General Information of Drug Off-Target (DOT) (ID: OTFH6BJS)

DOT Name E3 ubiquitin-protein ligase HUWE1 (HUWE1)
Synonyms
EC 2.3.2.26; ARF-binding protein 1; ARF-BP1; HECT, UBA and WWE domain-containing protein 1; HECT-type E3 ubiquitin transferase HUWE1; Homologous to E6AP carboxyl terminus homologous protein 9; HectH9; Large structure of UREB1; LASU1; Mcl-1 ubiquitin ligase E3; Mule; Upstream regulatory element-binding protein 1; URE-B1; URE-binding protein 1
Gene Name HUWE1
Related Disease
Intellectual disability, X-linked syndromic, Turner type ( )
Non-syndromic X-linked intellectual disability ( )
Advanced cancer ( )
Breast cancer ( )
Breast carcinoma ( )
Colorectal carcinoma ( )
Epithelial ovarian cancer ( )
Head-neck squamous cell carcinoma ( )
Intellectual disability ( )
Lung adenocarcinoma ( )
Mandibulofacial dysostosis-microcephaly syndrome ( )
Medulloblastoma ( )
Neoplasm ( )
Neurodevelopmental disorder ( )
Non-small-cell lung cancer ( )
Ovarian cancer ( )
Ovarian neoplasm ( )
Prostate cancer ( )
Prostate carcinoma ( )
X-linked intellectual disability ( )
B-cell neoplasm ( )
Bone osteosarcoma ( )
Hepatocellular carcinoma ( )
Leukopenia ( )
Lung carcinoma ( )
Osteosarcoma ( )
Severe congenital neutropenia ( )
Syndromic intellectual disability ( )
Metastatic malignant neoplasm ( )
Acute respiratory failure ( )
Carcinoma ( )
Lung cancer ( )
Rheumatic fever ( )
Thyroid cancer ( )
Thyroid gland carcinoma ( )
Thyroid tumor ( )
UniProt ID
HUWE1_HUMAN
PDB ID
2EKK; 2MUL; 3G1N; 3H1D; 5C6H; 5LP8; 6FYH; 6MIW; 6PFL; 7AZX; 7JQ9; 7MOP; 7MWD; 7MWE; 7MWF
EC Number
2.3.2.26
Pfam ID
PF06012 ; PF06025 ; PF00632 ; PF00627 ; PF14377 ; PF02825
Sequence
MKVDRTKLKKTPTEAPADCRALIDKLKVCNDEQLLLELQQIKTWNIGKCELYHWVDLLDR
FDGILADAGQTVENMSWMLVCDRPEREQLKMLLLAVLNFTALLIEYSFSRHLYSSIEHLT
TLLASSDMQVVLAVLNLLYVFSKRSNYITRLGSDKRTPLLTRLQHLAESWGGKENGFGLA
ECCRDLHMMKYPPSATTLHFEFYADPGAEVKIEKRTTSNTLHYIHIEQLDKISESPSEIM
ESLTKMYSIPKDKQMLLFTHIRLAHGFSNHRKRLQAVQARLHAISILVYSNALQESANSI
LYNGLIEELVDVLQITDKQLMEIKAASLRTLTSIVHLERTPKLSSIIDCTGTASYHGFLP
VLVRNCIQAMIDPSMDPYPHQFATALFSFLYHLASYDAGGEALVSCGMMEALLKVIKFLG
DEQDQITFVTRAVRVVDLITNLDMAAFQSHSGLSIFIYRLEHEVDLCRKECPFVIKPKIQ
RPNTTQEGEEMETDMDGVQCIPQRAALLKSMLNFLKKAIQDPAFSDGIRHVMDGSLPTSL
KHIISNAEYYGPSLFLLATEVVTVFVFQEPSLLSSLQDNGLTDVMLHALLIKDVPATREV
LGSLPNVFSALCLNARGLQSFVQCQPFERLFKVLLSPDYLPAMRRRRSSDPLGDTASNLG
SAVDELMRHQPTLKTDATTAIIKLLEEICNLGRDPKYICQKPSIQKADGTATAPPPRSNH
AAEEASSEDEEEEEVQAMQSFNSTQQNETEPNQQVVGTEERIPIPLMDYILNVMKFVESI
