Ring-like pore structures of SecA: implication for bacterial protein-conducting channels.
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SecA, a remarkable nanomachinePhospholipids induce conformational changes of SecA to form membrane-specific domains: AFM structures and implication on protein-conducting channelsSecA alone can promote protein translocation and ion channel activity: SecYEG increases efficiency and signal peptide specificityLoss of outer membrane proteins without inhibition of lipid export in an Escherichia coli YaeT mutant.Uptake of CdSe and CdSe/ZnS quantum dots into bacteria via purine-dependent mechanisms.Dimeric SecA couples the preprotein translocation in an asymmetric manner.Electrophysiological studies in Xenopus oocytes for the opening of Escherichia coli SecA-dependent protein-conducting channels.SecA: a potential antimicrobial target.Biological cryo-electron microscopy in ChinaEvaluation of small molecule SecA inhibitors against methicillin-resistant Staphylococcus aureus.Dissecting structures and functions of SecA-only protein-conducting channels: ATPase, pore structure, ion channel activity, protein translocation, and interaction with SecYEG/SecDF•YajC.Design, Synthesis and Evaluation of Triazole-Pyrimidine Analogues as SecA Inhibitors.Synthesis and antimicrobial activity of silver-doped hydroxyapatite nanoparticles.Bowl-shaped oligomeric structures on membranes as DegP's new functional forms in protein quality control.The active ring-like structure of SecA revealed by electron crystallography: conformational change upon interaction with SecB.Breaking on through to the other side: protein export through the bacterial Sec system.Using Chemical Probes to Assess the Feasibility of Targeting SecA for Developing Antimicrobial Agents against Gram-Negative Bacteria.Binding, activation and dissociation of the dimeric SecA ATPase at the dimeric SecYEG translocase.SecAAA trimer is fully functional as SecAA dimer in the membrane: existence of higher oligomers?Fluorescent nanocrystal quantum dots as medical diagnostic tools.Translocated intimin receptor and its chaperone interact with ATPase of the type III secretion apparatus of enteropathogenic Escherichia coli.Glyconanomaterials for Combating Bacterial Infections.Full-length Escherichia coli SecA dimerizes in a closed conformation in solution as determined by cryo-electron microscopy.Mechanisms of Rose Bengal inhibition on SecA ATPase and ion channel activities.Additional in vitro and in vivo evidence for SecA functioning as dimers in the membrane: dissociation into monomers is not essential for protein translocation in Escherichia coli.Sites of interaction between SecA and the chaperone SecB, two proteins involved in export.Prediction of lipid-binding regions in cytoplasmic and extracellular loops of membrane proteins as exemplified by protein translocation membrane proteins.Insights into the structure of human cytomegalovirus large terminase subunit pUL56.Penetration into Membrane of Amino-terminal Region of SecA when Associated with SecYEG in Active Complexes.The SecA protein deeply penetrates into the SecYEG channel during insertion, contacting most channel transmembrane helices and periplasmic regions.Escherichia coli membranes depleted of SecYEG elicit SecA-dependent ion-channel activity but lose signal peptide specificity.Electron microscopic visualization of asymmetric precursor translocation intermediates: SecA functions as a dimer.
P2860
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P2860
Ring-like pore structures of SecA: implication for bacterial protein-conducting channels.
description
2003 nî lūn-bûn
@nan
2003 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի մարտին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Ring-like pore structures of SecA: implication for bacterial protein-conducting channels.
@ast
Ring-like pore structures of SecA: implication for bacterial protein-conducting channels.
@en
Ring-like pore structures of SecA: implication for bacterial protein-conducting channels.
@nl
type
label
Ring-like pore structures of SecA: implication for bacterial protein-conducting channels.
@ast
Ring-like pore structures of SecA: implication for bacterial protein-conducting channels.
@en
Ring-like pore structures of SecA: implication for bacterial protein-conducting channels.
@nl
prefLabel
Ring-like pore structures of SecA: implication for bacterial protein-conducting channels.
@ast
Ring-like pore structures of SecA: implication for bacterial protein-conducting channels.
@en
Ring-like pore structures of SecA: implication for bacterial protein-conducting channels.
@nl
P2093
P2860
P356
P1476
Ring-like pore structures of SecA: implication for bacterial protein-conducting channels.
@en
P2093
Hong-Wei Wang
Hsiuchin Yang
Ming-Xing Duan
Phang C Tai
Sen-Fang Sui
Xianchuan Chen
P2860
P304
P356
10.1073/PNAS.0737415100
P407
P577
2003-03-17T00:00:00Z