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

Engineered eglin c variants inhibit yeast and human proprotein processing proteases, Kex2 and furin.

Biochemistry - 12 Dec 2000

Komiyama T, Fuller R S

Abstract excerpt

We engineered eglin c, a potent subtilisin inhibitor, to create inhibitors for enzymes of the Kex2/furin family of proprotein processing proteases. A structural gene was synthesized that encoded "R(1)-eglin", having Arg at P(1) in the reactive site loop in place of Leu(45). Ten additional variants were created by cassette mutagenesis of R(1)-eglin. These polypeptides were expressed in Escherichia coli, purified...

Read the complete abstract on PubMed

Topics

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

Share to Furin
Share to Models, Chemical
Share to Proprotein Convertases

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Protein Engineering

Share to Protein Precursors

Share to Protein Processing, Post-Translational

Share to Serpins

Share to Subtilisins

Source

Identifiers

PMID: 11106495
DOI: 10.1021/bi001907c

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Engineered eglin c variants inhibit yeast and human proprotein processing proteases, Kex2 and furin.PMID 11106495Read ↗

Comparative study of the binding pockets of mammalian proprotein convertases and its implications for the design of specific small molecule inhibitors.Semantic proximity Read ↗

Furin: a mammalian subtilisin/Kex2p-like endoprotease involved in processing of a wide variety of precursor proteins.Semantic proximity Read ↗

Plasticity of extended subsites facilitates divergent substrate recognition by Kex2 and furin.Semantic proximity Read ↗

Curbing activation: proprotein convertases in homeostasis and pathologySemantic proximity Read ↗

Disruption of the KEX1 gene inPichia pastoris allows expression of full-length murine and human endostatinSemantic proximity Read ↗

Mouse Models of Human Proprotein Convertase InsufficiencySemantic proximity Read ↗

Identification of serpin determinants of specificity and selectivity for furin inhibition through studies of α1PDX (α1-protease inhibitor Portland)-serpin B8 and furin active-site loop chimeras.Semantic proximity Read ↗

Single amino acid substitution in the PC1/3 propeptide can induce significant modifications of its inhibitory profile toward its cognate enzyme.Semantic proximity Read ↗

Engineering of Kex2 variants exhibiting altered substrate specificity.Semantic proximity Read ↗

Identification of furin pro-region determinants involved in folding and activation.Semantic proximity Read ↗

Structural insight into the CUB2 domain's role in enteropeptidase-mediated trypsinogen activation.Semantic proximity Read ↗

A look at the Caenorhabditis elegans Kex2/Subtilisin-like proprotein convertase family.Semantic proximity Read ↗

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