Vladislav Belyy
Biochemistry, Genetics and Molecular Biology · The Ohio State University
Publications
46
Citations
1,503
Est. group size
~2
Recurring co-author estimate
Active years
18
Publishing since 2009
Vladislav Belyy's research focuses on how cells detect and respond to stress in the endoplasmic reticulum, a compartment involved in protein folding, with particular attention to a key sensor protein called IRE1. His lab uses live-cell imaging, optogenetics (light-based control of proteins), and single-molecule techniques to study how proteins like IRE1 and other membrane-associated machines assemble and change behavior in real time. The work combines biophysics and cell biology approaches to understand molecular mechanisms of cellular stress responses and protein quality control.
Publication output has been relatively steady with some fluctuation, dipping in 2018 and 2023, but showing an uptick again in 2025-2026 based on recent submissions.
Generated by claude-sonnet-5 from public bibliographic data · Jul 20, 2026
- BPS2026 – Investigating activity of Eph receptors with direct control over oligomerization
Biophysical Journal · 2026
- BPS2026 – Dissecting the activation mechanism of the bi-functional kinase/RNase IRE1 with orthogonal control over oligomerization and phosphorylation
Biophysical Journal · 2026
- BPS2026 – Intricate regulation of RNA cleavage and splicing by the endoribonuclease IRE1
Biophysical Journal · 2026
- Dissecting ER stress signaling with live-cell single-molecule imaging and optogenetics
Biophysical Journal · 2024
- Optogenetic platform for dissecting IRE1's enzymatic mechanism
Biophysical Journal · 2024
- Endogenous tagging of IRE1 in U-2 OS cells
BIO-PROTOCOL · 2023
- Endoplasmic reticulum stress activates human IRE1α through reversible assembly of inactive dimers into small oligomers
eLife · 2022
- Conserved structural elements specialize ATAD1 as a membrane protein extraction machine
eLife · 2022
- Author response: Endoplasmic reticulum stress activates human IRE1α through reversible assembly of inactive dimers into small oligomers
2022
- Author response: Conserved structural elements specialize ATAD1 as a membrane protein extraction machine
2022
- Processed and additional data for our publication titled "Endoplasmic reticulum stress activates human IRE1α through reversible assembly of inactive dimers into small oligomers"
Zenodo (CERN European Organization for Nuclear Research) · 2022
- Processed and additional data for our publication titled "Endoplasmic reticulum stress activates human IRE1α through reversible assembly of inactive dimers into small oligomers"
Zenodo (CERN European Organization for Nuclear Research) · 2022
- Endoplasmic reticulum stress activates human IRE1α through reversible assembly of inactive dimers into small oligomers
bioRxiv (Cold Spring Harbor Laboratory) · 2021
- Conserved structural elements specialize ATAD1 as a membrane protein extraction machine
bioRxiv (Cold Spring Harbor Laboratory) · 2021
- Processed and additional data for our publication titled "Endoplasmic reticulum stress activates human IRE1α through reversible assembly of inactive dimers into small oligomers"
Zenodo (CERN European Organization for Nuclear Research) · 2021
- Biophysical Journal×7
- Zenodo (CERN European Organization for Nuclear Research)×5
- bioRxiv (Cold Spring Harbor Laboratory)×4
- eLife×2
- Science×1
- Shuliang Chen
Biochemistry, Genetics and Molecular Biology · The Ohio State University
- Sarah O’Keefe
Biochemistry, Genetics and Molecular Biology · Indiana University
- Avery M. Runnebohm
Biochemistry, Genetics and Molecular Biology · Indiana University
- Jagannath Misra
Biochemistry, Genetics and Molecular Biology · Indiana University
- Bei Liu
Biochemistry, Genetics and Molecular Biology · The Ohio State University
This profile was generated automatically from public scholarly data (OpenAlex). Group size and activity levels are estimates derived from co-authorship patterns.
Last updated Jul 19, 2026.
Claim or correct this profile