Evidence map›Paper›PMID 28904122›Full record

ReviewMolecular biology of the cell2017

Evolution of polymer formation within the actin superfamily.

Patrick R Stoddard, Tom A Williams, Ethan Garner, Buzz Baum

Open access · greenAbstract readReview
In one paragraph

Review in Molecular biology of the cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

15 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Building the Bacterial Divisome at the Septum.Sub-cellular biochemistry · 2024
    Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Atomic structure of theProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  11. Article
  12. Review
  13. Nuclear actin: ancient clue to evolution in eukaryotes?Histochemistry and cell biology · 2018
    Review
  14. Archaeal imaging: leading the hunt for new discoveries.Molecular biology of the cell · 2018
    Article
  15. Cryo-EM reconstruction of AlfA fromProceedings of the National Academy of Sciences of the United States of America · 2018
    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 3 institutions in 2 countries.

Patrick R StoddardMolecular and Cellular Biology, Faculty of Arts and Sciences Center for Systems Biology, Harvard University, Cambridge, MA 02138.
Tom A WilliamsSchool of Biological Sciences, University of Bristol, Bristol BS8 1TQ, UK.
Ethan GarnerMolecular and Cellular Biology, Faculty of Arts and Sciences Center for Systems Biology, Harvard University, Cambridge, MA 02138 b.baum@ucl.ac.uk egarner@g.harvard.edu.
Buzz BaumMRC-Laboratory for Molecular Cell Biology, University College London, London WC1E 6BT, UK b.baum@ucl.ac.uk egarner@g.harvard.edu.
Harvard University · USMRC Laboratory for Molecular Cell Biology · GBUniversity of Bristol · GB

Funding

Dissecting bacterial cell wall synthesis using in vivo single molecule trackingDP2AI117923 · NIAID · HARVARD UNIVERSITY · PI GARNER, ETHAN CLARK · 2014 to 2014
$2.3M
The Effects of Glucokinase Polymerization During Metabolic TransitionsF31GM116441 · NIGMS · HARVARD UNIVERSITY · PI STODDARD, PATRICK RENWICK · 2015 to 2017
$99k
Biotechnology and Biological Sciences Research Council BB/K009001/1Biotechnology and Biological Sciences Research Council BB/P001440/1Cancer Research UK 9786NIAID NIH HHS DP2 AI117923NIGMS NIH HHS F31 GM116441Wellcome Trust
6 · The paper itself

Abstract

While many are familiar with actin as a well-conserved component of the eukaryotic cytoskeleton, it is less often appreciated that actin is a member of a large superfamily of structurally related protein families found throughout the tree of life. Actin-related proteins include chaperones, carbohydrate kinases, and other enzymes, as well as a staggeringly diverse set of proteins that use the energy from ATP hydrolysis to form dynamic, linear polymers. Despite differing widely from one another in filament structure and dynamics, these polymers play important roles in ordering cell space in bacteria, archaea, and eukaryotes. It is not known whether these polymers descended from a single ancestral polymer or arose multiple times by convergent evolution from monomeric actin-like proteins. In this work, we provide an overview of the structures, dynamics, and functions of this diverse set. Then, using a phylogenetic analysis to examine actin evolution, we show that the actin-related protein families that form polymers are more closely related to one another than they are to other nonpolymerizing members of the actin superfamily. Thus all the known actin-like polymers are likely to be the descendants of a single, ancestral, polymer-forming actin-like protein.

Indexed as

ActinsAdenosine TriphosphateArchaeaBacteriaBiological EvolutionBiopolymersCytoskeletonEukaryotaEukaryotic CellsEvolution, MolecularHydrolysisPhylogenyActinsAdenosine TriphosphateBiopolymers

Identifiers

PMID28904122
PMCPMC5597319
OpenAlexW2754696304

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.