2021
Impact of Calreticulin and Its Mutants on Endoplasmic Reticulum Function in Health and Disease
Arshad N, Cresswell P. Impact of Calreticulin and Its Mutants on Endoplasmic Reticulum Function in Health and Disease. Progress In Molecular And Subcellular Biology 2021, 59: 163-180. PMID: 34050866, DOI: 10.1007/978-3-030-67696-4_8.ChaptersConceptsEndoplasmic reticulumProtein quality control machineryER-resident protein calreticulinQuality control machineryKey cellular functionsAmino acid sequenceEndoplasmic reticulum functionLectin chaperonesCellular functionsControl machineryProtein interactionsTerminal domainER healthER functionAcid sequenceMutant calreticulinCell homeostasisProtein calreticulinProtein synthesisCalreticulinVital playersDramatic alterationsLipid metabolismBlood tumorsMutations
2018
Tumor-associated calreticulin variants functionally compromise the peptide loading complex and impair its recruitment of MHC-I
Arshad N, Cresswell P. Tumor-associated calreticulin variants functionally compromise the peptide loading complex and impair its recruitment of MHC-I. Journal Of Biological Chemistry 2018, 293: 9555-9569. PMID: 29769311, PMCID: PMC6016473, DOI: 10.1074/jbc.ra118.002836.Peer-Reviewed Original ResearchConceptsMyeloproliferative neoplasmsPeptide loading complexMHC-I levelsMajor histocompatibility complexEffective immunotherapyAntigen presentationImmune surveillanceImmune systemBlood tumorsSomatic frameshift mutationsTumor cellsMHCHistocompatibility complexSurface expressionGlycan-dependent mannerNeoplasmsTumorsNormal cellsReduced bindingHigh-affinity peptidesEndoplasmic reticulumBind peptidesCellsCalreticulinFrameshift mutation