00968nam2 22002893i 450 99630154910331620190716140359.0978-88-288-0599-120190219d2018----||||0itac50 baitaIT<<La >> direzione e coordinamento delle imprese consorziatenatura e limitiGiovanni AgrustiMilanoGiuffrè Francis Lefebvre2018XII, 279 p.24 cmQuaderni di Giurisprudenza commerciale424001000312045Quaderni di giurisprudenza commerciale, 424ConsorziLegislazioneBNCF346.460668AGRUSTI,Giovanni<avvocato>766213ITsalbcISBD996301549103316CCXXV.3. Coll. 3/ 35990110 G.XXV.3. Coll. 3/00153000BKGIUDirezione e coordinamento delle imprese consorziate1558565UNISA05089nam 2201189z- 450 991057688620332120220621(CKB)5720000000008312(oapen)https://directory.doabooks.org/handle/20.500.12854/84433(oapen)doab84433(EXLCZ)99572000000000831220202206d2022 |y 0engurmn|---annantxtrdacontentcrdamediacrrdacarrierMechanisms of ER Protein ImportBaselMDPI - Multidisciplinary Digital Publishing Institute20221 online 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.Biology, life sciencesbicsscResearch and information: generalbicsscbimolecular luminescence complementationchaperonesco-translational translocationcompetitioncontact sitescyclotriazadisulfonamidedifferential protein abundance analysisDNAJC3EMCendoplasmic reticulumER protein translocaseER quality controlER transloconER-SURFfidelityfoldingGEThigh throughput screeninghydrophobicityinhibitorinsertionlabel-free quantitative mass spectrometrylipid dropletsmembrane extractionmembrane insertionmembrane proteinmembrane protein insertionmembrane proteinsmitochondriamolecular dockingmolecular dynamics simulationsmolecular modellingn/aNACnascent peptide chainnascent polypeptide-associated complexperoxisomesPEX3positive-inside rulepreproteinprotein targetingprotein translocationprotein transportprotein-protein interactionsribosomeribosome stallingSec61Sec61 complexSec61 dependent translocationSec61 translocaseSec61 transloconSec62Sec63signal peptidasesignal peptidesignal recognition particlesignal recognition particle dependent protein targetingsignal sequenceSNDsplit luciferaseSRPsynthetic peptide complementationtranslocontransmembrane helixtransmembrane segmentTRAP complexZellweger syndromeBiology, life sciencesResearch and information: generalZimmermann Richardedt1106845Lang SvenedtZimmermann RichardothLang SvenothBOOK9910576886203321Mechanisms of ER Protein Import3024210UNINA