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

A high-throughput pH indicator assay for screening glycosyltransferase saturation mutagenesis libraries.

Analytical biochemistry - 1 Jul 2008

Persson Mattias, Palcic Monica M

Abstract excerpt

Protein engineering using directed evolution or saturation mutagenesis at hot spots is often used to improve enzyme properties such as their substrate selectivity or stability. This requires access to robust high-throughput assays to facilitate the analysis of enzyme libraries. However, relativel...

Read the complete abstract on PubMed

Topics

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

Share to ABO Blood-Group System
Share to Glycosyltransferases
Share to Hydrogen-Ion Concentration

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Kinetics

Share to Molecular Structure

Share to Mutagenesis

Share to Peptide Library

Share to Substrate Specificity

Source

Identifiers

PMID: 18405657
DOI: 10.1016/j.ab.2008.03.006

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-18405657-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A high-throughput pH indicator assay for screening glycosyltransferase saturation mutagenesis libraries.PMID 18405657Read ↗

Rapid evolution of beta-glucuronidase specificity by saturation mutagenesis of an active site loop.Semantic proximity Read ↗

Semi-rationally designed site-saturation mutation of Helicobacter pylori α-1,2-fucosyltransferase for improved catalytic activity and thermostability.Semantic proximity Read ↗

Fluorescence activated cell sorting as a general ultra-high-throughput screening method for directed evolution of glycosyltransferases.Semantic proximity Read ↗

Screening glycosynthase libraries with a fluoride chemosensor assay independently of enzyme specificity: identification of a transitional hydrolase to synthase mutant.Semantic proximity Read ↗

Flexibility and mutagenic resiliency of glycosyltransferases.Semantic proximity Read ↗

Screening a limited structure-based library identifies UDP-GalNAc-specific mutants of alpha-1,3-galactosyltransferase.Semantic proximity Read ↗

High-throughput screening methodology for the directed evolution of glycosyltransferases.Semantic proximity Read ↗

Site-saturation mutagenesis: a powerful tool for structure-based design of combinatorial mutation libraries.Semantic proximity Read ↗

Directed evolution of a lysosomal enzyme with enhanced activity at neutral pH by mammalian cell-surface display.Semantic proximity Read ↗

A high-throughput fluorescence-based glycosyltransferase screen and its application in directed evolution.Semantic proximity Read ↗

High-throughput screening of B factor saturation mutated Rhizomucor miehei lipase thermostability based on synthetic reaction.Semantic proximity Read ↗

Engineering and rapid selection of a low-affinity glucose/galactose-binding protein for a glucose biosensor.Semantic proximity Read ↗

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