Daniel McQuaid
MD/PhD StudentAbout
Research
Publications
2026
Beta cell-derived cholecystokinin drives obesity-associated pancreatic adenocarcinoma development
Garcia CC, Venkat A, McQuaid DC, Agabiti SS, Tong A, Mathew B, Cardone RL, Starble R, Ruiz CF, Zheng C, Sogunro A, Jacox JB, Loh KH, Kibbey RG, Krishnaswamy S, Muzumdar MD. Beta cell-derived cholecystokinin drives obesity-associated pancreatic adenocarcinoma development. Nature Communications 2026 DOI: 10.1038/s41467-026-69821-2.Peer-Reviewed Original ResearchThis study investigates how beta cell-derived cholecystokinin drives obesity-associated pancreatic cancer development, showing that targeting endocrine signaling could prevent tumor progression in obesity-related contexts.Beta cell-derived cholecystokinin drives obesity-associated pancreatic adenocarcinoma development
Garcia C, Venkat A, McQuaid D, Agabiti S, Tong A, Mathew B, Cardone R, Starble R, Ruiz C, Zheng C, Sogunro A, Jacox J, Loh K, Kibbey R, Krishnaswamy S, Muzumdar M. Beta cell-derived cholecystokinin drives obesity-associated pancreatic adenocarcinoma development. Nature Communications 2026 PMID: 41760660, DOI: 10.1038/s41467-026-69821-2.Peer-Reviewed Original ResearchPancreatic adenocarcinomaImmature B cellsCell-derived tumorsCell secretionCell transcriptional statesSingle-cell RNA sequencingHost metabolic statePancreatic adenocarcinoma developmentBona fide driversExperimental lineagesPeptide hormone cholecystokininTranscriptional statesB cellsCholecystokinin expressionAdenocarcinoma developmentCCK signalingSecretion of insulinHormone cholecystokininCell expressionRNA sequencingTumor formationCholecystokininPDAC developmentPDAC progressionIslet beta
2025
Direct genetic transformation bypasses tumor-associated DNA methylation alterations
Hetzel S, Hodis E, Torlai Triglia E, Kovacsovics A, Steinmann K, Gnirke A, Cui M, McQuaid D, Weigert R, Pohl G, Muzumdar M, Leyvraz S, Keilholz U, Yaspo M, Regev A, Kretzmer H, Smith Z, Meissner A. Direct genetic transformation bypasses tumor-associated DNA methylation alterations. Genome Biology 2025, 26: 212. PMID: 40676699, PMCID: PMC12273271, DOI: 10.1186/s13059-025-03650-2.Peer-Reviewed Original ResearchConceptsDe novo methylationEpigenetic aspectsDNA methylation landscapeDNA methylation alterationsDNA methylation levelsMethylation landscapeMutant cellsPromoter sequencesExtensive proliferation in vitroMethylation alterationsCellular transformationMethylation levelsHuman cellsGenetic transformationGlobal changeHealthy human cellsClinical samplesAnimal systemsConclusionsOur resultsMolecular referenceProliferation in vitroCellsMouse modelTumor modelDNA
2023
Physical Restraints in Advanced Illness #462
McQuaid D, Roberts A, Lescott S, Prsic E. Physical Restraints in Advanced Illness #462. Journal Of Palliative Medicine 2023, 26: 1150-1152. DOI: 10.1089/jpm.2023.0174.Peer-Reviewed Original Research
2022
IRF8 as a Novel Marker to Differentiate Between CD30-Positive Large Cell Lymphomas
McQuaid DC, Katz SG, Xu ML. IRF8 as a Novel Marker to Differentiate Between CD30-Positive Large Cell Lymphomas. American Journal Of Clinical Pathology 2022, 158: 173-176. PMID: 35460405, PMCID: PMC10664184, DOI: 10.1093/ajcp/aqac044.Peer-Reviewed Original ResearchGlobal assessment of IRF8 as a novel cancer biomarker
McQuaid DC, Panse G, Wang WL, Pinkus GS, Katz SG, Xu ML. Global assessment of IRF8 as a novel cancer biomarker. Human Pathology 2022, 122: 1-10. PMID: 35085599, PMCID: PMC10621657, DOI: 10.1016/j.humpath.2022.01.004.Peer-Reviewed Original ResearchConceptsBlastic plasmacytoid dendritic cell neoplasmInterferon regulatory factor 8Myeloid sarcomaDifferential diagnosisPlasmacytoid dendritic cell neoplasmDesmoplastic small round cell tumorSmall round cell tumorTriple-negative breast cancerStrong uniform expressionDendritic cell neoplasmBroad differential diagnosisNegative breast cancerRound cell tumorAbsence of CD34IHC expression patternsAcute monocytic leukemiaNovel immunohistochemical markerTypes of cancerRegulatory factor 8Cancer Genome AtlasNovel cancer biomarkersRetrospective studySynovial sarcomaCell tumorsPleomorphic sarcoma
2018
Small molecule activators of protein phosphatase 2A for the treatment of castration-resistant prostate cancer.
