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Supplementary,Table,1.,Tangeretin,Targets,In,Human,,As,Retreived,From,Pubchem

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Supplementary,Table,1.,Tangeretin,targets,in,human,,as,retreived,from,PuBChem No Protein,name Symbol 1 Unspecific,Monooxygenase 2 Proline,Rich,Protein,Bstni,Subfamily,1 PRB1 3 Caspase,3 CASP3 4 Tumor,Necrosis,Factor CD40LG 5 Bcl2,,Apoptosis,Regulator BCL2 6 Cytochrome,P450,Family,3,Subfamily,A,Member,4CYP3A4 7 Atp,Binding,Cassette,Subfamily,B,Member,1 ABCB1 8 MitogenQActivated,Protein,Kinase MAP3K10 9 Akt,Serine/Threonine,Kinase,1 AKT1 10 Glucuronosyltransferase UGT2A3 11 Heme,Oxygenase,1 HMOX1 12 InterleukinQ6 IL6 13 MitogenQActivated,Protein,Kinase,8 MAPK8 14 InositolQ3QPhosphate,Synthase ISYNA1 15 Bcl2,Like,1 BCL2L1 16 Glutathione,Transferase GSTO1 17 MitogenQActivated,Protein,Kinase,3 MAPK3 18 PhosphatidylinositolQ4QPhosphate,3QKinase PIK3 19 ProstaglandinQEndoperoxide,Synthase,2 PTGS2 20 Tyrosinase TYR 21 Caspase,9 CASP9 22 Protein,Kinase,XQLinked PRKX 23 ProlineQRich,P65,Protein RELA 24 Cytochrome,P450,Family,1,Subfamily,A,Member,2CYP1A2 25 PhosphatidylinositolQ4,5QBisphosphate,3QKinase,Catalytic,Subunit,AlphaPIK3CA 26 Jagged,1 JAG1 27 Nad(+),AdpQRibosyltransferase ART1 28 Cadherin,1 CDH1 29 MitogenQActivated,Protein,Kinase,ErkQA ERK 30 P53 TP53 31 Nad(P)H,Dehydrogenase,(Quinone) NQO2 32 Notch,1 NOTCH1 33 Cyclin,B1 CCNB1 34 Peroxiredoxin,6,Pseudogene,2 PRDX6 35 Mcl1,,Bcl2,Family,Apoptosis,Regulator MCL1 36 Superoxide,Dismutase SOD2 37 Insulin INS 38 Interleukin,10 IL10 39 Cytochrome,P450,Family,1,Subfamily,A,Member,1CYP1A1 40 MethylQCpg,Binding,Domain,Protein,2 MBD2 41 Interleukin,17a IL17A 42 Caspase,8 CASP8 43 Poly,(AdpQRibose),Polymerase PARP 44 Vascular,Endothelial,Growth,Factor,A VEGFA 45 Proliferating,Cell,Nuclear,Antigen PCNA 46 Catalase CAT 47 Udp,Glucuronosyltransferase,Family,1,Member,A9UGT1A9 48 Macrophage,Scavenger,Receptor,1 MSR1 49 Solute,Carrier,Organic,Anion,Transporter,Family,Member,1a2SLCO1A2 50 Udp,Glucuronosyltransferase,Family,2,Member,B7UGT2B7 51 Signal,Transducer,And,Activator,Of,Transcription,3STAT3 52 CQC,Motif,Chemokine,Ligand,2 CCL2 53 Period,Circadian,Regulator,2 PER2 54 Myeloperoxidase MPO 55 Nuclear,Factor,Kappa,B,Subunit,1 NFKB1 56 Quinone,Oxidoreductase,1 CRYZL1 57 XQBox,Binding,Protein,1 XBP1 58 Leucine,Aminopeptidase,2 LAP3P2 59 40s,Ribosomal,Protein,S7 RPS7 60 Glutathione,Peroxidase GPX8 61 Mechanistic,Target,Of,Rapamycin,Kinase MTOR 62 Udp,Glucuronosyltransferase,Family,1,Member,A1UGT1A8 63 Interleukin,23,Subunit,Alpha IL23A 64 Resistin RETN 65 XQLinked,Inhibitor,Of,Apoptosis XIAP 66 Cadherin,17 CDH17 67 Nad(P)H,Quinone,Dehydrogenase,1 NQO1 68 Cd36,Molecule CD36 69 Cyclin,Dependent,Kinase,Inhibitor,1a CDKN1A 