LSNNTTDDHCQEFVNQKGLLPLVTILGLPNLPIDFPTSAACQAVAGVCKSILTLSHEPKV
LQEGLLQLDSILSSLEPLHRPIESPGGSVLLRELACAGNVADATLSAQATPLLHALTAAH
AYIMMFVHTCRVGQSEIRSISVNQWGSQLGLSVLSKLSQLYCSLVWESTVLLSLCTPNSL
PSGCEFGQADMQKLVPKDEKAGTTQGGKRSDGEQDGAAGSMDASTQGLLEGIGLDGDTLA
PMETDEPTASDSKGKSKITPAMAARIKQIKPLLSASSRLGRALAELFGLLVKLCVGSPVR
QRRSHHAASTTTAPTPAARSTASALTKLLTKGLSWQPPPYTPTPRFRLTFFICSVGFTSP
MLFDERKYPYHLMLQKFLCSGGHNALFETFNWALSMGGKVPVSEGLEHSDLPDGTGEFLD
AWLMLVEKMVNPTTVLESPHSLPAKLPGGVQNFPQFSALRFLVVTQKAAFTCIKNLWNRK
PLKVYGGRMAESMLAILCHILRGEPVIRERLSKEKEGSRGEEDTGQEEGGSRREPQVNQQ
QLQQLMDMGFTREHAMEALLNTSTMEQATEYLLTHPPPIMGGVVRDLSMSEEDQMMRAIA
MSLGQDIPMDQRAESPEEVACRKEEEERKAREKQEEEEAKCLEKFQDADPLEQDELHTFT
DTMLPGCFHLLDELPDTVYRVCDLIMTAIKRNGADYRDMILKQVVNQVWEAADVLIKAAL
PLTTSDTKTVSEWISQMATLPQASNLATRILLLTLLFEELKLPCAWVVESSGILNVLIKL
LEVVQPCLQAAKEQKEVQTPKWITPVLLLIDFYEKTAISSKRRAQMTKYLQSNSNNWRWF
DDRSGRWCSYSASNNSTIDSAWKSGETSVRFTAGRRRYTVQFTTMVQVNEETGNRRPVML
TLLRVPRLNKNSKNSNGQELEKTLEESKEMDIKRKENKGNDTPLALESTNTEKETSLEET
KIGEILIQGLTEDMVTVLIRACVSMLGVPVDPDTLHATLRLCLRLTRDHKYAMMFAELKS
TRMILNLTQSSGFNGFTPLVTLLLRHIIEDPCTLRHTMEKVVRSAATSGAGSTTSGVVSG
SLGSREINYILRVLGPAACRNPDIFTEVANCCIRIALPAPRGSGTASDDEFENLRIKGPN
AVQLVKTTPLKPSPLPVIPDTIKEVIYDMLNALAAYHAPEEADKSDPKPGVMTQEVGQLL
QDMGDDVYQQYRSLTRQSSDFDTQSGFSINSQVFAADGASTETSASGTSQGEASTPEESR
DGKKDKEGDRASEEGKQKGKGSKPLMPTSTILRLLAELVRSYVGIATLIANYSYTVGQSE
LIKEDCSVLAFVLDHLLPHTQNAEDKDTPALARLFLASLAAAGSGTDAQVALVNEVKAAL
GRALAMAESTEKHARLQAVMCIISTIMESCPSTSSFYSSATAKTQHNGMNNIIRLFLKKG
LVNDLARVPHSLDLSSPNMANTVNAALKPLETLSRIVNQPSSLFGSKSASSKNKSEQDAQ
GASQDSSSNQQDPGEPGEAEVQEEDHDVTQTEVADGDIMDGEAETDSVVIAGQPEVLSSQ
EMQVENELEDLIDELLERDGGSGNSTIIVSRSGEDESQEDVLMDEAPSNLSQASTLQANR
EDSMNILDPEDEEEHTQEEDSSGSNEDEDDSQDEEEEEEEDEEDDQEDDEGEEGDEDDDD
DGSEMELDEDYPDMNASPLVRFERFDREDDLIIEFDNMFSSATDIPPSPGNIPTTHPLMV
RHADHSSLTLGSGSSTTRLTQGIGRSQRTLRQLTANTGHTIHVHYPGNRQPNPPLILQRL
LGPSAAADILQLSSSLPLQSRGRARLLVGNDDVHIIARSDDELLDDFFHDQSTATSQAGT
LSSIPTALTRWTEECKVLDAESMHDCVSVVKVSIVNHLEFLRDEELEERREKRRKQLAEE
ETKITDKGKEDKENRDQSAQCTASKSNDSTEQNLSDGTPMPDSYPTTPSSTDAATSESKE
TLGTLQSSQQQPTLPTPPALGEVPQELQSPAGEGGSSTQLLMPVEPEELGPTRPSGEAET
TQMELSPAPTITSLSPERAEDSDALTAVSSQLEGSPMDTSSLASCTLEEAVGDTSAAGSS
EQPRAGSSTPGDAPPAVAEVQGRSDGSGESAQPPEDSSPPASSESSSTRDSAVAISGADS
RGILEEPLPSTSSEEEDPLAGISLPEGVDPSFLAALPDDIRREVLQNQLGIRPPTRTAPS
TNSSAPAVVGNPGVTEVSPEFLAALPPAIQEEVLAQQRAEQQRRELAQNASSDTPMDPVT
FIQTLPSDLRRSVLEDMEDSVLAVMPPDIAAEAQALRREQEARQRQLMHERLFGHSSTSA
LSAILRSPAFTSRLSGNRGVQYTRLAVQRGGTFQMGGSSSHNRPSGSNVDTLLRLRGRLL
LDHEALSCLLVLLFVDEPKLNTSRLHRVLRNLCYHAQTRHWVIRSLLSILQRSSESELCI
