Evidence map›Paper›PMID 22224599›Full record

ReviewAnnual review of biophysics2012

Prokaryotic diacylglycerol kinase and undecaprenol kinase.

Wade D Van Horn, Charles R Sanders

Abstract readReview
In one paragraph

Review in Annual review of biophysics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

36 citing papers in PubMed, 66 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Extracellular vesicles derived from CD4Cellular & molecular biology letters · 2023
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Frontiers in microbiology · 2021
    Article
  10. Involvement ofAntibiotics (Basel, Switzerland) · 2020
    Article
  11. Comparative Transcriptomics of Shiga Toxin-Producing and CommensalFrontiers in cellular and infection microbiology · 2020
    Article
  12. Article
  13. Article
  14. Diacylglycerol kinases: Relationship to other lipid kinases.Advances in biological regulation · 2019
    Review
  15. Membrane properties that shape the evolution of membrane enzymes.Current opinion in structural biology · 2018
    Review
  16. Article
  17. Review
  18. Review
  19. DGK-θ: Structure, Enzymology, and Physiological Roles.Frontiers in cell and developmental biology · 2016
    Review
  20. 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

2 authors at 1 institution in 1 country.

Wade D Van HornDepartment of Biochemistry and Center for Structural Biology, Vanderbilt University, Nashville, Tennessee 37232, USA.
Charles R Sanders
Vanderbilt University · US

Funding

STRUCTURE OF DIACYLGLYCEROL KINASER01GM047485 · NIGMS · VANDERBILT UNIVERSITY · PI SANDERS, CHARLES R · 1997 to 2010
$2.9M
Structure, Folding, and Misfolding of PMP22R01NS058815 · NINDS · VANDERBILT UNIVERSITY · PI CARTER, BRUCE D, SANDERS, CHARLES R · 2010 to 2012
$921k
NIGMS NIH HHS R01 GM047485NIGMS NIH HHS R01 GM47485NINDS NIH HHS R01 NS058815
6 · The paper itself

Abstract

Prokaryotic diacylglycerol kinase (DAGK) and undecaprenol kinase (UDPK) are the lone members of a family of multispan membrane enzymes that are very small, lack relationships to any other family of proteins-including water soluble kinases-and exhibit an unusual structure and active site architecture. Escherichia coli DAGK plays an important role in recycling diacylglycerol produced as a by-product of biosynthesis of molecules located in the periplasmic space. UDPK seems to play an analogous role in gram-positive bacteria, where its importance is evident because UDPK is essential for biofilm formation by the oral pathogen Streptococcus mutans. DAGK has also long served as a model system for studies of membrane protein biocatalysis, folding, stability, and structure. This review explores our current understanding of the microbial physiology, enzymology, structural biology, and folding of the prokaryotic DAGK family, which is based on over 40 years of studies.

Indexed as

Catalytic DomainDiacylglycerol KinaseEscherichia coliGram-Positive BacteriaPhosphotransferases (Alcohol Group Acceptor)PlantsProtein FoldingDiacylglycerol KinasePhosphotransferases (Alcohol Group Acceptor)undecaprenol kinase

Identifiers

PMID22224599
PMCPMC3575517
OpenAlexW2098158675

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.