Cullin-ring ligases

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E2-RING expansion of the NEDD8 cascade confers specificity to cullin modification

Ubiquitin and ubiquitin-like proteins (UBLs) are directed to targets by cascades of E1, E2, and E3 enzymes. The largest ubiquitin E3 subclass consists of cullin-RING ligases (CRLs), which contain one each of several cullins (CUL1, -2, -3, -4, or -5) and RING proteins (RBX1 or -2). CRLs are activated...

ORGANISM(S): Mus musculus

2009-03-23 | E-GEOD-14088 | biostudies-arrayexpress

Activity-based profiling of cullin-RING ligase networks by conformation-specific probes

The cullin-RING E3 ligase (CRL) network comprises over 300 unique complexes that switch from inactive to activated conformations upon site-specific cullin modification by the ubiquitin-like protein NEDD8. Assessing cellular repertoires of activated CRL complexes is critical for understanding eukaryo...

ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse)

2023-09-02 | PXD039649 | Pride

Cullin-RING ligases target substrates with geometrically optimized catalytic partners

Cullin-RING ubiquitin ligases (CRLs) control the degradation of a wide landscape of human proteins in combination with ubiquitin-carrying enzymes (UCEs). CRL expansion during evolution is apparent, with a few dozen in yeast that function with a single UCE and as many as 300 in humans that function w...

ORGANISM(S): Homo sapiens (Human)

2024-05-22 | PXD043523 | Pride

Ubiquitylation Cullin-ring ligase

Cullin-RING E3 Ubiquitin Ligases: Bridges to Destruction.

Not available

S-EPMC7205596 | biostudies-literature

Protein neddylation: beyond cullin-RING ligases.

Not available

S-EPMC5131867 | biostudies-literature

NEDD8 and ubiquitin ligation by cullin-RING E3 ligases.

Not available

S-EPMC8096640 | biostudies-literature