ArticleBiochemistry2010
Electron spin-echo envelope modulation (ESEEM) reveals water and phosphate interactions with the KcsA potassium channel.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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
18 citing papers in PubMed, 37 citations in OpenAlex.
- Advances in EPR Approaches for Studying Structural Properties of Membrane Proteins.Magnetic resonance in chemistry : MRC · 2026Review
- HDX-guided EPR spectroscopy to interrogate membrane protein dynamics.STAR protocols · 2022Article
- Pocket delipidation induced by membrane tension or modification leads to a structurally analogous mechanosensitive channel state.Structure (London, England : 1993) · 2022Article
- In-Lipid Structure of Pressure-Sensitive Domains Hints Mechanosensitive Channel Functional Diversity.Biophysical journal · 2020Article
- Electron Spin Relaxation of Photoexcited Porphyrin in Water-Glycerol Glass.Molecules (Basel, Switzerland) · 2020Article
- Electron Paramagnetic Resonance as a Tool for Studying Membrane Proteins.Biomolecules · 2020Review
- Allosteric activation of an ion channel triggered by modification of mechanosensitive nano-pockets.Nature communications · 2019Article
- Utilization ofBiochimica et biophysica acta. Biomembranes · 2018Article
- Site-Directed Spin Labeling EPR for Studying Membrane Proteins.BioMed research international · 2018Review
- SARS-CoV fusion peptides induce membrane surface ordering and curvature.Scientific reports · 2016Article
- Determining the Secondary Structure of Membrane Proteins and Peptides Via Electron Spin Echo Envelope Modulation (ESEEM) Spectroscopy.Methods in enzymology · 2015Article
- X-ray crystallography over the past decade for novel drug discovery - where are we heading next?Expert opinion on drug discovery · 2015Review
- Water penetration profile at the protein-lipid interface in Na,K-ATPase membranes.Biophysical journal · 2014Article
- Avoidable errors in deposited macromolecular structures: an impediment to efficient data mining.IUCrJ · 2014Article
- Site-directed spin labeling reveals pentameric ligand-gated ion channel gating motions.PLoS biology · 2013Article
- Use of electron paramagnetic resonance to solve biochemical problems.Biochemistry · 2013Review
- Electron Paramagnetic Resonance and Electron Spin Echo Studies of CoApplied magnetic resonance · 2013Article
- Probing the structure of membrane proteins with electron spin echo envelope modulation spectroscopy.Protein science : a publication of the Protein Society · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Electron spin-echo envelope modulation (ESEEM) spectroscopy is a well-established technique for the study of naturally occurring paramagnetic metal centers. The technique has been used to study copper complexes, hemes, enzyme mechanisms, micellar water content, and water permeation profiles in membranes, among other applications. In the present study, we combine ESEEM spectroscopy with site-directed spin labeling (SDSL) and X-ray crystallography in order to evaluate the technique's potential as a structural tool to describe the native environment of membrane proteins. Using the KcsA potassium channel as a model system, we demonstrate that deuterium ESEEM can detect water permeation along the lipid-exposed surface of the KcsA outer helix. We further demonstrate that (31)P ESEEM is able to identify channel residues that interact with the phosphate headgroup of the lipid bilayer. In combination with X-ray crystallography, the (31)P data may be used to define the phosphate interaction surface of the protein. The results presented here establish ESEEM as a highly informative technique for SDSL studies of membrane proteins.
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.