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

Upregulation of dendritic arborization by N-acetyl-D-glucosamine kinase is not dependent on its kinase activity.

Molecules and cells - 1 Apr 2014

Lee HyunSook, Dutta Samikshan, Moon Il Soo

Abstract excerpt

N-acetylglucosamine kinase (GlcNAc kinase or NAGK; EC 2.7.1.59) is highly expressed and plays a critical role in the development of dendrites in brain neurons. In this study, the authors conducted structure-function analysis to verify the previously proposed 3D model structure of GlcNAc/ ATP-bound NAGK. Three point NAGK mutants with different substrate binding capacities and reaction velocities were produced....

Read the complete abstract on PubMed

Topics

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

Share to Acetylglucosamine
Share to Cell Growth Processes
Share to Dendrites

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hippocampus

Share to Nerve Degeneration

Share to Neurogenesis

Share to Phosphotransferases (Alcohol Group Acceptor)

Share to Protein Engineering

Source

Open in PubMed Open full text

Identifiers

PMID: 24722415
DOI: 10.14348/molcells.2014.2377
PMCID: PMC4012081

Genes

NAGK

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Upregulation of dendritic arborization by N-acetyl-D-glucosamine kinase is not dependent on its kinase activity.PMID 24722415Read ↗

A structural and functional analysis of Nna1 in Purkinje cell degeneration (pcd) mice.Semantic proximity Read ↗

Determinants of ligand binding and catalytic activity in the myelin enzyme 2',3'-cyclic nucleotide 3'-phosphodiesterase.Semantic proximity Read ↗

Site-directed mutagenesis of Escherichia coli acetylglutamate kinase and aspartokinase III probes the catalytic and substrate-binding mechanisms of these amino acid kinase family enzymes and allows three-dimensional modelling of aspartokinase.Semantic proximity Read ↗

Crystallographic analysis of the reaction cycle of 2',3'-cyclic nucleotide 3'-phosphodiesterase, a unique member of the 2H phosphoesterase family.Semantic proximity Read ↗

Structure of a glutamate transporter homologue from Pyrococcus horikoshii.Semantic proximity Read ↗

Three dimensional structural studies of alpha-N-acetylgalactosaminidase (alpha-NAGA) in alpha-NAGA deficiency (Kanzaki disease): different gene mutations cause peculiar structural changes in alpha-NAGAs resulting in different substrate specificities and clinical phenotypes.Semantic proximity Read ↗

The aspartic acid of Fyn at 390 is critical for neuronal migration during corticogenesis.Semantic proximity Read ↗

Both the C1 domain and a basic amino acid cluster at the C-terminus are important for the neurite and branch induction ability of DGKβ.Semantic proximity Read ↗

Substituting c-Jun N-terminal kinase-3 (JNK3) ATP-binding site amino acid residues with their p38 counterparts affects binding of JNK- and p38-selective inhibitors.Semantic proximity Read ↗

Structure of N-acetyl-L-glutamate synthase/kinase from Maricaulis maris with the allosteric inhibitor L-arginine bound.Semantic proximity Read ↗

Evidence That the "Lid" Domain of Nicastrin Is Not Essential for Regulating γ-Secretase Activity.Semantic proximity Read ↗

The glutamate-rich region of the larger lamprey neurofilament sidearm is essential for proper neurofilament architecture.Semantic proximity Read ↗

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