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Substrate relay in an Hsp70‐cochaperone cascade safeguards tail‐anchored membrane protein targeting

The EMBO journal, 2018-08, Vol.37 (16), p.n/a

2018

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Mechanisms of Tail-Anchored Membrane Protein Targeting and Insertion

Annual review of cell and developmental biology, 2017-10, Vol.33 (1), p.417-438

2017

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Role of Hsp70 in Post-Translational Protein Targeting: Tail-Anchored Membrane Proteins and Beyond

International journal of molecular sciences, 2023-01, Vol.24 (2), p.1170

Shan, Shu-Ou

2023

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Signal recognition particle: an essential protein-targeting machine

Annual review of biochemistry, 2013-01, Vol.82 (1), p.693-721

2013

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A ribosome-associated chaperone enables substrate triage in a cotranslational protein targeting complex

Nature communications, 2020-11, Vol.11 (1), p.5840-5840, Article 5840

2020

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Mechanism of signal sequence handover from NAC to SRP on ribosomes during ER-protein targeting

Science (American Association for the Advancement of Science), 2022-02, Vol.375 (6583), p.839-844

2022

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Ribosome profiling reveals multiple roles of SecA in cotranslational protein export

Nature communications, 2022-06, Vol.13 (1), p.3393-3393, Article 3393

2022

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An ankyrin repeat chaperone targets toxic oligomers during amyloidogenesis

Protein science, 2023-08, Vol.32 (8), p.e4728-n/a

2023

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Fidelity of Cotranslational Protein Targeting by the Signal Recognition Particle

Annual review of biophysics, 2014-01, Vol.43 (1), p.381-408

2014

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Structure of a prehandover mammalian ribosomal SRP·SRP receptor targeting complex

Science (American Association for the Advancement of Science), 2018-04, Vol.360 (6386), p.323-327

2018

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Fidelity of Cotranslational Protein Targeting to the Endoplasmic Reticulum

International journal of molecular sciences, 2021-12, Vol.23 (1), p.281

2021

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Multiple selection filters ensure accurate tail-anchored membrane protein targeting

eLife, 2016-12, Vol.5

2016

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The molecular mechanism of cotranslational membrane protein recognition and targeting by SecA

Nature structural & molecular biology, 2019-10, Vol.26 (10), p.919-929

2019

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Dynamic stability of Sgt2 enables selective and privileged client handover in a chaperone triad

Nature communications, 2024-01, Vol.15 (1), p.134-16, Article 134

2024

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Chloroplast SRP43 autonomously protects chlorophyll biosynthesis proteins against heat shock

Nature plants, 2021-10, Vol.7 (10), p.1420-1432

2021

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Molecular Mechanism of Co‐translational Protein Targeting by the Signal Recognition Particle

Traffic (Copenhagen, Denmark), 2011-05, Vol.12 (5), p.535-542

2011

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Structure of the quaternary complex between SRP, SR, and translocon bound to the translating ribosome

Nature communications, 2017-05, Vol.8 (1), p.15470-15470, Article 15470

2017

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Molecular mechanism of cargo recognition and handover by the mammalian signal recognition particle

Cell reports (Cambridge), 2021-07, Vol.36 (2), p.109350-109350, Article 109350

2021

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Cand1 Promotes Assembly of New SCF Complexes through Dynamic Exchange of F Box Proteins

Cell, 2013-03, Vol.153 (1), p.206-215

2013

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Crystal Structure of the Signal Recognition Particle in Complex with Its Receptor

Science (American Association for the Advancement of Science), 2011-02, Vol.331 (6019), p.881-886

2011

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Guiding tail-anchored membrane proteins to the endoplasmic reticulum in a chaperone cascade

The Journal of biological chemistry, 2019-11, Vol.294 (45), p.16577-16586

Shan, Shu-ou

2019

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Sequential Checkpoints Govern Substrate Selection During Cotranslational Protein Targeting

Science (American Association for the Advancement of Science), 2010-05, Vol.328 (5979), p.757-760

2010

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Regulation by a chaperone improves substrate selectivity during cotranslational protein targeting

Proceedings of the National Academy of Sciences - PNAS, 2015-06, Vol.112 (25), p.E3169-E3178

2015

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The Mitochondrial Fission Receptor MiD51 Requires ADP as a Cofactor

Structure (London), 2014-03, Vol.22 (3), p.367-377

2014

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Multiple Conformational Switches in a GTPase Complex Control Co-Translational Protein Targeting

Proceedings of the National Academy of Sciences - PNAS, 2009-02, Vol.106 (6), p.1754-1759

2009

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Substrate relay in an Hsp70‐cochaperone cascade safeguards tail‐anchored membrane protein targeting

Mechanisms of Tail-Anchored Membrane Protein Targeting and Insertion

Role of Hsp70 in Post-Translational Protein Targeting: Tail-Anchored Membrane Proteins and Beyond

Signal recognition particle: an essential protein-targeting machine

A ribosome-associated chaperone enables substrate triage in a cotranslational protein targeting complex

Mechanism of signal sequence handover from NAC to SRP on ribosomes during ER-protein targeting

Ribosome profiling reveals multiple roles of SecA in cotranslational protein export

An ankyrin repeat chaperone targets toxic oligomers during amyloidogenesis

Fidelity of Cotranslational Protein Targeting by the Signal Recognition Particle

Structure of a prehandover mammalian ribosomal SRP·SRP receptor targeting complex

Fidelity of Cotranslational Protein Targeting to the Endoplasmic Reticulum

Multiple selection filters ensure accurate tail-anchored membrane protein targeting

The molecular mechanism of cotranslational membrane protein recognition and targeting by SecA

Dynamic stability of Sgt2 enables selective and privileged client handover in a chaperone triad

Chloroplast SRP43 autonomously protects chlorophyll biosynthesis proteins against heat shock

Molecular Mechanism of Co‐translational Protein Targeting by the Signal Recognition Particle

Structure of the quaternary complex between SRP, SR, and translocon bound to the translating ribosome

Molecular mechanism of cargo recognition and handover by the mammalian signal recognition particle

Cand1 Promotes Assembly of New SCF Complexes through Dynamic Exchange of F Box Proteins

Crystal Structure of the Signal Recognition Particle in Complex with Its Receptor

Guiding tail-anchored membrane proteins to the endoplasmic reticulum in a chaperone cascade

Sequential Checkpoints Govern Substrate Selection During Cotranslational Protein Targeting

Regulation by a chaperone improves substrate selectivity during cotranslational protein targeting

The Mitochondrial Fission Receptor MiD51 Requires ADP as a Cofactor

Multiple Conformational Switches in a GTPase Complex Control Co-Translational Protein Targeting

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