DOCSLIB.ORG

(CT Edit of Column Title).Xlsx

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
(CT Edit of Column Title).Xlsx Protein Protein Description Sequence MRM MS/MS 1433G_MOUSE 14-3-3 protein gamma AAMKNVTEL PSD12_MOUSE 26S proteasome non-ATPase regulatory subunit 12 SYLSICKHY K6PL_MOUSE 6-phosphofructokinase, liver type GYLATVTGI * ENOA_MOUSE Alpha-enolase VYHNLKNVI ** AINX_MOUSE Alpha-internexin GYQDSIGQL ** ALS2_MOUSE Alsin GYIASLHEL * * ALMS1_MOUSE Alstrom syndrome protein 1 homolog KYLLQCETSL AMPD2_MOUSE AMP deaminase 2 KYNPIGESVL ** AL2S8_MOUSE Amyotrophic lateral sclerosis 2 chromosomal region candid SYFPTVNDI * AP1S1_MOUSE AP-1 complex subunit sigma-1A KYFGSVCEL BAG4_MOUSE BAG family molecular chaperone regulator 4 SYNPSGQGL CAN6_MOUSE Calpain-6 TYIDTRTVF ** CSTN1_MOUSE Calsyntenin-1 SYEEVLHLL * CPT1A_MOUSE Carnitine O-palmitoyltransferase 1, liver isoform RYLESVRPLM C209A_MOUSE CD209 antigen-like protein A FSVAQKSWN * * CSTF1_MOUSE Cleavage stimulation factor subunit 1 GYISIANGL ** CDK14_MOUSE Cyclin-dependent kinase 14 SYIHQRYIL ** DP13B_MOUSE DCC-interacting protein 13-beta IYEAMRQVL * * DLP1_MOUSE Decaprenyl-diphosphate synthase subunit 2 NYSKLRETI * * MCM7_MOUSE DNA replication licensing factor MCM7 TYTSARTLL ** DJC25_MOUSE DnaJ homolog subfamily C member 25 SYNKAISYL * * RN220_MOUSE E3 ubiquitin-protein ligase Rnf220 SYSMPLTSI * EF2_MOUSE Elongation factor 2 AYLPVNESF * * ELP2_MOUSE Elongator complex protein 2 SAPRNFVENF ECE1_MOUSE Endothelin-converting enzyme 1 YYSPTKNEI ** EPHA7_MOUSE Ephrin type-A receptor 7 GYMPQQTGL * * ESF1_MOUSE ESF1 homolog AKYRQLLQVI EIF3B_MOUSE Eukaryotic translation initiation factor 3 subunit B RYLVTFSPLM EXT2_MOUSE Exostosin-2 AYFQSIKAI * XPO2_MOUSE Exportin-2 GYQTAFSQL * * FAS_MOUSE Fatty acid synthase YYIDCIKQV ** FAK1_MOUSE Focal adhesion kinase 1 SYWEMRGNAL * * GPR39_MOUSE G-protein coupled receptor 39 SYATLLHVL * * GBRT_MOUSE Gamma-aminobutyric acid receptor subunit theta IYVSSIEQI * * GEMI5_MOUSE Gem-associated protein 5 SYLLSIHKV ** GAN_MOUSE Gigaxonin SYGKLFESV * GNPI2_MOUSE Glucosamine-6-phosphate isomerase 2 YFKGLMHV * GRID1_MOUSE Glutamate receptor delta-1 subunit GYLQMLQISNL GPAT1_MOUSE Glycerol-3-phosphate acyltransferase 1, mitochondrial SYLPSSSEYSL GHITM_MOUSE Growth hormone-inducible transmembrane protein KYDPINSML ** GCH1_MOUSE GTP cyclohydrolase 1 GYQETISDVL * HA19_MOUSE H-2 class I histocompatibility antigen, Q9 alpha chain RYLELGKETL * CDC37_MOUSE Hsp90 co-chaperone Cdc37 KYLSDNVHL ** HD_MOUSE Huntingtin SYWLVRTELL * * IMA2_MOUSE Importin subunit alpha-2 VYKASLNLI * IRS2_MOUSE Insulin receptor substrate 2 DYMPMSPTSV * * INS2_MOUSE Insulin-2 FVKQHLCGS INS2_MOUSE Insulin-2 LELGGGPGAGDLQT * GBP2_MOUSE Interferon-induced guanylate-binding protein 2 SYILSYSSV * IAPP_MOUSE Islet amyloid polypeptide LVRSSNNLGP LAMA5_MOUSE Laminin subunit alpha-5 HYLPDLHHM LGMN_MOUSE Legumain MYQKMVFYI * KDM5B_MOUSE Lysine-specific demethylase 5B AYLPNGTVL * * LPCT4_MOUSE Lysophospholipid acyltransferase LPCAT4 LYKDGFSTI * * MMAD_MOUSE Methylmalonic aciduria and homocystinuria type D homologSYLPGFCSL * * UBA3_MOUSE NEDD8-activating enzyme E1 catalytic subunit LYLQSVTSI * * NBEA_MOUSE Neurobeachin SYSITVKEL ** NF1_MOUSE Neurofibromin TFMEVLTKI * * NFL_MOUSE Neurofilament light polypeptide SYSAPVSSSL ** NFM_MOUSE