Functional signal peptides bind a soluble N-terminal fragment of SecA and inhibit its ATPase activity.
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Structural Basis for Signal-Sequence Recognition by the Translocase Motor SecA as Determined by NMRThe conformation of a signal peptide bound by Escherichia coli preprotein translocase SecAUse of synthetic signal sequences to explore the protein export machinery.Mapping of the signal peptide-binding domain of Escherichia coli SecA using Förster resonance energy transfer.Dimeric SecA couples the preprotein translocation in an asymmetric manner.Structure and function of the bacterial Sec translocon.A novel class of secA alleles that exert a signal-sequence-dependent effect on protein export in Escherichia coli.Probing the affinity of SecA for signal peptide in different environments.Selective photoaffinity labeling identifies the signal peptide binding domain on SecARole of a conserved glutamate residue in the Escherichia coli SecA ATPase mechanism.Conserved SecA Signal Peptide-Binding Site Revealed by Engineered Protein Chimeras and Förster Resonance Energy Transfer.Dissociation of the dimeric SecA ATPase during protein translocation across the bacterial membrane.An alternate mode of oligomerization for E. coli SecA.Using a low denaturant model to explore the conformational features of translocation-active SecA.Identification of the preprotein binding domain of SecA.Global co-ordination of protein translocation by the SecA IRA1 switch.Characterization of a polypeptide-binding site in the DEAD Motor of the SecA ATPase.Electron microscopic visualization of asymmetric precursor translocation intermediates: SecA functions as a dimer.Phospholipid-induced monomerization and signal-peptide-induced oligomerization of SecA.Functionally significant mobile regions of Escherichia coli SecA ATPase identified by NMR.Allosteric communication between signal peptides and the SecA protein DEAD motor ATPase domain.Disorder-order folding transitions underlie catalysis in the helicase motor of SecA
P2860
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P2860
Functional signal peptides bind a soluble N-terminal fragment of SecA and inhibit its ATPase activity.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
2001年學術文章
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2001年學術文章
@zh-hant
name
Functional signal peptides bin ...... d inhibit its ATPase activity.
@en
Functional signal peptides bin ...... d inhibit its ATPase activity.
@nl
type
label
Functional signal peptides bin ...... d inhibit its ATPase activity.
@en
Functional signal peptides bin ...... d inhibit its ATPase activity.
@nl
prefLabel
Functional signal peptides bin ...... d inhibit its ATPase activity.
@en
Functional signal peptides bin ...... d inhibit its ATPase activity.
@nl
P2093
P2860
P356
P1476
Functional signal peptides bin ...... d inhibit its ATPase activity.
@en
P2093
A R Sgrignoli
L M Gierasch
T L Triplett
P2860
P304
19648-19655
P356
10.1074/JBC.M100098200
P407
P577
2001-03-06T00:00:00Z