Evidence map›Paper›PMID 17551844›Full record

ReviewPhotosynthesis research

The carboxyl-terminal processing of precursor D1 protein of the photosystem II reaction center.

Kimiyuki Satoh, Yumiko Yamamoto

Abstract readReview
PubMed Publisher
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 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

24 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
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  11. Review
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  15. Article
  16. C-terminal processing of reaction center protein D1 is essential for the function and assembly of photosystem II in Arabidopsis.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  17. Review
  18. Article
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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

2 authors at 1 institution in 1 country.

Kimiyuki SatohOkayama University, Okayama, 700-8530, Japan. kimiyuki@cc.okayama-u.ac.jp
Yumiko Yamamoto
Okayama University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The D1 protein, a key subunit of photosystem II reaction center, is synthesized as a precursor form with a carboxyl-terminal extension, in oxygenic photosynthetic organisms with some exceptions. This part of the protein is removed by the action of an endopeptidase, and the proteolytic processing is indispensable for the manifestation of oxygen-evolving activity in photosynthesis. The carboxyl-terminus of mature D1 protein, which appears upon the cleavage, has recently been demonstrated to be a ligand for a manganese atom in the Mn(4)Ca-cluster, which is responsible for the water oxidation chemistry in photosystem II, based on the isotope-edited Fourier transform infrared spectroscopy and the X-ray crystallography. On the other hand, the structure of a peptidase involved in the cleavage of precursor D1 protein has been resolved at a higher resolution, and the enzyme-substrate interactions have extensively been analyzed both in vivo and in vitro. The present article briefly summarizes the history of research and the present state of our knowledge on the carboxyl-terminal processing of precursor D1 protein in the photosystem II reaction center.

Indexed as

Protein Processing, Post-TranslationalModels, BiologicalPhotosynthetic Reaction Center Complex ProteinsPhotosystem II Protein ComplexProtein PrecursorsPhotosynthetic Reaction Center Complex ProteinsPhotosystem II Protein ComplexProtein Precursors

Identifiers

PMID17551844
OpenAlexW1980450707

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.