Neurofilament medium polypeptide AYSSAMLSSAES ** NPY_MOUSE Neuropeptide Y YYSALRHYI ** NPC1_MOUSE Niemann-Pick C1 protein TYFMTYHTI TYK2_MOUSE Non-receptor tyrosine-protein kinase TYK2 KYLATLERL ** NOL11_MOUSE Nucleolar protein 11 LYNFVKSQI * * PANK3_MOUSE Pantothenate kinase 3 NYKRVTGTSL ** PIGU_MOUSE Phosphatidylinositol glycan anchor biosynthesis class U proRYIPLKVAL * * PKHJ1_MOUSE Pleckstrin homology domain-containing family J member 1 SYEYMRQSL * PNPT1_MOUSE Polyribonucleotide nucleotidyltransferase 1, mitochondrial VYTATITEI * * NRG2_MOUSE Pro-neuregulin-2, membrane-bound isoform YYIEGINQL PCSK1_MOUSE ProSAAS HLLEAERQE * PSB6_MOUSE Proteasome subunit beta type-6 (LMP19 constituitive) TYQLGFHSI * AGO3_MOUSE Protein argonaute-3 DYQPGITYI * * NDRG1_MOUSE Protein NDRG1 GYMPSASMTRL * * RBGP1_MOUSE Rab GTPase-activating protein 1 GYCQGQSFL * RAB1B_MOUSE Ras-related protein Rab-1B SYANVKQWL ** RTN4_MOUSE Reticulon-4 GYLGNLSAV * RET4_MOUSE Retinol-binding protein 4 KYWGVASFL * * ROCK1_MOUSE Rho-associated protein kinase 1 RYKDTINKI ** AT2A2_MOUSE Sarcoplasmic/endoplasmic reticulum calcium ATPase 2 IYNNMKQFI ** SCG1_MOUSE Secretogranin-1 QKIAEKFSQ ** SCG1_MOUSE Secretogranin-1 YEGHPLSEE * SCG1_MOUSE Secretogranin-1 GAHSALDTREE * SCG2_MOUSE Secretogranin-2 RQYLDEDMLLK ** SCG2_MOUSE Secretogranin-2 VGSLKNEDTPN SKIT1_MOUSE Selection and upkeep of intraepithelial T-cells protein 1 VMFLLQMV * * SC5A6_MOUSE Sodium-dependent multivitamin transporter SFLPANVTV STMN3_MOUSE Stathmin-3 FYSQPHPNTI ** NSDHL_MOUSE Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylatiFIGTKTVI SODC_MOUSE Superoxide dismutase [Cu-Zn] AMKAVCVLKGD SYT13_MOUSE Synaptotagmin-13 SYLPAANRL ** SYTL5_MOUSE Synaptotagmin-like protein 5 KYTISHTQL * TPX2_MOUSE Targeting protein for Xklp2 TYVPIAQQV * * EI2BE_MOUSE Translation initiation factor eIF-2B subunit epsilon IYGDVISNI ** FRK_MOUSE Tyrosine-protein kinase FRK AYLESQNYI * UBP28_MOUSE Ubiquitin carboxyl-terminal hydrolase 28 KYQEALSYL * VPS11_MOUSE Vacuolar protein sorting-associated protein 11 homolog NYQEALRYI * * S39A6_MOUSE Zinc transporter ZIP6 AYLGMATGI ** Accession Protein Sequence MRM MS/MS FYV1_MOUSE 1-phosphatidylinositol-3-phosphate 5-kinase SCIKNPKILLL * * 1433G_MOUSE 14-3-3 protein gamma AAMKNVTEL * * bold - in all tissue PSMD6_MOUSE 26S proteasome non-ATPase regulatory subunit 6 AMMAKAEYL * * AKTIP_MOUSE AKT-interacting protein TSPLNPEAAVL * * ALMS1_MOUSE Alstrom syndrome protein 1 homolog SALSNEETV ** AIMP2_MOUSE Aminoacyl tRNA synthase complex-interacting multifunctional proteiSSVKNVPENL * * BRCA2_MOUSE Breast cancer type 2 susceptibility protein homolog HAIENIDTF ** C1TC_MOUSE C-1-tetrahydrofolate synthase, cytoplasmic AGILNGKLV * KKCC1_MOUSE Calcium/calmodulin-dependent protein kinase kinase 1 VAAINVAHL * * CMC1_MOUSE Calcium/calmodulin-dependent protein kinase kinase 1 NSLLNNMEL * * CALR_MOUSE Calreticulin EEESPGQAKDEL * CMGA_MOUSE Chromogranin-A AAAEVPSRDTM * * CLSPN_MOUSE Claspin SVLRNPFETI COPG_MOUSE Coatomer subunit gamma SAIVNLPGCSA ** CCD21_MOUSE Coiled-coil domain-containing protein 21 LSILNSNEHLL * * CND1_MOUSE Condensin complex subunit 1 NMCILLDHL * * CSN1_MOUSE COP9 signalosome complex subunit 1 SCLKMLDEM * * DCA10_MOUSE DDB1- and CUL4-associated factor 10 VSPRNSLEVL DTL_MOUSE DDB1- and CUL4-associated factor 10 SSPENKNWLL ** DPOD2_MOUSE