacylglycerol maternal regulation of transcytosis biosynthetic process aggressive fatty acid Cell oocyte fate detection of sialic acid transport determination Cellular behavior gurken signaling transport differentiation muscle stretch biosynthetic pathway regulation of Cdc42 protein oenocyte differentiation process Reproductive signal transduction process regulation of prostaglandin biosynthetic process sperm ejaculation negative stomatogastric post-embryonic Catabolism negative regulation of involuntary skeletal regulation of nervous system limb transcription of muscle contraction ribonucleoside regulation of nuclear large rRNA post-translational development morphogenesis polyamine U2 snRNA 3’-end triphosphate processing growth rate transcript from RNA protein catabolic process polymerase I promoter Multicellular organismal catabolic process antigen processing and modification presentation of cell cycle phase process exogenous peptide tracheal pit regulation of germ-band antigen via MHC class I Regulation of biological process formation in open R8 cell spacing shortening regulation of tracheal system in compound eye Cellular endosome size component organization dosage induction of compensation by programmed nuclear matrix intercellular bridge gas homeostasis regulation of cell death comma-shaped organization organization hydrogen peroxide hypoactivation blood vessel interleukin-10 contact inhibition body biosynthesis of X chromosome positive regulation of maturation biosynthetic morphogenesis anterior head development process UCE TB I COL PR1 PNT2 4 9 6 9 0 TAM 9 CNG 1 A V 00 0 0 100 1 BAR C 93 98 100 100 IV VRN 8 9 100 POL 1 III 0 0 HON SAL B BOA PED VI SEV II F1 0.04 LOY REVIGO Gene Ontology treemap chromosome organization dosage compensation complex assembly CRD−mediated mRNA stabilization dosage compensation involved in dosage compensation by hyperactivation of X chromosome chromosome organization single−organism process mitotic sister biological_process organelle chromatid organization segregation positive regulation protein−DNA protein−DNA complex of macromolecule regulation of metabolic process complex assembly subunit organization metabolic process establishment of regulation of cortical protein negative regulation of mitochondrion cellular process transcription regulation biological quality anchoring cholesterol efflux localization negative regulation of cellular catabolic process response to Ral protein low−density single−organism cellular process signal lipoprotein modulation by positive regulation transduction positive regulation of particle symbiont of host of killing of cells cholesterol storage multicellular apoptotic process of other organism cellular component DNA organismal regulation of cellular organization or metabolism process response to low−density biogenesis metabolic process multicellular organism development multicellular lipoprotein particle regulation of negative regulation regulation of exocyst response to cellular organism development RNA stability of metabolic process localization lipoprotein response regulation of particle to heat odontogenesis mitotic biological negative regulation of autophagy regulation of regulation of regulation of nurse cell nucleus developmental process anaphase B regulation transcription from RNA catabolic process cellular process anchoring SMAD protein signal polymerase II promoter transduction REVIGO Gene Ontology treemap ethanolamine kinase activity ATP−dependent RNA helicase activity kinase activity binding protein binding RNA−dependent ATPase activity RNA helicase activity choline kinase activity RNA−dependent ATPase activity chromatin binding R−SMAD binding GTPase activator activity nucleic acid bindingdouble−stranded RNA bindingdouble−stranded RNA binding REVIGO Gene Ontology treemap dosage CRD−mediated mRNA kinesin complex compensation stability complex complex intracellular cell part cell part cellular_component cytoskeletal part cytoskeleton intracellular organelle intracellular part complexes intracellular chromosomal part microtubule plus−end chromosome organelle part intracellular polytene sex chromosome non−membrane−bounded Noc complex organelle chromosome cell Noc1p−Noc2p organelle complexesx complex non−membrane−bounded SREBP−SCAP−Insig organelle part protein complex organelle complex.
Recommended publications
  • Gene Symbol Gene Description ACVR1B Activin a Receptor, Type IB

