ArticleThe journal of physical chemistry. B2019
Control of Solvent Dynamics around the B
Article in The journal of physical chemistry. B, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
10 citing papers in PubMed, 10 citations in OpenAlex.
- Protein structure and coupled solvent dynamics in α-synuclein fibrils under controlled confinement.Biophysical journal · 2026Article
- Select Configurational Dynamics in Ethanolamine Ammonia-Lyase Radical Enzyme Catalysis.ACS physical chemistry Au · 2025Article
- Physical and Mechanical Properties of Monomeric Alpha-Synuclein Provide Leads to Molecular Function.The journal of physical chemistry. B · 2025Article
- Oligomeric and Fibrillar α-Synuclein Display Persistent Dynamics and Compressibility under Controlled Confinement.ACS chemical neuroscience · 2023Article
- Native and nonnative reactions in ethanolamine ammonia-lyase are actuated by different dynamics.Biophysical journal · 2023Article
- Reactivity Tracking of an Enzyme Progress Coordinate.The journal of physical chemistry letters · 2023Article
- Confinement dependence of protein-associated solvent dynamics around different classes of proteins, from the EPR spin probe perspective.Physical chemistry chemical physics : PCCP · 2022Article
- Resolution and characterization of contributions of select protein and coupled solvent configurational fluctuations to radical rearrangement catalysis in coenzyme BMethods in enzymology · 2022Article
- Resolution and characterization of confinement- and temperature-dependent dynamics in solvent phases that surround proteins in frozen aqueous solution by using spin-probe EPR spectroscopy.Methods in enzymology · 2022Article
- Coupling of ethanolamine ammonia-lyase protein and solvent dynamics characterized by the temperature-dependence of EPR spin probe mobility and dielectric permittivity.The Journal of chemical physics · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The temperature-dependent structure and dynamics of two concentric solvent phases, the protein-associated domain (PAD) and the mesodomain, that surround the ethanolamine ammonia-lyase (EAL) protein from Salmonella typhimurium in frozen polycrystalline aqueous solution are addressed by using electron paramagnetic resonance spectroscopy of the paramagnetic nitroxide spin probe, TEMPOL, over the temperature ( T) range 190-265 K. Dimethyl sulfoxide (DMSO), added at 0.5, 2.0, and 4.0% v/v and present at the maximum freeze concentration at T ≤ 245 K, varies the volume of the interstitial aqueous DMSO mesodomain ( V
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.