The fate of membrane-bound ribosomes following the termination of protein synthesis.
about
p180 promotes the ribosome-independent localization of a subset of mRNA to the endoplasmic reticulumDetection of cellular responses to toxicants by dielectrophoresisThe endoplasmic reticulum: structure, function and response to cellular signalingRibosome binding to the Oxa1 complex facilitates co-translational protein insertion in mitochondria.Germ cell-specific gene 1 targets testis-specific poly(A) polymerase to the endoplasmic reticulum through protein-protein interactionsElaborate uORF/IRES features control expression and localization of human glycyl-tRNA synthetaseBlocking variant surface glycoprotein synthesis in Trypanosoma brucei triggers a general arrest in translation initiation.New prospects in studying the bacterial signal recognition particle pathway.Stable ribosome binding to the endoplasmic reticulum enables compartment-specific regulation of mRNA translationPartitioning and translation of mRNAs encoding soluble proteins on membrane-bound ribosomesmRNA translation is compartmentalized to the endoplasmic reticulum following physiological inhibition of cap-dependent translation.Multifaceted physiological response allows yeast to adapt to the loss of the signal recognition particle-dependent protein-targeting pathway.Primary role for endoplasmic reticulum-bound ribosomes in cellular translation identified by ribosome profilingDiversity and selectivity in mRNA translation on the endoplasmic reticulumEndoplasmic reticulum remains continuous and undergoes sheet-to-tubule transformation during cell division in mammalian cells.Long-timescale dynamics and regulation of Sec-facilitated protein translocation.Divergent regulation of protein synthesis in the cytosol and endoplasmic reticulum compartments of mammalian cells.Signaling-mediated functional activation of inducible nitric-oxide synthase and its role in stimulating platelet activation.Localization of mRNAs to the endoplasmic reticulum.Direct imaging electron microscopy (EM) methods in modern structural biology: overview and comparison with X-ray crystallography and single-particle cryo-EM reconstruction in the studies of large macromolecules.The selective recruitment of mRNA to the ER and an increase in initiation are important for glucose-stimulated proinsulin synthesis in pancreatic beta-cells.LOCAL TRANSLATION. Comment on "Principles of ER cotranslational translocation revealed by proximity-specific ribosome profiling".N-myristoylation determines dual targeting of mammalian NADH-cytochrome b5 reductase to ER and mitochondrial outer membranes by a mechanism of kinetic partitioningSignal sequence-independent SRP-SR complex formation at the membrane suggests an alternative targeting pathway within the SRP cycle.Translocon pores in the endoplasmic reticulum are permeable to small anions.Translocon pores in the endoplasmic reticulum are permeable to a neutral, polar molecule.In the Archaea Haloferax volcanii, membrane protein biogenesis and protein synthesis rates are affected by decreased ribosomal binding to the translocon.An energy-dependent maturation step is required for release of the cystic fibrosis transmembrane conductance regulator from early endoplasmic reticulum biosynthetic machinery.Ultrastructure of Highly Ordered Granules in Alveolar Type II Cells in Several Species.GRP78 Promotes Neural Stem Cell Antiapoptosis and Survival in Response to Oxygen-Glucose Deprivation (OGD)/Reoxygenation through PI3K/Akt, ERK1/2, and NF-κB/p65 Pathways.
P2860
Q21145739-22F98784-F9BE-480C-9025-AACD93ECD5F0Q24652320-BCF918BA-99BD-44D1-A212-ECCCD11FE37EQ26782462-233BE0FC-6B2E-4B06-ABF2-FA085231549FQ27932930-9261D797-9A66-4388-9E87-00D8AF2F1EC9Q28508269-D42C7D02-5AD8-4619-94FC-9AA32FEC0D47Q28600852-68EB6FFD-F4D7-49D8-9EA8-511859210EBCQ33512519-3AD9855C-C0AF-4CD0-8B99-C10567B94181Q34109335-58DA7DDB-3BD0-4043-8936-C53BE7E341BDQ34148249-BCA8154A-FA3E-456B-AB54-A607FABA0207Q34365293-B61E802E-3ED5-43F8-81C6-ACC7398EE590Q34547670-13EB2350-F8C7-4D17-99E0-47DE4061BFD8Q34987145-65819809-54A9-478C-9FAC-D835FC89FEC5Q35773992-26B50CA3-1D7A-4503-AD17-D75F5D81F86DQ35827837-82F846AA-B3DD-4475-84B7-D675FB49520FQ36176591-D89A7D90-F534-4358-B0A0-1D502DF48ADFQ36355150-F16142CB-2228-413F-8D9B-3714C7C96DB8Q36438789-E325BD59-7B5C-4929-A3DF-872A13D2654AQ36944838-22A948B9-87F1-4F41-B1D2-6784F46E12E0Q38197141-8513E455-7507-49E6-ACEC-8A799167CCA5Q38231426-93750851-945E-4A19-928F-C73D666EFC81Q39498096-82F4B915-1470-4004-A52C-2839618F93D5Q41265257-B2D67161-C578-4254-B6D9-AE2BC5DE08D7Q41847788-142F8F22-A8AC-4B88-9C58-D5A3AE2291CBQ42277688-C7FEFBFD-7267-4D61-9728-110D6E76455CQ42493299-2CAAA70B-AC20-46CA-A281-C1E07F440886Q42502796-7A65C8E4-9A46-4BF6-A67C-F78D062734E0Q43016555-3C770407-8EBA-466A-9D2E-EF5667932ADAQ46705910-BB6EDE7F-CD46-4F3A-A390-4151493B53A8Q52726359-24DF8B97-6C4E-4F85-AE7B-C58BF88B010FQ55251729-5F136648-829F-4452-9105-137EA1D568FD
P2860
The fate of membrane-bound ribosomes following the termination of protein synthesis.
description
2000 nî lūn-bûn
@nan
2000 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
The fate of membrane-bound ribosomes following the termination of protein synthesis.
@ast
The fate of membrane-bound ribosomes following the termination of protein synthesis.
@en
type
label
The fate of membrane-bound ribosomes following the termination of protein synthesis.
@ast
The fate of membrane-bound ribosomes following the termination of protein synthesis.
@en
prefLabel
The fate of membrane-bound ribosomes following the termination of protein synthesis.
@ast
The fate of membrane-bound ribosomes following the termination of protein synthesis.
@en
P2860
P356
P1476
The fate of membrane-bound ribosomes following the termination of protein synthesis.
@en
P2093
Nicchitta CV
P2860
P304
33820-33827
P356
10.1074/JBC.M004462200
P407
P577
2000-10-01T00:00:00Z