about
SecA, a remarkable nanomachineThe Sec-dependent pathwayADP-dependent conformational changes distinguish Mycobacterium tuberculosis SecA2 from SecA1Using nanoelectrospray ion mobility spectrometry (GEMMA) to determine the size and relative molecular mass of proteins and protein assemblies: a comparison with MALLS and QELS.Analysis of SecA dimerization in solution.Development and application of a cellular, gain-of-signal, bioluminescent reporter screen for inhibitors of type II secretion in Pseudomonas aeruginosa and Burkholderia pseudomallei.The sortase A substrates FnbpA, FnbpB, ClfA and ClfB antagonize colony spreading of Staphylococcus aureus.Energetics of SecA dimerization.The use of analytical sedimentation velocity to extract thermodynamic linkage.Dynamic distribution of the SecA and SecY translocase subunits and septal localization of the HtrA surface chaperone/protease during Streptococcus pneumoniae D39 cell division.In Vitro Interaction of the Housekeeping SecA1 with the Accessory SecA2 Protein of Mycobacterium tuberculosis.Functional implementation of the posttranslational SecB-SecA protein-targeting pathway in Bacillus subtilis.Position-dependent effects of polylysine on Sec protein transportSecretion genes as determinants of Bacillus anthracis chain length.Emerging themes in SecA2-mediated protein export.Energetic cost of protein import across the envelope membranes of chloroplasts.Protein export by the mycobacterial SecA2 system is determined by the preprotein mature domain.Glycolipozyme MPIase is essential for topology inversion of SecG during preprotein translocationDefining the solution state dimer structure of Escherichia coli SecA using Förster resonance energy transferCryo-electron microscopic structure of SecA protein bound to the 70S ribosome.Protein export systems of Mycobacterium tuberculosis: novel targets for drug development?Protein Secretion Systems in Pseudomonas aeruginosa: An Essay on Diversity, Evolution, and Function.Breaking on through to the other side: protein export through the bacterial Sec system.Multiple SecA molecules drive protein translocation across a single translocon with SecG inversion.Identification of small-molecule inhibitors against SecA by structure-based virtual ligand screening.An alternate mode of oligomerization for E. coli SecA.Using a low denaturant model to explore the conformational features of translocation-active SecA.The variable subdomain of Escherichia coli SecA functions to regulate SecA ATPase activity and ADP release.SecA functions in vivo as a discrete anti-parallel dimer to promote protein transport.Novel translocation intermediate allows re-evaluation of roles of ATP, proton motive force and SecG at the late stage of preprotein translocation.Large conformational changes of a highly dynamic pre-protein binding domain in SecA
P2860
Q24631210-37A2B4AF-E017-490C-802D-FFB7648F6D30Q27010633-80262370-D9FB-472C-9961-BE5B309D637EQ28660158-13DE4585-FEA6-41F3-8DD5-C3EEE4DB17D3Q30398578-3CE60394-2EDC-4E15-8F8E-14F085A35E63Q33649362-E1B4EBD4-4C68-4302-A01A-55CB28455A29Q33908076-2FE129FD-298D-4965-BCF0-C655573E2FAFQ34412649-D38DDEEE-E0C9-4A91-ADB1-70ADE7CCF537Q34761920-ECACF990-0F65-4DE0-8BE3-67A220E21866Q35196339-DCB2411A-2417-43AF-94FA-F4CE2AF6D32AQ35280903-9C229B1A-764F-4607-98E9-D38DB2CD8AF1Q35654435-88E21099-80BE-4C1F-AEC2-34D741FD7505Q35688908-508083CD-2036-4B46-84D9-A1B3B4838896Q35921553-5552DF96-C3B2-4550-A437-3E376D6ECACEQ36156338-5F513000-CA9B-4D55-983C-ED680FC30D61Q36206572-01172350-8DE8-4152-8938-A1CC7346DB5CQ36545433-13A545C8-F4C2-470C-AAFC-3B17454E7D7BQ36581196-C5C10E40-168C-494F-A1FD-A6BEFB5C6133Q36932458-D0DB86FD-DE29-490A-BFE4-5DFEC7806604Q37029669-67BC89E3-5F1E-48FC-BC8D-FF029D6FFB7EQ37622672-922145FE-3BFF-4528-9B39-9E7548F2E19EQ37809066-A08FAE4A-FD44-43AC-AC06-EDB828E63F86Q37910755-E1BCFB37-9503-4FA2-9ADF-54B06C4F4CBEQ38065265-7434AE26-A986-4FCD-886E-DC51F642CA11Q40082687-C1610CFC-7C74-41B3-B79C-2CE53000BEC0Q41216402-AEA216B1-FCDF-44F3-8632-C23FBAE08A9BQ41718064-7F19EEFE-E7D6-44A9-97C7-2E7E67B6D33CQ41808503-C5822F78-5177-45BF-B220-6B3BEE7AC337Q42152267-976195E5-CDB8-4D5D-92E3-5325D72AF660Q50307534-CABDABF0-C26A-4D52-81B3-39E0265BB4C5Q51344912-4EDCBFEE-E792-4414-99D9-2B1FA596879AQ57118357-707764EB-E283-4BF9-9AFE-475B1A572267
P2860
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 23 April 2010
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
SecA: a tale of two protomers.
@en
SecA: a tale of two protomers.
@nl
type
label
SecA: a tale of two protomers.
@en
SecA: a tale of two protomers.
@nl
prefLabel
SecA: a tale of two protomers.
@en
SecA: a tale of two protomers.
@nl
P1476
SecA: a tale of two protomers.
@en
P304
P356
10.1111/J.1365-2958.2010.07176.X
P407
P577
2010-04-23T00:00:00Z