Evidence map›Paper›PMID 27703410›Full record

ReviewArchaea (Vancouver, B.C.)2016

Fundamental Characteristics of AAA+ Protein Family Structure and Function.

Justin M Miller, Eric J Enemark

Open access · hybridAbstract readReview
In one paragraph

Review in Archaea (Vancouver, B.C.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
3.8field-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

59 citing papers in PubMed, 107 citations in OpenAlex.

  1. Article
  2. Article
  3. HELZ2 RegulatesCirculation · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. NAL1 forms a molecular cage to regulate FZP phase separation.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Article
  9. Article
  10. Structural modeling and biochemical characterization of MSMEG_0748, a MoxR ATPase fromComputational and structural biotechnology journal · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. New insights into the domain of unknown function (DUF) of EccCActa crystallographica. Section D, Structural biology · 2024
    Article
  17. Cryo-EM reveals a nearly complete PCNA loading process and unique features of the human alternative clamp loader CTF18-RFC.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  18. Article
  19. Review
  20. 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

2 authors at 1 institution in 1 country.

Justin M MillerDepartment of Structural Biology, St. Jude Children's Research Hospital, 262 Danny Thomas Place, Memphis, TN 38105, USA.ORCID 0000-0001-9230-9483
Eric J EnemarkDepartment of Structural Biology, St. Jude Children's Research Hospital, 262 Danny Thomas Place, Memphis, TN 38105, USA.ORCID 0000-0003-4055-633X
St. Jude Children's Research Hospital · US

Funding

Molecular mechanisms of DNA replicationR01GM098771 · NIGMS · UNIV OF ARKANSAS FOR MED SCIS · PI ENEMARK, ERIC · 2011 to 2019
$3.1M
NIGMS NIH HHS R01 GM098771
6 · The paper itself

Abstract

Many complex cellular events depend on multiprotein complexes known as molecular machines to efficiently couple the energy derived from adenosine triphosphate hydrolysis to the generation of mechanical force. Members of the AAA+ ATPase superfamily (ATPases Associated with various cellular Activities) are critical components of many molecular machines. AAA+ proteins are defined by conserved modules that precisely position the active site elements of two adjacent subunits to catalyze ATP hydrolysis. In many cases, AAA+ proteins form a ring structure that translocates a polymeric substrate through the central channel using specialized loops that project into the central channel. We discuss the major features of AAA+ protein structure and function with an emphasis on pivotal aspects elucidated with archaeal proteins.

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateArchaeaArchaeal ProteinsHydrolysisModels, MolecularProtein ConformationAdenosine TriphosphatasesAdenosine TriphosphateArchaeal Proteins

Identifiers

PMID27703410
PMCPMC5039278
OpenAlexW2521404215

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.