grant

ER and post-ER quality control of integral membrane proteins

Organization UNIVERSITY OF PITTSBURGH AT PITTSBURGHLocation PITTSBURGH, UNITED STATESPosted 1 Jun 2019Deadline 31 May 2029
NIHUS FederalResearch GrantFY202526 S proteasome complex26S ATP-Dependent Protease26S ATP-Dependent Proteasome26S Proteasome Complex26S Proteosome26S protease26S proteasomeAddressAmino AcidsBiologic ModelsBiological ModelsCausalityCell BodyCellsCellular biologyChargeChemicalsCollaborationsCommunitiesCytoplasmCytosolDNA mutationDedicationsDegradation PathwayDegradative PathwayDiseaseDisorderEndoplasmic ReticulumEnvironmentErgastoplasmEtiologyFaceGene AlterationGene MutationGenerationsGenesGenetic ChangeGenetic defectGenetic mutationGoalsHereditaryHumanIndividualInheritedIntegral Membrane ProteinIntrinsic Membrane ProteinIon ChannelIon TransportIonic ChannelsKnowledgeLinkMembraneMembrane ChannelsMembrane Protein GeneMembrane ProteinsMembrane-Associated ProteinsMethodsModel SystemModelingModern ManMolecularMutationNamesPathway interactionsProtein BiosynthesisProtein TraffickingQuality ControlResearchRibosomal Peptide BiosynthesisRibosomal Protein BiosynthesisRibosomal Protein SynthesisSideSurface ProteinsTM DomainTechniquesToxic effectToxicitiesTranslatingTransmembrane DomainTransmembrane ProteinTransmembrane Protein GeneTransmembrane RegionUbiquitilationUbiquitinationUbiquitinoylationVariantVariationaberrant folded proteinaberrant folded proteinsabnormal folded proteinabnormal folded proteinsaminoacidcausationcell biologydisease causationfacesfacialgene defectgenome mutationhydrophilicityinnovateinnovationinnovativeloss of functionmembrane structuremisfolded proteinmisfolded proteinsmutant allelenamenamednamingnon-Nativenonnativenovelpathwaypersonalization of treatmentpersonalized medicinepersonalized therapypersonalized treatmentposterspreventpreventingprotein foldingprotein synthesisprotein transportproteotoxic proteinproteotoxinreconstitutereconstitutionsolutetooltraffickingubiquinationubiquitin conjugation
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Description preview

Approximately one-quarter of all proteins synthesized in human cells integrate into the membrane of the
endoplasmic reticulum (ER) as they are translated. However, membrane protein folding is problematic. First,

structurally diverse integral membrane proteins face the challenge of folding co-translationally and post-

translationally in three…

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ER and post-ER quality control of integral membrane proteins — UNIVERSITY OF PITTSBURGH AT PITTSBURGH | UNITED STATES | | Dev Procure