Evidence map›Paper›PMID 21282052›Full record

ReviewCurrent opinion in structural biology2011

The nuts and bolts of ring-translocase structure and mechanism.

Artem Y Lyubimov, Melania Strycharska, James M Berger

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in structural biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed
4.5field-weighted citation impact, top 4% 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

83 citing papers in PubMed, 127 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Viral Genomic DNA Packaging Machinery.Sub-cellular biochemistry · 2024
    Review
  5. Article
  6. Article
  7. SV40 T-antigen uses a DNA shearing mechanism to initiate origin unwinding.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  8. Article
  9. Article
  10. CMG helicase can use ATPγS to unwind DNA: Implications for the rate-limiting step in the reaction mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  11. Article
  12. Review
  13. Mechanisms of hexameric helicases.Critical reviews in biochemistry and molecular biology · 2021
    Review
  14. Article
  15. Article
  16. Article
  17. FtsK in motion reveals its mechanism for double-stranded DNA translocation.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  18. Article
  19. Article
  20. Article

23 more citing papers are in PubMed but not listed here.

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

3 authors at 2 institutions in 1 country.

Artem Y LyubimovDepartment of Molecular and Cell Biology, University of California, Berkeley, 360 Stanley Hall, Berkeley, CA, USA.
Melania Strycharska
James M Berger
University of California, Berkeley · USQB3 · US

Funding

Mechanistic Studies of Replication Initiation in ProkaryotesR37GM071747 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI James M. Berger · 2017 to 2026
$4.4M
Structure/Function Studies of DNA Replication InitiationR01GM071747 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI BERGER, JAMES M. · 2005 to 2016
$4.0M
NIGMS NIH HHS GM071747NIGMS NIH HHS R01 GM071747NIGMS NIH HHS R37 GM071747
6 · The paper itself

Abstract

Ring-shaped, oligomeric translocases are multisubunit enzymes that couple the hydrolysis of Nucleoside TriPhosphates (NTPs) to directed movement along extended biopolymer substrates. These motors help unwind nucleic acid duplexes, unfold protein chains, and shepherd nucleic acids between cellular and/or viral compartments. Substrates are translocated through a central pore formed by a circular array of catalytic subunits. Cycles of nucleotide binding, hydrolysis, and product release help reposition translocation loops in the pore to direct movement. How NTP turnover allosterically induces these conformational changes, and the extent of mechanistic divergence between motor families, remain outstanding problems. This review examines the current models for ring-translocase function and highlights the fundamental gaps remaining in our understanding of these molecular machines.

Indexed as

Models, MolecularComputer SimulationNucleoside-TriphosphataseProtein ConformationProtein TransportSubstrate SpecificityNucleoside-Triphosphatase

Identifiers

PMID21282052
PMCPMC3070846
OpenAlexW2022965635

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.