    Gene Symbol Gene Description ACVR1B Activin a Receptor, Type IB

    Table S1. Kinase clones included in human kinase cDNA library for yeast two-hybrid screening Gene Symbol Gene Description ACVR1B activin A receptor, type IB ADCK2 aarF domain containing kinase 2 ADCK4 aarF domain containing kinase 4 AGK multiple substrate lipid kinase;MULK AK1 adenylate kinase 1 AK3 adenylate kinase 3 like 1 AK3L1 adenylate kinase 3 ALDH18A1 aldehyde dehydrogenase 18 family, member A1;ALDH18A1 ALK anaplastic lymphoma kinase (Ki-1) ALPK1 alpha-kinase 1 ALPK2 alpha-kinase 2 AMHR2 anti-Mullerian hormone receptor, type II ARAF v-raf murine sarcoma 3611 viral oncogene homolog 1 ARSG arylsulfatase G;ARSG AURKB aurora kinase B AURKC aurora kinase C BCKDK branched chain alpha-ketoacid dehydrogenase kinase BMPR1A bone morphogenetic protein receptor, type IA BMPR2 bone morphogenetic protein receptor, type II (serine/threonine kinase) BRAF v-raf murine sarcoma viral oncogene homolog B1 BRD3 bromodomain containing 3 BRD4 bromodomain containing 4 BTK Bruton agammaglobulinemia tyrosine kinase BUB1 BUB1 budding uninhibited by benzimidazoles 1 homolog (yeast) BUB1B BUB1 budding uninhibited by benzimidazoles 1 homolog beta (yeast) C9orf98 chromosome 9 open reading frame 98;C9orf98 CABC1 chaperone, ABC1 activity of bc1 complex like (S. pombe) CALM1 calmodulin 1 (phosphorylase kinase, delta) CALM2 calmodulin 2 (phosphorylase kinase, delta) CALM3 calmodulin 3 (phosphorylase kinase, delta) CAMK1 calcium/calmodulin-dependent protein kinase I CAMK2A calcium/calmodulin-dependent protein kinase (CaM kinase) II alpha CAMK2B calcium/calmodulin-dependent
  • Conserved Phosphoryl Transfer Mechanisms Within Kinase Families

    Conserved Phosphoryl Transfer Mechanisms Within Kinase Families

    Kenyon et al. BMC Research Notes 2012, 5:131 http://www.biomedcentral.com/1756-0500/5/131 RESEARCHARTICLE Open Access Conserved phosphoryl transfer mechanisms within kinase families and the role of the C8 proton of ATP in the activation of phosphoryl transfer Colin P Kenyon*, Robyn L Roth, Chris W van der Westhuyzen and Christopher J Parkinson Abstract Background: The kinome is made up of a large number of functionally diverse enzymes, with the classification indicating very little about the extent of the conserved kinetic mechanisms associated with phosphoryl transfer. It has been demonstrated that C8-H of ATP plays a critical role in the activity of a range of kinase and synthetase enzymes. Results: A number of conserved mechanisms within the prescribed kinase fold families have been identified directly utilizing the C8-H of ATP in the initiation of phosphoryl transfer. These mechanisms are based on structurally conserved amino acid residues that are within hydrogen bonding distance of a co-crystallized nucleotide. On the basis of these conserved mechanisms, the role of the nucleotide C8-H in initiating the formation of a pentavalent intermediate between the g-phosphate of the ATP and the substrate nucleophile is defined. All reactions can be clustered into two mechanisms by which the C8-H is induced to be labile via the coordination of a backbone carbonyl to C6-NH2 of the adenyl moiety, namely a “push” mechanism, and a “pull” mechanism, based on the protonation of N7. Associated with the “push” mechanism and “pull” mechanisms are a series of proton transfer cascades, initiated from C8-H, via the tri-phosphate backbone, culminating in the formation of the pentavalent transition state between the g-phosphate of the ATP and the substrate nucleophile.
  • Choline Kinase Inhibition As a Treatment Strategy for Cancers With

