Evidence map›Paper›PMID 39465903›Full record

ReviewProtein science : a publication of the Protein Society2024

Diversity and structural-functional insights of alpha-solenoid proteins.

Paula Nazarena Arrías, Zarifa Osmanli, Estefanía Peralta, Patricio Manuel Chinestrad, Alexander Miguel Monzon, Silvio C E Tosatto

Abstract readReview
In one paragraph

Review in Protein science : a publication of the Protein Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
–field-weighted citation impact
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

9 citing papers in PubMed.

  1. Article
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  6. Review
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  8. Article
  9. Diversity and structural-functional insights of alpha-solenoid proteins.Protein science : a publication of the Protein Society · 2024
    Review
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.

Paula Nazarena ArríasDepartment of Biomedical Sciences, University of Padova, Padova, Italy.ORCID 0000-0001-5668-768X
Zarifa OsmanliDepartment of Biomedical Sciences, University of Padova, Padova, Italy.ORCID 0000-0003-2460-1989
Estefanía PeraltaLaboratorio de Investigación y Desarrollo de Bioactivos (LIDeB), Departamento de Ciencias Biológicas, Facultad de Ciencias Exactas, Universidad Nacional de La Plata, La Plata, Buenos Aires, Argentina.
Patricio Manuel ChinestradLaboratorio de Farmacología Molecular, Universidad Nacional de Quilmes, Bernal, Buenos Aires, Argentina.
Alexander Miguel MonzonDepartment of Information Engineering, University of Padova, Padova, Italy.ORCID 0000-0003-0362-8218
Silvio C E TosattoDepartment of Biomedical Sciences, University of Padova, Padova, Italy.ORCID 0000-0003-4525-7793

Funding

European Cooperation in Science and TechnologyEuropean Union's Horizon 2020 823886 (H2020 MSCA-RISE "REFRACT")
6 · The paper itself

Abstract

Alpha-solenoids are a significant and diverse subset of structured tandem repeat proteins (STRPs) that are important in various domains of life. This review examines their structural and functional diversity and highlights their role in critical cellular processes such as signaling, apoptosis, and transcriptional regulation. Alpha-solenoids can be classified into three geometric folds: low curvature, high curvature, and corkscrew, as well as eight subfolds: ankyrin repeats; Huntingtin, elongation factor 3, protein phosphatase 2A, and target of rapamycin; armadillo repeats; tetratricopeptide repeats; pentatricopeptide repeats; Pumilio repeats; transcription activator-like; and Sel-1 and Sel-1-like repeats. These subfolds represent distinct protein families with unique structural properties and functions, highlighting the versatility of alpha-solenoids. The review also discusses their association with disease, highlighting their potential as therapeutic targets and their role in protein design. Advances in state-of-the-art structure prediction methods provide new opportunities and challenges in the functional characterization and classification of this kind of fold, emphasizing the need for continued development of methods for their identification and proper data curation and deposition in the main databases.

Indexed as

Models, MolecularAnimalsHumansProteinsProteinsalpha‐solenoidsankyrinsarmadillo repeatsHEATstructured tandem repeatstandem repeat classificationTPR repeats

Identifiers

PMID39465903
PMCPMC11514114

What OpenQuestion holds

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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.