Evidence map›Paper›PMID 24610582›Full record

ReviewPlant & cell physiology2014

Quality control of PSII: behavior of PSII in the highly crowded grana thylakoids under excessive light.

Yasusi Yamamoto, Suguru Kai, Atsuki Ohnishi, Nodoka Tsumura, Tomomi Ishikawa, Haruka Hori, Noriko Morita, Yasuo Ishikawa

Open access · hybridAbstract readReview
In one paragraph

Review in Plant & cell physiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.1field-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

15 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Review
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  7. Article
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  10. Review
  11. Article
  12. Born in 1949 in postwar Japan.Photosynthesis research · 2016
    Article
  13. Review
  14. Review
  15. 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

8 authors at 1 institution in 1 country.

Yasusi YamamotoGraduate School of Natural Science and Technology, Okayama University, Okayama, 700-8530 Japan yasusiya@cc.okayama-u.ac.jp.
Suguru KaiGraduate School of Natural Science and Technology, Okayama University, Okayama, 700-8530 Japan.
Atsuki OhnishiGraduate School of Natural Science and Technology, Okayama University, Okayama, 700-8530 Japan.
Nodoka TsumuraGraduate School of Natural Science and Technology, Okayama University, Okayama, 700-8530 Japan.
Tomomi IshikawaGraduate School of Natural Science and Technology, Okayama University, Okayama, 700-8530 Japan.
Haruka HoriGraduate School of Natural Science and Technology, Okayama University, Okayama, 700-8530 Japan.
Noriko MoritaGraduate School of Natural Science and Technology, Okayama University, Okayama, 700-8530 Japan.
Yasuo IshikawaGraduate School of Natural Science and Technology, Okayama University, Okayama, 700-8530 Japan.
Okayama University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The grana thylakoids of higher plant chloroplasts are crowded with PSII and the associated light-harvesting complexes (LHCIIs). They constitute supercomplexes, and often form semi-crystalline arrays in the grana. The crowded condition of the grana may be necessary for efficient trapping of excitation energy by LHCII under weak light, but it might hinder proper movement of LHCII necessary for reversible aggregation of LHCII in the energy-dependent quenching of Chl fluorescence under moderate high light. When the thylakoids are illuminated with extreme high light, the reaction center-binding D1 protein of PSII is photodamaged, and the damaged protein migrates to the grana margins for degradation and subsequent repair. In both moderate and extreme high-light conditions, fluidity of the thylakoid membrane is crucial. In this review, we first provide an overview of photoprotective processes, then discuss changes in membrane fluidity and mobility of the protein complexes in the grana under excessive light, which are closely associated with photoprotection of PSII. We hypothesize that reversible aggregation of LHCII, which is necessary to avoid light stress under moderate high light, and swift turnover of the photodamaged D1 protein under extreme high light are threatened by irreversible protein aggregation induced by reactive oxygen species in photochemical reactions.

Indexed as

PhotosynthesisLightLight-Harvesting Protein ComplexesPhotosystem II Protein ComplexPlantsProtein AggregatesReactive Oxygen SpeciesStress, PhysiologicalThylakoidsLight-Harvesting Protein ComplexesPhotosystem II Protein ComplexProtein AggregatesReactive Oxygen SpeciesLight stressMembrane crowdednessNon-photochemical quenchingPhotoinhibitionPhotosystem IIProtein aggregation

Identifiers

PMID24610582
PMCPMC4080270
OpenAlexW2153353543

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.