2017
Comparative Proteomics Enables Identification of Nonannotated Cold Shock Proteins in E. coli
D’Lima N, Khitun A, Rosenbloom AD, Yuan P, Gassaway BM, Barber KW, Rinehart J, Slavoff SA. Comparative Proteomics Enables Identification of Nonannotated Cold Shock Proteins in E. coli. Journal Of Proteome Research 2017, 16: 3722-3731. PMID: 28861998, PMCID: PMC5647875, DOI: 10.1021/acs.jproteome.7b00419.Peer-Reviewed Original ResearchConceptsCold shock proteinsComparative proteomicsShock proteinsRelated Gram-negative bacteriaMass spectrometry-based proteomicsSmall open reading framesMolecular genetic approachesWhole genome databaseSpectrometry-based proteomicsOpen reading frameE. coliEukaryotic genomesGram-negative bacteriaCellular functionsDifferent organismsGenetic approachesReading frameBiological roleProteomicsMicroproteinsEnable identificationProteinColiGenomeRecent advances
2008
Expanding the Substrate Tolerance of Biotin Ligase through Exploration of Enzymes from Diverse Species
Slavoff SA, Chen I, Choi YA, Ting AY. Expanding the Substrate Tolerance of Biotin Ligase through Exploration of Enzymes from Diverse Species. Journal Of The American Chemical Society 2008, 130: 1160-1162. PMID: 18171066, PMCID: PMC3501195, DOI: 10.1021/ja076655i.Peer-Reviewed Original ResearchConceptsLigation reactionProtein labeling applicationsDifferential substrate specificitySite-specific conjugationBiotin acceptor domainPhosphine probesStaudinger ligationDiverse speciesBiotin ligaseChemical probesDifferent organismsMass spectrometry assayPyrococcus horikoshiiSubstrate specificityCell biologyUnnatural analoguesLabeling applicationsAcceptor domainsSubstrate toleranceLigasesDifferent speciesSpectrometry assayReactionSpeciesBiotin