Evidence map›Paper›PMID 32226850›Full record

ArticleACS omega2020

Theoretical Analysis of Dynamics of Kinesin Molecular Motors.

Ping Xie

Open access · goldAbstract read
In one paragraph

Article in ACS omega, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

5 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Modeling processive motion of kinesin-13 MCAK and kinesin-14 Cik1-Kar3 molecular motors.Protein science : a publication of the Protein Society · 2021
    Article
  3. Article
  4. Article
  5. 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

1 author at 1 institution in 1 country.

Ping XieKey Laboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing 100190, China.
Institute of Physics · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Kinesin is a typical molecular motor that can step processively on microtubules powered by hydrolysis of adenosine triphosphate (ATP) molecules, playing a critical role in intracellular transports. Its dynamical properties such as its velocity, stepping ratio, run length, dissociation rate, etc. as well as the load dependencies of these quantities have been well documented through single-molecule experimental methods. In particular, the run length shows a dramatic asymmetry with respect to the direction of the load, and the dissociation rate exhibits a slip-catch-slip bond behavior under the backward load. Here, an analytic theory was provided for the dynamics of kinesin motors under both forward and backward loads, explaining consistently and quantitatively the diverse available experimental results.

Identifiers

PMID32226850
PMCPMC7097908
OpenAlexW3010716404

What OpenQuestion holds

Textmetadata
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.