The plug domain of yeast Sec61p is important for efficient protein translocation, but is not essential for cell viability.
about
SecA, a remarkable nanomachineThe SWISS-MODEL Repository and associated resourcesLateral opening of a translocon upon entry of protein suggests the mechanism of insertion into membranesHeterozygous Loss-of-Function SEC61A1 Mutations Cause Autosomal-Dominant Tubulo-Interstitial and Glomerulocystic Kidney Disease with AnemiaAutomated protein structure modeling with SWISS-MODEL Workspace and the Protein Model Portal.Mutations in the CYP1B1 gene may contribute to juvenile-onset open-angle glaucomaHydrophobically stabilized open state for the lateral gate of the Sec translocon.The hydrophobic core of the Sec61 translocon defines the hydrophobicity threshold for membrane integration.A novel missense mutation in the connexin30 causes nonsyndromic hearing loss.Translocation of proteins through the Sec61 and SecYEG channelsStructural and functional profiling of the lateral gate of the Sec61 transloconMembrane protein insertion at the endoplasmic reticulum.Stability and function of the Sec61 translocation complex depends on the Sss1p tail-anchor sequenceDecatransin, a new natural product inhibiting protein translocation at the Sec61/SecYEG translocon.The bacterial Sec-translocase: structure and mechanism.Direct simulation of early-stage Sec-facilitated protein translocationProtein translocation across the rough endoplasmic reticulum.The roles of pore ring and plug in the SecY protein-conducting channel.Functional asymmetry within the Sec61p translocon.Secretion by numbers: Protein traffic in prokaryotes.The Sec translocon mediated protein transport in prokaryotes and eukaryotes.Conformational dynamics of the plug domain of the SecYEG protein-conducting channel.The bacterial translocon SecYEG opens upon ribosome binding.Immobilization of the plug domain inside the SecY channel allows unrestricted protein translocation.Visualization of distinct entities of the SecYEG translocon during translocation and integration of bacterial proteinsThe SecY complex forms a channel capable of ionic discrimination.Synthetic peptides identify a second periplasmic site for the plug of the SecYEG protein translocation complex.Protein transport across the endoplasmic reticulum membrane.Ion conductivity of the bacterial translocation channel SecYEG engaged in translocation.Protein translocation through the Sec61/SecY channel.Endoplasmic Reticulum Transport of Glutathione by Sec61 Is Regulated by Ero1 and Bip.Escherichia coli membranes depleted of SecYEG elicit SecA-dependent ion-channel activity but lose signal peptide specificity.The active protein-conducting channel of Escherichia coli contains an apolar patch.Deregulation of the SecYEG translocation channel upon removal of the plug domain.Mutations in the Sec61p Channel Affecting Signal Sequence Recognition and Membrane Protein Topology
P2860
Q24631210-9F7E3A8E-6078-4107-8483-6B1F437AA839Q24656047-81621C8F-878E-4063-8B60-4099B912373DQ27664605-327CA19C-6025-40CE-96EB-E4207D11E006Q28118506-72653CEE-300B-4235-B8FA-31F8081EC119Q30412875-745D88B0-E694-4AED-925B-EE27CBAFDF1DQ30420204-2FD1A173-AF36-4193-B5E4-5AED5E98377AQ33777810-33DC7795-2AEA-4E62-BAE2-F3DB8D0A18DEQ33848740-6ADD65D7-158E-4661-B48B-9CFD0C9F62FEQ33952479-4CDFE10A-5BBF-4172-9BDC-15BD0D43FB82Q34046866-798FF0FE-C2D0-4327-9771-B265CBFCD2E0Q34076055-05E42C98-2482-494F-B3D6-327933E592B9Q34179638-5008BF58-44C1-49FA-932D-69FA9323E524Q34984631-D62168FC-CB64-4313-9B9B-38B5EB8D8AAEQ35178294-0B5DFB6F-2283-419B-9FE1-766F941EAB30Q35814696-9B3D07E7-3FA9-4B00-9A8A-BE8B60123619Q36200511-D38228DA-FC77-4E7D-8ACD-FE9007C1B9E4Q36555178-74203C59-5195-4F6E-A1FB-5E89B095A45AQ36980008-31B0451A-0682-4E68-A467-0C2778FA9853Q37340628-10ED0632-805A-4BF9-9B8B-ADE53C1AEDCFQ37416226-5D1B2CCE-3C95-4CDF-B39F-5FD798051EF3Q38206834-73A94791-8108-462B-AFF3-8B534A761D8CQ39935945-FF6B8D50-3AFF-4DEB-BDED-D064CB05D8BAQ41786954-8C5BB8D1-1BA7-44CE-BC8A-881937DE7C0DQ41936753-0C16F148-62FF-44C3-9A20-7BB3BB3A4965Q41960890-62B94540-F633-47C2-AA26-44235FE42714Q42268573-ED29C2EC-ADA2-43E9-8431-C893274BF8E0Q42606260-4EA4968E-786C-47D3-B15F-D503B40C1C0BQ42663824-98A127A6-02E9-4CEF-8F4B-5668F084055CQ42850306-6F41889D-F4E3-4B44-9234-08BAB50C9E0DQ44220424-288268E5-A80B-4D3F-9BE2-4CBFE8299E6EQ47790181-B8F621B5-9A26-4441-AD32-268CC5494D81Q48642879-B874A1FD-46CB-4C47-845C-69544661CC2EQ54436247-EE165534-5FC5-413C-9707-9218CE4D248FQ54452284-A48186EB-A3BF-46F2-85C5-84DF563E4B02Q56775244-1C71505F-5761-4FAD-A47C-605534B83580
P2860
The plug domain of yeast Sec61p is important for efficient protein translocation, but is not essential for cell viability.
description
2006 nî lūn-bûn
@nan
2006 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
The plug domain of yeast Sec61 ...... essential for cell viability.
@ast
The plug domain of yeast Sec61 ...... essential for cell viability.
@en
type
label
The plug domain of yeast Sec61 ...... essential for cell viability.
@ast
The plug domain of yeast Sec61 ...... essential for cell viability.
@en
prefLabel
The plug domain of yeast Sec61 ...... essential for cell viability.
@ast
The plug domain of yeast Sec61 ...... essential for cell viability.
@en
P2860
P50
P356
P1476
The plug domain of yeast Sec61 ...... essential for cell viability.
@en
P2093
Tina Junne
P2860
P304
P356
10.1091/MBC.E06-03-0200
P577
2006-07-05T00:00:00Z