70 MitogenQActivated,Protein,Kinase,1 MAPK1 71 Gap,Junction,Protein,Alpha,1 GJA1 72 Forkhead,Box,P3 FOXP3 73 Cd4,Molecule CD4 74 Janus,Kinase,2 JAK2 75 Gelatinase,B MMP9 76 Synuclein,Alpha SNCA 77 Interferon,Lambda,Receptor,1 IFNLR1 78 Atp,Binding,Cassette,Subfamily,G,Member,2,(Junior,Blood,Group)ABCG2 79 Pyruvate,Kinase PKLR 80 Protein,Kinase,AmpQActivated,Catalytic,Subunit,Alpha,2PRKAA2 81 AlphaQAmylase AMY2A 82 Polyamine,Modulated,Factor,1 PMF1 83 Dna,Nucleotidylexotransferase DNTT 84 GlucoseQ6QPhosphate,Dehydrogenase G6PD 85 CyclinQD1Q1 CCND1 86 Taste,2,Receptor,Member,14 TAS2R14 87 Apolipoprotein,B APOB 88 Jun,ProtoQOncogene,,ApQ1,Transcription,Factor,SubunitJUN 89 Adiponectin,,C1q,And,Collagen,Domain,ContainingADIPOQ 90 Cyclin,D CCND1 91 Tyrosine,Hydroxylase TH 92 Tetraspanin,12 TSPAN12 93 Catenin,Beta,1 CTNNB1 94 MitogenQActivated,Protein,Kinase,14 MAPK14 95 Phosphatidylinositol,3QKinase PI3K Supplementary,Table,2.,Genes,related,to,metastatic,breast,cancer,,as,retreived,from,PubMed Symbol Aliases description BRCA2 BRCC2,,BROVCA2,,FACD,,FAD,,FAD1,,FANCD,,FANCD1,,GLM3,,PNCA2,,XRCC11BRCA2,DNA,repair,associated BRMS1 BRMS1,transcriptional,repressor,and,anoikis,regulator BRCA1 BRCAI,,BRCC1,,BROVCA1,,FANCS,,IRIS,,PNCA4,,PPP1R53,,PSCP,,RNF53BRCA1,DNA,repair,associated ESR1 ER,,ESR,,ESRA,,ESTRR,,Era,,NR3A1 estrogen,receptor,1 TERT CMM9,,DKCA2,,DKCB4,,EST2,,PFBMFT1,,TCS1,,TP2,,TRT,,hEST2,,hTRTtelomerase,reverse,transcriptase CCND1 BCL1,,D11S287E,,PRAD1,,U21B31 cyclin,D1 ABCG2 ABC15,,ABCP,,BCRP,,BCRP1,,BMDP,,CD338,,CDw338,,EST157481,,GOUT1,,MRX,,MXR,,MXRV1,,MXR1,,UAQTL1ATP,binding,cassette,subfamily,G,member,2,(Junior,blood,group) FGFR2 BBDS,,BEK,,BFRV1,,CD332,,CEK3,,CFD1,,ECT1,,JWS,,KVSAM,,KGFR,,TK14,,TK25fibroblast,growth,factor,receptor,2 CDKN2A ARF,,CDK4I,,CDKN2,,CMM2,,INK4,,INK4A,,MLM,,MTSV1,,MTS1,,P14,,P14ARF,,P16,,P16VINK4A,,P16INK4,,P16INK4A,,P19,,P19ARF,,TP16cyclin,dependent,kinase,inhibitor,2A BCAS3 GAOB1,,MAAB BCAS3,microtubule,associated,cell,migration,factor MALAT1 HCN,,LINC00047,,NCRNA00047,,NEAT2,,PRO2853metastasis,associated,lung,adenocarcinoma,transcript,1 NME1 AWD,,GAAD,,NB,,NBS,,NDKA,,NDPKVA,,NDPKA,,NM23,,NM23VH1NME/NM23,nucleoside,diphosphate,kinase,1 MTA1 metastasis,associated,1 MTDH 3D3,,AEGV1,,AEG1,,LYRIC,,LYRIC/3D3metadherin KISS1 HH13,,KiSSV1 KiSSV1,metastasis,suppressor PTHLH BDE2,,HHM,,PLP,,PTHR,,PTHRP parathyroid,hormone,like,hormone BRMS1L BRMS1 BRMS1,like,transcriptional,repressor NCOA3 ACTR,,AIBV1,,AIB1,,CAGH16,,CTG26,,KAT13B,,RAC3,,SRCV3,,SRC3,,TNRC14,,TNRC16,,TRAMV1,,bHLHe42,,pCIPnuclear,receptor,coactivator,3 CD82 4F9,,C33,,GR15,,IA4,,KAI1,,R2,,SAR2,,ST6,,TSPAN27CD82,molecule MDM4 HDMX,,MDMX,,MRP1 MDM4,regulator,of,p53 TIAM1 TIAMV1 TIAM,Rac1,associated,GEF,1 SNCG BCSG1,,SR synuclein,gamma MACC1 