about
Protein quality control in the bacterial periplasmL25 functions as a conserved ribosomal docking site shared by nascent chain-associated complex and signal-recognition particle.Differential bacterial surface display of peptides by the transmembrane domain of OmpAPredominant membrane localization is an essential feature of the bacterial signal recognition particle receptor.The conformation of a nascent polypeptide inside the ribosome tunnel affects protein targeting and protein folding.Trigger factor binds to ribosome-signal-recognition particle (SRP) complexes and is excluded by binding of the SRP receptor.SecB is a bona fide generalized chaperone in Escherichia coliSignal recognition particle and SecA cooperate during export of secretory proteins with highly hydrophobic signal sequences.Mapping the pathways to staphylococcal pathogenesis by comparative secretomicsSecA Cotranslationally Interacts with Nascent Substrate Proteins In Vivo.Identification of nascent chain interaction sites on trigger factor.Sequence-specific interactions of nascent Escherichia coli polypeptides with trigger factor and signal recognition particle.Functional dissection of Escherichia coli trigger factor: unraveling the function of individual domains.TatB functions as an oligomeric binding site for folded Tat precursor proteins.Signal sequence-independent SRP-SR complex formation at the membrane suggests an alternative targeting pathway within the SRP cycle.Versatility of trigger factor interactions with ribosome-nascent chain complexes.An unusual signal peptide extension inhibits the binding of bacterial presecretory proteins to the signal recognition particle, trigger factor, and the SecYEG complex.Targeting and translocation of two lipoproteins in Escherichia coli via the SRP/Sec/YidC pathway.The way is the goal: how SecA transports proteins across the cytoplasmic membrane in bacteria.A derivative of lipid A is involved in signal recognition particle/SecYEG-dependent and -independent membrane integrations.Trigger factor binding to ribosomes with nascent peptide chains of varying lengths and sequences.Selective SecA association with signal sequences in ribosome-bound nascent chains: a potential role for SecA in ribosome targeting to the bacterial membrane.Ribosome-based protein folding systems are structurally divergent but functionally universal across biological kingdoms.Membrane targeting of a bacterial virulence factor harbouring an extended signal peptide.
P2860
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P2860
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
2003年學術文章
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2003年學術文章
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name
Ligand crowding at a nascent signal sequence.
@ast
Ligand crowding at a nascent signal sequence.
@en
type
label
Ligand crowding at a nascent signal sequence.
@ast
Ligand crowding at a nascent signal sequence.
@en
prefLabel
Ligand crowding at a nascent signal sequence.
@ast
Ligand crowding at a nascent signal sequence.
@en
P2093
P2860
P356
P1476
Ligand crowding at a nascent signal sequence.
@en
P2093
Gottfried Eisner
Hans-Georg Koch
Joseph Brunner
Konstanze Beck
Matthias Muller
P2860
P356
10.1083/JCB.200306069
P407
P577
2003-10-06T00:00:00Z