Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane.
about
p180 promotes the ribosome-independent localization of a subset of mRNA to the endoplasmic reticulumStress-associated endoplasmic reticulum protein 1 (SERP1)/Ribosome-associated membrane protein 4 (RAMP4) stabilizes membrane proteins during stress and facilitates subsequent glycosylationMammalian Sec61 is associated with Sec62 and Sec63BiP-mediated closing of the Sec61 channel limits Ca2+ leakage from the ERNecessary role for the Lag1p motif in (dihydro)ceramide synthase activityTranslocon-associated protein TRAP delta and a novel TRAP-like protein are coordinately expressed with pro-opiomelanocortin in Xenopus intermediate pituitaryDifferent effects of Sec61α, Sec62 and Sec63 depletion on transport of polypeptides into the endoplasmic reticulum of mammalian cellsTRAM2 protein interacts with endoplasmic reticulum Ca2+ pump Serca2b and is necessary for collagen type I synthesisMembrane topology of the 12- and the 25-kDa subunits of the mammalian signal peptidase complexThe N-terminal region of the alpha-subunit of the TRAP complex has a conserved cluster of negative chargesProfile of Tom A. Rapoport.Membrane integration of Sec61alpha: a core component of the endoplasmic reticulum translocation complexStructure of the E. coli protein-conducting channel bound to a translating ribosomeSignal peptide-dependent protein transport in Bacillus subtilis: a genome-based survey of the secretomeThe R-SNARE endobrevin/VAMP-8 mediates homotypic fusion of early endosomes and late endosomesE2-25K mediates US11-triggered retro-translocation of MHC class I heavy chains in a permeabilized cell systemTransport route for synaptobrevin via a novel pathway of insertion into the endoplasmic reticulum membraneThe concept of translocational regulationThe beta subunit of the signal recognition particle receptor is a transmembrane GTPase that anchors the alpha subunit, a peripheral membrane GTPase, to the endoplasmic reticulum membraneUnfolded cholera toxin is transferred to the ER membrane and released from protein disulfide isomerase upon oxidation by Ero1Characterization of individual polynucleotide molecules using a membrane channelThe beta subunit of the Sec61 complex facilitates cotranslational protein transport and interacts with the signal peptidase during translocationThe ribosome regulates the GTPase of the beta-subunit of the signal recognition particle receptorChannel crossing: how are proteins shipped across the bacterial plasma membrane?Mechanisms for quality control of misfolded transmembrane proteinsHow viruses use the endoplasmic reticulum for entry, replication, and assemblyThe Aspergillus nidulans peripheral ER: disorganization by ER stress and persistence during mitosisStructure of the Sec61 channel opened by a signal sequenceEvidence that flavivirus NS1-NS2A cleavage is mediated by a membrane-bound host protease in the endoplasmic reticulumX-ray structure of a protein-conducting channelThe mechanism of membrane-associated steps in tail-anchored protein insertionStructures of the Sec61 complex engaged in nascent peptide translocation or membrane insertionThe yeast SPC22/23 homolog Spc3p is essential for signal peptidase activity.Sec63p and Kar2p are required for the translocation of SRP-dependent precursors into the yeast endoplasmic reticulum in vivo.The reticulon and DP1/Yop1p proteins form immobile oligomers in the tubular endoplasmic reticulum.A novel Hsp70 of the yeast ER lumen is required for the efficient translocation of a number of protein precursorsA functional GTPase domain, but not its transmembrane domain, is required for function of the SRP receptor beta-subunit.BiP and Sec63p are required for both co- and posttranslational protein translocation into the yeast endoplasmic reticulum.A second trimeric complex containing homologs of the Sec61p complex functions in protein transport across the ER membrane of S. cerevisiaeSec61p serves multiple roles in secretory precursor binding and translocation into the endoplasmic reticulum membrane.
