Evidence map›Paper›PMID 29683665›Full record

ArticleBiochemistry2018

Convergence of Artificial Protein Polymers and Intrinsically Disordered Proteins.

Michael Dzuricky, Stefan Roberts, Ashutosh Chilkoti

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

41 citing papers in PubMed, 88 citations in OpenAlex.

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  13. Contribution of the ELRs to the development of advancedFrontiers in bioengineering and biotechnology · 2024
    Review
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  20. Protein Based Biomaterials for Therapeutic and Diagnostic Applications.Progress in biomedical engineering (Bristol, England) · 2022
    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

3 authors at 1 institution in 1 country.

Michael DzurickyDepartment of Biomedical Engineering , Duke University , Durham , North Carolina 27708-0281 , United States.ORCID http://orcid.org/0000-0002-1775-2132
Stefan RobertsDepartment of Biomedical Engineering , Duke University , Durham , North Carolina 27708-0281 , United States.
Ashutosh ChilkotiDepartment of Biomedical Engineering , Duke University , Durham , North Carolina 27708-0281 , United States.
Duke University · US

Funding

ELASTIN FUSION PROTEINSR01GM061232 · NIGMS · DUKE UNIVERSITY · PI CHILKOTI, ASHUTOSH · 2000 to 2017
$4.6M
NIGMS NIH HHS R01 GM061232
6 · The paper itself

Abstract

A flurry of research in recent years has revealed the molecular origins of many membraneless organelles to be the liquid phase separation of intrinsically disordered proteins (IDPs). Consequently, protein disorder has emerged as an important driver of intracellular compartmentalization by providing specialized microenvironments chemically distinct from the surrounding medium. Though the importance of protein disorder and its relationship to intracellular phase behavior are clear, a detailed understanding of how such phase behavior can be predicted and controlled remains elusive. While research in IDPs has largely focused on the implications of structural disorder on cellular function and disease, another field, that of artificial protein polymers, has focused on the de novo design of protein polymers with controllable material properties. A subset of these polymers, specifically those derived from structural proteins such as elastin and resilin, are also disordered sequences that undergo liquid-liquid phase separation. This phase separation has been used in a variety of biomedical applications, and researchers studying these polymers have developed methods to precisely characterize and tune their phase behavior. Despite their disparate origins, both fields are complementary as they study the phase behavior of intrinsically disordered polypeptides. This Perspective hopes to stimulate collaborative efforts by highlighting the similarities between these two fields and by providing examples of how such collaboration could be mutually beneficial.

Indexed as

Cell CompartmentationCell MembraneCellular MicroenvironmentElastinHumansInsect ProteinsIntrinsically Disordered ProteinsOrganellesPeptidesPolymersProtein ConformationElastinInsect ProteinsIntrinsically Disordered ProteinsPeptidesPolymersresilin

Identifiers

PMID29683665
PMCPMC6311704
OpenAlexW2801628171

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.