7A5,,SH3BP4L MET,transcriptional,regulator,MACC1 MYC MRTLC,,bHLHe39,,cVMyc,,MYC MYC,protoVoncogene,,bHLH,transcription,factor RECK ST15 reversion,inducing,cysteine,rich,protein,with,kazal,motifs IGF1 IGF,,IGFVI,,IGFI,,MGF insulin,like,growth,factor,1 CHEK2 CDS1,,CHK2,,HuCds1,,LFS2,,PP1425,,RAD53,,hCds1checkpoint,kinase,2 TFF1 BCEI,,D21S21,,HP1.A,,HPS2,,pNRV2,,pS2trefoil,factor,1 MRTFA BSAC,,MAL,,MKL,,MKL1,,MRTFVA myocardin,related,transcription,factor,A TP53 BCC7,,BMFS5,,LFS1,,P53,,TRP53 tumor,protein,p53 MTA2 MTA1L1,,PID metastasis,associated,1,family,member,2 MTSS1 MIM,,MIMA,,MIMB MTSS,IVBAR,domain,containing,1 MAP3K1 MAPKKK1,,MEKK,,MEKK,1,,MEKK1,,SRXY6mitogenVactivated,protein,kinase,kinase,kinase,1 EGFR ERBB,,ERBB1,,HER1,,NISBD2,,PIG61,,mENAepidermal,growth,factor,receptor ERBB4 ALS19,,HER4,,p180erbB4 erbVb2,receptor,tyrosine,kinase,4 TNF DIFValpha,,TNFA,,TNFSF2,,TNLG1F,,TNFtumor,necrosis,factor VEGFA MVCD1,,VEGF,,VPF vascular,endothelial,growth,factor,A CCAR2 DBCV1,,DBC1,,KIAA1967,,NET35,,p30,DBC,,p30DBCcell,cycle,and,apoptosis,regulator,2 IL6 BSFV2,,BSF2,,CDF,,HGF,,HSF,,IFNVbetaV2,,IFNB2,,ILV6interleukin,6 CDKN2B CDK4I,,INK4B,,MTS2,,P15,,TP15,,p15INK4bcyclin,dependent,kinase,inhibitor,2B TGFB1 CED,,DPD1,,IBDIMDE,,LAP,,TGFVbeta1,,TGFB,,TGFbetatransforming,growth,factor,beta,1 MTA3 metastasis,associated,1,family,member,3 TCF7L2 TCFV4,,TCF4 transcription,factor,7,like,2 ERBB2 CD340,,HERV2,,HERV2/neu,,HER2,,MLN,19,,NEU,,NGL,,TKR1erbVb2,receptor,tyrosine,kinase,2 TGFBR2 AAT3,,FAA3,,LDS1B,,LDS2,,LDS2B,,MFS2,,RIIC,,TAAD2,,TBRVii,,TBRII,,TGFRV2,,TGFbetaVRIItransforming,growth,factor,beta,receptor,2 CDKN2BVAS1ANRIL,,CDKN2BVAS,,CDKN2BAS,,NCRNA00089,,PCAT12,,p15ASCDKN2B,antisense,RNA,1 HIF1A HIFV1Valpha,,HIFV1A,,HIFV1alpha,,HIF1,,HIF1VALPHA,,MOP1,,PASD8,,bHLHe78hypoxia,inducible,factor,1,subunit,alpha AREG ARB,,CRDGF,,SDGF,,AREG amphiregulin MMP9 CLG4B,,GELB,,MANDP2,,MMPV9 matrix,metallopeptidase,9 AR AIS8,,DHTR,,HUMARA,,HYSP1,,KD,,NR3C4,,SBMA,,SMAX1,,TFM,,ARandrogen,receptor AKT1 AKT,,CWS6,,PKB,,PKBVALPHA,,PRKBA,,RAC,,RACVALPHAAKT,serine/threonine,kinase,1 NFKB1 CVID12,,EBPV1,,KBF1,,NFVkB,,NFVkB1,,NFVkappaVB1,,NFVkappaB,,NFKBVp105,,NFKBVp50,,NFkappaB,,p105,,p50nuclear,factor,kappa,B,subunit,1 KLF4 EZF,,GKLF Kruppel,like,factor,4 STAT3 ADMIO,,ADMIO1,,APRF,,HIES signal,transducer,and,activator,of,transcription,3 KRAS 'CVKVRAS,,CVKVRAS,,CFC2,,KVRAS2A,,KVRAS2B,,KVRAS4A,,KVRAS4B,,KVRas,,KVRas,2,,KIVRAS1,,KRAS2,,NS,,NS3,,OES,,RALD,,RASK2,,cVKiVras,,cVKiVras2,,KRASKRAS,protoVoncogene,,GTPase CERS2 L3,,LASS2,,SP260,,TMSG1 ceramide,synthase,2 IL1B ILV1,,IL1VBETA,,IL1F2,,IL1beta interleukin,1,beta PTGS2 COXV2,,COX2,,GRIPGHS,,PGG/HS,,PGHSV2,,PHSV2,,hCoxV2prostaglandinVendoperoxide,synthase,2 IL10 CSIF,,GVHDS,,ILV10A,,TGIF,,IL10 interleukin,10 CRP