01245nam2 22002771i 450 SUN002339120050405120000.020040910d1979 |0itac50 baitaIT|||| |||||ˆ2: ‰1945-1964Anna FreudTorinoBoringhieri1979P. 402-75623 cm.001SUN00233892001 OpereAnna Freud2210 TorinoBoringhieri1978-1979215 3 v.23 cm.TorinoSUNL000001Freud, AnnaSUNV015338159314BoringhieriSUNV001017650ITSOL20181109RICASUN0023391UFFICIO DI BIBLIOTECA DEL DIPARTIMENTO DI PSICOLOGIA16 CONS 679 16 VS 2358 UFFICIO DI BIBLIOTECA DEL DIPARTIMENTO DI PSICOLOGIA16 CONS 1296 16 VS 676 UFFICIO DI BIBLIOTECA DEL DIPARTIMENTO DI PSICOLOGIAIT-CE0119VS2358CONS 679caUFFICIO DI BIBLIOTECA DEL DIPARTIMENTO DI PSICOLOGIAIT-CE0119VS676CONS 1296ca1945-19641403066UNICAMPANIA05050nam 2201165z- 450 991057688620332120231214133054.0(CKB)5720000000008312(oapen)https://directory.doabooks.org/handle/20.500.12854/84433(EXLCZ)99572000000000831220202206d2022 |y 0engurmn|---annantxtrdacontentcrdamediacrrdacarrierMechanisms of ER Protein ImportBaselMDPI - Multidisciplinary Digital Publishing Institute20221 electronic resource (258 p.)3-0365-4094-6 3-0365-4093-8 Protein import into the endoplasmic reticulum (ER) is the first step in the biogenesis of approximately 10,000 different soluble and membrane proteins of human cells, which amounts to about 30% of the proteome. Most of these proteins fulfill their functions either in the membrane or lumen of the ER plus the nuclear envelope, in one of the organelles of the pathways for endo- and exocytosis (ERGIC, Golgi apparatus, endosome, lysosome, and trafficking vesicles), or at the cell surface as plasma membrane or secreted proteins. An increasing number of membrane proteins destined to lipid droplets, peroxisomes or mitochondria are first targeted to and inserted into the ER membrane prior to their integration into budding lipid droplets or peroxisomes or prior to their delivery to mitochondria via the ER-SURF pathway. ER protein import involves two stages, ER targeting, which guarantees membrane specificity, and the insertion of nascent membrane proteins into or translocation of soluble precursor polypeptides across the ER membrane. In most cases, both processes depend on amino-terminal signal peptides or transmembrane helices, which serve as signal peptide equivalents. However, the targeting reaction can also involve the ER targeting of specific mRNAs or ribosome–nascent chain complexes. Both processes may occur co- or post-translationally and are facilitated by various sophisticated machineries, which reside in the cytosol and the ER membrane, respectively. Except for resident ER and mitochondrial membrane proteins, the mature proteins are delivered to their functional locations by vesicular transport.Research & information: generalbicsscBiology, life sciencesbicsscchaperonescontact sitesendoplasmic reticulumER-SURFmembrane extractionmitochondriaprotein targetingbimolecular luminescence complementationcompetitionsplit luciferasemembrane proteinsprotein-protein interactionsSec61 complexSec63synthetic peptide complementationTRAP complexER protein translocasesignal peptideprotein translocationnascent peptide chainmembrane insertionmolecular modellingmolecular dynamics simulationsmolecular dockingsignal peptidaseER transloconsignal recognition particle dependent protein targetingSec61 dependent translocationco-translational translocationinhibitorhigh throughput screeningSec61Sec62foldinginsertionmembrane proteintransloconribosometransmembrane segmentlipid dropletsperoxisomesPEX3membrane protein insertionlabel-free quantitative mass spectrometrydifferential protein abundance analysisZellweger syndromeGETprotein transportSNDSRPEMCpositive-inside rulehydrophobicitytransmembrane helixsignal recognition particlenascent polypeptide-associated complexfidelitycyclotriazadisulfonamideER quality controlDNAJC3preproteinSec61 transloconribosome stallingsignal sequenceSec61 translocaseNACResearch & information: generalBiology, life sciencesZimmermann Richardedt1106845Lang SvenedtZimmermann RichardothLang SvenothBOOK9910576886203321Mechanisms of ER Protein Import3024210UNINA