Evidence map›Paper›PMID 18791807›Full record

ReviewPhotosynthesis research

Structure, function, and evolution of the PsbP protein family in higher plants.

Kentaro Ifuku, Seiko Ishihara, Ren Shimamoto, Kunio Ido, Fumihiko Sato

Abstract readReview
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In one paragraph

Review in Photosynthesis research. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed.

  1. Article
  2. Article
  3. A newly identified photosystem II Subunit P geneFrontiers in plant science · 2024
    Article
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  6. Review
  7. Review
  8. Article
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  18. Review
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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

5 authors.

Kentaro IfukuGraduate School of Biostudies, Kyoto University, Kyoto 606-8502, Japan. ifuku@kais.kyoto-u.ac.jp
Seiko Ishihara
Ren Shimamoto
Kunio Ido
Fumihiko Sato

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The PsbP is a thylakoid lumenal subunit of photosystem II (PSII), which has developed specifically in higher plants and green algae. In higher plants, the molecular function of PsbP has been intensively investigated by release-reconstitution experiments in vitro. Recently, solution of a high-resolution structure of PsbP has enabled investigation of structure-function relationships, and efficient gene-silencing techniques have demonstrated the crucial role of PsbP in PSII activity in vivo. Furthermore, genomic and proteomic studies have shown that PsbP belongs to the divergent PsbP protein family, which consists of about 10 members in model plants such as Arabidopsis and rice. Characterization of the molecular function of PsbP homologs using Arabidopsis mutants suggests that each plays a distinct and important function in maintaining photosynthetic electron transfer. In this review, recent findings regarding the molecular functions of PsbP and other PsbP homologs in higher plants are summarized, and the molecular evolution of these proteins is discussed.

Indexed as

Evolution, MolecularPhotosynthesisArabidopsis ProteinsMultigene FamilyPhotosystem II Protein ComplexPlantsProtein ConformationStructure-Activity RelationshipArabidopsis ProteinsPhotosystem II Protein Complex

Identifiers

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.