Sort   by:  
 Page size 
ProteomicsCryo-EM structures of Gid12-bound GID E3 reveal steric blockade as a mechanism inhibiting substrate ubiquitylation
Protein degradation, a major eukaryotic response to cellular signals, is subject to numerous layers of regulation. In yeast, the evolutionarily conserved GID E3 ligase mediates glucose-induced degradation of fructose-1,6-bisphosphatase (Fbp1) and other gluconeogenic enzymes. “GID” is a collection of...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2022-05-29 | PXD028579 | Pride
Gid E3 ligase complex Crzoem 
ProteomicsDoa10/MARCH6 architecture interconnects E3 ligase activity with lipid-binding transmembrane channel to regulate SQLE
Transmembrane E3 ligases play crucial roles in homeostasis. Much protein and organelle quality control, and metabolic regulation, are determined by ER-resident MARCH6 E3 ligases, including Doa10 in yeast. Here, we present Doa10/MARCH6 structural analysis by cryo-EM and AlphaFold predictions, and a s...
ORGANISM(S): Homo sapiens (Human) 
2024-01-26 | PXD047499 | Pride
Ubiquitylation E3 ubiquitin ligases March6 Membrane proteins Doa10 Cryo-em Sqle 
ProteomicsProfiling of activated RBR E3 ligases using E2V derived activity-based probes
Structure-based E2 enzyme variants (E2Vs) were used to create biotinylated activity-based probes use as handles for affinity purification-mass spectrometry to identify interacting E3s.
ORGANISM(S): Homo sapiens (Human) 
2026-01-05 | PXD068594 | Pride
E2 enzyme E3 ligase Activity-based probe 
ProteomicsPrinciples of isoform-specific targeted protein degradation engaging the C-degron E3 KLHDC2
Targeted protein degradation (TPD) via molecular glues or PROTACs (Proteolysis-targeting chimeras) is an up-and-coming drug modality holding promise to drug the “undrugabbles.” Further expanding the collection of targetable E3 ligases for TPD, we report the discovery of ligands targeting the C-END d...
ORGANISM(S): Homo sapiens (Human) 
2025-01-18 | PXD051581 | Pride
Protac Tpd Ubiquitin Brd3 Klhdc2 
ProteomicsCullin-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 
TranscriptomicsE2-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
ProteomicsCTLH E3 Ligase Regulates the Degradation of HMG-CoA Synthase 1 Through the Pro/N-end Rule Pathway
Supporting raw MS data for paper (doi: 10.1016/j.molcel.2024.04.026) by Yi S.A. et al, titled "CTLH E3 Ligase Regulates the Degradation of HMG-CoA Synthase 1 Through the Pro/N-end Rule Pathway". Index of RAW files uploaded: - Related to Supplementary Table 1 (HA-9-81-X | WT (1), ATG7KO (2), RB1CC1 ...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2022-11-29 | MSV000090814 | MassIVE
ProteomicsARIH2 is a novel Vif-dependent regulator of CUL5-mediated APOBEC3G degradation in HIV infection
Discovery of novel host-virus interactions leads to a better understanding of mechanisms underlying infection and points to potential therapeutic targets at the interface between virus and host proteins. Recently, global, virus-host interaction networks have been mapped using affinity purification-m...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2020-01-29 | MSV000084855 | MassIVE
UnknownIn situ cryo-electron tomography of autophagic structures in S. cerevisiae
Not available
EMPIAR-11166 | biostudies-other
ProteomicsARIH2 is a Vif-dependent regulator of CUL5-mediated APOBEC3G degradation in HIV infection: SRM_CBFB_CUL2_CUL5_interactors
SRM assays were generated for selected interactors of CUL5, CBFB and ELOB. SRM assay generation was performed using Skyline. For all targeted proteins, proteotypic peptides and optimal transitions for identification and quantification were selected based on the Skyline spectral library generated fro...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) Human Immunodeficiency Virus 1 (ncbitaxon:11676) 
2020-02-17 | MSV000084965 | MassIVE
Sort   by:  
 Page size