2023
ATG9 vesicles comprise the seed membrane of mammalian autophagosomes
Olivas T, Wu Y, Yu S, Luan L, Choi P, Guinn E, Nag S, De Camilli P, Gupta K, Melia T. ATG9 vesicles comprise the seed membrane of mammalian autophagosomes. Journal Of Cell Biology 2023, 222: e202208088. PMID: 37115958, PMCID: PMC10148236, DOI: 10.1083/jcb.202208088.Peer-Reviewed Original ResearchConceptsAtg9 vesiclesMammalian autophagosomesStyrene maleic acid lipid particlesLipid scramblase activityLC3-IIAutophagosomes formAutophagosome membraneMature autophagosomesScramblase activityAutophagosome formationAtg9Lipid transportMembrane growthAutophagosomesNanoscale organizationProtein-mediated transferProteinMembrane surface areaOrganellesVesiclesSeed membraneMembraneLipid particlesLipidsDifferent stages
2016
Mass spectrometric analysis of dimer-disrupting mutations in Plasmodium triosephosphate isomerase
Bandyopadhyay D, Prakash S, Gupta K, Balaram P. Mass spectrometric analysis of dimer-disrupting mutations in Plasmodium triosephosphate isomerase. Analytical Biochemistry 2016, 500: 45-50. PMID: 26919806, DOI: 10.1016/j.ab.2016.02.011.Peer-Reviewed Original Research
2013
Mammalian Neuronal Sodium Channel Blocker μ‑Conotoxin BuIIIB Has a Structured N‑Terminus That Influences Potency
Kuang Z, Zhang MM, Gupta K, Gajewiak J, Gulyas J, Balaram P, Rivier JE, Olivera BM, Yoshikami D, Bulaj G, Norton RS. Mammalian Neuronal Sodium Channel Blocker μ‑Conotoxin BuIIIB Has a Structured N‑Terminus That Influences Potency. ACS Chemical Biology 2013, 8: 1344-1351. PMID: 23557677, PMCID: PMC4201638, DOI: 10.1021/cb300674x.Peer-Reviewed Original Research
2010
Disulfide Bond Assignments by Mass Spectrometry of Native Natural Peptides: Cysteine Pairing in Disulfide Bonded Conotoxins
Gupta K, Kumar M, Balaram P. Disulfide Bond Assignments by Mass Spectrometry of Native Natural Peptides: Cysteine Pairing in Disulfide Bonded Conotoxins. Analytical Chemistry 2010, 82: 8313-8319. PMID: 20843009, DOI: 10.1021/ac101867e.Peer-Reviewed Original ResearchConceptsS bond cleavageBond cleavageNatural peptidesDisulfide bondsProduct ion yieldsMass spectral fragmentationDisulfide bond assignmentsDisulfide pairingFragment ionsStructure elucidationPeptide backboneBond assignmentDissociation conditionsMass spectrometryMultiple disulfide bondsCysteine pairingsSpectral fragmentationPossible disulfideMultiple cysteine residuesNative peptideAnalytical methodologyBondsCorrect disulfide pairingIon yieldFurther fragmentation