Evidence map›Paper›PMID 39950263›Full record

ReviewWiley interdisciplinary reviews. Nanomedicine and nanobiotechnology

Spontaneous Self-Organized Order Emerging From Intrinsically Disordered Protein Polymers.

Sergio Acosta, Pablo Rodríguez-Alonso, Viktoriya Chaskovska, Julio Fernández-Fernández, José Carlos Rodríguez-Cabello

Abstract readReview
In one paragraph

Review in Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology. 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
–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

5 citing papers in PubMed.

  1. Article
  2. Article
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  5. 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

5 authors.

Sergio AcostaBioforge Lab (Group for Advanced Materials and Nanobiotechnology), Laboratory for Disruptive Interdisciplinary Science (LaDIS), CIBER-BBN, Edificio LUCIA, Universidad de Valladolid, Valladolid, Spain.ORCID 0000-0002-8175-6963
Pablo Rodríguez-AlonsoBioforge Lab (Group for Advanced Materials and Nanobiotechnology), Laboratory for Disruptive Interdisciplinary Science (LaDIS), CIBER-BBN, Edificio LUCIA, Universidad de Valladolid, Valladolid, Spain.
Viktoriya ChaskovskaBioforge Lab (Group for Advanced Materials and Nanobiotechnology), Laboratory for Disruptive Interdisciplinary Science (LaDIS), CIBER-BBN, Edificio LUCIA, Universidad de Valladolid, Valladolid, Spain.
Julio Fernández-FernándezBioforge Lab (Group for Advanced Materials and Nanobiotechnology), Laboratory for Disruptive Interdisciplinary Science (LaDIS), CIBER-BBN, Edificio LUCIA, Universidad de Valladolid, Valladolid, Spain.
José Carlos Rodríguez-CabelloBioforge Lab (Group for Advanced Materials and Nanobiotechnology), Laboratory for Disruptive Interdisciplinary Science (LaDIS), CIBER-BBN, Edificio LUCIA, Universidad de Valladolid, Valladolid, Spain.ORCID 0000-0002-3438-858X

Funding

Banco SantanderCentro en Red de Medicina Regenerativa y Terapia Celular de Castilla y LeónDepartment of Education, la Junta de Castilla y León CLU-2023-1-05Department of Education, la Junta de Castilla y León VA188P23ERDF, EUESF+, EUEuropean Commission H2020-MSCA-ITN-2020-956621-BioBased ValueCircleEuropean Commission HORIZON-CL4-2022-RESILIENCE-01-13-101091766-ELR-SCARGovernment of Spain MCIN/AEI/10.13039/501100011033Government of Spain PID2021-122444OB-100Government of Spain PID2022-137484OB-I00
6 · The paper itself

Abstract

Intrinsically disordered proteins (IDPs) are proteins that, despite lacking a defined 3D structure, are capable of adopting dynamic conformations. This structural adaptability allows them to play not only essential roles in crucial cellular processes, such as subcellular organization or transcriptional control, but also in coordinating the assembly of macromolecules during different stages of development. Thus, in order to artificially replicate the complex processes of morphogenesis and their dynamics, it is crucial to have materials that recapitulate the structural plasticity of IDPs. In this regard, intrinsically disordered protein polymers (IDPPs) emerge as promising materials for engineering synthetic condensates and creating hierarchically self-assembled materials. IDPPs exhibit remarkable properties for their use in biofabrication, such as functional versatility, tunable sequence order-disorder, and the ability to undergo liquid-liquid phase separation (LLPS). Recent research has focused on harnessing the intrinsic disorder of IDPPs to design complex protein architectures with tailored properties. Taking advantage of their stimuli-responsiveness and degree of disorder, researchers have developed innovative strategies to control the self-assembly of IDPPs, resulting in the creation of hierarchically organized structures and intricate morphologies. In this review, we aim to provide an overview of the latest advances in the design and application of IDPP-based materials, shedding light on the fundamental principles that control their supramolecular assembly, and discussing their application in the biomedical and nanobiotechnological fields.

Indexed as

Intrinsically Disordered ProteinsPolymersAnimalsHumansIntrinsically Disordered ProteinsPolymerscomplex morphogenesiselastin‐like recombinamersintrinsically disordered proteinsliquid–liquid phase separationresilin‐like recombinamers

Identifiers

PMID39950263
PMCPMC11826379

What OpenQuestion holds

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Registered trials

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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.