DNA polymerase delta subunit 2 ACLVNLRSL * * RAD52_MOUSE DNA repair protein RAD52 homolog NCILDKDYL * * TOP2A_MOUSE DNA topoisomerase 2-alpha VAILDSTTI * TOP2A_MOUSE DNA topoisomerase 2-alpha NSMVLFDHV * * TTK_MOUSE Dual specificity protein kinase TTK SSPLNDDLL * * NSE2_MOUSE E3 SUMO-protein ligase NSE2 SSLKNFQSCI ** EF1A1_MOUSE Elongation factor 1-alpha 1 ISGWNGDNM * * EPC2_MOUSE Enhancer of polycomb homolog 2 SCLTNAVHL * * DHB1_MOUSE Estradiol 17-beta-dehydrogenase 1 AVGAVLDVNVL * FBX18_MOUSE F-box only protein 18 SSCVNDIQHL ** FBX18_MOUSE F-box only protein 18 SSCVNDIQHLL * * FXRD2_MOUSE FAD-dependent oxidoreductase domain-containing protein 2 LGVTNFVHM * * FACD2_MOUSE Fanconi anemia group D2 protein homolog VAPVNLQHDFI * * FAS_MOUSE Fatty acid synthase TALENLSTL ** FHOD3_MOUSE FH1/FH2 domain-containing protein 3 NGVINHSETI ** FOXD1_MOUSE Forkhead box protein D1 SSVENFTARI * * GRIN1_MOUSE G protein-regulated inducer of neurite outgrowth 1 AAVGNSETL ** G2E3_MOUSE G2/M phase-specific E3 ubiquitin-protein ligase YGPENTLPTL * * GCSP_MOUSE Glycine dehydrogenase [decarboxylating], mitochondrial IAILNANYM * GL8D2_MOUSE Glycosyltransferase 8 domain-containing protein 2 SSLGGGVATSPML GTPB8_MOUSE GTP-binding protein 8 SAVTNSGVHLL * H2B1A_MOUSE Histone H2B type 1-A RIASEASRLAHY EHMT1_MOUSE Histone-lysine N-methyltransferase EHMT1 SLPQNQCYM * * MLL4_MOUSE Histone-lysine N-methyltransferase MLL4 SCLSNFHFM * * CDC37_MOUSE Hsp90 co-chaperone Cdc37 NMPWNVDTL AQR_MOUSE Intron-binding protein aquarius NCFELTPAFSQL IREB2_MOUSE Iron-responsive element-binding protein 2 GFDKTKLESM * G6PC2_MOUSE Islet-specific glucose-6-phosphatase catalytic subunit-related proteinSGVLIIHHL * * G6PC2_MOUSE Islet-specific glucose-6-phosphatase catalytic subunit-related proteinLRLFGIDLL * * G6PC2_MOUSE Islet-specific glucose-6-phosphatase catalytic subunit-related proteinKWCANPDWI KI20A_MOUSE Kinesin-like protein KIF20A VCIENTETL * * KI20B_MOUSE Kinesin-like protein KIF20B SSPINISGQVI MPI_MOUSE Mannose-6-phosphate isomerase SALRNCFSHL * * AMP1D_MOUSE Methionine aminopeptidase 1D, mitochondrial SSPLNHIYL * HM13_MOUSE Minor histocompatibility antigen H13 VALAKGEVAEM PUR6_MOUSE Multifunctional protein ADE2 AAISNKITSCI ** MYBB_MOUSE Myb-related protein B NAVKNHWNSTI MTMR7_MOUSE Myotubularin-related protein 7 IGIENIHVM * * NEUA_MOUSE N-acylneuraminate cytidylyltransferase GCLTNGHIYV * SYNE2_MOUSE Nesprin-2 TAVLNLHEHL * NPY_MOUSE Neuropeptide Y RYYSALRHYINLITR NPY_MOUSE Neuropeptide Y SALRHYINL ** NPY_MOUSE Neuropeptide Y SSPETLISDLL * * NPC1_MOUSE Niemann-Pick C1 protein VAVVNKVDI ** NR1D2_MOUSE Nuclear receptor subfamily 1 group D member 2 SGIENVNSV NUP53_MOUSE Nucleoporin NUP53 GNILKHVM * FKBP4_MOUSE Peptidyl-prolyl cis-trans isomerase FKBP4 ASHLNLAMCHL * * FKBP4_MOUSE Peptidyl-prolyl cis-trans isomerase FKBP4 SHLNLAMCHL OCTC_MOUSE Peroxisomal carnitine O-octanoyltransferase IQLMNTAHL ** KPRB_MOUSE Phosphoribosyl pyrophosphate synthase-associated protein 2 AGLTHLITM * * PTBP1_MOUSE Polypyrimidine tract-binding protein 1 TCVSNGPFIM * * DDX5_MOUSE Probable
Load more

Recommended publications
  • Human Cellular Retinaldehyde-Binding Protein Has Secondary Thermal 9-Cis-Retinal Isomerase Activity
