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

Refolding of human beta-1-2 GlcNAc transferase (GnT1) and the role of its unpaired Cys 121.

Biochemical and biophysical research communications - 19 Oct 2007

Saribas A Sami, Johnson Karl, Liu Li, Bezila Dan, Hakes David

Abstract excerpt

Human beta1-2N-acetylglucosaminyltransferase (hGnT1) lacking the first 103 amino acids was expressed as a maltose binding protein (MBP) fusion protein in inclusion bodies (IBs) in Escherichia coli and refolded using an oxido-shuffling method. GnT1 mutants were prepared by replacing a predicted un...

Read the complete abstract on PubMed

Topics

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

Share to Catalysis
Share to Maltose-Binding Proteins
Share to Mutant Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to N-Acetylglucosaminyltransferases

Share to Polysaccharides

Share to Rabbits

Share to Ribonucleases

Share to Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

Source

Identifiers

PMID: 17716624
DOI: 10.1016/j.bbrc.2007.07.199

Genes

MBP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-17716624-2026-09-02.1. Manifest publication-graph-cohort-2026-09-02.1.

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

Refolding of human beta-1-2 GlcNAc transferase (GnT1) and the role of its unpaired Cys 121.PMID 17716624Read ↗

The K346T mutant of GnT-III bearing weak in vitro and potent intracellular activity.Semantic proximity Read ↗

Mutational analysis of the catalytic domain of O-linked N-acetylglucosaminyl transferase.Semantic proximity Read ↗

Structure and function of beta -1,4-galactosyltransferase.Semantic proximity Read ↗

Highly conserved cysteines of mouse core 2 beta1,6-N-acetylglucosaminyltransferase I form a network of disulfide bonds and include a thiol that affects enzyme activity.Semantic proximity Read ↗

The first crystal structure of a family 129 glycoside hydrolase from a probiotic bacterium reveals critical residues and metal cofactors.Semantic proximity Read ↗

Growth-regulatory human galectin-1: crystallographic characterisation of the structural changes induced by single-site mutations and their impact on the thermodynamics of ligand binding.Semantic proximity Read ↗

Overexpression, purification, and refolding of link module from human TSG-6 in Escherichia coli: effect of temperature, media, and mutagenesis on lysine misincorporation at arginine AGA codons.Semantic proximity Read ↗

Crystal structure of the Ate1 arginyl-tRNA-protein transferase and arginylation of N-degron substrates.Semantic proximity Read ↗

Structural and functional perturbation of Giardia lamblia triosephosphate isomerase by modification of a non-catalytic, non-conserved region.Semantic proximity Read ↗

Structural basis for transglycosylation in glycoside hydrolase family GH116 glycosynthases.Semantic proximity Read ↗

Structural and biochemical characterization of a trapped coenzyme A adduct of Caenorhabditis elegans glucosamine-6-phosphate N-acetyltransferase 1.Semantic proximity Read ↗

Soluble human core 2 beta6-N-acetylglucosaminyltransferase C2GnT1 requires its conserved cysteine residues for full activity.Semantic proximity Read ↗

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