    Choline Kinase Inhibition As a Treatment Strategy for Cancers With

    Choline Kinase Inhibition as a Treatment Strategy of Cancers with Deregulated Lipid Metabolism Sebastian Trousil Imperial College London Department of Surgery and Cancer A dissertation submitted for the degree of Doctor of Philosophy 2 Declaration I declare that this dissertation is my own and original work, except where explicitly acknowledged. The copyright of this thesis rests with the author and is made available under a Creative Commons Attribution Non-Commercial No Derivatives licence. Researchers are free to copy, distribute or transmit the thesis on the condition that they attribute it, that they do not use it for commercial purposes and that they do not alter, transform or build upon it. For any reuse or redistribution, researchers must make clear to others the licence terms of this work. Abstract Aberrant choline metabolism is a characteristic shared by many human cancers. It is predominantly caused by elevated expression of choline kinase alpha, which catalyses the phosphorylation of choline to phosphocholine, an essential precursor of membrane lipids. In this thesis, a novel choline kinase inhibitor has been developed and its therapeutic potential evaluated. Furthermore the probe was used to elaborate choline kinase biology. A lead compound, ICL-CCIC-0019 (IC50 of 0.27 0.06 µM), was identified through a focused library screen. ICL-CCIC-0019 was competitive± with choline and non-competitive with ATP. In a selectivity screen of 131 human kinases, ICL-CCIC-0019 inhibited only 5 kinases more than 20% at a concentration of 10 µM(< 35% in all 131 kinases). ICL- CCIC-0019 potently inhibited cell growth in a panel of 60 cancer cell lines (NCI-60 screen) with a median GI50 of 1.12 µM (range: 0.00389–16.2 µM).
  • Change in Brain Plasmalogen Composition by Exposure to Prenatal Undernutrition Leads to Behavioral Impairment of Rats

    Change in Brain Plasmalogen Composition by Exposure to Prenatal Undernutrition Leads to Behavioral Impairment of Rats

    Research Articles: Behavioral/Cognitive Change in brain plasmalogen composition by exposure to prenatal undernutrition leads to behavioral impairment of rats https://doi.org/10.1523/JNEUROSCI.2721-18.2019 Cite as: J. Neurosci 2019; 10.1523/JNEUROSCI.2721-18.2019 Received: 21 October 2018 Revised: 28 July 2019 Accepted: 31 July 2019 This Early Release article has been peer-reviewed and accepted, but has not been through the composition and copyediting processes. The final version may differ slightly in style or formatting and will contain links to any extended data. Alerts: Sign up at www.jneurosci.org/alerts to receive customized email alerts when the fully formatted version of this article is published. Copyright © 2019 the authors 1 Change in brain plasmalogen composition by exposure to prenatal 2 undernutrition leads to behavioral impairment of rats 3 4 Abbreviated title: Ethanolamine plasmalogen and behavior 5 6 Kodai Hino1, Shunya Kaneko1, Toshiya Harasawa1, Tomoko Kimura1, Shiro Takei2, 7 Masakazu Shinohara3,4, Fumiyoshi Yamazaki5, Shin-ya Morita6, Shumpei Sato5, 8 Yoshihito Kubo1, Tadaaki Kono1, Mitsutoshi Setou5,7,8, Mina Yoshioka1, Junya Fujino1, 9 Hiroyuki Sugihara9, Hideto Kojima10, Naoto Yamada11, Jun Udagawa1 10 11 1Division of Anatomy and Cell Biology, Department of Anatomy, Shiga University of 12 Medical Science, Otsu 520-2192, Japan 13 2Department of Environmental Biology, College of Bioscience and Biotechnology, 14 Chubu University, Kasugai, 487-8501, Japan 15 3Division of Epidemiology, Kobe University Graduate School
  • O O2 Enzymes Available from Sigma Enzymes Available from Sigma