P2860
Q21145739-19A2C88C-BA29-4BE4-AB6D-0DB7F75EE7ACQ22010942-069A3A91-A3D8-4A48-AA6D-DF3D6441DC84Q22254037-3DB0AF1E-A6EA-4116-BD99-267ADD6BA77CQ24293288-40241999-3AC4-4A46-9B27-1F7F977F6A10Q24301554-545532AB-C899-4F81-96A2-F86AC888025CQ24303980-E4FBE3DC-E535-469B-B624-44CDA4BDA04AQ24306519-9E5D2EF3-18A9-4166-B7F5-256AB967518DQ24306604-1F1F2099-B338-4A3E-9D16-858043A8CA5AQ24311608-C5E6C6A3-1445-4284-A4FD-8F108E8ED7CBQ24316131-1519F97F-6265-4FE1-B910-A488B458DE62Q24530346-EF6E767C-B36D-4454-ADA7-024A9385A52DQ24530719-2C9EE905-29FB-4AC9-BEA4-5CCA8FA39DBFQ24539141-07740367-2FFC-4455-8C21-91B583386178Q24548495-28312E0E-DDDD-4332-BC0A-649365E0D939Q24550767-1F214740-CBB0-4ACE-B661-C2E239E0C3F6Q24554438-C9777558-FA9C-4F72-A4F7-EEF0D387C4CDQ24568369-B1D3CC36-364D-4AAE-A47C-19F333F20C3AQ24654677-045B264C-EF3C-4461-AE28-88BB204A0D89Q24672874-E9920ABB-724E-4C59-B9FC-344CE2987EBEQ24674605-81E6A219-3B31-4302-BD6E-1D07FAEF0242Q24681325-59F44B53-3E7E-4AE0-85A3-C83A48A3C7A8Q24683072-31AA219D-6896-4D7F-BBF4-2100BBDA0806Q24683394-B278EF63-1F72-44A7-803E-9E464405A7BAQ26786998-16572119-94C9-4F3F-B5CE-E1A12DA6DB3CQ26830475-2D2B5E0F-47B6-4A23-8A2F-26CABAFEE209Q26996825-43BB7DC5-CF6C-4D69-9E74-2C83EE7E23BBQ27312475-90E9AD7D-FBDA-4376-AB65-9456AD52D0B5Q27330079-248E9A88-FBD1-421C-9C64-33C40B14BAB4Q27480313-4EE72965-FBF2-4D47-9189-B7D971C9A90CQ27642744-4002A6CC-EDDD-47EB-90A5-206167CE3AE9Q27671975-65588FE6-4BA8-4585-BCCC-C79E7AFF1462Q27689043-0FCC8118-773A-41CB-9212-FD2D38CF6F9DQ27930503-5EB20A85-1D44-46A2-A401-5F824AE0BEA1Q27930764-F55B6BBE-F67C-4F76-B925-427C604F10A3Q27932262-82C234BB-3E27-4366-AEB5-7F97105D354FQ27932477-3370F128-B072-4DB4-8FC9-11AE852A646BQ27933510-D3EF4137-A0D9-4286-A35F-76717C10FA80Q27935171-9077DDF1-AF55-481D-A1F1-18C2B16CA0DFQ27935591-BB50D862-D6F2-4C10-B5AB-5BBBB692CF7CQ27938591-B3C64FD7-D7DD-416F-B216-87B98479282A
P2860
Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane.
description
1993 nî lūn-bûn
@nan
1993 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1993 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
name
Protein translocation into pro ...... ndoplasmic reticulum membrane.
@ast
Protein translocation into pro ...... ndoplasmic reticulum membrane.
@en
Protein translocation into pro ...... ndoplasmic reticulum membrane.
@nl
type
label
Protein translocation into pro ...... ndoplasmic reticulum membrane.
@ast
Protein translocation into pro ...... ndoplasmic reticulum membrane.
@en
Protein translocation into pro ...... ndoplasmic reticulum membrane.
@nl
prefLabel
Protein translocation into pro ...... ndoplasmic reticulum membrane.
@ast
Protein translocation into pro ...... ndoplasmic reticulum membrane.
@en
Protein translocation into pro ...... ndoplasmic reticulum membrane.
@nl
P1433
P1476
Protein translocation into pro ...... ndoplasmic reticulum membrane.
@en
P304
P356
10.1016/0092-8674(93)90483-7
P407
P577
1993-11-01T00:00:00Z