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Oxidative stress protein Oxr1 promotes V‐ATPase holoenzyme disassembly in catalytic activity‐independent manner

The EMBO journal, 2022-02, Vol.41 (3), p.e109360-n/a

2022

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Affinity Purification and Structural Features of the Yeast Vacuolar ATPase Vo Membrane Sector

The Journal of biological chemistry, 2015-11, Vol.290 (46), p.27959-27971

2015

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Breaking up and making up: The secret life of the vacuolar H+‐ATPase

Protein science, 2017-05, Vol.26 (5), p.896-909

2017

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The 3.5-Å CryoEM Structure of Nanodisc-Reconstituted Yeast Vacuolar ATPase Vo Proton Channel

Molecular cell, 2018-03, Vol.69 (6), p.993-1004.e3

2018

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Beyond the MUN domain, Munc13 controls priming and depriming of synaptic vesicles

Cell reports (Cambridge), 2024-05, Vol.43 (5), p.114026-114026, Article 114026

2024

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Structure of Dimeric F1F0-ATP Synthase

The Journal of biological chemistry, 2010-11, Vol.285 (47), p.36447-36455

2010

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The signaling lipid PI(3,5)P2 stabilizes V1–Vo sector interactions and activates the V-ATPase

Molecular biology of the cell, 2014-04, Vol.25 (8), p.1251-1262

2014

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Yeast V-ATPase Proteolipid Ring Acts as a Large-conductance Transmembrane Protein Pore

Scientific reports, 2016-04, Vol.6 (1), p.24774-24774, Article 24774

2016

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Functional Reconstitution of V-ATPase Proteolipid Ring into a Planar Lipid Membrane

Biophysical journal, 2017-02, Vol.112 (3), p.185a-185a

2017

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Nanomolar inhibition of SARS-CoV-2 infection by an unmodified peptide targeting the prehairpin intermediate of the spike protein

Proceedings of the National Academy of Sciences - PNAS, 2022-10, Vol.119 (40), p.e2210990119-e2210990119

2022

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Drug discovery targeting SARS-CoV-2 membrane fusion

Biophysical journal, 2023-02, Vol.122 (3), p.322a-322a

2023

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The signaling lipid PI(3,5)P 2 stabilizes V 1 –V o sector interactions and activates the V-ATPase

Molecular biology of the cell, 2014-04, Vol.25 (8), p.1251-1262

2014

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The 3.5-Å CryoEM Structure of Nanodisc-Reconstituted Yeast Vacuolar ATPase V o Proton Channel

Molecular cell, 2018-03, Vol.69 (6), p.993

2018

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The signaling lipid PI(3,5)P₂ stabilizes V₁-V(o) sector interactions and activates the V-ATPase

Molecular biology of the cell, 2014-04, Vol.25 (8), p.1251-1262

2014

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Oxidative stress protein Oxr1 promotes V‐ATPase holoenzyme disassembly in catalytic activity‐independent manner

Affinity Purification and Structural Features of the Yeast Vacuolar ATPase Vo Membrane Sector

Breaking up and making up: The secret life of the vacuolar H+‐ATPase

The 3.5-Å CryoEM Structure of Nanodisc-Reconstituted Yeast Vacuolar ATPase Vo Proton Channel

Beyond the MUN domain, Munc13 controls priming and depriming of synaptic vesicles

Structure of Dimeric F1F0-ATP Synthase

The signaling lipid PI(3,5)P2 stabilizes V1–Vo sector interactions and activates the V-ATPase

Yeast V-ATPase Proteolipid Ring Acts as a Large-conductance Transmembrane Protein Pore

Functional Reconstitution of V-ATPase Proteolipid Ring into a Planar Lipid Membrane

Nanomolar inhibition of SARS-CoV-2 infection by an unmodified peptide targeting the prehairpin intermediate of the spike protein

Drug discovery targeting SARS-CoV-2 membrane fusion

The signaling lipid PI(3,5)P 2 stabilizes V 1 –V o sector interactions and activates the V-ATPase

The 3.5-Å CryoEM Structure of Nanodisc-Reconstituted Yeast Vacuolar ATPase V o Proton Channel

The signaling lipid PI(3,5)P₂ stabilizes V₁-V(o) sector interactions and activates the V-ATPase

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