Mechanisms of ribosome stalling by SecM at multiple elongation steps.
about
Ribosome rearrangements at the onset of translational bypassingThe force-sensing peptide VemP employs extreme compaction and secondary structure formation to induce ribosomal stalling.Translocation as continuous movement through the ribosome.Molecular insights into protein synthesis with proline residues.SecA mediates cotranslational targeting and translocation of an inner membrane protein.Identification and characterization of a translation arrest motif in VemP by systematic mutational analysis.Aminoglycoside interactions and impacts on the eukaryotic ribosome.
P2860
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P2860
Mechanisms of ribosome stalling by SecM at multiple elongation steps.
description
2015 nî lūn-bûn
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2015年の論文
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2015年論文
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2015年論文
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2015年論文
@zh-hk
2015年論文
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2015年論文
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2015年论文
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2015年论文
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2015年论文
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name
Mechanisms of ribosome stalling by SecM at multiple elongation steps.
@ast
Mechanisms of ribosome stalling by SecM at multiple elongation steps.
@en
type
label
Mechanisms of ribosome stalling by SecM at multiple elongation steps.
@ast
Mechanisms of ribosome stalling by SecM at multiple elongation steps.
@en
prefLabel
Mechanisms of ribosome stalling by SecM at multiple elongation steps.
@ast
Mechanisms of ribosome stalling by SecM at multiple elongation steps.
@en
P2093
P2860
P356
P1433
P1476
Mechanisms of ribosome stalling by SecM at multiple elongation steps.
@en
P2093
P2860
P356
10.7554/ELIFE.09684
P407
P577
2015-12-14T00:00:00Z