    O O2 Enzymes Available from Sigma Enzymes Available from Sigma

    COO 2.7.1.15 Ribokinase OXIDOREDUCTASES CONH2 COO 2.7.1.16 Ribulokinase 1.1.1.1 Alcohol dehydrogenase BLOOD GROUP + O O + O O 1.1.1.3 Homoserine dehydrogenase HYALURONIC ACID DERMATAN ALGINATES O-ANTIGENS STARCH GLYCOGEN CH COO N COO 2.7.1.17 Xylulokinase P GLYCOPROTEINS SUBSTANCES 2 OH N + COO 1.1.1.8 Glycerol-3-phosphate dehydrogenase Ribose -O - P - O - P - O- Adenosine(P) Ribose - O - P - O - P - O -Adenosine NICOTINATE 2.7.1.19 Phosphoribulokinase GANGLIOSIDES PEPTIDO- CH OH CH OH N 1 + COO 1.1.1.9 D-Xylulose reductase 2 2 NH .2.1 2.7.1.24 Dephospho-CoA kinase O CHITIN CHONDROITIN PECTIN INULIN CELLULOSE O O NH O O O O Ribose- P 2.4 N N RP 1.1.1.10 l-Xylulose reductase MUCINS GLYCAN 6.3.5.1 2.7.7.18 2.7.1.25 Adenylylsulfate kinase CH2OH HO Indoleacetate Indoxyl + 1.1.1.14 l-Iditol dehydrogenase L O O O Desamino-NAD Nicotinate- Quinolinate- A 2.7.1.28 Triokinase O O 1.1.1.132 HO (Auxin) NAD(P) 6.3.1.5 2.4.2.19 1.1.1.19 Glucuronate reductase CHOH - 2.4.1.68 CH3 OH OH OH nucleotide 2.7.1.30 Glycerol kinase Y - COO nucleotide 2.7.1.31 Glycerate kinase 1.1.1.21 Aldehyde reductase AcNH CHOH COO 6.3.2.7-10 2.4.1.69 O 1.2.3.7 2.4.2.19 R OPPT OH OH + 1.1.1.22 UDPglucose dehydrogenase 2.4.99.7 HO O OPPU HO 2.7.1.32 Choline kinase S CH2OH 6.3.2.13 OH OPPU CH HO CH2CH(NH3)COO HO CH CH NH HO CH2CH2NHCOCH3 CH O CH CH NHCOCH COO 1.1.1.23 Histidinol dehydrogenase OPC 2.4.1.17 3 2.4.1.29 CH CHO 2 2 2 3 2 2 3 O 2.7.1.33 Pantothenate kinase CH3CH NHAC OH OH OH LACTOSE 2 COO 1.1.1.25 Shikimate dehydrogenase A HO HO OPPG CH OH 2.7.1.34 Pantetheine kinase UDP- TDP-Rhamnose 2 NH NH NH NH N M 2.7.1.36 Mevalonate kinase 1.1.1.27 Lactate dehydrogenase HO COO- GDP- 2.4.1.21 O NH NH 4.1.1.28 2.3.1.5 2.1.1.4 1.1.1.29 Glycerate dehydrogenase C UDP-N-Ac-Muramate Iduronate OH 2.4.1.1 2.4.1.11 HO 5-Hydroxy- 5-Hydroxytryptamine N-Acetyl-serotonin N-Acetyl-5-O-methyl-serotonin Quinolinate 2.7.1.39 Homoserine kinase Mannuronate CH3 etc.
  • 12) United States Patent (10

    12) United States Patent (10

    US007635572B2 (12) UnitedO States Patent (10) Patent No.: US 7,635,572 B2 Zhou et al. (45) Date of Patent: Dec. 22, 2009 (54) METHODS FOR CONDUCTING ASSAYS FOR 5,506,121 A 4/1996 Skerra et al. ENZYME ACTIVITY ON PROTEIN 5,510,270 A 4/1996 Fodor et al. MICROARRAYS 5,512,492 A 4/1996 Herron et al. 5,516,635 A 5/1996 Ekins et al. (75) Inventors: Fang X. Zhou, New Haven, CT (US); 5,532,128 A 7/1996 Eggers Barry Schweitzer, Cheshire, CT (US) 5,538,897 A 7/1996 Yates, III et al. s s 5,541,070 A 7/1996 Kauvar (73) Assignee: Life Technologies Corporation, .. S.E. al Carlsbad, CA (US) 5,585,069 A 12/1996 Zanzucchi et al. 5,585,639 A 12/1996 Dorsel et al. (*) Notice: Subject to any disclaimer, the term of this 5,593,838 A 1/1997 Zanzucchi et al. patent is extended or adjusted under 35 5,605,662 A 2f1997 Heller et al. U.S.C. 154(b) by 0 days. 5,620,850 A 4/1997 Bamdad et al. 5,624,711 A 4/1997 Sundberg et al. (21) Appl. No.: 10/865,431 5,627,369 A 5/1997 Vestal et al. 5,629,213 A 5/1997 Kornguth et al. (22) Filed: Jun. 9, 2004 (Continued) (65) Prior Publication Data FOREIGN PATENT DOCUMENTS US 2005/O118665 A1 Jun. 2, 2005 EP 596421 10, 1993 EP 0619321 12/1994 (51) Int. Cl. EP O664452 7, 1995 CI2O 1/50 (2006.01) EP O818467 1, 1998 (52) U.S.
  • Dema and Faust Et Al., Suppl. Material 2020.02.03

