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引用本文的文献

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Ribosome-nascent Chain Interaction Regulates N-terminal Protein Modification.
J Mol Biol. 2022 May 15;434(9):167535. doi: 10.1016/j.jmb.2022.167535. Epub 2022 Mar 10.
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An intrinsic FRET sensor of protein-ligand interactions.
Org Biomol Chem. 2020 Jun 7;18(21):4079-4084. doi: 10.1039/d0ob00793e. Epub 2020 May 19.
3
Timing and specificity of cotranslational nascent protein modification in bacteria.
Proc Natl Acad Sci U S A. 2019 Nov 12;116(46):23050-23060. doi: 10.1073/pnas.1912264116. Epub 2019 Oct 30.
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A Chaperone Lid Ensures Efficient and Privileged Client Transfer during Tail-Anchored Protein Targeting.
Cell Rep. 2019 Jan 2;26(1):37-44.e7. doi: 10.1016/j.celrep.2018.12.035.
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In vitro Assays for Targeting and Insertion of Tail-Anchored Proteins Into the ER Membrane.
Curr Protoc Cell Biol. 2018 Dec;81(1):e63. doi: 10.1002/cpcb.63. Epub 2018 Sep 25.
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Two distinct sites of client protein interaction with the chaperone cpSRP43.
J Biol Chem. 2018 Jun 8;293(23):8861-8873. doi: 10.1074/jbc.RA118.002215. Epub 2018 Apr 18.
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A protean clamp guides membrane targeting of tail-anchored proteins.
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SecA mediates cotranslational targeting and translocation of an inner membrane protein.
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本文引用的文献

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Subcellular protein localization by using a genetically encoded fluorescent amino acid.
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Protein folding at the exit tunnel.
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Structural basis of signal-sequence recognition by the signal recognition particle.
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SecA interacts with ribosomes in order to facilitate posttranslational translocation in bacteria.
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New scenarios of protein folding can occur on the ribosome.
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Sequential checkpoints govern substrate selection during cotranslational protein targeting.
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Recognition of a signal peptide by the signal recognition particle.
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An enhanced system for unnatural amino acid mutagenesis in E. coli.
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Probing side-chain dynamics of a ribosome-bound nascent chain using methyl NMR spectroscopy.
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