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

DEN1 deneddylates non-cullin proteins in vivo.

Journal of cell science - 1 Oct 2008

Chan Yaru, Yoon Jeongsook, Wu June-Tai, Kim Hyung-Jun, Pan Kuan-Ting, Yim Jeongbin, Chien Cheng-Ting

Abstract excerpt

The ubiquitin-like protein Nedd8/Rub1 covalently modifies and activates cullin ubiquitin ligases. However, the repertoire of Nedd8-modified proteins and the regulation of protein neddylation status are not clear. The cysteine protease DEN1/NEDP1 specifically processes the Nedd8 precursor and has been suggested to deconjugate Nedd8 from cullin proteins. By characterizing the Drosophila DEN1 protein and DEN1 null...

Read the complete abstract on PubMed

Topics

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

Share to Cullin Proteins
Share to Drosophila melanogaster
Share to Drosophila Proteins

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Endopeptidases

Share to Green Fluorescent Proteins

Share to Protein Processing, Post-Translational

Share to Recombinant Fusion Proteins

Share to Ubiquitins

Source

Identifiers

PMID: 18782863
DOI: 10.1242/jcs.030445

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

DEN1 deneddylates non-cullin proteins in vivo.PMID 18782863Read ↗

Deneddylase 1 regulates deneddylase activity of the Cop9 signalosome in Drosophila melanogaster.Semantic proximity Read ↗

DENEDDYLASE1 deconjugates NEDD8 from non-cullin protein substrates in Arabidopsis thaliana.Semantic proximity Read ↗

DENEDDYLASE1 Protein Counters Automodification of Neddylating Enzymes to Maintain NEDD8 Protein Homeostasis in Arabidopsis.Semantic proximity Read ↗

Increasing the Unneddylated Cullin1 Portion Rescues the csn Phenotypes by Stabilizing Adaptor Modules To Drive SCF Assembly.Semantic proximity Read ↗

The human Dcn1-like protein DCNL3 promotes Cul3 neddylation at membranes.Semantic proximity Read ↗

Arabidopsis CAND1, an unmodified CUL1-interacting protein, is involved in multiple developmental pathways controlled by ubiquitin/proteasome-mediated protein Degradation.Semantic proximity Read ↗

Control of multicellular development by the physically interacting deneddylases DEN1/DenA and COP9 signalosome.Semantic proximity Read ↗

MLN4924 is an efficient inhibitor of NEDD8 conjugation in plants.Semantic proximity Read ↗

C. elegans CAND-1 regulates cullin neddylation, cell proliferation and morphogenesis in specific tissues.Semantic proximity Read ↗

Transcriptome and functional analysis in a Drosophila model of NGLY1 deficiency provides insight into therapeutic approachesSemantic proximity Read ↗

The fission yeast COP9/signalosome is involved in cullin modification by ubiquitin-related Ned8p.Semantic proximity Read ↗

Natural <i>SEL1L</i> variants modify ERAD, proteasome function, and survival in a <i>Drosophila</i> model of NGLY1 deficiencySemantic proximity Read ↗

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