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

O-GlcNAc regulates NEDD4-1 stability via caspase-mediated pathway.

Biochemical and biophysical research communications - 18 Mar 2016

Jiang Kuan, Bai Bingyang, Ta Yajie, Zhang Tingling, Xiao Zikang, Wang Peng George, Zhang Lianwen

Abstract excerpt

O-GlcNAc modification of cytosolic and nuclear proteins regulates essential cellular processes such as stress responses, transcription, translation, and protein degradation. Emerging evidence indicates O-GlcNAcylation has a dynamic interplay with ubiquitination in cellular regulation. Here, we report that O-GlcNAc indirectly targets a vital E3 ubiquitin ligase enzyme of NEDD4-1. The protein level of NEDD4-1 is...

Read the complete abstract on PubMed

Topics

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

Share to Acetylglucosamine
Share to Acylation
Share to Caspases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Endosomal Sorting Complexes Required for Transport

Share to MCF-7 Cells

Share to N-Acetylglucosaminyltransferases

Share to Nedd4 Ubiquitin Protein Ligases

Share to Oximes

Source

Identifiers

PMID: 26876577
DOI: 10.1016/j.bbrc.2016.02.037

Genes

NEDD4
OGT

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

O-GlcNAc regulates NEDD4-1 stability via caspase-mediated pathway.PMID 26876577Read ↗

Unraveling the Potential Role of NEDD4-like E3 Ligases in CancerSemantic proximity Read ↗

Cancer-derived mutation in the OGA stalk domain promotes cell malignancy through dysregulating PDLIM7 and p53Semantic proximity Read ↗

Dynamic O-GlcNAcylation coordinates etoposide-triggered tumor cell pyroptosis by regulating p53 stabilitySemantic proximity Read ↗

OGA mutant aberrantly hydrolyzes O-GlcNAc modification from PDLIM7 to modulate p53 and cytoskeleton in promoting cancer cell malignancy.Semantic proximity Read ↗

Post-translational modifications of cancer immune checkpoints: mechanisms and therapeutic strategiesSemantic proximity Read ↗

Peptide: N-Glycanase 1 and Its Relationship with Congenital Disorder of DeglycosylationSemantic proximity Read ↗

O-GlcNAcylation and stablization of SIRT7 promote pancreatic cancer progression by blocking the SIRT7-REGγ interactionSemantic proximity Read ↗

Feedback Regulation of O-GlcNAc Transferase through Translation Control to Maintain Intracellular O-GlcNAc Homeostasis.Semantic proximity Read ↗

Cytosolic Peptide: N-Glycanase (NGLY1)-from Basic Biology to Genetic Disorder, NGLY1 Deficiency.Semantic proximity Read ↗

Expression and regulatory network of E3 ubiquitin ligase NEDD4 family in cancersSemantic proximity Read ↗

The hexosamine signaling pathway: deciphering the "O-GlcNAc code".Semantic proximity Read ↗

The regulatory roles of the E3 ubiquitin ligase NEDD4 family in DNA damage responseSemantic proximity Read ↗

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