2022
Carbonyl Posttranslational Modification Associated With Early-Onset Type 1 Diabetes Autoimmunity.
Yang ML, Connolly SE, Gee RJ, Lam TT, Kanyo J, Peng J, Guyer P, Syed F, Tse HM, Clarke SG, Clarke CF, James EA, Speake C, Evans-Molina C, Arvan P, Herold KC, Wen L, Mamula MJ. Carbonyl Posttranslational Modification Associated With Early-Onset Type 1 Diabetes Autoimmunity. Diabetes 2022, 71: 1979-1993. PMID: 35730902, PMCID: PMC9450849, DOI: 10.2337/db21-0989.Peer-Reviewed Original ResearchConceptsType 1 diabetesNOD miceMurine type 1 diabetesHuman type 1 diabetesDecreased glucose-stimulated insulin secretionAnti-insulin autoimmunityPrediabetic NOD miceGlucose-stimulated insulin secretionOnset Type 1T cell responsesOnset of hyperglycemiaCirculation of patientsAutoreactive CD4Insulin ratioInsulin secretionDiabetesPancreatic isletsType 1Islet proteinsOxidative stressAutoimmunitySelect groupMiceCarbonyl modificationOnset
2018
Quantification of Urinary Protein Biomarkers of Autosomal Dominant Polycystic Kidney Disease by Parallel Reaction Monitoring
Rauniyar N, Yu X, Cantley J, Voss EZ, Belcher J, Colangelo CM, Stone KL, Dahl N, Parikh C, Lam TT, Cantley LG. Quantification of Urinary Protein Biomarkers of Autosomal Dominant Polycystic Kidney Disease by Parallel Reaction Monitoring. Proteomics Clinical Applications 2018, 12: e1700157. PMID: 29573172, PMCID: PMC6736530, DOI: 10.1002/prca.201700157.Peer-Reviewed Original ResearchMeSH KeywordsBiomarkersFemaleHumansKidneyMalePolycystic Kidney, Autosomal DominantProteinsProteomeUrineConceptsAutosomal dominant polycystic kidney diseaseDominant polycystic kidney diseasePolycystic kidney diseaseCyst growthKidney diseaseUrinary proteinNormal controlsEnd-stage renal failureUrine samplesUrinary protein biomarkersLife-long diseasePresence of cystsRespective urine samplesMost patientsRenal failureADPKD patientsEarly diagnosisClinical relevanceUrinary proteomeParallel reaction monitoringPatientsCyst formationDiseaseWater intakePathogenesis
2004
Identification of Sites of Ubiquitination in Proteins: A Fourier Transform Ion Cyclotron Resonance Mass Spectrometry Approach
Cooper HJ, Heath JK, Jaffray E, Hay RT, Lam TT, Marshall AG. Identification of Sites of Ubiquitination in Proteins: A Fourier Transform Ion Cyclotron Resonance Mass Spectrometry Approach. Analytical Chemistry 2004, 76: 6982-6988. PMID: 15571350, DOI: 10.1021/ac0401063.Peer-Reviewed Original ResearchConceptsSites of ubiquitinationPolyubiquitin chainsFourier transform ion cyclotron resonance mass spectrometryTransform ion cyclotron resonance mass spectrometryIon electron capture dissociationIon cyclotron resonance mass spectrometryCyclotron resonance mass spectrometryLysine residuesTandem mass spectrometric techniquesElectron capture dissociationResonance mass spectrometryExtensive sequence coverageMass spectrometric techniquesConsequences of ubiquitinationCapture dissociationMass spectrometry approachPolyubiquitinated speciesSingle ubiquitinFT-ICRStructural elucidationCellular functionsUbiquitinated proteinsModified peptideUbiquitination modificationSpectrometric techniques