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

Functional expression on bacteriophage of the mustard trypsin inhibitor MTI-2.

Biochemical and biophysical research communications - 26 Jan 2001

Volpicella M, Ceci L R, Gallerani R, Jongsma M A, Beekwilder J

Abstract excerpt

The mustard trypsin inhibitor MTI-2 is a potential tool in the study of interactions between pest insects and plants. It can be applied to study the adaptations of digestive proteases in pest insects. Phage display allows a rapid and exhaustive system for the selection of heterologous protein variants with novel specificities. Here we describe a bacteriophage expression system which permits functional expression...

Read the complete abstract on PubMed

Topics

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

Share to DNA Primers
Share to Mustard Plant
Share to Peptide Library

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Pichia

Share to Plant Proteins

Share to Plants, Medicinal

Share to Protein Engineering

Share to Trypsin Inhibitors

Source

Identifiers

PMID: 11162593
DOI: 10.1006/bbrc.2000.4182

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

Functional expression on bacteriophage of the mustard trypsin inhibitor MTI-2.PMID 11162593Read ↗

Analysis by phage display selection and site-directed retromutagenesis of the Mustard Trypsin Inhibitor 2 reactive site.Semantic proximity Read ↗

Selection for protease inhibitors using bacteriophage display.Semantic proximity Read ↗

Phage display of proteases and macromolecular inhibitors.Semantic proximity Read ↗

A versatile inhibitor of digestive enzymes in Aedes aegypti larvae selected from a pacifastin (TiPI) phage display library.Semantic proximity Read ↗

Selection of potent chymotrypsin and elastase inhibitors from M13 phage library of basic pancreatic trypsin inhibitor (BPTI).Semantic proximity Read ↗

Validation of phage display method for protease inhibitor selection using synthetic hybrid peptides.Semantic proximity Read ↗

Selective inhibitors of digestive enzymes from Aedes aegypti larvae identified by phage display.Semantic proximity Read ↗

Reliable titration of filamentous bacteriophages independent of pIII fusion moiety and genome size by using trypsin to restore wild-type pIII phenotype.Semantic proximity Read ↗

Heterogeneous catalysis on the phage surface: Display of active human enteropeptidase.Semantic proximity Read ↗

A Kunitz trypsin inhibitor gene family from trembling aspen (Populus tremuloides Michx.): cloning, functional expression, and induction by wounding and herbivory.Semantic proximity Read ↗

Phage display of tissue inhibitor of metalloproteinases-2 (TIMP-2): identification of selective inhibitors of collagenase-1 (metalloproteinase 1 (MMP-1)).Semantic proximity Read ↗

Crystal structure of the bacteriophage P2 integrase catalytic domain.Semantic proximity Read ↗

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