Evidence map›Paper›PMID 35531282›Full record

ReviewFrontiers in microbiology2022

F

Sándor Volkán-Kacsó, Rudolph A Marcus

Abstract readReview
In one paragraph

Review in Frontiers in microbiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. 2-Site versus 3-site models of ATP hydrolysis by FTheory in biosciences = Theorie in den Biowissenschaften · 2024
    Article
  2. 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.

Sándor Volkán-KacsóNoyes Laboratory of Chemical Physics, California Institute of Technology, Pasadena, CA, United States.
Rudolph A MarcusNoyes Laboratory of Chemical Physics, California Institute of Technology, Pasadena, CA, United States.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In this chapter, we review single-molecule observations of rotary motors, focusing on the general theme that their mechanical motion proceeds in substeps with each substep described by an angle-dependent rate constant. In the molecular machine F1-ATPase, the stepping rotation is described for individual steps by forward and back reaction rate constants, some of which depend strongly on the rotation angle. The rotation of a central shaft is typically monitored by an optical probe. We review our recent work on the theory for the angle-dependent rate constants built to treat a variety of single-molecule and ensemble experiments on the F

Indexed as

ATP bindingconcerted kineticscryo-electron microscopyF1-ATPasemulti-state theoryrotary biomolecular motorssingle-molecule imagingstepping rotation of F1-ATPase

Identifiers

PMID35531282
PMCPMC9072658

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.