Evidence map›Paper›PMID 32902806›Full record

ArticleCell stress & chaperones2021

Towards an understanding of the role of intrinsic protein disorder on plant adaptation to environmental challenges.

Jesús Alejandro Zamora-Briseño, Alejandro Pereira-Santana, Sandi Julissa Reyes-Hernández, Daniel Cerqueda-García, Enrique Castaño, Luis Carlos Rodríguez-Zapata

Open access · greenAbstract read
In one paragraph

Article in Cell stress & chaperones, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

10 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. The Analysis ofCurrent issues in molecular biology · 2025
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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 3 institutions in 2 countries.

Jesús Alejandro Zamora-BriseñoUnidad de Biotecnología, Centro de Investigación Científica de Yucatán, Calle 43, Número 130, Chuburná de Hidalgo, C.P. 97205, Mérida, Yucatán, México.
Alejandro Pereira-SantanaDivisión de Biotecnología Industrial, Centro de Investigación y Asistencia en Tecnología y Diseño del estado de Jalisco, Camino Arenero 1227, El Bajio, C.P. 45019, Zapopan, Jalisco, México.
Sandi Julissa Reyes-HernándezUnidad de Biotecnología, Centro de Investigación Científica de Yucatán, Calle 43, Número 130, Chuburná de Hidalgo, C.P. 97205, Mérida, Yucatán, México.
Daniel Cerqueda-GarcíaDepartamento de Recursos del Mar, Centro de Investigación y de Estudios Avanzados del Instituto Politécnico Nacional- Unidad Mérida, Carr. Mérida - Progreso, colonia Loma Bonita, C.P. 97205, Mérida, Yucatán, México.
Enrique CastañoUnidad de Bioquímica y Biología Molecular de Plantas, Centro de Investigación Científica de Yucatán, Calle 43, Número 130, Chuburná de Hidalgo, C.P. 97205, Mérida, Yucatán, México.
Luis Carlos Rodríguez-ZapataUnidad de Biotecnología, Centro de Investigación Científica de Yucatán, Calle 43, Número 130, Chuburná de Hidalgo, C.P. 97205, Mérida, Yucatán, México. lcrz@cicy.mx.
Secretaría de Investigación, Innovación y Educación Superior · MXCentro de Investigación y Asistencia en Tecnología y Diseño del Estado de JaliscoInstituto Politécnico Nacional · MX

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Intrinsic protein disorder is an interesting structural feature where fully functional proteins lack a three-dimensional structure in solution. In this work, we estimated the relative content of intrinsic protein disorder in 96 plant proteomes including monocots and eudicots. In this analysis, we found variation in the relative abundance of intrinsic protein disorder among these major clades; the relative level of disorder is higher in monocots than eudicots. In turn, there is an inverse relationship between the degree of intrinsic protein disorder and protein length, with smaller proteins being more disordered. The relative abundance of amino acids depends on intrinsic disorder and also varies among clades. Within the nucleus, intrinsically disordered proteins are more abundant than ordered proteins. Intrinsically disordered proteins are specialized in regulatory functions, nucleic acid binding, RNA processing, and in response to environmental stimuli. The implications of this on plants' responses to their environment are discussed.

Indexed as

Adaptation, PhysiologicalDatabases, ProteinIntrinsically Disordered ProteinsPlant Physiological PhenomenaPlant ProteinsPlantsProtein Interaction MapsStress, PhysiologicalIntrinsically Disordered ProteinsPlant ProteinsEudicotsIntrinsic disorderMonocotsNucleusStress

Identifiers

PMID32902806
PMCPMC7736417
OpenAlexW3084773400

What Socratic 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 Socratic graph.