Evidence map›Paper›PMID 37628689›Full record

ArticleGenes2023

Exploring the Binding Affinity of the ARR2 GARP DNA Binding Domain via Comparative Methods.

Janine Rieger, Michael Fitz, Stefan Markus Fischer, Niklas Wallmeroth, Hector Flores-Romero, Nina Monika Fischer, Luise Helene Brand, Ana J García-Sáez, Kenneth Wayne Berendzen, Virtudes Mira-Rodado

Open access · goldAbstract read
In one paragraph

Article in Genes, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.4field-weighted citation impact, top 23% 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

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. Article
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

10 authors at 2 institutions in 1 country.

Janine RiegerCenter for Plant Molecular Biology (ZMBP), Tübingen University, 72076 Tübingen, Germany.
Michael FitzCenter for Plant Molecular Biology (ZMBP), Tübingen University, 72076 Tübingen, Germany.
Stefan Markus FischerCenter for Plant Molecular Biology (ZMBP), Tübingen University, 72076 Tübingen, Germany.ORCID 0000-0003-0096-4961
Niklas WallmerothCenter for Plant Molecular Biology (ZMBP), Tübingen University, 72076 Tübingen, Germany.
Hector Flores-RomeroInterfaculty Institute of Biochemistry (IFIB), Tübingen University, 72076 Tübingen, Germany.ORCID 0000-0003-0996-5717
Nina Monika FischerInstitute for Bioinformatics and Medical Informatics, Tübingen University, 72076 Tübingen, Germany.
Luise Helene BrandCenter for Plant Molecular Biology (ZMBP), Tübingen University, 72076 Tübingen, Germany.
Ana J García-SáezInterfaculty Institute of Biochemistry (IFIB), Tübingen University, 72076 Tübingen, Germany.ORCID 0000-0002-3894-5945
Kenneth Wayne BerendzenCenter for Plant Molecular Biology (ZMBP), Tübingen University, 72076 Tübingen, Germany.ORCID 0000-0001-9870-6164
Virtudes Mira-RodadoCenter for Plant Molecular Biology (ZMBP), Tübingen University, 72076 Tübingen, Germany.
University of Tübingen · DECologne Excellence Cluster on Cellular Stress Responses in Aging Associated Diseases · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plants have evolved signaling mechanisms such as the multi-step phosphorelay (MSP) to respond to different internal and external stimuli. MSP responses often result in gene transcription regulation that is modulated through transcription factors such as B-type Arabidopsis response regulator (ARR) proteins. Among these proteins, ARR2 is a key component that is expressed ubiquitously and is involved in many aspects of plant development. Although it has been noted that B-type ARRs bind to their cognate genes through a DNA-binding domain termed the GARP domain, little is known about the structure and function of this type of DNA-binding domain; thus, how ARRs bind to DNA at a structural level is still poorly understood. In order to understand how the MSP functions in planta, it is crucial to unravel both the kinetics as well as the structural identity of the components involved in such interactions. For this reason, this work focusses on resolving how the GARP domain of ARR2 (GARP2) binds to the promoter region of

Indexed as

ArabidopsisEnzyme-Linked Immunosorbent AssayKineticsMutationPlant DevelopmentARR2DPI-ELISAFCSGARPMSTreporter genestructural modelingtranscription factor

Identifiers

PMID37628689
PMCPMC10454580
OpenAlexW4385949088

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.