ETPKLTTSEEKGKKSSKSCGSSSHENRPLDLLHKMESKSSNQLSWLSVSMDAALGCRTNI
FQIQRSGGRKHTEKHASGGSTVHIHPQAAPVVCRHVLDTLIQLAKVFPSHFTQQRTKETN
CESDRERGNKACSPCSSQSSSSGICTDFWDLLVKLDNMNVSRKGKNSVKSVPVSAGGEGE
TSPYSLEASPLGQLMNMLSHPVIRRSSLLTEKLLRLLSLISIALPENKVSEAQANSGSGA
SSTTTATSTTSTTTTTAASTTPTPPTAPTPVTSAPALVAATAISTIVVAASTTVTTPTTA
TTTVSISPTTKGSKSPAKVSDGGSSSTDFKMVSSGLTENQLQLSVEVLTSHSCSEEGLED
AANVLLQLSRGDSGTRDTVLKLLLNGARHLGYTLCKQIGTLLAELREYNLEQQRRAQCET
LSPDGLPEEQPQTTKLKGKMQSRFDMAENVVIVASQKRPLGGRELQLPSMSMLTSKTSTQ
KFFLRVLQVIIQLRDDTRRANKKAKQTGRLGSSGLGSASSIQAAVRQLEAEADAIIQMVR
EGQRARRQQQAATSESSQSEASVRREESPMDVDQPSPSAQDTQSIASDGTPQGEKEKEER
PPELPLLSEQLSLDELWDMLGECLKELEESHDQHAVLVLQPAVEAFFLVHATERESKPPV
RDTRESQLAHIKDEPPPLSPAPLTPATPSSLDPFFSREPSSMHISSSLPPDTQKFLRFAE
THRTVLNQILRQSTTHLADGPFAVLVDYIRVLDFDVKRKYFRQELERLDEGLRKEDMAVH
VRRDHVFEDSYRELHRKSPEEMKNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYAL
FRTSPGDRVTYTINPSSHCNPNHLSYFKFVGRIVAKAVYDNRLLECYFTRSFYKHILGKS
VRYTDMESEDYHFYQGLVYLLENDVSTLGYDLTFSTEVQEFGVCEVRDLKPNGANILVTE
ENKKEYVHLVCQMRMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLPTIDID
DLKSNTEYHKYQSNSIQIQWFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEGMNGI
QKFQIHRDDRSTDRLPSAHTCFNQLDLPAYESFEKLRHMLLLAIQECSEGFGLA
Function
E3 ubiquitin-protein ligase which mediates ubiquitination and subsequent proteasomal degradation of target proteins. Regulates apoptosis by catalyzing the polyubiquitination and degradation of MCL1. Mediates monoubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair. Also ubiquitinates the p53/TP53 tumor suppressor and core histones including H1, H2A, H2B, H3 and H4. Ubiquitinates MFN2 to negatively regulate mitochondrial fusion in response to decreased stearoylation of TFRC. Ubiquitination of MFN2 also takes place following induction of mitophagy; AMBRA1 acts as a cofactor for HUWE1-mediated ubiquitination. Regulates neural differentiation and proliferation by catalyzing the polyubiquitination and degradation of MYCN. May regulate abundance of CDC6 after DNA damage by polyubiquitinating and targeting CDC6 to degradation. Mediates polyubiquitination of isoform 2 of PA2G4. Acts in concert with MYCBP2 to regulate the circadian clock gene expression by promoting the lithium-induced ubiquination and degradation of NR1D1. Binds to an upstream initiator-like sequence in the preprodynorphin gene. Mediates HAPSTR1 degradation, but is also a required cofactor in the pathway by which HAPSTR1 governs stress signaling.
