Evidence map›Paper›PMID 30340038›Full record

ArticleCell2018

Flipping ATP to AMPlify Kinase Functions.

Joshua B Sheetz, Mark A Lemmon

Abstract readComment
In one paragraph

Article in Cell, 2018. 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
–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

3 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors.

Joshua B SheetzDepartment of Pharmacology, Yale University School of Medicine, New Haven, CT 06520, USA; Cancer Biology Institute, Yale University, West Haven, CT 06516, USA.
Mark A LemmonDepartment of Pharmacology, Yale University School of Medicine, New Haven, CT 06520, USA; Cancer Biology Institute, Yale University, West Haven, CT 06516, USA. Electronic address: mark.lemmon@yale.edu.

Funding

Understanding Signaling by Non-Canonical Receptor Tyrosine KinasesR35GM122485 · NIGMS · YALE UNIVERSITY · PI Mark A Lemmon · 2017 to 2026
$7.9M
NIGMS NIH HHS R35 GM122485
6 · The paper itself

Abstract

Understanding protein kinase family members that lack key catalytic residues-or pseudokinases-is a major challenge in cell signaling. In this issue of Cell, Sreelatha et al. (2018) describe how one pseudokinase transfers adenosine monophosphate (AMP) rather than phosphate to protein substrates, revealing unexpected catalytic diversity for the kinase fold.

Indexed as

Protein KinasesSignal TransductionAdenosine TriphosphateProteolysisAdenosine TriphosphateProtein Kinases

Identifiers

PMID30340038
PMCPMC6421561

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.