    See discussions, stats, and author profiles for this publication at: https://www.researchgate.net/publication/259313787 Human Cellular Retinaldehyde-Binding Protein Has Secondary Thermal 9-cis-Retinal Isomerase Activity Article in Journal of the American Chemical Society · January 2014 DOI: 10.1021/ja411366w · Source: PubMed CITATIONS READS 6 123 12 authors, including: Christin Bolze Rachel E. Helbling Vifor Pharma 13 PUBLICATIONS 21 CITATIONS 3 PUBLICATIONS 13 CITATIONS SEE PROFILE SEE PROFILE Arwen Pearson Guillaume Pompidor University of Hamburg European Molecular Biology Laboratory 78 PUBLICATIONS 1,083 CITATIONS 37 PUBLICATIONS 286 CITATIONS SEE PROFILE SEE PROFILE Some of the authors of this publication are also working on these related projects: Melanopsin View project AdPLA LRAT View project All content following this page was uploaded by Achim Stocker on 10 November 2017. The user has requested enhancement of the downloaded file. Article pubs.acs.org/JACS Human Cellular Retinaldehyde-Binding Protein Has Secondary Thermal 9-cis-Retinal Isomerase Activity † ‡ † § ∥ ⊥ ∇ Christin S. Bolze, , Rachel E. Helbling, Robin L. Owen, Arwen R. Pearson, Guillaume Pompidor, , ⊥ ⊥ ○ † # # Florian Dworkowski, Martin R. Fuchs, , Julien Furrer, Marcin Golczak, Krzysztof Palczewski, † † Michele Cascella,*, and Achim Stocker*, † ‡ Department of Chemistry and Biochemistry, and Graduate School for Cellular and Biomedical Sciences, University of Bern, Freiestrasse 3, 3012 Bern, Switzerland § Diamond Light Source, Harwell Science and Innovation Campus,
    [Show full text]
  • Dynamic Molecular Linkers of the Genome: the First Decade of SMC Proteins
    Downloaded from genesdev.cshlp.org on October 8, 2021 - Published by Cold Spring Harbor Laboratory Press REVIEW Dynamic molecular linkers of the genome: the first decade of SMC proteins Ana Losada1 and Tatsuya Hirano2,3 1Spanish National Cancer Center (CNIO), Madrid E-28029, Spain; 2Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724, USA Structural maintenance of chromosomes (SMC) proteins in eukaryotes. The proposed actions of cohesin and con- are chromosomal ATPases, highly conserved from bac- densins offer a plausible, if not complete, explanation for teria to humans, that play fundamental roles in many the sudden appearance of thread-like “substances” (the aspects of higher-order chromosome organization and chromosomes) and their longitudinal splitting during dynamics. In eukaryotes, SMC1 and SMC3 act as the mitosis, first described by Walther Flemming (1882). core of the cohesin complexes that mediate sister chro- Remarkably, SMC proteins are conserved among the matid cohesion, whereas SMC2 and SMC4 function as three phyla of life, indicating that the basic strategy of the core of the condensin complexes that are essential chromosome organization may be evolutionarily con- for chromosome assembly and segregation. Another served from bacteria to humans. An emerging theme is complex containing SMC5 and SMC6 is implicated in that SMC proteins are dynamic molecular linkers of the DNA repair and checkpoint responses. The SMC com- genome that actively fold, tether, and manipulate DNA plexes form unique ring- or V-shaped structures with strands. Their diverse functions range far beyond chro- long coiled-coil arms, and function as ATP-modulated, mosome segregation, and involve nearly all aspects of dynamic molecular linkers of the genome.