Tissue Specificity Weakly expressed in heart, brain and placenta but not in other tissues. Expressed in a number of cell lines, predominantly in those from colorectal carcinomas.
KEGG Pathway
Ubiquitin mediated proteolysis (hsa04120 )
Mitophagy - animal (hsa04137 )
Reactome Pathway
Antigen processing (R-HSA-983168 )
Neutrophil degranulation (R-HSA-6798695 )

Molecular Interaction Atlas (MIA) of This DOT

36 Disease(s) Related to This DOT
Disease Name Disease ID Evidence Level Mode of Inheritance REF
Intellectual disability, X-linked syndromic, Turner type DISBRA3L Definitive X-linked [1]
Non-syndromic X-linked intellectual disability DIS71AI3 Definitive X-linked [2]
Advanced cancer DISAT1Z9 Strong Biomarker [3]
Breast cancer DIS7DPX1 Strong Biomarker [4]
Breast carcinoma DIS2UE88 Strong Biomarker [4]
Colorectal carcinoma DIS5PYL0 Strong Biomarker [3]
Epithelial ovarian cancer DIS56MH2 Strong Biomarker [5]
Head-neck squamous cell carcinoma DISF7P24 Strong Altered Expression [6]
Intellectual disability DISMBNXP Strong Biomarker [7]
Lung adenocarcinoma DISD51WR Strong Altered Expression [6]
Mandibulofacial dysostosis-microcephaly syndrome DISSZWPO Strong Biomarker [8]
Medulloblastoma DISZD2ZL Strong Biomarker [9]
Neoplasm DISZKGEW Strong Biomarker [10]
Neurodevelopmental disorder DIS372XH Strong Genetic Variation [11]
Non-small-cell lung cancer DIS5Y6R9 Strong Biomarker [12]
Ovarian cancer DISZJHAP Strong Biomarker [5]
Ovarian neoplasm DISEAFTY Strong Biomarker [5]
Prostate cancer DISF190Y Strong Biomarker [3]
Prostate carcinoma DISMJPLE Strong Biomarker [3]
X-linked intellectual disability DISYJBY3 Strong Genetic Variation [13]
B-cell neoplasm DISVY326 moderate Biomarker [4]
Bone osteosarcoma DIST1004 moderate Biomarker [14]
Hepatocellular carcinoma DIS0J828 moderate Biomarker [15]
Leukopenia DISJMBMM moderate Genetic Variation [11]
Lung carcinoma DISTR26C moderate Biomarker [16]
Osteosarcoma DISLQ7E2 moderate Biomarker [14]
Severe congenital neutropenia DISES99N moderate Genetic Variation [11]
Syndromic intellectual disability DISH7SDF Supportive Autosomal dominant [17]
Metastatic malignant neoplasm DIS86UK6 Disputed Biomarker [18]
Acute respiratory failure DIS5KQ5Y Limited Biomarker [19]
Carcinoma DISH9F1N Limited Altered Expression [20]
Lung cancer DISCM4YA Limited Biomarker [3]
Rheumatic fever DISLUF66 Limited Biomarker [19]
Thyroid cancer DIS3VLDH Limited Biomarker [21]
Thyroid gland carcinoma DISMNGZ0 Limited Biomarker [21]
Thyroid tumor DISLVKMD Limited Biomarker [21]
