Evidence map›Paper›PMID 37291396›Full record

ArticleNature plants2023

The structure of Arabidopsis phytochrome A reveals topological and functional diversification among the plant photoreceptor isoforms.

E Sethe Burgie, Hua Li, Zira T K Gannam, Katrice E McLoughlin, Richard D Vierstra, Huilin Li

Open access · greenAbstract read
In one paragraph

Article in Nature plants, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
9.1field-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

11 citing papers in PubMed, 23 citations in OpenAlex.

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  7. Review of protein structure-based analyses that illuminate plant stress mechanisms.Computational and structural biotechnology journal · 2025
    Review
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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

6 authors at 2 institutions in 2 countries.

E Sethe Burgie *Department of Biology, Washington University in St. Louis, St. Louis, MO, USA.ORCID http://orcid.org/0000-0002-6520-9126
Hua Li *Department of Structural Biology, Van Andel Institute, Grand Rapids, MI, USA.
Zira T K Gannam *Department of Biology, Washington University in St. Louis, St. Louis, MO, USA.
Katrice E McLoughlinDepartment of Biology, Washington University in St. Louis, St. Louis, MO, USA.
Richard D VierstraDepartment of Biology, Washington University in St. Louis, St. Louis, MO, USA. rdvierstra@wustl.edu.ORCID http://orcid.org/0000-0003-0210-3516
Huilin LiDepartment of Structural Biology, Van Andel Institute, Grand Rapids, MI, USA. Huilin.Li@vai.org.ORCID http://orcid.org/0000-0001-8085-8928
Washington University in St. Louis · USVan Andel Institute · US

Funding

Structural mechanism of DNA replicationR35GM131754 · NIGMS · VAN ANDEL RESEARCH INSTITUTE · PI Huilin Li · 2019 to 2026
$6.0M
Phytochromes: Structural Perspectives on Photoactivation and SignalingR01GM127892 · NIGMS · WASHINGTON UNIVERSITY · PI JEZ, JOSEPH MARTIN · 2018 to 2025
$2.5M
NIGMS NIH HHS R01 GM127892NIGMS NIH HHS R35 GM131754
6 · The paper itself

Abstract

Plants employ a divergent cohort of phytochrome (Phy) photoreceptors to govern many aspects of morphogenesis through reversible photointerconversion between inactive Pr and active Pfr conformers. The two most influential are PhyA whose retention of Pfr enables sensation of dim light, while the relative instability of Pfr for PhyB makes it better suited for detecting full sun and temperature. To better understand these contrasts, we solved, by cryo-electron microscopy, the three-dimensional structure of full-length PhyA as Pr. Like PhyB, PhyA dimerizes through head-to-head assembly of its C-terminal histidine kinase-related domains (HKRDs), while the remainder assembles as a head-to-tail light-responsive platform. Whereas the platform and HKRDs associate asymmetrically in PhyB dimers, these lopsided connections are absent in PhyA. Analysis of truncation and site-directed mutants revealed that this decoupling and altered platform assembly have functional consequences for Pfr stability of PhyA and highlights how plant Phy structural diversification has extended light and temperature perception.

Indexed as

ArabidopsisArabidopsis ProteinsPhytochromeCryoelectron MicroscopyLightPhotoreceptors, PlantPhytochrome APhytochrome BPlantsProtein IsoformsArabidopsis ProteinsPhotoreceptors, PlantPHYA protein, ArabidopsisPhytochromePhytochrome APhytochrome BProtein Isoforms

Identifiers

PMID37291396
PMCPMC10546791
OpenAlexW4379875449

What OpenQuestion holds

Textmetadata
LicenceTDM
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.