Evidence map›Paper›PMID 35269663›Full record

ReviewInternational journal of molecular sciences2022

Processing of D1 Protein: A Mysterious Process Carried Out in Thylakoid Lumen.

Noritoshi Inagaki

Abstract readReview
In one paragraph

Review in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Review
  2. Very high CONAR genomics and bioinformatics · 2026
    Article
  3. Article
  4. Article
  5. Isolation of a NovelToxins · 2025
    Article
  6. Article
  7. Article
  8. Hydrogen peroxide as a mitigation againstAquaculture (Amsterdam, Netherlands) · 2023
    Article
  9. Article
  10. Review
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.

Noritoshi InagakiResearch Center for Advanced Analysis, National Agriculture and Food Research Organization (NARO), Tsukuba 305-8518, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In oxygenic photosynthetic organisms, D1 protein, a core subunit of photosystem II (PSII), displays a rapid turnover in the light, in which D1 proteins are distinctively damaged and immediately removed from the PSII. In parallel, as a repair process, D1 proteins are synthesized and simultaneously assembled into the PSII. On this flow, the D1 protein is synthesized as a precursor with a carboxyl-terminal extension, and the D1 processing is defined as a step for proteolytic removal of the extension by a specific protease, CtpA. The D1 processing plays a crucial role in appearance of water-oxidizing capacity of PSII, because the main chain carboxyl group at carboxyl-terminus of the D1 protein, exposed by the D1 processing, ligates a manganese and a calcium atom in the Mn

Indexed as

Photosystem II Protein ComplexThylakoidsEndopeptidasesManganeseWaterEndopeptidasesManganesePhotosystem II Protein ComplexWaterassemblycarboxyl-terminal extensioncarboxyl-terminal processing protease (CtpA)D1 protein (psbA)Mn4CaO5 cluster (Mn-cluster)oxygen evolutionphotosystem II (PSII)serine-lysine dyadthylakoid lumenwater oxidation

Identifiers

PMID35269663
PMCPMC8909930

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.