    [Show full text]
  • Shedding New Light on the Generation of the Visual Chromophore PERSPECTIVE Krzysztof Palczewskia,B,C,1 and Philip D
    PERSPECTIVE Shedding new light on the generation of the visual chromophore PERSPECTIVE Krzysztof Palczewskia,b,c,1 and Philip D. Kiserb,d Edited by Jeremy Nathans, Johns Hopkins University School of Medicine, Baltimore, MD, and approved July 9, 2020 (received for review May 16, 2020) The visual phototransduction cascade begins with a cis–trans photoisomerization of a retinylidene chro- mophore associated with the visual pigments of rod and cone photoreceptors. Visual opsins release their all-trans-retinal chromophore following photoactivation, which necessitates the existence of pathways that produce 11-cis-retinal for continued formation of visual pigments and sustained vision. Proteins in the retinal pigment epithelium (RPE), a cell layer adjacent to the photoreceptor outer segments, form the well- established “dark” regeneration pathway known as the classical visual cycle. This pathway is sufficient to maintain continuous rod function and support cone photoreceptors as well although its throughput has to be augmented by additional mechanism(s) to maintain pigment levels in the face of high rates of photon capture. Recent studies indicate that the classical visual cycle works together with light-dependent pro- cesses in both the RPE and neural retina to ensure adequate 11-cis-retinal production under natural illu- minances that can span ten orders of magnitude. Further elucidation of the interplay between these complementary systems is fundamental to understanding how cone-mediated vision is sustained in vivo. Here, we describe recent
    [Show full text]
  • Building the Interphase Nucleus: a Study on the Kinetics of 3D Chromosome Formation, Temporal Relation to Active Transcription, and the Role of Nuclear Rnas
    University of Massachusetts Medical School eScholarship@UMMS GSBS Dissertations and Theses Graduate School of Biomedical Sciences 2020-07-28 Building the Interphase Nucleus: A study on the kinetics of 3D chromosome formation, temporal relation to active transcription, and the role of nuclear RNAs Kristin N. Abramo University of Massachusetts Medical School Let us know how access to this document benefits ou.y Follow this and additional works at: https://escholarship.umassmed.edu/gsbs_diss Part of the Bioinformatics Commons, Cell Biology Commons, Computational Biology Commons, Genomics Commons, Laboratory and Basic Science Research Commons, Molecular Biology Commons, Molecular Genetics Commons, and the Systems Biology Commons Repository Citation Abramo KN. (2020). Building the Interphase Nucleus: A study on the kinetics of 3D chromosome formation, temporal relation to active transcription, and the role of nuclear RNAs. GSBS Dissertations and Theses. https://doi.org/10.13028/a9gd-gw44. Retrieved from https://escholarship.umassmed.edu/ gsbs_diss/1099 Creative Commons License This work is licensed under a Creative Commons Attribution-Noncommercial 4.0 License This material is brought to you by eScholarship@UMMS. It has been accepted for inclusion in GSBS Dissertations and Theses by an authorized administrator of eScholarship@UMMS. For more information, please contact [email protected]. BUILDING THE INTERPHASE NUCLEUS: A STUDY ON THE KINETICS OF 3D CHROMOSOME FORMATION, TEMPORAL RELATION TO ACTIVE TRANSCRIPTION, AND THE ROLE OF NUCLEAR RNAS A Dissertation Presented By KRISTIN N. ABRAMO Submitted to the Faculty of the University of Massachusetts Graduate School of Biomedical Sciences, Worcester in partial fulfillment of the requirements for the degree of DOCTOR OF PHILOSPOPHY July 28, 2020 Program in Systems Biology, Interdisciplinary Graduate Program BUILDING THE INTERPHASE NUCLEUS: A STUDY ON THE KINETICS OF 3D CHROMOSOME FORMATION, TEMPORAL RELATION TO ACTIVE TRANSCRIPTION, AND THE ROLE OF NUCLEAR RNAS A Dissertation Presented By KRISTIN N.
