Evidence map›Paper›PMID 24961229›Full record

ArticleJournal of visualized experiments : JoVE2014

Non-chromatographic purification of recombinant elastin-like polypeptides and their fusions with peptides and proteins from Escherichia coli.

Sarah R MacEwan, Wafa Hassouneh, Ashutosh Chilkoti

Abstract readVideo-Audio Media
In one paragraph

Article in Journal of visualized experiments : JoVE, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

34 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
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  3. A Novel Gene Synthesis Platform for Designing Functional Protein Polymers.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 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

3 authors at 2 institutions in 1 country.

Sarah R MacEwanDepartment of Biomedical Engineering, Duke University; Research Triangle MRSEC, Duke University.
Wafa HassounehDepartment of Biomedical Engineering, Duke University; Research Triangle MRSEC, Duke University.
Ashutosh ChilkotiDepartment of Biomedical Engineering, Duke University; Research Triangle MRSEC, Duke University; chilkoti@duke.edu.
Research Triangle Park Foundation · USDuke University · US

Funding

Thermally Triggered Multivalent Targeting of TumorsR01EB007205 · NIBIB · DUKE UNIVERSITY · PI CHILKOTI, ASHUTOSH · 2007 to 2015
$2.7M
NIBIB NIH HHS R01 EB007205
6 · The paper itself

Abstract

Elastin-like polypeptides are repetitive biopolymers that exhibit a lower critical solution temperature phase transition behavior, existing as soluble unimers below a characteristic transition temperature and aggregating into micron-scale coacervates above their transition temperature. The design of elastin-like polypeptides at the genetic level permits precise control of their sequence and length, which dictates their thermal properties. Elastin-like polypeptides are used in a variety of applications including biosensing, tissue engineering, and drug delivery, where the transition temperature and biopolymer architecture of the ELP can be tuned for the specific application of interest. Furthermore, the lower critical solution temperature phase transition behavior of elastin-like polypeptides allows their purification by their thermal response, such that their selective coacervation and resolubilization allows the removal of both soluble and insoluble contaminants following expression in Escherichia coli. This approach can be used for the purification of elastin-like polypeptides alone or as a purification tool for peptide or protein fusions where recombinant peptides or proteins genetically appended to elastin-like polypeptide tags can be purified without chromatography. This protocol describes the purification of elastin-like polypeptides and their peptide or protein fusions and discusses basic characterization techniques to assess the thermal behavior of pure elastin-like polypeptide products.

Indexed as

ElastinEscherichia coliPeptidesProteinsRecombinant Fusion ProteinsElastinPeptidesProteinsRecombinant Fusion Proteins

Identifiers

PMID24961229
PMCPMC4188175
OpenAlexW2030257456

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.