2024
A fluorescence-based assay for measuring polyamine biosynthesis aminopropyl transferase–mediated catalysis
Singh P, Choi J, Wang W, T Lam T, Lechner P, Vanderwal C, Pou S, Nilsen A, Ben Mamoun C. A fluorescence-based assay for measuring polyamine biosynthesis aminopropyl transferase–mediated catalysis. Journal Of Biological Chemistry 2024, 300: 107832. PMID: 39342998, DOI: 10.1016/j.jbc.2024.107832.Peer-Reviewed Original ResearchAminopropyl transferaseFluorescence-based assayLack of high-throughput assaysHigh-throughput screeningCarbon chain lengthChemical librariesMass spectrometryChain lengthHigh-throughput assayDrug discoveryMass spectrometry analysisSaccharomyces cerevisiaeThin-layer chromatographyFluorescence intensityCellular functionsSpectrometry analysisPolycationic moleculesFluorescent conjugatesIsoindoleAPT activityCatalysisAssayBenzeneAdductsEnzymeA complex of the lipid transport ER proteins TMEM24 and C2CD2 with band 4.1 at cell–cell contacts
Johnson B, Iuliano M, Lam T, Biederer T, De Camilli P. A complex of the lipid transport ER proteins TMEM24 and C2CD2 with band 4.1 at cell–cell contacts. Journal Of Cell Biology 2024, 223: e202311137. PMID: 39158698, PMCID: PMC11334333, DOI: 10.1083/jcb.202311137.Peer-Reviewed Original ResearchConceptsPlasma membraneNon-vesicular lipid transferSites of cell contactC-terminus motifsCell contact-dependent signalsContact-dependent signalingCell-cell contactER/PM junctionsTMEM24ER proteinsPM proteinsSynCAM 1Cell adhesion moleculesCellular functionsLipid transferC2CD2Phospholipid transportLipid transportCell contactProteinAdhesion moleculesCalcium homeostasisCellsFamily membersParalogs
2023
Multi-omics profiling reveals cellular pathways and functions regulated by ALDH1B1 in colon cancer cells
Wang Y, Popovic Z, Charkoftaki G, Garcia-Milian R, Lam T, Thompson D, Chen Y, Vasiliou V. Multi-omics profiling reveals cellular pathways and functions regulated by ALDH1B1 in colon cancer cells. Chemico-Biological Interactions 2023, 384: 110714. PMID: 37716420, PMCID: PMC10807983, DOI: 10.1016/j.cbi.2023.110714.Peer-Reviewed Original ResearchColon cancer cellsCellular stress response pathwaysStress response pathwaysMulti-omics analysisCancer cellsSecond messenger signalingMulti-omics profilingNew molecular informationFunctional annotationCellular functionsResponse pathwaysKinase signalingCellular pathwaysColon adenocarcinoma cell lineHuman colon adenocarcinoma cell lineApoptosis signalingEnrichment analysisAldehyde dehydrogenase 1B1Molecular signaturesAdenocarcinoma cell lineMolecular informationSignalingNovel targetProtein expressionCell lines
2020
Cerebrospinal fluid proteome evaluation in major depressive disorder by mass spectrometry
Franzen AD, Lam TT, Williams KR, Nairn AC, Duman RS, Sathyanesan M, Kumar V, Carpenter LL, Newton SS. Cerebrospinal fluid proteome evaluation in major depressive disorder by mass spectrometry. BMC Psychiatry 2020, 20: 481. PMID: 32998701, PMCID: PMC7528485, DOI: 10.1186/s12888-020-02874-9.Peer-Reviewed Original ResearchConceptsPR domain zinc finger protein 1Bioinformatics analysisZinc finger protein 1Quantitative mass spectrometryFinger protein 1Potential biological functionsMajor canonical pathwaysPeroxisome proliferator-activated receptor gamma coactivatorProliferator-activated receptor gamma coactivatorCellular functionsCellular movementCellular compromiseCell signalingCellular developmentOrganismal injuryBiological functionsReceptor gamma coactivatorCanonical pathwaysSignal transducerUpstream regulatorTranscription 3Protein profilesDifferential expressionProtein synthesisProteomics software
2009
Diversification of a Salmonella Virulence Protein Function by Ubiquitin-Dependent Differential Localization
Patel JC, Hueffer K, Lam TT, Galán JE. Diversification of a Salmonella Virulence Protein Function by Ubiquitin-Dependent Differential Localization. Cell 2009, 137: 283-294. PMID: 19379694, PMCID: PMC2673707, DOI: 10.1016/j.cell.2009.01.056.Peer-Reviewed Original ResearchConceptsEffector proteinsCellular functionsType III secretion systemBacterial effector proteinsUbiquitin-dependent mannerDifferent cellular compartmentsHost cellular machinerySame enzymatic activityVesicular traffickingCellular machineryProtein functionSecretion systemCellular compartmentsBacterial internalizationFunctional repertoirePlasma membraneRegulated mannerAkt activationHost cellsDifferential localizationBacterial replicationVirulence factorsEnzymatic activityBacterial pathogensProtein
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