Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Engineering soluble tobacco etch virus protease accompanies the loss of stability.

Protein expression and purification - 1 Nov 2013

Fang Jie, Chen Ling, Cheng Beijiu, Fan Jun

Abstract excerpt

Tobacco etch virus protease (TEVp) is a widely used tool enzyme in biological studies. To improve the solubility of recombinant TEVp, three variants, including the double mutant (L56V/S135G), the triple mutant (T17S/N68D/I77V), and the quintuple mutant (T17S/L56V/N68D/I77V/S135G), have been developed, however, with little information on functional stability. Here we investigated the solubility and stability of...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Endopeptidases
Share to Escherichia coli
Share to Molecular Chaperones

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Nicotiana

Share to Protein Engineering

Share to Protein Stability

Share to Recombinant Fusion Proteins

Share to Solubility

Source

Identifiers

PMID: 24012464
DOI: 10.1016/j.pep.2013.08.015

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Engineering soluble tobacco etch virus protease accompanies the loss of stability.PMID 24012464Read ↗

Combination of the mutations for improving activity of TEV protease in inclusion bodies.Semantic proximity Read ↗

Construction, Investigation and Application of TEV Protease Variants with Improved Oxidative Stability.Semantic proximity Read ↗

In vivo and in vitro characterization of TEV protease mutants.Semantic proximity Read ↗

An improved variant of tobacco etch virus (TEV) protease that does not need reducing agents.Semantic proximity Read ↗

Tobacco etch virus (TEV) protease with multiple mutations to improve solubility and reduce self-cleavage exhibits enhanced enzymatic activity.Semantic proximity Read ↗

Enhancing the stability and solubility of TEV protease using in silico design.Semantic proximity Read ↗

P1' specificity of the S219V/R203G mutant tobacco etch virus protease.Semantic proximity Read ↗

Insight into the structural stability of wild type and mutants of the tobacco etch virus protease with molecular dynamics simulations.Semantic proximity Read ↗

Improved solubility of TEV protease by directed evolutionSemantic proximity Read ↗

Engineered tobacco etch virus (TEV) protease active in the secretory pathway of mammalian cells.Semantic proximity Read ↗

Tobacco etch virus protease: mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency.Semantic proximity Read ↗

[Tobacco etch virus proteinase: crystal structure of the active enzyme and its inactive mutant].Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.