Evidence map›Paper›PMID 27214582›Full record

ArticleJournal of magnetic resonance (San Diego, Calif. : 1997)2016

A triarylmethyl spin label for long-range distance measurement at physiological temperatures using T1 relaxation enhancement.

Zhongyu Yang, Michael D Bridges, Carlos J López, Olga Yu Rogozhnikova, Dmitry V Trukhin, Evan K Brooks, Victor Tormyshev, Howard J Halpern, Wayne L Hubbell

Abstract read
In one paragraph

Article in Journal of magnetic resonance (San Diego, Calif. : 1997), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
13.1field-weighted citation impact, top 2% of its field
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

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.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 57 citations in OpenAlex.

  1. Review
  2. Article
  3. Cucurbit[7]uril Enhances Distance Measurements of Spin-Labeled Proteins.Journal of the American Chemical Society · 2023
    Article
  4. A newJournal of magnetic resonance (San Diego, Calif. : 1997) · 2023
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  8. Review
  9. Article
  10. Journal of magnetic resonance (San Diego, Calif. : 1997) · 2020
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Triarylmethyl Radicals: EPR Study ofZeitschrift fur physikalische Chemie (Frankfurt am Main, Germany) · 2017
    Article
  16. Article
  17. Article
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

9 authors at 3 institutions in 2 countries.

Zhongyu YangJules Stein Eye Institute and Department of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, CA 90095, USA.
Michael D BridgesJules Stein Eye Institute and Department of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, CA 90095, USA.
Carlos J LópezJules Stein Eye Institute and Department of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, CA 90095, USA.
Olga Yu RogozhnikovaN.N. Vorozhtsov Novosibirsk Institute of Organic Chemistry, Novosibirsk 630090, Russia; Novosibirsk State University, Novosibirsk 630090, Russia.
Dmitry V TrukhinN.N. Vorozhtsov Novosibirsk Institute of Organic Chemistry, Novosibirsk 630090, Russia; Novosibirsk State University, Novosibirsk 630090, Russia.
Evan K BrooksJules Stein Eye Institute and Department of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, CA 90095, USA.
Victor TormyshevN.N. Vorozhtsov Novosibirsk Institute of Organic Chemistry, Novosibirsk 630090, Russia; Novosibirsk State University, Novosibirsk 630090, Russia. Electronic address: torm@nioch.nsc.ru.
Howard J HalpernThe Center for EPR Imaging in vivo Physiology, Department of Radiation and Cellular Oncology, University of Chicago, Chicago, IL 60637, USA. Electronic address: h-halpern@uchicago.edu.
Wayne L HubbellJules Stein Eye Institute and Department of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, CA 90095, USA. Electronic address: hubbellw@jsei.ucla.edu.
University of California, Los Angeles · USNovosibirsk State University · RUUniversity of Chicago · US

Funding

Vision Research Core at UCLAP30EY000331 · NEI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI Xian-Jie Yang · 1985 to 2026
$16.8M
Very Low Frequency EPR Imaging in Vivo Phisiology P41 EB02034P41EB002034 · NIBIB · UNIVERSITY OF CHICAGO · PI HALPERN, HOWARD J · 2003 to 2017
$16.1M
MOLECULAR BASIS OF MEMBRANE EXCITATIONR01EY005216 · NEI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI HUBBELL, WAYNE L · 1985 to 2019
$9.8M
Radiation Biology of EPR Oxygen ImagesR01CA098575 · NCI · UNIVERSITY OF CHICAGO · PI HALPERN, HOWARD J · 2003 to 2022
$4.5M
MOLECULAR BASIS OF MEMBRANE EXCITATIONR37EY005216 · NEI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI HUBBELL, WAYNE L · 1990 to 1999
–
NCI NIH HHS R01 CA098575NEI NIH HHS P30 EY000331NEI NIH HHS R01 EY005216NEI NIH HHS R37 EY005216NIBIB NIH HHS P41 EB002034
6 · The paper itself

Abstract

Site-directed spin labeling (SDSL) in combination with electron paramagnetic resonance (EPR) spectroscopy has become an important tool for measuring distances in proteins on the order of a few nm. For this purpose pairs of spin labels, most commonly nitroxides, are site-selectively introduced into the protein. Recent efforts to develop new spin labels are focused on tailoring the intrinsic properties of the label to either extend the upper limit of measurable distances at physiological temperature, or to provide a unique spectral lineshape so that selective pairwise distances can be measured in a protein or complex containing multiple spin label species. Triarylmethyl (TAM) radicals are the foundation for a new class of spin labels that promise to provide both capabilities. Here we report a new methanethiosulfonate derivative of a TAM radical that reacts rapidly and selectively with an engineered cysteine residue to generate a TAM containing side chain (TAM1) in high yield. With a TAM1 residue and Cu(2+) bound to an engineered Cu(2+) binding site, enhanced T1 relaxation of TAM should enable measurement of interspin distances up to 50Å at physiological temperature. To achieve favorable TAM1-labeled protein concentrations without aggregation, proteins are tethered to a solid support either site-selectively using an unnatural amino acid or via native lysine residues. The methodology is general and readily extendable to complex systems, including membrane proteins.

Indexed as

Electron Spin Resonance SpectroscopySpin LabelsBinding SitesProteinsTemperatureProteinsSpin LabelsDistance measurement at physiological temperatureRelaxation enhancementSaturation recoverySpin labelingTriarylmethyl radical

Identifiers

PMID27214582
PMCPMC4958593
OpenAlexW2389594097

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.