Evidence map›Paper›PMID 24184090›Full record

ArticleJournal of biotechnology2013

Do-it-yourself histidine-tagged bovine enterokinase: a handy member of the protein engineer's toolbox.

Wolfgang Skala, Peter Goettig, Hans Brandstetter

Open access · hybridAbstract read
In one paragraph

Article in Journal of biotechnology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.4field-weighted citation impact, top 13% 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

16 citing papers in PubMed, 34 citations in OpenAlex.

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  3. Molecular mechanisms controlling the biogenesis of the TGF-β signal Vg1.Proceedings of the National Academy of Sciences of the United States of America · 2023
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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 1 institution in 1 country.

Wolfgang SkalaDivision of Structural Biology, Department of Molecular Biology, University of Salzburg, Billrothstraße 11, 5020 Salzburg, Austria.
Peter Goettig
Hans Brandstetter
University of Salzburg · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enterokinase, a two-chain duodenal serine protease, activates trypsinogen by removing its N-terminal propeptide. Due to a clean cut after the non-primed site recognition sequence, the enterokinase light chain is frequently employed in biotechnology to separate N-terminal affinity tags from target proteins with authentic N-termini. In order to obtain large quantities of this protease, we adapted an in vitro folding protocol for a pentahistidine-tagged triple mutant of the bovine enterokinase light chain. The purified, highly active enzyme successfully processed recombinant target proteins, while the pentahistidine-tag facilitated post-cleavage removal. Hence, we conclude that producing enterokinase in one's own laboratory is an efficient alternative to the commercial enzyme.

Indexed as

Protein EngineeringAnimalsCattleCloning, MolecularEnteropeptidaseEscherichia coliHistidineInclusion BodiesProtein FoldingRecombinant ProteinsEnteropeptidaseHistidineRecombinant ProteinsBENACbenzamidine affinity chromatographyBiotechnologyEKenterokinaseEnteropeptidaseglutathione-S-transferaseGSTIBIECIMACInclusion bodiesinclusion bodyIn vitro foldingion exchange chromatographykallikrein-related peptidaseKLKmmobilized metal ion affinity chromatographySerine proteasessmall ubiquitin-like modifierSUMOTEVtobacco etch virusuPAurokinase-type plasminogen activator

Identifiers

PMID24184090
PMCPMC3863954
OpenAlexW2030101006

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.