P3373
The signal sequence coding region promotes nuclear export of mRNAA visual screen of a GFP-fusion library identifies a new type of nuclear envelope membrane proteinCargo of kinesin identified as JIP scaffolding proteins and associated signaling moleculesA membrane protein complex mediates retro-translocation from the ER lumen into the cytosolFunction of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chainsRegulation by the ribosome of the GTPase of the signal-recognition particle during protein targetingA class of dynamin-like GTPases involved in the generation of the tubular ER networkEvolutionary conservation of components of the protein translocation complexSec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destructionA protein of the endoplasmic reticulum involved early in polypeptide translocationRecruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membraneStructural organization of the endoplasmic reticulum.E2-25K 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 membraneUnfolded cholera toxin is transferred to the ER membrane and released from protein disulfide isomerase upon oxidation by Ero1The beta subunit of the Sec61 complex facilitates cotranslational protein transport and interacts with the signal peptidase during translocationX-ray structure of a protein-conducting channelRibosome binding of a single copy of the SecY complex: implications for protein translocationSingle Copies of Sec61 and TRAP Associate with a Nontranslating Mammalian RibosomeStructure of a complex of the ATPase SecA and the protein-translocation channelConformational Flexibility and Peptide Interaction of the Translocation ATPase SecAStructure of a bacterial homologue of vitamin K epoxide reductaseStructures of the atlastin GTPase provide insight into homotypic fusion of endoplasmic reticulum membranesStructure of the SecY channel during initiation of protein translocationStructural Analysis and Optimization of the Covalent Association between SpyCatcher and a Peptide TagKey steps in ERAD of luminal ER proteins reconstituted with purified componentsDistinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins.The reticulon and DP1/Yop1p proteins form immobile oligomers in the tubular endoplasmic reticulum.Control of glycosylation of MHC class II-associated invariant chain by translocon-associated RAMP4.BiP acts as a molecular ratchet during posttranslational transport of prepro-alpha factor across the ER membrane.The ER-associated degradation component Der1p and its homolog Dfm1p are contained in complexes with distinct cofactors of the ATPase Cdc48pThe dynamin-like GTPase Sey1p mediates homotypic ER fusion in S. cerevisiaeProtein transport by purified yeast Sec complex and Kar2p without membranes.Autoubiquitination of the Hrd1 Ligase Triggers Protein Retrotranslocation in ERAD.A second trimeric complex containing homologs of the Sec61p complex functions in protein transport across the ER membrane of S. cerevisiaeThe AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol.Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p.Retrotranslocation of a misfolded luminal ER protein by the ubiquitin-ligase Hrd1p.Membrane proteins of the endoplasmic reticulum induce high-curvature tubules.A class of membrane proteins shaping the tubular endoplasmic reticulum.
