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

α2-6-Neosialidase: A Sialyltransferase Mutant as a Sialyl Linkage-Specific Sialidase.

ACS chemical biology - 18 May 2018

McArthur John B, Yu Hai, Tasnima Nova, Lee Christie M, Fisher Andrew J, Chen Xi

Abstract excerpt

The lack of α2-6-linkage specific sialidases limits the structural and functional studies of sialic-acid-containing molecules. Photobacterium damselae α2-6-sialyltransferase (Pd2,6ST) was shown previously to have α2-6-specific, but weak, sialidase activity. Here, we develop a high-throughput blue-white colony screening method to identify Pd2,6ST mutants with improved α2-6-sialidase activity from mutant libraries...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Proteins
Share to High-Throughput Screening Assays

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrogen-Ion Concentration

Share to Kinetics

Share to Mutagenesis

Share to Neuraminidase

Share to Sialyltransferases

Share to Substrate Specificity

Source

Open in PubMed Open full text

Identifiers

PMID: 29543427
DOI: 10.1021/acschembio.8b00002
PMCID: PMC5978697

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

α2-6-Neosialidase: A Sialyltransferase Mutant as a Sialyl Linkage-Specific Sialidase.PMID 29543427Read ↗

A Photobacterium sp. α2-6-sialyltransferase (Psp2,6ST) mutant with an increased expression level and improved activities in sialylating Tn antigens.Semantic proximity Read ↗

Loss-of-function mutation in bi-functional marine bacterial sialyltransferase.Semantic proximity Read ↗

Bacterial exo-α-sialidases subvert the complement system through desialylationSemantic proximity Read ↗

A sialyltransferase mutant with decreased donor hydrolysis and reduced sialidase activities for directly sialylating LewisX.Semantic proximity Read ↗

Identification of an N-acetylneuraminic acid-presenting bacteria isolated from a healthy human microbiomeSemantic proximity Read ↗

A pseudaminic acid or a legionaminic acid derivative transferase is strain-specifically implicated in the general protein O-glycosylation system of the periodontal pathogen Tannerella forsythia.Semantic proximity Read ↗

Highly efficient biosynthesis of 3'-sialyllactose in engineered Escherichia coli.Semantic proximity Read ↗

Integrated Genome and Protein Editing Swaps α‐2,6 Sialylation for α‐2,3 Sialic Acid on Recombinant Antibodies from CHOSemantic proximity Read ↗

The group B streptococcal sialic acid O-acetyltransferase is encoded by neuD, a conserved component of bacterial sialic acid biosynthetic gene clusters.Semantic proximity Read ↗

Sialyltransferases with enhanced legionaminic acid transferase activity for the preparation of analogs of sialoglycoconjugates.Semantic proximity Read ↗

Generation of efficient mutants of endoglycosidase from Streptococcus pyogenes and their application in a novel one-pot transglycosylation reaction for antibody modification.Semantic proximity Read ↗

Genetic and biochemical modulation of sialic acid O-acetylation on group B Streptococcus: phenotypic and functional impact.Semantic proximity Read ↗

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