Evidence map›Paper›PMID 34922895›Full record

ReviewAdvances in biological regulation2022

Elusive structure of mammalian DGKs.

Qianqian Ma, Lakshmi Srinivasan, Sandra B Gabelli, Daniel M Raben

Open access · greenAbstract readReview
In one paragraph

Review in Advances in biological regulation, 2022. 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
0.4field-weighted citation impact, top 36% 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, 6 citations in OpenAlex.

  1. Review
  2. Article
  3. 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

4 authors at 2 institutions in 1 country.

Qianqian MaDepartment of Biological Chemistry, The Johns Hopkins University School of Medicine, Baltimore, MD, USA.
Lakshmi SrinivasanDepartment of Biophysics and Biophysical Chemistry, The Johns Hopkins University School of Medicine, Baltimore, MD, USA.
Sandra B GabelliDepartment of Biophysics and Biophysical Chemistry, The Johns Hopkins University School of Medicine, Baltimore, MD, USA; Department of Oncology, The Johns Hopkins University School of Medicine, Baltimore, MD, USA; Department of Medicine, The Johns Hopkins University School of Medicine, Baltimore, MD, USA. Electronic address: gabelli@jhmi.edu.
Daniel M RabenDepartment of Biological Chemistry, The Johns Hopkins University School of Medicine, Baltimore, MD, USA; Department of Oncology, The Johns Hopkins University School of Medicine, Baltimore, MD, USA. Electronic address: draben@jhmi.edu.
Johns Hopkins University · USJohns Hopkins Medicine · US

Funding

Biochemistry and Physiological Role of Diacylglycerol Kinase ThetaR01NS077923 · NINDS · JOHNS HOPKINS UNIVERSITY · PI RABEN, DANIEL M. · 2013 to 2016
$1.4M
NINDS NIH HHS R01 NS077923
6 · The paper itself

Abstract

Mammalian diacylglycerol kinases (DGKs) are a group of enzymes that catalyze the ATP-dependent phosphorylation of diacylglycerol (DAG) to produce phosphatidic acid (PtdOH). In doing so, they modulate the levels of these two important signaling lipids. Currently, ten mammalian DGKs are organized into five classes that vary with respect to domain organization, regulation, and cellular/subcellular distribution. As lipids play critical roles in cells, it is not surprising that there is increasing interest in understanding the mechanism underlying the catalysis and regulation of lipid modulating enzymes such as DGKs. However, there are no solved 3D structures for any of the eukaryotic DGKs. In this review, we summarize what is known and the current challenges in determining the structures of these important enzymes. In addition to gain critical insights into their mechanisms of catalysis and regulation, DGK structures will provide a platform for the design of isoform specific inhibitors.

Indexed as

Diacylglycerol KinasePhosphatidic AcidsAnimalsHumansMammalsPhosphorylationProtein IsoformsSignal TransductionDiacylglycerol KinasePhosphatidic AcidsProtein Isoforms

Identifiers

PMID34922895
PMCPMC8858910
OpenAlexW4200170570

What Socratic 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 Socratic graph.