    [Show full text]
  • Understanding Molecular Functions of the SMC5/6 Complex
    G C A T T A C G G C A T genes Review Scaffolding for Repair: Understanding Molecular Functions of the SMC5/6 Complex Mariana Diaz 1,2 and Ales Pecinka 1,* ID 1 Institute of Experimental Botany of the Czech Academy of Sciences (IEB), Centre of the Region Haná for Biotechnological and Agricultural Research, Šlechtitelu˚ 31, 77900 Olomouc-Holice, Czech Republic 2 Max Planck Institute for Plant Breeding Research (MPIPZ), Carl-von-Linné-Weg 10, 50829 Cologne, Germany; [email protected] * Correspondence: [email protected]; Tel.: +420-585-238-709 Received: 15 November 2017; Accepted: 4 January 2018; Published: 12 January 2018 Abstract: Chromosome organization, dynamics and stability are required for successful passage through cellular generations and transmission of genetic information to offspring. The key components involved are Structural maintenance of chromosomes (SMC) complexes. Cohesin complex ensures proper chromatid alignment, condensin complex chromosome condensation and the SMC5/6 complex is specialized in the maintenance of genome stability. Here we summarize recent knowledge on the composition and molecular functions of SMC5/6 complex. SMC5/6 complex was originally identified based on the sensitivity of its mutants to genotoxic stress but there is increasing number of studies demonstrating its roles in the control of DNA replication, sister chromatid resolution and genomic location-dependent promotion or suppression of homologous recombination. Some of these functions appear to be due to a very dynamic interaction with cohesin or other repair complexes. Studies in Arabidopsis indicate that, besides its canonical function in repair of damaged DNA, the SMC5/6 complex plays important roles in regulating plant development, abiotic stress responses, suppression of autoimmune responses and sexual reproduction.
    [Show full text]
  • The Architecture of a Eukaryotic Replisome
    The Architecture of a Eukaryotic Replisome Jingchuan Sun1,2, Yi Shi3, Roxana E. Georgescu3,4, Zuanning Yuan1,2, Brian T. Chait3, Huilin Li*1,2, Michael E. O’Donnell*3,4 1 Biosciences Department, Brookhaven National Laboratory, Upton, New York, USA 2 Department of Biochemistry & Cell Biology, Stony Brook University, Stony Brook, New York, USA. 3 The Rockefeller University, 1230 York Avenue, New York, New York, USA. 4 Howard Hughes Medical Institute *Correspondence and requests for materials should be addressed to M.O.D. ([email protected]) or H.L. ([email protected]) ABSTRACT At the eukaryotic DNA replication fork, it is widely believed that the Cdc45-Mcm2-7-GINS (CMG) helicase leads the way in front to unwind DNA, and that DNA polymerases (Pol) trail behind the helicase. Here we use single particle electron microscopy to directly image a replisome. Contrary to expectations, the leading strand Pol ε is positioned ahead of CMG helicase, while Ctf4 and the lagging strand Pol α-primase (Pol α) are behind the helicase. This unexpected architecture indicates that the leading strand DNA travels a long distance before reaching Pol ε, it first threads through the Mcm2-7 ring, then makes a U-turn at the bottom to reach Pol ε at the top of CMG. Our work reveals an unexpected configuration of the eukaryotic replisome, suggests possible reasons for this architecture, and provides a basis for further structural and biochemical replisome studies. INTRODUCTION DNA is replicated by a multi-protein machinery referred to as a replisome 1,2. Replisomes contain a helicase to unwind DNA, DNA polymerases that synthesize the leading and lagging strands, and a primase that makes short primed sites to initiate DNA synthesis on both strands.
    [Show full text]
  • Neurofilament Depletion Improves Microtubule Dynamics Via Modulation of Stat3/Stathmin Signaling
    Edinburgh Research Explorer Neurofilament depletion improves microtubule dynamics via modulation of Stat3/stathmin signaling Citation for published version: Yadav, P, Selvaraj, BT, Bender, FLP, Behringer, M, Moradi, M, Sivadasan, R, Dombert, B, Blum, R, Asan, E, Sauer, M, Julien, JP & Sendtner, M 2016, 'Neurofilament depletion improves microtubule dynamics via modulation of Stat3/stathmin signaling', Acta Neuropathologica, vol. 132, no. 1, pp. 93-110. https://doi.org/10.1007/s00401-016-1564-y Digital Object Identifier (DOI): 10.1007/s00401-016-1564-y Link: Link to publication record in Edinburgh Research Explorer Document Version: Publisher's PDF, also known as Version of record Published In: Acta Neuropathologica Publisher Rights Statement: This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. 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. If you believe that the public display of this file breaches copyright please contact [email protected] providing details, and we will remove access to the work immediately and investigate your claim.
