Evidence map›Paper›PMID 29091276›Full record

ArticleCurrent protocols in protein science2017

Simple and Efficient Purification of Recombinant Proteins Using the Heparin-Binding Affinity Tag.

Srinivas Jayanthi, Ravi Kumar Gundampati, Thallapuranam Krishnaswamy Suresh Kumar

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Current protocols in protein science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.4field-weighted citation impact, top 40% 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

2 citing papers in PubMed, 9 citations in OpenAlex.

  1. Review
  2. New tools for recombinant protein production in Escherichia coli: A 5-year update.Protein science : a publication of the Protein Society · 2019
    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

3 authors at 1 institution in 1 country.

Srinivas JayanthiDepartment of Chemistry and Biochemistry, University of Arkansas, Fayetteville, Arkansas.
Ravi Kumar GundampatiDepartment of Chemistry and Biochemistry, University of Arkansas, Fayetteville, Arkansas.
Thallapuranam Krishnaswamy Suresh KumarDepartment of Chemistry and Biochemistry, University of Arkansas, Fayetteville, Arkansas.
University of Arkansas at Fayetteville · US

Funding

Structure based drug discoveryP20RR015569 · NCRR · UNIVERSITY OF ARKANSAS AT FAYETTEVILLE · PI MILLETT, FRANCIS S · 2000 to 2009
$21.4M
Center for Protein Structure and FunctionP30GM103450 · NIGMS · UNIVERSITY OF ARKANSAS AT FAYETTEVILLE · PI MILLETT, FRANCIS S · 2012 to 2014
$3.2M
NCRR NIH HHS P20 RR015569NIGMS NIH HHS P30 GM103450
6 · The paper itself

Abstract

Heparin, a member of the glycosaminoglycan family, is known to interact with more than 400 different types of proteins. For the past few decades, significant progress has been made to understand the molecular details involved in heparin-protein interactions. Based on the structural knowledge available from the FGF1-heparin interaction studies, we have designed a novel heparin-binding peptide (HBP) affinity tag that can be used for the simple, efficient, and cost-effective purification of recombinant proteins of interest. HBP-tagged fusion proteins can be purified by heparin Sepharose affinity chromatography using a simple sodium chloride gradient to elute the bound fusion protein. In addition, owing to the high density of positive charges on the HBP tag, recombinant target proteins are preferably expressed in their soluble forms. The purification of HBP-fusion proteins can also be achieved in the presence of chemical denaturants, including urea. Additionally, polyclonal antibodies raised against the affinity tag can be used to detect HBP-fused target proteins with high sensitivity. © 2017 by John Wiley & Sons, Inc.

Indexed as

Amino Acid SequenceAntimicrobial Cationic PeptidesBlood ProteinsCarrier ProteinsChromatography, AffinityChromatography, AgaroseCloning, MolecularEscherichia coliGene ExpressionGenetic VectorsRecombinant Fusion ProteinsSepharoseSodium ChlorideAntimicrobial Cationic PeptidesAZU1 protein, humanBlood ProteinsCarrier Proteinsheparin-sepharoseRecombinant Fusion ProteinsSepharoseSodium Chlorideaffinity chromatographyfusion tagheparin sepharoserecombinant proteinresin

Identifiers

PMID29091276
PMCPMC5710805
OpenAlexW2765800033

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.