    Dema and Faust Et Al., Suppl. Material 2020.02.03

    Supplementary Materials Cyclin-dependent kinase 18 controls trafficking of aquaporin-2 and its abundance through ubiquitin ligase STUB1, which functions as an AKAP Dema Alessandro1,2¶, Dörte Faust1¶, Katina Lazarow3, Marc Wippich3, Martin Neuenschwander3, Kerstin Zühlke1, Andrea Geelhaar1, Tamara Pallien1, Eileen Hallscheidt1, Jenny Eichhorst3, Burkhard Wiesner3, Hana Černecká1, Oliver Popp1, Philipp Mertins1, Gunnar Dittmar1, Jens Peter von Kries3, Enno Klussmann1,4* ¶These authors contributed equally to this work 1Max Delbrück Center for Molecular Medicine in the Helmholtz Association (MDC), Robert- Rössle-Strasse 10, 13125 Berlin, Germany 2current address: University of California, San Francisco, 513 Parnassus Avenue, CA 94122 USA 3Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), Robert-Rössle-Strasse 10, 13125 Berlin, Germany 4DZHK (German Centre for Cardiovascular Research), Partner Site Berlin, Oudenarder Strasse 16, 13347 Berlin, Germany *Corresponding author Enno Klussmann Max Delbrück Center for Molecular Medicine Berlin in the Helmholtz Association (MDC) Robert-Rössle-Str. 10, 13125 Berlin Germany Tel. +49-30-9406 2596 FAX +49-30-9406 2593 E-mail: [email protected] 1 Content 1. CELL-BASED SCREENING BY AUTOMATED IMMUNOFLUORESCENCE MICROSCOPY 3 1.1 Screening plates 3 1.2 Image analysis using CellProfiler 17 1.4 Identification of siRNA affecting cell viability 18 1.7 Hits 18 2. SUPPLEMENTARY TABLE S4, FIGURES S2-S4 20 2 1. Cell-based screening by automated immunofluorescence microscopy 1.1 Screening plates Table S1. Genes targeted with the Mouse Protein Kinases siRNA sub-library. Genes are sorted by plate and well. Accessions refer to National Center for Biotechnology Information (NCBI, BLA) entries. The siRNAs were arranged on three 384-well microtitre platres.
  • Expression Profiling of Choline and Ethanolamine Kinases in MCF7, HCT116 and Hepg2 Cells, and the Transcriptional Regulation by Epigenetic Modification

    Expression Profiling of Choline and Ethanolamine Kinases in MCF7, HCT116 and Hepg2 Cells, and the Transcriptional Regulation by Epigenetic Modification