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⏷ Show the Full List of 36 Disease(s)
Molecular Interaction Atlas (MIA) Jump to Detail Molecular Interaction Atlas of This DOT
5 Drug(s) Affected the Post-Translational Modifications of This DOT
Drug Name Drug ID Highest Status Interaction REF
Valproate DMCFE9I Approved Valproate decreases the methylation of E3 ubiquitin-protein ligase HUWE1 (HUWE1). [22]
PMID28870136-Compound-52 DMFDERP Patented PMID28870136-Compound-52 affects the phosphorylation of E3 ubiquitin-protein ligase HUWE1 (HUWE1). [30]
Bisphenol A DM2ZLD7 Investigative Bisphenol A decreases the methylation of E3 ubiquitin-protein ligase HUWE1 (HUWE1). [31]
Coumarin DM0N8ZM Investigative Coumarin affects the phosphorylation of E3 ubiquitin-protein ligase HUWE1 (HUWE1). [30]
Hexadecanoic acid DMWUXDZ Investigative Hexadecanoic acid increases the phosphorylation of E3 ubiquitin-protein ligase HUWE1 (HUWE1). [33]
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9 Drug(s) Affected the Gene/Protein Processing of This DOT
Drug Name Drug ID Highest Status Interaction REF
Doxorubicin DMVP5YE Approved Doxorubicin increases the expression of E3 ubiquitin-protein ligase HUWE1 (HUWE1). [23]
Ivermectin DMDBX5F Approved Ivermectin decreases the expression of E3 ubiquitin-protein ligase HUWE1 (HUWE1). [24]
Arsenic trioxide DM61TA4 Approved Arsenic trioxide increases the expression of E3 ubiquitin-protein ligase HUWE1 (HUWE1). [25]
Marinol DM70IK5 Approved Marinol increases the expression of E3 ubiquitin-protein ligase HUWE1 (HUWE1). [26]
Benzo(a)pyrene DMN7J43 Phase 1 Benzo(a)pyrene increases the mutagenesis of E3 ubiquitin-protein ligase HUWE1 (HUWE1). [27]
(+)-JQ1 DM1CZSJ Phase 1 (+)-JQ1 increases the expression of E3 ubiquitin-protein ligase HUWE1 (HUWE1). [28]
AMG 176 DM0Q7NO Phase 1 AMG 176 decreases the expression of E3 ubiquitin-protein ligase HUWE1 (HUWE1). [29]
AZD5991 DM7QGHO Phase 1 AZD5991 decreases the expression of E3 ubiquitin-protein ligase HUWE1 (HUWE1). [29]
Milchsaure DM462BT Investigative Milchsaure increases the expression of E3 ubiquitin-protein ligase HUWE1 (HUWE1). [32]
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⏷ Show the Full List of 9 Drug(s)

References

1 Classification of Genes: Standardized Clinical Validity Assessment of Gene-Disease Associations Aids Diagnostic Exome Analysis and Reclassifications. Hum Mutat. 2017 May;38(5):600-608. doi: 10.1002/humu.23183. Epub 2017 Feb 13.
