Evidence map›Paper›PMID 36845545›Full record

ReviewFrontiers in molecular biosciences2023

Molecular mechanism of Rubisco activase: Dynamic assembly and Rubisco remodeling.

Kazi Waheeda, Heidi Kitchel, Quan Wang, Po-Lin Chiu

Abstract readReview
In one paragraph

Review in Frontiers in molecular biosciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. SyntheticmicroPublication biology · 2025
    Article
  6. Article
  7. Article
  8. Review
  9. Physiological and Proteomic Responses of the TetraploidInternational journal of molecular sciences · 2024
    Article
  10. Article
  11. Calcium-Dependent Protein Kinase 5 (Plants (Basel, Switzerland) · 2023
    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.

Kazi WaheedaSchool of Molecular Sciences, Arizona State University, Tempe, AZ, United States.
Heidi KitchelSchool of Molecular Sciences, Arizona State University, Tempe, AZ, United States.
Quan WangLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, United States.
Po-Lin ChiuSchool of Molecular Sciences, Arizona State University, Tempe, AZ, United States.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ribulose-1,5-bisphosphate (RuBP) carboxylase-oxygenase (Rubisco) enzyme is the limiting step of photosynthetic carbon fixation, and its activation is regulated by its co-evolved chaperone, Rubisco activase (Rca). Rca removes the intrinsic sugar phosphate inhibitors occupying the Rubisco active site, allowing RuBP to split into two 3-phosphoglycerate (3PGA) molecules. This review summarizes the evolution, structure, and function of Rca and describes the recent findings regarding the mechanistic model of Rubisco activation by Rca. New knowledge in these areas can significantly enhance crop engineering techniques used to improve crop productivity.

Indexed as

AAA+ ATPasecarbon fixationphotosynthesisredoxRubiscoRubisco activase

Identifiers

PMID36845545
PMCPMC9951593

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.