    MOLECULAR MEDICINE REPORTS 11: 611-618, 2015 Expression profiling of choline and ethanolamine kinases in MCF7, HCT116 and HepG2 cells, and the transcriptional regulation by epigenetic modification CHUA SIANG LING1, KHOO BOON YIN2, SEE TOO WEI CUN1 and FEW LING LING1 1School of Health Sciences, Universiti Sains Malaysia, Kubang Kerian, Kelantan 16150; 2Institute for Research in Molecular Medicine, Universiti Sains Malaysia, Penang 11800, Malaysia Received December 10, 2013; Accepted September 4, 2014 DOI: 10.3892/mmr.2014.2707 Abstract. The function of choline kinase (CK) and etha- cell lines were varied. The effects of TSA treatment on the nolamine kinase (EK) is to catalyse the phosphorylation mRNA expression levels of ck and ek imply that ck and ek of choline and ethanolamine, respectively, in order to yield mRNA expression may be regulated by epigenetic modifica- phosphocholine (PCho) and phosphoethanolamine (PEtn). A tion. high expression level of PCho, due to elevated CK activity, has previously been associated with malignant transformation. In Introduction the present study, a quantitative polymerase chain reaction was performed to determine the mRNA expression profiles of ck Choline kinase (CK) and ethanolamine kinase (EK) are enzymes and ek mRNA variants in MCF7 breast, HCT116 colon and that initiate the first step in the Kennedy pathway, resulting in HepG2 liver cancer cells. The ck and ek mRNA expression the biosynthesis of phosphatidylcholine and phosphatidyletha- profiles showed that total ckα was expressed most abundantly nolamine (1). In the presence of Mg2+, CK and EK catalyse the in the HepG2 cells. The HCT116 cells exhibited the highest ATP-dependent phosphorylation of choline and ethanolamine ckβ and ek1 mRNA expression levels, whereas the highest into phosphocholine (PCho) and phoshoethanolamine (PEtn), ek2α mRNA expression levels were detected in the MCF7 respectively.
  • Lipid Biosynthesis

    Lipid Biosynthesis

    Lipid Biosynthesis Objectives: I. Describe how excess carbohydrate and/or amino acid consumption leads to fatty acid and triacylglycerol production. II. What is the precursor of fatty acid biosynthesis (lipogenesis)? A. Where is it generated? B. How is it transported to the site of fatty acid biosynthesis? C. What other necessary precursors can be / are generated as part of the transport process? III. Describe how the precursor is activated for the biosynthesis pathway. IV. The Fatty Acid Biosynthesis Complex. A. Describe the Fatty Acid Biosynthesis Complex. B. Describe the six recurring reactions of fatty acid biosynthesis. C. What coenzymes are required for lipogenesis D. What is the final product of the Fatty Acid Biosynthesis Complex? V. What other reactions are necessary for the complete biosynthesis of the fatty acids needed by the cell? VI. Compare / Contrast β-oxidation of fatty acids and fatty acid biosynthesis. A. State at least three differences between lipogenesis (fatty acid synthesis) and β oxidation. VII. Describe the control points of fatty acid biosynthesis. A. Allosteric control B. Control by Reversible Covalent Modification C. Hormonal control 1. How does the control of lipogenesis integrate with the control of β-oxidation? 2. What is the Triacylglycerol Cycle and Glyceroneogenesis? VIII.Integrate fatty acid biosynthesis with carbohydrate metabolism. A. Describe the regulation of lipid and carbohydrate metabolism in relation to the liver, adipose tissue, and skeletal muscle B. Summarize the antagonistic effects of glucagon and insulin. IX. Describe the synthesis of A. Phosphatidate. B. The Triacylglycerols. C. The Phosphoglycerides. D. Sphingosine / Ceramide. X. Cholesterol Biosynthesis. A. In general terms, describe the synthesis of cholesterol.

  • Generate Metabolic Map Poster

    Authors: J. Michael Cherry Eurie Hong Benjamin Vincent Cynthia Krieger 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. Rama Balakrishnan Ron Caspi Periplasmic (where appropriate) and extracellular reactions and proteins may also be shown. Pathways are colored according to their cellular function. YeastCyc: Saccharomyces cerevisiae S288c Cellular Overview Connections between pathways are omitted for legibility.
  • A Meta-Analysis of the Effects of High-LET Ionizing Radiations in Human Gene Expression

    A Meta-Analysis of the Effects of High-LET Ionizing Radiations in Human Gene Expression

