about
Protein translocation: what's the problem?Channel crossing: how are proteins shipped across the bacterial plasma membrane?Unlocking the Bacterial SecY Translocon.Composition and Activity of the Non-canonical Gram-positive SecY2 Complex.Two-way communication between SecY and SecA suggests a Brownian ratchet mechanism for protein translocation.Dynamic action of the Sec machinery during initiation, protein translocation and termination.Dynamic action of the Sec machinery during initiation, protein translocation and termination revealed by single molecule fluorescenceATP-induced asymmetric pre-protein folding: a driver of protein translocation?Specific cardiolipin-SecY interactions are required for proton-motive-force stimulation of protein secretionATP-induced asymmetric pre-protein folding as a driver of protein translocation through the Sec machinerySpecific cardiolipin-SecY interactions are required for proton-motive force stimulation of protein secretionA lipid gating mechanism for the channel-forming O antigen ABC transporterHDX-MS reveals nucleotide-dependent, anti-correlated opening and closure of SecA and SecY channels of the bacterial transloconStructural basis of proton-coupled potassium transport in the KUP familyDefining how multiple lipid species interact with inward rectifier potassium (Kir2) channelsStructural basis for substrate specificity and regulation of nucleotide sugar transporters in the lipid bilayerLipid Interactions of a Ciliary Membrane TRP Channel: Simulation and Structural Studies of Polycystin-2Structure and Dynamics of the Central Lipid Pool and Proteins of the Bacterial Holo-TransloconThe energetics of protein-lipid interactions as viewed by molecular simulationsA Mass-Spectrometry-Based Approach to Distinguish Annular and Specific Lipid Binding to Membrane ProteinsA bipartite structural organization defines the SERINC family of HIV-1 restriction factorsInsights into Membrane Protein-Lipid Interactions from Free Energy CalculationsThe structural basis of lipid scrambling and inactivation in the endoplasmic reticulum scramblase TMEM16K
P50
Q26747205-32E25F19-AA13-4FE3-ACBF-77FE0AD637D2Q26786998-2347DA3E-0A98-427F-95F6-B656DEBF7CE5Q39923654-F7628539-686D-4A50-B338-AFC895F6D5D9Q41551854-A7872352-DAED-402C-8DD8-CADDCDCA093AQ42576947-4546BB7C-C0FE-4AD0-B355-6ECC005A243AQ55513394-E7F2A0BC-33E2-4F11-87A5-3790C69FB5D0Q56422877-6FA96645-51DC-47FF-B9FD-2F3D5D6F9EB6Q57840318-01A15FA0-9458-49BE-8B70-59CA8B934559Q57840323-E4A0F874-99EC-4B7B-AA64-AA37D4BB4A2EQ61451642-2B512B52-0879-4D75-96E3-2DBFCF655A35Q61928097-C07F48DB-03DF-40A7-88A9-7D99C21A2261Q63976765-52174611-7F4B-423A-B91E-1380F143ED8CQ83231318-B3475893-7B58-4AFC-9F39-E4A1C061D6D2Q89474567-240A26B6-33B4-44EA-B5D2-E579F98A5DDDQ90660490-66442EF5-A76B-447E-8054-38010BCE0E4AQ90663058-21A8205C-F0E6-4D61-9B75-F715553C9BACQ91731845-E78D48A2-353D-4DDC-A07F-2AF02346FBC9Q91748316-1A6C22A2-2FEE-4161-926F-A6F81C124E97Q92224343-FA711947-E663-45B5-AEBC-1F95971CB70DQ92316340-0275480E-E894-447E-9381-6A24CC333865Q92453927-176D8F18-E271-4034-8070-0CBAA01DA049Q93054851-C681DD28-0581-4BB8-852D-64EC8EFE2740Q93063701-1B770D13-C225-4065-81CD-530C491D1A79
P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Robin A Corey
@ast
Robin A Corey
@en
Robin A Corey
@es
Robin A Corey
@sl
type
label
Robin A Corey
@ast
Robin A Corey
@en
Robin A Corey
@es
Robin A Corey
@sl
prefLabel
Robin A Corey
@ast
Robin A Corey
@en
Robin A Corey
@es
Robin A Corey
@sl
P106
P21
P31
P496
0000-0003-1820-7993