P50
Q21092749-EC1946BA-92CE-4482-A0E2-2AADA0CFD302Q22010249-222723D0-D9B7-4959-94B3-8A5D22544619Q24290899-1EFBB02D-0729-4C57-9972-13D592D41C01Q24297732-9E65C150-FE56-4FCA-9E89-B3BB64FFBE39Q24307429-EABAB4DB-1F46-4AFF-BDF8-EAE2A4835C34Q24308691-72044664-E0E4-4A6A-A6D8-448FAD1A2C8FQ24322595-AA572B45-175E-4A41-9743-6F7F0FFC2DEAQ24323353-D162A35E-266D-4DF9-ADE1-485010AA46F5Q24324602-C2E830DC-776B-4190-95C7-BB0803882522Q24336350-D002D602-5451-44FA-BD23-22A5F955DEF4Q24336904-64781FA9-F838-4AB6-9C7B-CE273BADE4E9Q24538821-17C25438-CAD5-4F3E-8811-94B4B67294FCQ24554438-046674AD-D085-476E-84E9-1F6CA11CD5A4Q24568369-1649D953-B14A-4390-BADB-96F3C126ECCFQ24674605-EB4FDB70-8938-4E21-9FB6-C9DF08E3BD56Q24683072-0FAFC5B1-974F-42D6-A195-9D06C57E7DD5Q27642744-1A42EFC4-F7FD-43DC-A17A-06154AE66832Q27649425-F2984C0A-E55B-4A71-853D-EA74DBD62B8AQ27651087-04982729-A740-40ED-864E-5F69C95988B9Q27652526-31D09364-2C0D-4ECC-8E71-F97EB14E9A3CQ27657911-8A3DDE0E-C970-43F4-ADB6-19B27991B4FCQ27659264-4F01FCC6-9F90-41F6-8FA3-6BAEAC1D9B00Q27667148-F80FE100-6AB4-42BB-8553-FD6FB552AFBEQ27680440-7C007012-CADD-4764-AD3C-E89A323AC9EAQ27680463-132451A0-AEFA-470A-A0AF-E1386C74DC53Q27929992-4CA579AE-A756-44A6-9143-5ECC1E8C3342Q27931299-585661E7-8CF0-40C4-9FB4-E45A588B21B0Q27932262-D93DE0B6-5E7B-4650-80F6-31F4CF393487Q27932315-CE969641-A5E1-4EEE-A5AA-AFCDFD202EBBQ27932673-E8AB4574-4F00-4634-AFE8-CD2869F6384CQ27934285-7C71A236-F88E-4FA7-9A93-DB922B9A56BCQ27934843-2603DBC1-0117-411C-B44D-E04DD393BEC4Q27934892-EA28EDDD-6A91-4BB6-92C4-D6F98111E9DDQ27935283-9F93D415-CBE2-48F5-9165-CF8D58CFBD68Q27935591-0AF92370-B330-4943-92BE-9353C1739AC4Q27936514-42E7D2AD-2343-4675-AD66-9600A44F8CFDQ27937164-798A2CCE-4B48-4020-9D53-A39978B9905EQ27938951-8511E3AA-7D66-47EC-9ABB-48184CBBD502Q27939309-E42927E5-95D7-49AD-A692-47F1EBF460B8Q27940194-810EDD6C-0B27-45C6-84FE-ED0F4C327620
P50
description
Amerikaans bioloog
@nl
German biologist
@en
German biologist
@en-ca
German biologist
@en-gb
ahli biologi asal Amerika Serikat
@id
bitheolaí Gearmánach
@ga
biólogo alemán
@es
deutsch-amerikanischer Biochemiker
@de
немецкий биолог
@ru
عالم أحياء ألماني
@ar
name
Tom Rapoport
@aa
Tom Rapoport
@ace
Tom Rapoport
@af
Tom Rapoport
@ak
Tom Rapoport
@an
Tom Rapoport
@ang
Tom Rapoport
@ast
Tom Rapoport
@ay
Tom Rapoport
@az
Tom Rapoport
@bar
type
label
Tom Rapoport
@aa
Tom Rapoport
@ace
Tom Rapoport
@af
Tom Rapoport
@ak
Tom Rapoport
@an
Tom Rapoport
@ang
Tom Rapoport
@ast
Tom Rapoport
@ay
Tom Rapoport
@az
Tom Rapoport
@bar
altLabel
T A Rapoport
@en
T Rapoport
@en
T. A. Rapoport
@en
T. Rapoport
@en
Tom A Rapoport
@en
Tom A. Rapoport
@en
Tom Abraham Rapoport
@en
Рапопорт, Том
@ru
prefLabel
Tom Rapoport
@aa
Tom Rapoport
@ace
Tom Rapoport
@af
Tom Rapoport
@ak
Tom Rapoport
@an
Tom Rapoport
@ang
Tom Rapoport
@ast
Tom Rapoport
@ay
Tom Rapoport
@az
Tom Rapoport
@bar
P106
P166
P463
P214
P227
P244
P166
P19
P21
P213
0000 0000 3258 1752
P214
P227
P2381
P244
n2002135656