Evidence map›Paper›PMID 34971616›Full record

ArticleBiophysical journal2022

Protein dynamics and lipid affinity of monomeric, zeaxanthin-binding LHCII in thylakoid membranes.

Fatemeh Azadi-Chegeni, Sebastian Thallmair, Meaghan E Ward, Giorgio Perin, Siewert J Marrink, Marc Baldus, Tomas Morosinotto, Anjali Pandit

Open access · bronzeAbstract read
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Article in Biophysical journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

5 citing papers in PubMed, 17 citations in OpenAlex.

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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

8 authors at 4 institutions in 3 countries.

Fatemeh Azadi-ChegeniLeiden Institute of Chemistry, Department of Solid-State NMR, Leiden University, Leiden, the Netherlands.
Sebastian ThallmairGroningen Biomolecular Sciences and Biotechnology Institute and Zernike Institute for Advanced Materials, University of Groningen, Groningen, the Netherlands; Frankfurt Institute for Advanced Studies, Frankfurt am Main, Germany.
Meaghan E WardNMR Spectroscopy, Bijvoet Center for Biomolecular Research, Utrecht University, Utrecht, the Netherlands.
Giorgio PerinDepartment of Biology, University of Padua, Padua, Italy.
Siewert J MarrinkGroningen Biomolecular Sciences and Biotechnology Institute and Zernike Institute for Advanced Materials, University of Groningen, Groningen, the Netherlands.
Marc BaldusNMR Spectroscopy, Bijvoet Center for Biomolecular Research, Utrecht University, Utrecht, the Netherlands.
Tomas MorosinottoDepartment of Biology, University of Padua, Padua, Italy.
Anjali PanditLeiden Institute of Chemistry, Department of Solid-State NMR, Leiden University, Leiden, the Netherlands. Electronic address: a.pandit@chem.leidenuniv.nl.
Leiden University · NLUniversity of Groningen · NLUniversity of Padua · ITUtrecht University · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The xanthophyll cycle in the antenna of photosynthetic organisms under light stress is one of the most well-known processes in photosynthesis, but its role is not well understood. In the xanthophyll cycle, violaxanthin (Vio) is reversibly transformed to zeaxanthin (Zea) that occupies Vio binding sites of light-harvesting antenna proteins. Higher monomer/trimer ratios of the most abundant light-harvesting protein, the light-harvesting complex II (LHCII), usually occur in Zea accumulating membranes and have been observed in plants after prolonged illumination and during high-light acclimation. We present a combined NMR and coarse-grained simulation study on monomeric LHCII from the npq2 mutant that constitutively binds Zea in the Vio binding pocket. LHCII was isolated from

Indexed as

Light-Harvesting Protein ComplexesThylakoidsPhotosynthesisPhotosystem II Protein ComplexProteinsZeaxanthinsLight-Harvesting Protein ComplexesPhotosystem II Protein ComplexProteinsZeaxanthins

Identifiers

PMID34971616
PMCPMC8822613
OpenAlexW4200162586

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.