Evidence map›Paper›PMID 26325592›Full record

ReviewFEBS letters2015

Elastin-like polypeptides as models of intrinsically disordered proteins.

Stefan Roberts, Michael Dzuricky, Ashutosh Chilkoti

Open access · bronzeAbstract readReview
In one paragraph

Review in FEBS letters, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 122 papers.

0numbers the graph read from it
0cells of the map it votes in
122citing papers in PubMed
10.4field-weighted citation impact, top 1% 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

122 citing papers in PubMed, 310 citations in OpenAlex.

  1. Article
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  15. Engineered Hydrogels for Organoid Models of Human Nonalcoholic Fatty Liver Disease.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  16. Review
  17. A Novel Gene Synthesis Platform for Designing Functional Protein Polymers.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  18. Article
  19. Article
  20. Review

62 more citing papers are in PubMed but not listed here.

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.

Stefan RobertsDuke University, Durham, NC, United States.
Michael DzurickyDuke University, Durham, NC, United States. Electronic address: mjd46@duke.edu.
Ashutosh ChilkotiDuke University, Durham, NC, 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

Elastin-like polypeptides (ELPs) are a class of stimuli-responsive biopolymers inspired by the intrinsically disordered domains of tropoelastin that are composed of repeats of the VPGXG pentapeptide motif, where X is a "guest residue". They undergo a reversible, thermally triggered lower critical solution temperature (LCST) phase transition, which has been utilized for a variety of applications including protein purification, affinity capture, immunoassays, and drug delivery. ELPs have been extensively studied as protein polymers and as biomaterials, but their relationship to other disordered proteins has heretofore not been established. The biophysical properties of ELPs that lend them their unique material behavior are similar to the properties of many intrinsically disordered proteins (IDP). Their low sequence complexity, phase behavior, and elastic properties make them an interesting "minimal" artificial IDP, and the study of ELPs can hence provide insights into the behavior of other more complex IDPs. Motivated by this emerging realization of the similarities between ELPs and IDPs, this review discusses the biophysical properties of ELPs, their biomedical utility, and their relationship to other disordered polypeptide sequences.

Indexed as

Transition TemperatureAmino Acid SequenceElastinHumansHydrophobic and Hydrophilic InteractionsIntrinsically Disordered ProteinsModels, ChemicalModels, MolecularPeptidesProtein ConformationElastinIntrinsically Disordered ProteinsPeptidesBiopolymerElastin-like polypeptideIntrinsically disordered proteinPhase transitionProtein engineeringTandem repeat

Identifiers

PMID26325592
PMCPMC4599720
OpenAlexW1823263094

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.