McClinch K, Avelar R, Callejas D, Izadmehr S, Wiredja D, Perl A, Sangodkar J, Kastrinsky D, Schlatzer D, Cooper M, Kiselar J, Stachnik A, Yao S, Hoon D, McQuaid D, Zaware N, Gong Y, Brautigan D, Plymate S, Sprenger C, Oh W, Levine A, Kirschenbaum A, Sfakianos J, Sears R, DiFeo A, Ioannou Y, Ohlmeyer M, Narla G, Galsky M. Small molecule activators of protein phosphatase 2A for the treatment of castration-resistant prostate cancer. Cancer Research 2018, 78: canres.0123.2017. PMID: 29358171, PMCID: PMC5899650, DOI: 10.1158/0008-5472.can-17-0123.Peer-Reviewed Original ResearchConceptsCastrate-resistant prostate cancerAndrogen receptorProstate cancerCRPC cellsHuman castrate-resistant prostate cancerMultiple oncogenic signaling pathwaysSmall molecule activatorsAndrogen deprivation therapyAdvanced prostate cancerPrimary prostate cancerMurine xenograft modelGrowth inhibitory effectsDeprivation therapyCRPC treatmentTime-dependent mannerOncogenic signaling pathwaysPreclinical proofXenograft modelAR degradationCancer ResTumor suppressor PP2ATumor formationCancerAberrant reactivationSignaling pathways
2017
The Advantages of Targeted Protein Degradation Over Inhibition: An RTK Case Study
Burslem GM, Smith BE, Lai AC, Jaime-Figueroa S, McQuaid DC, Bondeson DP, Toure M, Dong H, Qian Y, Wang J, Crew AP, Hines J, Crews CM. The Advantages of Targeted Protein Degradation Over Inhibition: An RTK Case Study. Cell Chemical Biology 2017, 25: 67-77.e3. PMID: 29129716, PMCID: PMC5831399, DOI: 10.1016/j.chembiol.2017.09.009.Peer-Reviewed Original ResearchConceptsReceptor tyrosine kinasesProtein familyProtein degradationTyrosine kinaseDownstream signaling responseTargeted Protein DegradationDevelopment of PROTACsTargeted degradationEndogenous proteinsSignaling responseChimera technologyCell proliferationPROTACsPROTAC technologyKinaseKinase inhibitorsLigand showAdvantages of degradationReceptor tyrosine kinase inhibitorsTyrosine kinase inhibitorsInhibitionDegradationFamilyPowerful toolProteolysisActivation of tumor suppressor protein PP2A inhibits KRAS-driven tumor growth
Sangodkar J, Perl A, Tohme R, Kiselar J, Kastrinsky D, Zaware N, Izadmehr S, Mazhar S, Wiredja D, O’Connor C, Hoon D, Dhawan N, Schlatzer D, Yao S, Leonard D, Borczuk A, Gokulrangan G, Wang L, Svenson E, Farrington C, Yuan E, Avelar R, Stachnik A, Smith B, Gidwani V, Giannini H, McQuaid D, McClinch K, Wang Z, Levine A, Sears R, Chen E, Duan Q, Datt M, Haider S, Ma’ayan A, DiFeo A, Sharma N, Galsky M, Brautigan D, Ioannou Y, Xu W, Chance M, Ohlmeyer M, Narla G. Activation of tumor suppressor protein PP2A inhibits KRAS-driven tumor growth. Journal Of Clinical Investigation 2017, 127: 2081-2090. PMID: 28504649, PMCID: PMC5451217, DOI: 10.1172/jci89548.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntineoplastic AgentsCell Line, TumorCell SurvivalDrug Resistance, NeoplasmEnzyme ActivationEnzyme ActivatorsHumansMaleMice, Inbred BALB CMice, NudeMice, TransgenicProtein BindingProtein Phosphatase 2Proto-Oncogene Proteins p21(ras)Signal TransductionTumor BurdenXenograft Model Antitumor AssaysConceptsTumor suppressor proteinSmall molecule activatorsSuppressor proteinTumor suppressor protein phosphatase 2AMolecule activatorsProtein phosphatase 2AInactivation of kinasesOncogenic signaling proteinsPhosphatase 2AScaffold subunitSignaling proteinsEndogenous phosphatasesNegative regulatorOncogenic kinasesConformational changesCancer-associated molecular targetsKRAS-mutant lung cancerPP2AMolecular targetsProteinCancer cellsKinaseMouse xenograftsTreatment of cancerActivator