Evidence map›Paper›PMID 18709440›Full record

ReviewPhotosynthesis research

D1-protein dynamics in photosystem II: the lingering enigma.

Marvin Edelman, Autar K Mattoo

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 82 papers.

0numbers the graph read from it
0cells of the map it votes in
82citing papers in PubMed
5.5field-weighted citation impact, top 3% 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

82 citing papers in PubMed, 201 citations in OpenAlex.

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22 more citing papers are in PubMed but not listed here.

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 2 institutions in 2 countries.

Marvin EdelmanDepartment of Plant Sciences, The Weizmann Institute of Science, Rehovot, Israel. marvin.edelman@weizmann.ac.il
Autar K Mattoo
United States Department of Agriculture · USWeizmann Institute of Science · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The D1/D2 heterodimer core is the heart of the photosystem II reaction center. A characteristic feature of this heterodimer is the differentially rapid, light-dependent degradation of the D1 protein. The D1 protein is possibly the most researched photosynthetic polypeptide, with aspects of structure-function, gene, messenger and protein regulation, electron transport, reactive oxygen species, photoinhibition, herbicide binding, stromal-granal translocations, reversible phosphorylation, and specific proteases, all under intensive investigation more than three decades after the protein's debut in the literature. This review will touch on some treaded areas of D1 research that have, so far, defied clear resolution, as well as cutting edge research on mechanisms and consequences of D1 protein degradation.

Indexed as

Peptide HydrolasesPhosphorylationPhotonsPhotosynthesisPhotosystem II Protein ComplexSinglet OxygenPeptide HydrolasesPhotosystem II Protein ComplexSinglet Oxygen

Identifiers

PMID18709440
OpenAlexW1989805009

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.