    [Show full text]
  • Neurofilaments: Neurobiological Foundations for Biomarker Applications
    Neurofilaments: neurobiological foundations for biomarker applications Arie R. Gafson1, Nicolas R. Barthelmy2*, Pascale Bomont3*, Roxana O. Carare4*, Heather D. Durham5*, Jean-Pierre Julien6,7*, Jens Kuhle8*, David Leppert8*, Ralph A. Nixon9,10,11,12*, Roy Weller4*, Henrik Zetterberg13,14,15,16*, Paul M. Matthews1,17 1 Department of Brain Sciences, Imperial College, London, UK 2 Department of Neurology, Washington University School of Medicine, St Louis, MO, USA 3 a ATIP-Avenir team, INM, INSERM , Montpellier university , Montpellier , France. 4 Clinical Neurosciences, Faculty of Medicine, University of Southampton, Southampton General Hospital, Southampton, United Kingdom 5 Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, Québec, Canada 6 Department of Psychiatry and Neuroscience, Laval University, Quebec, Canada. 7 CERVO Brain Research Center, 2601 Chemin de la Canardière, Québec, QC, G1J 2G3, Canada 8 Neurologic Clinic and Policlinic, Departments of Medicine, Biomedicine and Clinical Research, University Hospital Basel, University of Basel, Basel, Switzerland. 9 Center for Dementia Research, Nathan Kline Institute, Orangeburg, NY, 10962, USA. 10Departments of Psychiatry, New York University School of Medicine, New York, NY, 10016, 11 Neuroscience Institute, New York University School of Medicine, New York, NY, 10016, USA. 12Department of Cell Biology, New York University School of Medicine, New York, NY, 10016, USA 13 University College London Queen Square Institute of Neurology, London, UK 14 UK Dementia Research Institute at University College London 15 Department of Psychiatry and Neurochemistry, Institute of Neuroscience and Physiology, the Sahlgrenska Academy at the University of Gothenburg, Mölndal, Sweden 16 Clinical Neurochemistry Laboratory, Sahlgrenska University Hospital, Mölndal, Sweden 17 UK Dementia Research Institute at Imperial College, London * Co-authors ordered alphabetically Address for correspondence: Prof.
    [Show full text]
  • Supplementary Table S4. FGA Co-Expressed Gene List in LUAD
    Supplementary Table S4. FGA co-expressed gene list in LUAD tumors Symbol R Locus Description FGG 0.919 4q28 fibrinogen gamma chain FGL1 0.635 8p22 fibrinogen-like 1 SLC7A2 0.536 8p22 solute carrier family 7 (cationic amino acid transporter, y+ system), member 2 DUSP4 0.521 8p12-p11 dual specificity phosphatase 4 HAL 0.51 12q22-q24.1histidine ammonia-lyase PDE4D 0.499 5q12 phosphodiesterase 4D, cAMP-specific FURIN 0.497 15q26.1 furin (paired basic amino acid cleaving enzyme) CPS1 0.49 2q35 carbamoyl-phosphate synthase 1, mitochondrial TESC 0.478 12q24.22 tescalcin INHA 0.465 2q35 inhibin, alpha S100P 0.461 4p16 S100 calcium binding protein P VPS37A 0.447 8p22 vacuolar protein sorting 37 homolog A (S. cerevisiae) SLC16A14 0.447 2q36.3 solute carrier family 16, member 14 PPARGC1A 0.443 4p15.1 peroxisome proliferator-activated receptor gamma, coactivator 1 alpha SIK1 0.435 21q22.3 salt-inducible kinase 1 IRS2 0.434 13q34 insulin receptor substrate 2 RND1 0.433 12q12 Rho family GTPase 1 HGD 0.433 3q13.33 homogentisate 1,2-dioxygenase PTP4A1 0.432 6q12 protein tyrosine phosphatase type IVA, member 1 C8orf4 0.428 8p11.2 chromosome 8 open reading frame 4 DDC 0.427 7p12.2 dopa decarboxylase (aromatic L-amino acid decarboxylase) TACC2 0.427 10q26 transforming, acidic coiled-coil containing protein 2 MUC13 0.422 3q21.2 mucin 13, cell surface associated C5 0.412 9q33-q34 complement component 5 NR4A2 0.412 2q22-q23 nuclear receptor subfamily 4, group A, member 2 EYS 0.411 6q12 eyes shut homolog (Drosophila) GPX2 0.406 14q24.1 glutathione peroxidase
    [Show full text]
  • (10) Patent No.: US 8119385 B2
    US008119385B2 (12) United States Patent (10) Patent No.: US 8,119,385 B2 Mathur et al. (45) Date of Patent: Feb. 21, 2012 (54) NUCLEICACIDS AND PROTEINS AND (52) U.S. Cl. ........................................ 435/212:530/350 METHODS FOR MAKING AND USING THEMI (58) Field of Classification Search ........................ None (75) Inventors: Eric J. Mathur, San Diego, CA (US); See application file for complete search history. Cathy Chang, San Diego, CA (US) (56) References Cited (73) Assignee: BP Corporation North America Inc., Houston, TX (US) OTHER PUBLICATIONS c Mount, Bioinformatics, Cold Spring Harbor Press, Cold Spring Har (*) Notice: Subject to any disclaimer, the term of this bor New York, 2001, pp. 382-393.* patent is extended or adjusted under 35 Spencer et al., “Whole-Genome Sequence Variation among Multiple U.S.C. 154(b) by 689 days. Isolates of Pseudomonas aeruginosa” J. Bacteriol. (2003) 185: 1316 1325. (21) Appl. No.: 11/817,403 Database Sequence GenBank Accession No. BZ569932 Dec. 17. 1-1. 2002. (22) PCT Fled: Mar. 3, 2006 Omiecinski et al., “Epoxide Hydrolase-Polymorphism and role in (86). PCT No.: PCT/US2OO6/OOT642 toxicology” Toxicol. Lett. (2000) 1.12: 365-370. S371 (c)(1), * cited by examiner (2), (4) Date: May 7, 2008 Primary Examiner — James Martinell (87) PCT Pub. No.: WO2006/096527 (74) Attorney, Agent, or Firm — Kalim S. Fuzail PCT Pub. Date: Sep. 14, 2006 (57) ABSTRACT (65) Prior Publication Data The invention provides polypeptides, including enzymes, structural proteins and binding proteins, polynucleotides US 201O/OO11456A1 Jan. 14, 2010 encoding these polypeptides, and methods of making and using these polynucleotides and polypeptides.
