Evidence map›Paper›PMID 32972035›Full record

ReviewInternational journal of molecular sciences2020

How Kinesin-1 Utilize the Energy of Nucleotide: The Conformational Changes and Mechanochemical Coupling in the Unidirectional Motion of Kinesin-1.

Jingyu Qin, Hui Zhang, Yizhao Geng, Qing Ji

Abstract readReview
In one paragraph

Review in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed, 1 pooled it
–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

12 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. A Model for Chemomechanical Coupling of Kinesin-3 Motor.Cellular and molecular bioengineering · 2024
    Article
  3. Review
  4. Article
  5. Review
  6. Selective motor activation in organelle transport along axons.Nature reviews. Molecular cell biology · 2022
    Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. 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.

Jingyu QinCollege of Education, Shanghai Normal University, Shanghai 200234, China.
Hui ZhangSchool of Science, Hebei University of Technology, Tianjin 300401, China.
Yizhao GengSchool of Science, Hebei University of Technology, Tianjin 300401, China.
Qing JiSchool of Science, Hebei University of Technology, Tianjin 300401, China.

Funding

National Natural Science Foundation of China 11605038Natural Science Foundation of Hebei Province A2020202007
6 · The paper itself

Abstract

Kinesin-1 is a typical motile molecular motor and the founding member of the kinesin family. The most significant feature in the unidirectional motion of kinesin-1 is its processivity. To realize the fast and processive movement on the microtubule lattice, kinesin-1 efficiently transforms the chemical energy of nucleotide binding and hydrolysis to the energy of mechanical movement. The chemical and mechanical cycle of kinesin-1 are coupled to avoid futile nucleotide hydrolysis. In this paper, the research on the mechanical pathway of energy transition and the regulating mechanism of the mechanochemical cycle of kinesin-1 is reviewed.

Indexed as

KinesinsNucleotidesAnimalsHumansHydrolysisProtein ConformationKIF5B protein, humanKinesinsNucleotidesconformational changeKinesin-1mechanochemical couplingmicrotubuleneck linkernucleotide

Identifiers

PMID32972035
PMCPMC7555842

What OpenQuestion holds

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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.