Single molecule mass photometry reveals the dynamic oligomerization of human and plant peroxiredoxins

Single molecule mass photometry reveals the dynamic oligomerization of human and plant peroxiredoxins

Protein oligomerization is central to biological function and regulation, yet its experimental quantification and measurement of dynamic transitions in solution remain challenging. Here, we show that single molecule mass photometry quantifies affinity and polydispersity of heterogeneous protein comp...

Descrizione completa

Dettagli Bibliografici
Autori principali:	Liebthal, M, Kushwah, MS, Kukura, P, Dietz, K-J
Natura:	Journal article
Lingua:	English
Pubblicazione:	Cell Press 2021

Documenti analoghi

Single molecule mass photometry reveals the dynamic oligomerization of human and plant peroxiredoxins
di: Michael Liebthal, et al.
Pubblicazione: (2021-11-01)

Single molecule mass photometry of nucleic acids
di: Li, Y, et al.
Pubblicazione: (2020)

Combination of single-molecule fluorescence and mass photometry
di: Pfitzner, E, et al.
Pubblicazione: (2022)

Mass photometry enables label-free tracking and mass measurement of single proteins on lipid bilayers
di: Foley, EDB, et al.
Pubblicazione: (2021)

Label-free single-molecule quantification of DNA by mass photometry
di: Li, Y, et al.
Pubblicazione: (2020)

Mass photometry enables label-free tracking and mass measurement of single proteins on lipid bilayers
di: Foley, E, et al.
Pubblicazione: (2021)

Characterising biomolecular interactions and dynamics with mass photometry
di: Asor, R, et al.
Pubblicazione: (2022)

Revisiting the structure-function relationship with mass photometry
di: Kukura, P
Pubblicazione: (2019)

Specificity of Human Sulfiredoxin for Reductant and Peroxiredoxin Oligomeric State
di: Tom E. Forshaw, et al.
Pubblicazione: (2021-06-01)

Single molecule mass photometry of DNA and DNA-protein interactions
di: Li, Y
Pubblicazione: (2022)

Mass photometry: weighing single molecules with interferometric scattering microscopy
di: Young, G
Pubblicazione: (2019)

Redox Conformation-Specific Protein–Protein Interactions of the 2-Cysteine Peroxiredoxin in Arabidopsis
di: Michael Liebthal, et al.
Pubblicazione: (2020-06-01)

Quantifying the monomer-dimer equilibrium of tubulin with mass photometry
di: Fineberg, A, et al.
Pubblicazione: (2020)

Lifting the concentration limit of mass photometry by PEG nanopattering
di: Kratochvil, J, et al.
Pubblicazione: (2024)

Overoxidation and Oligomerization of <i>Trypanosoma cruzi</i> Cytosolic and Mitochondrial Peroxiredoxins
di: María Dolores Piñeyro, et al.
Pubblicazione: (2023-10-01)

Hyperoxidation of Peroxiredoxin 6 Induces Alteration from Dimeric to Oligomeric State
di: Sharifun Shahnaj, et al.
Pubblicazione: (2019-02-01)

BPS2025 - Multi-channel mass photometry
di: Peters, JS, et al.
Pubblicazione: (2025)

Mass photometry of membrane proteins
di: Olerinyova, A, et al.
Pubblicazione: (2020)

Mass Photometry of Membrane Proteins
di: Olerinyova, A, et al.
Pubblicazione: (2020)

Dissecting FOXP2 oligomerization and DNA binding
di: Haeussermann, K, et al.
Pubblicazione: (2019)

Label-free tracking and mass measurement of single protein complexes on lipid bilayers
di: Foley, EDB, et al.
Pubblicazione: (2022)

Characterization of membrane protein interactions by peptidisc-mediated mass photometry
di: Young, JW, et al.
Pubblicazione: (2024)

The chloroplast 2-cysteine peroxiredoxin functions as thioredoxin oxidase in redox regulation of chloroplast metabolism
di: Mohamad-Javad Vaseghi, et al.
Pubblicazione: (2018-10-01)

Quantifying protein-protein interactions by molecular counting with mass photometry
di: Soltermann, F, et al.
Pubblicazione: (2020)

Characterization of membrane protein interactions by peptidisc-mediated mass photometry
di: John William Young, et al.
Pubblicazione: (2024-02-01)

Quantifying the heterogeneity of macromolecular machines by mass photometry
di: Sonn-Segev, A, et al.
Pubblicazione: (2020)

Quantifying binding affinities, kinetics and stoichiometry of biomolecular complexes with mass photometry
di: Soltermann, F, et al.
Pubblicazione: (2020)

Multidimensional mass photometry
di: Bishop, J
Pubblicazione: (2023)

Quantifying the heterogeneity of macromolecular machines by mass photometry
di: Sonn-Segev, Adar, et al.
Pubblicazione: (2021)

Quantifying the heterogeneity of macromolecular machines by mass photometry
di: Adar Sonn-Segev, et al.
Pubblicazione: (2020-04-01)

Advancing the limits of mass photometry
di: Priest, L
Pubblicazione: (2023)

Active site CP-loop dynamics modulate substrate binding, catalysis, oligomerization, stability, over-oxidation and recycling of 2-Cys Peroxiredoxins
di: Kamariah, Neelagandan, et al.
Pubblicazione: (2020)

Discovery of fragment molecules that bind the human peroxiredoxin 5 active site.
di: Sarah Barelier, et al.
Pubblicazione: (2010-01-01)

The architecture of redox microdomains: Cascading gradients and peroxiredoxins’ redox-oligomeric coupling integrate redox signaling and antioxidant protection
di: Matthew Griffith, et al.
Pubblicazione: (2024-02-01)

NADH oxidase and alkyl hydroperoxide reductase subunit C (peroxiredoxin) fromAmphibacillus xylanus form an oligomeric assembly
di: Toshiaki Arai, et al.
Pubblicazione: (2015-01-01)

Function and Regulation of Chloroplast Peroxiredoxin IIE
di: Anna Dreyer, et al.
Pubblicazione: (2021-01-01)

Single-particle mass analysis of intact ribosomes by mass photometry and Orbitrap-based charge detection mass spectrometry
di: Szu-Hsueh Lai, et al.
Pubblicazione: (2021-11-01)

Quantifying the heterogeneity of macromolecular machines by mass photometry
di: Sonn-Segev, A
Pubblicazione: (2020)

Oligomeric MHC molecules and their homologues: state of the art.
di: Dunbar, P, et al.
Pubblicazione: (2002)

A workflow for sizing oligomeric biomolecules based on cryo single molecule localization microscopy.
di: Magdalena C Schneider, et al.
Pubblicazione: (2021-01-01)