    Supplementary Materials A Meta-Analysis of the Effects of High-LET Ionizing Radiations in Human Gene Expression Table S1. Statistically significant DEGs (Adj. p-value < 0.01) derived from meta-analysis for samples irradiated with high doses of HZE particles, collected 6-24 h post-IR not common with any other meta- analysis group. This meta-analysis group consists of 3 DEG lists obtained from DGEA, using a total of 11 control and 11 irradiated samples [Data Series: E-MTAB-5761 and E-MTAB-5754]. Ensembl ID Gene Symbol Gene Description Up-Regulated Genes ↑ (2425) ENSG00000000938 FGR FGR proto-oncogene, Src family tyrosine kinase ENSG00000001036 FUCA2 alpha-L-fucosidase 2 ENSG00000001084 GCLC glutamate-cysteine ligase catalytic subunit ENSG00000001631 KRIT1 KRIT1 ankyrin repeat containing ENSG00000002079 MYH16 myosin heavy chain 16 pseudogene ENSG00000002587 HS3ST1 heparan sulfate-glucosamine 3-sulfotransferase 1 ENSG00000003056 M6PR mannose-6-phosphate receptor, cation dependent ENSG00000004059 ARF5 ADP ribosylation factor 5 ENSG00000004777 ARHGAP33 Rho GTPase activating protein 33 ENSG00000004799 PDK4 pyruvate dehydrogenase kinase 4 ENSG00000004848 ARX aristaless related homeobox ENSG00000005022 SLC25A5 solute carrier family 25 member 5 ENSG00000005108 THSD7A thrombospondin type 1 domain containing 7A ENSG00000005194 CIAPIN1 cytokine induced apoptosis inhibitor 1 ENSG00000005381 MPO myeloperoxidase ENSG00000005486 RHBDD2 rhomboid domain containing 2 ENSG00000005884 ITGA3 integrin subunit alpha 3 ENSG00000006016 CRLF1 cytokine receptor like
  • 1787 Genome-Wide Identification and Characterization of Eukaryotic Protein Kinases Kanhu Charan Das1, Parismita Kalita1, Timir

    1787 Genome-Wide Identification and Characterization of Eukaryotic Protein Kinases Kanhu Charan Das1, Parismita Kalita1, Timir

    [Frontiers in Bioscience, Landmark, 25, 1787-1827, June 1, 2020] Genome-wide identification and characterization of eukaryotic protein kinases Kanhu Charan Das1, Parismita Kalita1, Timir Tripathi1 1Molecular and Structural Biophysics Laboratory, Department of Biochemistry, North-Eastern Hill University, Shillong 793022, India TABLE OF CONTENTS 1. Abstract 2. Introduction 3. Methods 3.1. F. gigantica gene sequence retrieval 3.2. Generation of hidden markov models (HMMs) 3.3. Classification and domain analysis of FgePKs 4. Results 4.1. Identification of kinase-like proteins in F. gigantica genome 4.2. Classification and domain analysis of FgePKs 4.2.1. Ser/Thr kinase group 4.2.1.1. cAMP-dependent protein kinase (AGC) group 4.2.1.1.1. Protein kinase C (PKC) 4.2.1.1.2. Protein kinase A (PKA) 4.2.1.2. Calmodulin kinase (CaMK) group 4.2.1.3. Cyclin-dependent kinase and other close relatives (CMGC) group 4.2.1.3.1. Cyclin dependent kinases (CDK) 4.2.1.3.2. Mitogen activated protein kinases (MAPK) 4.2.1.3.3. Glycogen synthase 3 kinases (GSK3) 4.2.1.3.4. Dual-specificity Tyr regulated kinases (DYRK) 4.2.1.4. Sterile Ser/Thr kinase (STE) group 4.2.1.5. Casein kinase 1 (CK1) group 4.2.2. Tyr kinase group 4.3.3. Hybrid group 4.3.3.1. Tyr kinase-like (TKL) group 4.3.3.2. Others 5. Discussion 6. Acknowledgments 7. References 1. ABSTRACT The tropical liver fluke, Fasciola gigantica is kinases (ePKs) are regulators of cellular a food-borne parasite responsible for the phosphorylation.