2 Technical standards for the interpretation and reporting of constitutional copy-number variants: a joint consensus recommendation of the American College of Medical Genetics and Genomics (ACMG) and the Clinical Genome Resource (ClinGen). Genet Med. 2020 Feb;22(2):245-257. doi: 10.1038/s41436-019-0686-8. Epub 2019 Nov 6.
3 Meta-analysis of gene expression alterations and clinical significance of the HECT domain-containing ubiquitin ligase HUWE1 in cancer.Oncol Lett. 2019 Sep;18(3):2292-2303. doi: 10.3892/ol.2019.10579. Epub 2019 Jul 5.
4 Global Analysis of miRNA-mRNA Interaction Network in Breast Cancer with Brain Metastasis.Anticancer Res. 2017 Aug;37(8):4455-4468. doi: 10.21873/anticanres.11841.
5 Huwe1 Sustains Normal Ovarian Epithelial Cell Transformation and Tumor Growth through the Histone H1.3-H19 Cascade.Cancer Res. 2017 Sep 15;77(18):4773-4784. doi: 10.1158/0008-5472.CAN-16-2597. Epub 2017 Jul 7.
6 Regulation of miRNA Biogenesis and Histone Modification by K63-Polyubiquitinated DDX17 Controls Cancer Stem-like Features.Cancer Res. 2019 May 15;79(10):2549-2563. doi: 10.1158/0008-5472.CAN-18-2376. Epub 2019 Mar 15.
7 Publisher Correction: Impaired oxidative stress response characterizes HUWE1-promoted X-linked intellectual disability.Sci Rep. 2018 Apr 12;8(1):6010. doi: 10.1038/s41598-018-24189-2.
8 Under the mask of Kabuki syndrome: Elucidation of genetic-and phenotypic heterogeneity in patients with Kabuki-like phenotype.Eur J Med Genet. 2018 Jun;61(6):315-321. doi: 10.1016/j.ejmg.2018.01.005. Epub 2018 Jan 4.
9 Shh signaling protects Atoh1 from degradation mediated by the E3 ubiquitin ligase Huwe1 in neural precursors.Dev Cell. 2014 Jun 23;29(6):649-61. doi: 10.1016/j.devcel.2014.05.014.
10 Non-proteolytic ubiquitination of Hexokinase 2 by HectH9 controls tumor metabolism and cancer stem cell expansion.Nat Commun. 2019 Jun 14;10(1):2625. doi: 10.1038/s41467-019-10374-y.
11 Application of whole-exome sequencing to unravel the molecular basis of undiagnosed syndromic congenital neutropenia with intellectual disability.Am J Med Genet A. 2017 Jan;173(1):62-71. doi: 10.1002/ajmg.a.37969. Epub 2016 Sep 12.
12 HUWE1 controls the development of non-small cell lung cancer through down-regulation of p53.Theranostics. 2018 Jun 6;8(13):3517-3529. doi: 10.7150/thno.24401. eCollection 2018.
13 Submicroscopic duplications of the hydroxysteroid dehydrogenase HSD17B10 and the E3 ubiquitin ligase HUWE1 are associated with mental retardation. Am J Hum Genet. 2008 Feb;82(2):432-43. doi: 10.1016/j.ajhg.2007.11.002. Epub 2008 Jan 24.
14 MiR-542-5p is a negative prognostic factor and promotes osteosarcoma tumorigenesis by targeting HUWE1.Oncotarget. 2015 Dec 15;6(40):42761-72. doi: 10.18632/oncotarget.6199.
15 Characterization of the GNMT-HectH9-PREX2 tripartite relationship in the pathogenesis of hepatocellular carcinoma.Int J Cancer. 2017 May 15;140(10):2284-2297. doi: 10.1002/ijc.30652.
16 LIMCH1 suppress the growth of lung cancer by interacting with HUWE1 to sustain p53 stability.Gene. 2019 Sep 5;712:143963. doi: 10.1016/j.gene.2019.143963. Epub 2019 Jul 5.
