Evidence map›Paper›PMID 31541260›Full record

ArticleThe Journal of membrane biology2020

Location of TEMPO-PC in Lipid Bilayers: Implications for Fluorescence Quenching.

Alexander Kyrychenko, Alexey S Ladokhin

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Article in The Journal of membrane biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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3 · Its place in the literature

Who cites it

5 citing papers in PubMed.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Alexander KyrychenkoInstitute of Chemistry and School of Chemistry, V. N. Karazin Kharkiv National University, 4 Svobody Square, Kharkiv, 61022, Ukraine. a.v.kyrychenko@karazin.ua.ORCID 0000-0002-6223-0990
Alexey S LadokhinDepartment of Biochemistry and Molecular Biology, Kansas University Medical Center, Kansas City, KS, 66160-7421, USA.

Funding

Membrane-Mediated Interactions of the Bcl-xL/Bid/Bax Triad of Apoptotic RegulatorsR01GM126778 · NIGMS · UNIVERSITY OF KANSAS MEDICAL CENTER · PI LADOKHIN, ALEXEY, LANGEN, RALF · 2019 to 2022
$1.7M
NIGMS NIH HHS R01 GM126778
6 · The paper itself

Abstract

The characterization of the behavior of lipid-attached spin probes in a bilayer is of fundamental importance for correct interpretation of the results of both EPR and fluorescence studies of protein-membrane interactions. The knowledge of the immersion depth of TEMPO spin probe attached to lipid headgroup in TEMPO-PC is critical for the determination of the transverse location of fluorescence probes attached to proteins and peptides. The question of bilayer penetration of TEMPO moiety in TEMPO-PC has recently came into prominence in two studies of interfacial solvation (Cheng et al. in Biophys J 109:330-339, 2015; Lee et al. in Biophys J 111:2481-2491, 2016). Here, we re-examine the arguments on TEMPO penetration using the cross-validation of MD simulations and depth-dependent fluorescence-quenching experiments, which confirms that TEMPO in TEMPO-PC penetrates below the level of phosphate groups. The proper analysis of fluorescence quenching requires the use of Tempo position below the level of phosphate groups; and failure to do so will result in substantial systematic errors in determining the penetration of the labeled site on a membrane protein.

Indexed as

AlgorithmsCyclic N-OxidesLipid BilayersMembrane LipidsModels, TheoreticalMolecular Dynamics SimulationSpectrometry, FluorescenceStructure-Activity RelationshipCyclic N-OxidesLipid BilayersMembrane LipidsTEMPODepth-dependent fluorescence quenchingMolecular dynamics simulationTEMPO

Identifiers

PMID31541260
PMCPMC6960341

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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.