PTX1 CVreactive,protein TLR4 ARMD10,,CD284,,TLRV4,,TOLL toll,like,receptor,4 CTNNB1 CTNNB,,EVR7,,MRD19,,NEDSDV,,armadillocatenin,beta,1 PTEN 10q23del,,BZS,,CWS1,,DEC,,GLM2,,MHAM,,MMAC11,,PTENbeta,,TEP1,,PTENphosphatase,and,tensin,homolog CXCL8 GCPV1,,GCP1,,IL8,,LECT,,LUCT,,LYNAP,,MDNCF,,MONAP,,NAF,,NAPV1,,NAP1CVXVC,motif,chemokine,ligand,8 NUPR1 COM1,,P8 nuclear,protein,1,,transcriptional,regulator CD44 CDW44,,CSPG8,,ECMRVIII,,HCELL,,HUTCHVI,,IN,,LHR,,MC56,,MDU2,,MDU3,,MIC4,,Pgp1CD44,molecule,(Indian,blood,group) CDH1 ArcV1,,BCDS1,,CD324,,CDHE,,ECAD,,LCAM,,UVOcadherin,1 MTOR FRAP,,FRAP1,,FRAP2,,RAFT1,,RAPT1,,SKSmechanistic,target,of,rapamycin,kinase BCL2 BclV2,,PPP1R50 BCL2,apoptosis,regulator SERPINB5 PI5,,maspin serpin,family,B,member,5 CXCR4 CD184,,D2S201E,,FB22,,HM89,,HSY3RR,,LAPV3,,LAP3,,LCR1,,LESTR,,NPY3R,,NPYR,,NPYRL,,NPYY3R,,WHIM,,WHIMSCVXVC,motif,chemokine,receptor,4 MED19 DT2P1G7,,LCMR1AS,,MED19 mediator,complex,subunit,19 S100A14 BCMP84,,S100A15 S100,calcium,binding,protein,A14 MDM2 ACTFS,,HDMX,,LSKB,,hdm2 MDM2,protoVoncogene MMP2 CLG4,,CLG4A,,MMPV2,,MMPVII,,MONA,,TBEV1matrix,metallopeptidase,2 ACE ACE1,,CD143,,DCP,,DCP1 angiotensin,I,converting,enzyme MAPK1 ERK,,ERKV2,,ERK2,,ERT1,,MAPK2,,P42MAPK,,PRKM1,,PRKM2,,p38,,p40,,p41,,p41mapk,,p42VMAPKmitogenVactivated,protein,kinase,1 CD274 B7VH,,B7H1,,PDVL1,,PDCD1L1,,PDCD1LG1,,PDL1,,hPDVL1CD274,molecule SERPINE1 PAI,,PAIV1,,PAI1,,PLANH1 serpin,family,E,member,1 FHIT AP3Aase,,FRA3B
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  • Interplay Between Epigenetics and Metabolism in Oncogenesis: Mechanisms and Therapeutic Approaches

    Interplay Between Epigenetics and Metabolism in Oncogenesis: Mechanisms and Therapeutic Approaches

    OPEN Oncogene (2017) 36, 3359–3374 www.nature.com/onc REVIEW Interplay between epigenetics and metabolism in oncogenesis: mechanisms and therapeutic approaches CC Wong1, Y Qian2,3 and J Yu1 Epigenetic and metabolic alterations in cancer cells are highly intertwined. Oncogene-driven metabolic rewiring modifies the epigenetic landscape via modulating the activities of DNA and histone modification enzymes at the metabolite level. Conversely, epigenetic mechanisms regulate the expression of metabolic genes, thereby altering the metabolome. Epigenetic-metabolomic interplay has a critical role in tumourigenesis by coordinately sustaining cell proliferation, metastasis and pluripotency. Understanding the link between epigenetics and metabolism could unravel novel molecular targets, whose intervention may lead to improvements in cancer treatment. In this review, we summarized the recent discoveries linking epigenetics and metabolism and their underlying roles in tumorigenesis; and highlighted the promising molecular targets, with an update on the