    [Show full text]
  • Supp Table 6.Pdf
    Supplementary Table 6. Processes associated to the 2037 SCL candidate target genes ID Symbol Entrez Gene Name Process NM_178114 AMIGO2 adhesion molecule with Ig-like domain 2 adhesion NM_033474 ARVCF armadillo repeat gene deletes in velocardiofacial syndrome adhesion NM_027060 BTBD9 BTB (POZ) domain containing 9 adhesion NM_001039149 CD226 CD226 molecule adhesion NM_010581 CD47 CD47 molecule adhesion NM_023370 CDH23 cadherin-like 23 adhesion NM_207298 CERCAM cerebral endothelial cell adhesion molecule adhesion NM_021719 CLDN15 claudin 15 adhesion NM_009902 CLDN3 claudin 3 adhesion NM_008779 CNTN3 contactin 3 (plasmacytoma associated) adhesion NM_015734 COL5A1 collagen, type V, alpha 1 adhesion NM_007803 CTTN cortactin adhesion NM_009142 CX3CL1 chemokine (C-X3-C motif) ligand 1 adhesion NM_031174 DSCAM Down syndrome cell adhesion molecule adhesion NM_145158 EMILIN2 elastin microfibril interfacer 2 adhesion NM_001081286 FAT1 FAT tumor suppressor homolog 1 (Drosophila) adhesion NM_001080814 FAT3 FAT tumor suppressor homolog 3 (Drosophila) adhesion NM_153795 FERMT3 fermitin family homolog 3 (Drosophila) adhesion NM_010494 ICAM2 intercellular adhesion molecule 2 adhesion NM_023892 ICAM4 (includes EG:3386) intercellular adhesion molecule 4 (Landsteiner-Wiener blood group)adhesion NM_001001979 MEGF10 multiple EGF-like-domains 10 adhesion NM_172522 MEGF11 multiple EGF-like-domains 11 adhesion NM_010739 MUC13 mucin 13, cell surface associated adhesion NM_013610 NINJ1 ninjurin 1 adhesion NM_016718 NINJ2 ninjurin 2 adhesion NM_172932 NLGN3 neuroligin
    [Show full text]
  • 1 the Nucleoporin ELYS Regulates Nuclear Size by Controlling NPC
    bioRxiv preprint doi: https://doi.org/10.1101/510230; this version posted January 2, 2019. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC-ND 4.0 International license. The nucleoporin ELYS regulates nuclear size by controlling NPC number and nuclear import capacity Predrag Jevtić1,4, Andria C. Schibler2,4, Gianluca Pegoraro3, Tom Misteli2,*, Daniel L. Levy1,* 1 Department of Molecular Biology, University of Wyoming, Laramie, WY, 82071 2 National Cancer Institute, NIH, Bethesda, MD, 20892 3 High Throughput Imaging Facility (HiTIF), National Cancer Institute, NIH, Bethesda, MD, 20892 4 Co-first authors *Corresponding authors: Daniel L. Levy Tom Misteli University of Wyoming National Cancer Institute, NIH Department of Molecular Biology Center for Cancer Research 1000 E. University Avenue 41 Library Drive, Bldg. 41, B610 Laramie, WY, 82071 Bethesda, MD, 20892 Phone: 307-766-4806 Phone: 240-760-6669 Fax: 307-766-5098 Fax: 301-496-4951 E-mail: [email protected] E-mail: [email protected] Running Head: ELYS is a nuclear size effector Abbreviations: NE, nuclear envelope; NPC, nuclear pore complex; ER, endoplasmic reticulum; Nup, nucleoporin; FG-Nup, phenylalanine-glycine repeat nucleoporin 1 bioRxiv preprint doi: https://doi.org/10.1101/510230; this version posted January 2, 2019. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC-ND 4.0 International license.
    [Show full text]