17 HUWE1 variants cause dominant X-linked intellectual disability: a clinical study of 21 patients. Eur J Hum Genet. 2018 Jan;26(1):64-74. doi: 10.1038/s41431-017-0038-6. Epub 2017 Nov 27.
18 Gene expression profile analysis of ENO1 knockdown in gastric cancer cell line MGC-803.Oncol Lett. 2019 Apr;17(4):3881-3889. doi: 10.3892/ol.2019.10053. Epub 2019 Feb 19.
19 ARF-BP1/Mule is a critical mediator of the ARF tumor suppressor.Cell. 2005 Jul 1;121(7):1071-83. doi: 10.1016/j.cell.2005.03.037.
20 HUWE1 ubiquitylates and degrades the RAC activator TIAM1 promoting cell-cell adhesion disassembly, migration, and invasion.Cell Rep. 2015 Jan 6;10(1):88-102. doi: 10.1016/j.celrep.2014.12.012. Epub 2014 Dec 24.
21 Tumour suppressive function of HUWE1 in thyroid cancer.J Biosci. 2016 Sep;41(3):395-405. doi: 10.1007/s12038-016-9623-z.
22 Integrative omics data analyses of repeated dose toxicity of valproic acid in vitro reveal new mechanisms of steatosis induction. Toxicology. 2018 Jan 15;393:160-170.
23 Gamma-irradiation and doxorubicin treatment of normal human cells cause cell cycle arrest via different pathways. Mol Cells. 2005 Dec 31;20(3):331-8.
24 Quantitative proteomics reveals a broad-spectrum antiviral property of ivermectin, benefiting for COVID-19 treatment. J Cell Physiol. 2021 Apr;236(4):2959-2975. doi: 10.1002/jcp.30055. Epub 2020 Sep 22.
25 Essential role of cell cycle regulatory genes p21 and p27 expression in inhibition of breast cancer cells by arsenic trioxide. Med Oncol. 2011 Dec;28(4):1225-54.
26 THC exposure of human iPSC neurons impacts genes associated with neuropsychiatric disorders. Transl Psychiatry. 2018 Apr 25;8(1):89. doi: 10.1038/s41398-018-0137-3.
27 Exome-wide mutation profile in benzo[a]pyrene-derived post-stasis and immortal human mammary epithelial cells. Mutat Res Genet Toxicol Environ Mutagen. 2014 Dec;775-776:48-54. doi: 10.1016/j.mrgentox.2014.10.011. Epub 2014 Nov 4.
28 Inhibition of BRD4 attenuates tumor cell self-renewal and suppresses stem cell signaling in MYC driven medulloblastoma. Oncotarget. 2014 May 15;5(9):2355-71.
29 Mechanisms of MCL-1 Protein Stability Induced by MCL-1 Antagonists in B-Cell Malignancies. Clin Cancer Res. 2023 Jan 17;29(2):446-457. doi: 10.1158/1078-0432.CCR-22-2088.
30 Quantitative phosphoproteomics reveal cellular responses from caffeine, coumarin and quercetin in treated HepG2 cells. Toxicol Appl Pharmacol. 2022 Aug 15;449:116110. doi: 10.1016/j.taap.2022.116110. Epub 2022 Jun 7.
31 DNA methylome-wide alterations associated with estrogen receptor-dependent effects of bisphenols in breast cancer. Clin Epigenetics. 2019 Oct 10;11(1):138. doi: 10.1186/s13148-019-0725-y.
32 Transcriptional profiling of lactic acid treated reconstructed human epidermis reveals pathways underlying stinging and itch. Toxicol In Vitro. 2019 Jun;57:164-173.
33 Functional lipidomics: Palmitic acid impairs hepatocellular carcinoma development by modulating membrane fluidity and glucose metabolism. Hepatology. 2017 Aug;66(2):432-448. doi: 10.1002/hep.29033. Epub 2017 Jun 16.