development of small molecule or biologic inhibitors against these abnormalities in cancer. Oncogene (2017) 36, 3359–3374; doi:10.1038/onc.2016.485; published online 16 January 2017 INTRODUCTION metabolic genes have also been identified as driver genes It has been appreciated since the early days of cancer research mutated in some cancers, such as isocitrate dehydrogenase 1 16 17 that the metabolic profiles of tumor cells differ significantly from and 2 (IDH1/2) in gliomas and acute myeloid leukemia (AML), 18 normal cells. Cancer cells have high metabolic demands and they succinate dehydrogenase (SDH) in paragangliomas and fuma- utilize nutrients with an altered metabolic program to support rate hydratase (FH) in hereditary leiomyomatosis and renal cell 19 their high proliferative rates and adapt to the hostile tumor cancer (HLRCC).
  • Mutant IDH, (R)-2-Hydroxyglutarate, and Cancer

    Mutant IDH, (R)-2-Hydroxyglutarate, and Cancer

    Downloaded from genesdev.cshlp.org on October 1, 2021 - Published by Cold Spring Harbor Laboratory Press REVIEW What a difference a hydroxyl makes: mutant IDH, (R)-2-hydroxyglutarate, and cancer Julie-Aurore Losman1 and William G. Kaelin Jr.1,2,3 1Department of Medical Oncology, Dana-Farber Cancer Institute, Brigham and Women’s Hospital, Harvard Medical School, Boston, Massachusetts 02215, USA; 2Howard Hughes Medical Institute, Chevy Chase, Maryland 20815, USA Mutations in metabolic enzymes, including isocitrate whether altered cellular metabolism is a cause of cancer dehydrogenase 1 (IDH1) and IDH2, in cancer strongly or merely an adaptive response of cancer cells in the face implicate altered metabolism in tumorigenesis. IDH1 of accelerated cell proliferation is still a topic of some and IDH2 catalyze the interconversion of isocitrate and debate. 2-oxoglutarate (2OG). 2OG is a TCA cycle intermediate The recent identification of cancer-associated muta- and an essential cofactor for many enzymes, including tions in three metabolic enzymes suggests that altered JmjC domain-containing histone demethylases, TET cellular metabolism can indeed be a cause of some 5-methylcytosine hydroxylases, and EglN prolyl-4-hydrox- cancers (Pollard et al. 2003; King et al. 2006; Raimundo ylases. Cancer-associated IDH mutations alter the enzymes et al. 2011). Two of these enzymes, fumarate hydratase such that they reduce 2OG to the structurally similar (FH) and succinate dehydrogenase (SDH), are bone fide metabolite (R)-2-hydroxyglutarate [(R)-2HG]. Here we tumor suppressors, and loss-of-function mutations in FH review what is known about the molecular mechanisms and SDH have been identified in various cancers, in- of transformation by mutant IDH and discuss their im- cluding renal cell carcinomas and paragangliomas.
