Evidence map›Paper›PMID 37394020›Full record

ReviewBiochimica et biophysica acta. Reviews on cancer2023

Structural and mechanistic insights provided by single particle cryo-EM analysis of phosphoinositide 3-kinase (PI3Kα).

Peter K Vogt, Jonathan R Hart, Su Yang, Qingtong Zhou, Dehua Yang, Ming-Wei Wang

Open access · greenAbstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Biochimica et biophysica acta. Reviews on cancer, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.8field-weighted citation impact, top 27% 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

3 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. Making PI3K superfamily enzymes run faster.Advances in biological regulation · 2025
    Review
  3. Review
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

6 authors at 4 institutions in 3 countries.

Peter K VogtDepartment of Molecular Medicine, The Scripps Research Institute, La Jolla, CA 92037, United States of America. Electronic address: pkvogt@scripps.edu.
Jonathan R HartDepartment of Molecular Medicine, The Scripps Research Institute, La Jolla, CA 92037, United States of America.
Su YangDepartment of Molecular Medicine, The Scripps Research Institute, La Jolla, CA 92037, United States of America.
Qingtong ZhouDepartment of Pharmacology, School of Basic Medical Sciences, Fudan University, Shanghai 200032, China.
Dehua YangThe National Center for Drug Screening, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.
Ming-Wei WangDepartment of Pharmacology, School of Basic Medical Sciences, Fudan University, Shanghai 200032, China; Research Center for Deepsea Bioresources, Sanya 572025, China; Department of Chemistry, School of Science, The University of Tokyo, Tokyo 113-0033, Japan.
Scripps Research Institute · USFudan University · CNInstitute of Deep-Sea Science and Engineering · CNShanghai Institute of Materia Medica · CN

Funding

Cancer genes: translating basics to applicationsR35CA197582 · NCI · SCRIPPS RESEARCH INSTITUTE, THE · PI VOGT, PETER K · 2016 to 2022
$7.8M
Investigating Cancer-Specific Long Noncoding RNAs for Early Cancer DetectionR50CA243899 · NCI · SCRIPPS RESEARCH INSTITUTE, THE · PI HART, JONATHAN ROSS · 2019 to 2021
$434k
NCI NIH HHS R35 CA197582NCI NIH HHS R50 CA243899
6 · The paper itself

Abstract

Recent cryo-electron microscopic (cryo-EM) investigations have succeeded in the analysis of various structural conformations and functional states of PI3Kα, a dimer consisting of the catalytic subunit p110α and the regulatory subunit p85α of class IA of phosphoinositide 3-kinase. High resolution structures have been obtained of the unliganded and of BYL-719-bound PI3Kα. The latter provides information on excessively flexible domains of p85α that are then further analyzed with nanobodies and CXMS (chemical cross-linking, digestion and mass spectrometry). Analysis of p110α helical and kinase domain mutations reveals mutant-specific features that can be linked to the gain of function in enzymatic and signaling activities.

Indexed as

Phosphatidylinositol 3-KinasePhosphatidylinositol 3-KinasesCatalytic DomainCryoelectron MicroscopyHumansMutationPhosphatidylinositol 3-KinasePhosphatidylinositol 3-KinasesBYL-719CXMSMutantsNanobodyPhosphoinositide 3-kinase

Identifiers

PMID37394020
PMCPMC10530483
OpenAlexW4382681111

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.