Signal sequence recognition in cotranslational translocation by protein components of the endoplasmic reticulum membrane.
about
Mammalian Sec61 is associated with Sec62 and Sec63Structure of the Sec61 channel opened by a signal sequenceTopological changes in the transmembrane domains of hepatitis C virus envelope glycoproteinsStructure of Monomeric Yeast and Mammalian Sec61 Complexes Interacting with the Translating RibosomeActivated GTPase movement on an RNA scaffold drives co-translational protein targetingSubstrate-specific translocational attenuation during ER stress defines a pre-emptive quality control pathway.Posttranslational protein translocation across the membrane of the endoplasmic reticulum.Roles of molecular chaperones in pancreatic secretion and their involvement in intestinal absorption.Defining the specificity of cotranslationally acting chaperones by systematic analysis of mRNAs associated with ribosome-nascent chain complexes.Cotranslational partitioning of nascent prion protein into multiple populations at the translocation channel.Topogenesis of membrane proteins: determinants and dynamics.The active 80S ribosome-Sec61 complex.Molecular mechanism of signal sequence orientation in the endoplasmic reticulum.Sec-dependent protein translocation across biological membranes: evolutionary conservation of an essential protein transport pathway (review).Substrate-specific function of the translocon-associated protein complex during translocation across the ER membraneGlycosylation can influence topogenesis of membrane proteins and reveals dynamic reorientation of nascent polypeptides within the translocon.SecYEG activates GTPases to drive the completion of cotranslational protein targeting.Sec61p contributes to signal sequence orientation according to the positive-inside rule.In vivo kinetics of protein targeting to the endoplasmic reticulum determined by site-specific phosphorylationCo-translational protein targeting to the bacterial membrane.A phaseolin domain involved directly in trimer assembly is a determinant for binding by the chaperone BiP.Signal peptide cleavage of a type I membrane protein, HCMV US11, is dependent on its membrane anchor.The translocation inhibitor CAM741 interferes with vascular cell adhesion molecule 1 signal peptide insertion at the translocon.Cholera toxin is exported from microsomes by the Sec61p complex.Effects of 'hydrophobic mismatch' on the location of transmembrane helices in the ER membrane.Co-translational, intraribosomal cleavage of polypeptides by the foot-and-mouth disease virus 2A peptide.Signal sequences initiate the pathway of maturation in the endoplasmic reticulum lumen.A substrate-specific inhibitor of protein translocation into the endoplasmic reticulum.An energy-dependent maturation step is required for release of the cystic fibrosis transmembrane conductance regulator from early endoplasmic reticulum biosynthetic machinery.Discovery of functional motifs in h-regions of trypanosome signal sequences.The Topogenic Contribution of Uncharged Amino Acids on Signal Sequence Orientation in the Endoplasmic Reticulum
P2860
Q22254037-64119D0F-872D-4FEA-BC4E-EB7AC3BAD5D0Q27330079-2D732773-D0D0-4D5F-9F95-D771B5DFF995Q27472616-22B3342E-D640-467C-8D00-AFD8CFBA2B75Q27658307-2A5E387C-5F8A-44E6-9A07-A810AC8DB9A8Q30530761-B3FFAA15-191B-4B31-9F47-F373C4211E7EQ33264756-17B30AD7-A1C0-4464-A943-8EEC8A078CE3Q33792998-7321485B-FB53-45DD-8FA5-FEF6939F75EDQ33924089-3E900ACA-E2E1-4630-806F-D8BE75E7AB0FQ33963685-D3C1CC44-53F1-4674-B0B1-F613921ED303Q34274103-7DB441A6-8CFD-4A9F-AC1A-C18C8B9CEB6AQ34353219-D3CC0810-BB47-4B22-A101-4FE9AD6429F8Q35133791-9E04B17A-6E60-478A-B157-BDD3F0F8A74DQ35160351-8834532A-D3D1-4373-8F6E-E9B7B7D18D04Q36224492-8FAA49E8-6FE2-40EA-AF1C-58A0141F21DEQ36325004-9B6F66D9-02E0-4770-BB0D-7A07BD555986Q36326048-7F3CEB77-31DC-4DF7-8A97-6ABF50613A55Q36618916-307026DD-A08D-4B5F-96EC-0BCE13AC33DEQ36782186-343BF938-1316-49CE-8B0C-E9ED1A5DF9E7Q36883283-21117655-69C5-4CDD-9BE0-964EDF23854BQ38186912-A927A380-2BEC-4F3B-89F7-AD74014C57C0Q38350038-1B026D7D-E11C-4FBC-9BB6-30B7266E627DQ39714879-1C77E69E-9784-4AF8-A036-6F11432519C7Q40242713-1912F467-D4F5-47B2-941F-3C23D9B0373CQ41861735-0F0AF9D3-5CEF-4B4A-B0A2-BB2ADC6E2532Q43610196-F07950EE-2F9A-4031-9546-AC9BBADC7901Q45729586-E8170987-C695-477A-AE4B-BA19F9DFAA60Q46274296-DAC69A3C-F4BA-4A3B-9FBE-A4FCBFD7C0EEQ46562004-1BC3C5B3-7809-4DD2-9C7A-B7DB277997DAQ46705910-A73C1492-A4CE-4A84-8749-B3135CF0C176Q46781255-6E6A85D1-38F1-496D-B4AE-912608719669Q56775266-830B99DF-C42F-4DD1-A2F0-857CAAEFDC0C
P2860
Signal sequence recognition in cotranslational translocation by protein components of the endoplasmic reticulum membrane.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
1998年學術文章
@zh
1998年學術文章
@zh-hant
name
Signal sequence recognition in ...... ndoplasmic reticulum membrane.
@ast
Signal sequence recognition in ...... ndoplasmic reticulum membrane.
@en
type
label
Signal sequence recognition in ...... ndoplasmic reticulum membrane.
@ast
Signal sequence recognition in ...... ndoplasmic reticulum membrane.
@en
prefLabel
Signal sequence recognition in ...... ndoplasmic reticulum membrane.
@ast
Signal sequence recognition in ...... ndoplasmic reticulum membrane.
@en
P2093
P2860
P356
P1476
Signal sequence recognition in ...... ndoplasmic reticulum membrane.
@en
P2093
P2860
P304
P356
10.1083/JCB.142.2.355
P407
P50
P577
1998-07-01T00:00:00Z