  • To Study Mutant P53 Gain of Function, Various Tumor-Derived P53 Mutants

    To Study Mutant P53 Gain of Function, Various Tumor-Derived P53 Mutants

    Differential effects of mutant TAp63γ on transactivation of p53 and/or p63 responsive genes and their effects on global gene expression. A thesis submitted in partial fulfillment of the requirements for the degree of Master of Science By Shama K Khokhar M.Sc., Bilaspur University, 2004 B.Sc., Bhopal University, 2002 2007 1 COPYRIGHT SHAMA K KHOKHAR 2007 2 WRIGHT STATE UNIVERSITY SCHOOL OF GRADUATE STUDIES Date of Defense: 12-03-07 I HEREBY RECOMMEND THAT THE THESIS PREPARED UNDER MY SUPERVISION BY SHAMA KHAN KHOKHAR ENTITLED Differential effects of mutant TAp63γ on transactivation of p53 and/or p63 responsive genes and their effects on global gene expression BE ACCEPTED IN PARTIAL FULFILLMENT OF THE REQUIREMENTS FOR THE DEGREE OF Master of Science Madhavi P. Kadakia, Ph.D. Thesis Director Daniel Organisciak , Ph.D. Department Chair Committee on Final Examination Madhavi P. Kadakia, Ph.D. Steven J. Berberich, Ph.D. Michael Leffak, Ph.D. Joseph F. Thomas, Jr., Ph.D. Dean, School of Graduate Studies 3 Abstract Khokhar, Shama K. M.S., Department of Biochemistry and Molecular Biology, Wright State University, 2007 Differential effect of TAp63γ mutants on transactivation of p53 and/or p63 responsive genes and their effects on global gene expression. p63, a member of the p53 gene family, known to play a role in development, has more recently also been implicated in cancer progression. Mice lacking p63 exhibit severe developmental defects such as limb truncations, abnormal skin, and absence of hair follicles, teeth, and mammary glands. Germline missense mutations of p63 have been shown to be responsible for several human developmental syndromes including SHFM, EEC and ADULT syndromes and are associated with anomalies in the development of organs of epithelial origin.
  • Cellular and Molecular Signatures in the Disease Tissue of Early

    Cellular and Molecular Signatures in the Disease Tissue of Early

    Cellular and Molecular Signatures in the Disease Tissue of Early Rheumatoid Arthritis Stratify Clinical Response to csDMARD-Therapy and Predict Radiographic Progression Frances Humby1,* Myles Lewis1,* Nandhini Ramamoorthi2, Jason Hackney3, Michael Barnes1, Michele Bombardieri1, Francesca Setiadi2, Stephen Kelly1, Fabiola Bene1, Maria di Cicco1, Sudeh Riahi1, Vidalba Rocher-Ros1, Nora Ng1, Ilias Lazorou1, Rebecca E. Hands1, Desiree van der Heijde4, Robert Landewé5, Annette van der Helm-van Mil4, Alberto Cauli6, Iain B. McInnes7, Christopher D. Buckley8, Ernest Choy9, Peter Taylor10, Michael J. Townsend2 & Costantino Pitzalis1 1Centre for Experimental Medicine and Rheumatology, William Harvey Research Institute, Barts and The London School of Medicine and Dentistry, Queen Mary University of London, Charterhouse Square, London EC1M 6BQ, UK. Departments of 2Biomarker Discovery OMNI, 3Bioinformatics and Computational Biology, Genentech Research and Early Development, South San Francisco, California 94080 USA 4Department of Rheumatology, Leiden University Medical Center, The Netherlands 5Department of Clinical Immunology & Rheumatology, Amsterdam Rheumatology & Immunology Center, Amsterdam, The Netherlands 6Rheumatology Unit, Department of Medical Sciences, Policlinico of the University of Cagliari, Cagliari, Italy 7Institute of Infection, Immunity and Inflammation, University of Glasgow, Glasgow G12 8TA, UK 8Rheumatology Research Group, Institute of Inflammation and Ageing (IIA), University of Birmingham, Birmingham B15 2WB, UK 9Institute of