Evidence map›Paper›PMID 39322225›Full record

ArticleJournal of the American Chemical Society2024

Topological Heterogeneity of Protein Kinase C Modulators in Human T-Cells Resolved with In-Cell Dynamic Nuclear Polarization NMR Spectroscopy.

Sarah A Overall, Sina J Hartmann, Quang H Luu-Nguyen, Patrick Judge, Dorothea Pinotsi, Lea Marti, Snorri Th Sigurdsson, Paul A Wender, Alexander B Barnes

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

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

2 citing papers in PubMed.

  1. Article
  2. 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.

Sarah A OverallInstitute of Molecular Physical Science, ETH Zurich, 8093 Zurich, Switzerland.ORCID 0000-0002-9906-2791
Sina J HartmannInstitute of Molecular Physical Science, ETH Zurich, 8093 Zurich, Switzerland.
Quang H Luu-NguyenDepartment of Chemistry, Stanford University, Stanford, California 94305-5080, United States.
Patrick JudgeDepartment of Biochemistry, Biophysics, & Structural Biology, Washington University in St. Louis, St. Louis, Missouri 63110, United States.
Dorothea PinotsiScientific Center for Optical and Electron Microscopy, ETH Zurich, 8093 Zurich, Switzerland.
Lea MartiInstitute of Molecular Physical Science, ETH Zurich, 8093 Zurich, Switzerland.
Snorri Th SigurdssonScience Institute, University of Iceland, Dunhagi 5, 107 Reykjavik, Iceland.ORCID 0000-0003-2492-1456
Paul A WenderDepartment of Chemistry, Stanford University, Stanford, California 94305-5080, United States.ORCID 0000-0001-6319-2829
Alexander B BarnesInstitute of Molecular Physical Science, ETH Zurich, 8093 Zurich, Switzerland.ORCID 0000-0003-3748-8508

Funding

SYNTHETIC STUDIES RELATED TO CANCER RESEARCH/TREATMENTR01CA031845 · NCI · STANFORD UNIVERSITY · PI PAUL Anthony WENDER · 1985 to 2026
$6.9M
Synthetic Studies Related to Cancer Research/TreatmentR37CA031845 · NCI · STANFORD UNIVERSITY · PI WENDER, PAUL ANTHONY · 2006 to 2015
$4.5M
Towards HIV eradication: New concepts and potent compounds for PKC-mediated latency reversalR01AI172410 · NIAID · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI PAUL Anthony WENDER, Jerome A. Zack · 2023 to 2026
$2.7M
Towards HIV eradication: New concepts and potent compounds for PKC-mediated latency reversalR56AI172410 · NIAID · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI WENDER, PAUL ANTHONY, ZACK, JEROME A. · 2022 to 2022
$798k
NCI NIH HHS R01 CA031845NCI NIH HHS R37 CA031845NIAID NIH HHS R01 AI172410NIAID NIH HHS R56 AI172410
6 · The paper itself

Abstract

Phorbol ester analogs are a promising class of anticancer therapeutics and HIV latency reversing agents that interact with cellular membranes to recruit and activate protein kinase C (PKC) isoforms. However, it is unclear how these esters interact with membranes and how this might correlate with the biological activity of different phorbol ester analogs. Here, we have employed dynamic nuclear polarization (DNP) NMR to characterize phorbol esters in a native cellular context. The enhanced NMR sensitivity afforded by DNP and cryogenic operation reveals topological heterogeneity of

Indexed as

Protein Kinase CT-LymphocytesCell MembraneHumansMagnetic Resonance SpectroscopyPhorbol EstersTetradecanoylphorbol AcetatePhorbol EstersProtein Kinase CTetradecanoylphorbol Acetate

Identifiers

PMID39322225
PMCPMC11468733

What OpenQuestion holds

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LicenceCC BY
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.