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

Mass spectrometric analysis of mutant mice.

Methods in enzymology - 1 Jan 2010

North Simon J, Jang-Lee Jihye, Harrison Rebecca, Canis Kévin, Ismail Mohd Nazri, Trollope Alana, Antonopoulos Aristotelis, Pang Poh-Choo, Grassi Paola, Al-Chalabi Sara, Etienne A Tony, Dell Anne, Haslam Stuart M

Abstract excerpt

Mass spectrometry (MS) has proven to be the preeminent tool for the rapid, high-sensitivity analysis of the primary structure of glycans derived from diverse biological sources including cells, fluids, secretions, tissues, and organs. These analyses are anchored by matrix-assisted laser desorptio...

Read the complete abstract on PubMed

Topics

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

Share to Polysaccharides
Share to Pancreas
Share to alpha-Galactosidase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mass Spectrometry

Share to Mice, Knockout

Share to Mutation

Source

Identifiers

PMID: 20816474
DOI: 10.1016/S0076-6879(10)78002-2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-20816474-2026-09-02.2. 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

Mass spectrometric analysis of mutant mice.PMID 20816474Read ↗

Glycomic analyses of mouse models of congenital muscular dystrophy.Semantic proximity Read ↗

Modeling human congenital disorder of glycosylation type IIa in the mouse: conservation of asparagine-linked glycan-dependent functions in mammalian physiology and insights into disease pathogenesis.Semantic proximity Read ↗

What Have We Learned from Glycosyltransferase Knockouts in Mice?Semantic proximity Read ↗

A phenotype survey of 36 mutant mouse strains with gene-targeted defects in glycosyltransferases or glycan-binding proteins.Semantic proximity Read ↗

System-wide quantitative proteomics of the metabolic syndrome in mice: genotypic and dietary effectsSemantic proximity Read ↗

The remodeling of glycoconjugates in mice.Semantic proximity Read ↗

Differentiating inbred mouse strains from each other and those with single gene mutations using hair proteomics.Semantic proximity Read ↗

Profiling and genetic control of the murine immunoglobulin G glycome.Semantic proximity Read ↗

A hypomorphic Mpi mutation unlocks an in vivo tool for studying global N-glycosylation deficiency.Semantic proximity Read ↗

MIgGGly (mouse IgG glycosylation analysis) - a high-throughput method for studying Fc-linked IgG N-glycosylation in mice with nanoUPLC-ESI-MSSemantic proximity Read ↗

Mice with a homozygous deletion of the Mgat2 gene encoding UDP-N-acetylglucosamine:alpha-6-D-mannoside beta1,2-N-acetylglucosaminyltransferase II: a model for congenital disorder of glycosylation type IIa.Semantic proximity Read ↗

Characterization of mice with targeted deletion of the gene encoding core 2 beta1,6-N-acetylglucosaminyltransferase-2.Semantic proximity Read ↗

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