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UnknownDipole source analyses of laser evoked potentials obtained from subdural grid recordings from primary somatic sensory cortex.
Not available
S-EPMC3154813 | biostudies-literature
TranscriptomicsGEP of PMBCs during treatment with a gene-modified allogeneic tumor cell vaccine in advanced renal cell cancer (RCC) patients
Tumor-induced immunosuppression remains a major challenge for immunotherapy of cancer patients. To further elucidate why an allogeneic gene-modified (Interleukin-7(IL-7)/CD80 co-transfected) renal cell cancer vaccine failed to induce clinically relevant TH1-polarized immune responses, peripheral blo...
ORGANISM(S): Homo sapiens 
2014-09-24 | E-GEOD-51490 | biostudies-arrayexpress
UnknownGene therapy for <i>fat-1</i> prevents obesity-induced metabolic dysfunction, cellular senescence, and osteoarthritis.
Not available
S-EPMC11513907 | biostudies-literature
TranscriptomicsIkB-like protein NFKBIZ regulates NF-kB signaling and is critical for survival of ABC DLBCL (MALT inhibition)
Constitutive activation of the nuclear factor-kappa B (NF-kB) pathway is a hallmark of the activated B-cell-like (ABC) subtype of diffuse large B-cell lymphoma (DLBCL). Recurrent mutations of NF-kB regulators that cause constitutive activity of this oncogenic pathway have been identified. However, i...
ORGANISM(S): Homo sapiens 
2013-07-22 | E-GEOD-46973 | biostudies-arrayexpress
ProteomicsDiscovery of an Exquisitely Selective WDR5 Chemical Probe Accelerated by a High-Quality DEL-ML Hit
A chemoproteomics experiment was performed to investigate the selectivity of the WDR5 targeting compound LH168. Therefore, a biotinylated adduct of LH168, namely LH205, was used to enrich potential target proteins of LH168. The addition of LH168 in excess competed only the interaction with LH168, de...
ORGANISM(S): Homo sapiens (Human) 
2025-09-15 | PXD063455 | Pride
Chemoproteomics Wdr5 
TranscriptomicsEssential role of MALT1 protease activity in activated B cell-like diffuse large B-cell lymphoma
A key element for the development of suitable anti-cancer drugs is the identification of cancer-specific enzymatic activities that can be therapeutically targeted. Mucosa-associated lymphoid tissue transformation protein 1 (MALT1) is a proto-oncogene that contributes to tumorigenesis in diffuse larg...
ORGANISM(S): Homo sapiens 
2012-09-20 | E-GEOD-41034 | biostudies-arrayexpress
ProteomicsSelective ubiquitination of drug-like small molecules by the ubiquitin ligase HUWE1
The ubiquitin system regulates eukaryotic physiology by modifying specific substrate proteins. Substrate recruitment and the assembly of ubiquitin signals are determined by ubiquitin ligases, some of which also modify non-protein biomolecules. Here we expand this substrate realm, revealing that the ...
ORGANISM(S): Homo sapiens (Human) 
2025-09-02 | PXD066563 | Pride
Small-molecule inhibitor Hect e3 Mass spectrometry Enzymology Click chemistry Non-protein ubiquitination 
ProteomicsSelective ubiquitination of drug-like small molecules by the ubiquitin ligase HUWE1
The ubiquitin system regulates myriad pathways in eukaryotic physiology by modifying specific substrate proteins. The recognition of the substrates and the assembly of ubiquitin signals on them – key specificity determinants in ubiquitin signaling - are determined by the diversified class of ubiquit...
ORGANISM(S): Homo sapiens (Human) 
2025-09-03 | PXD063550 | Pride
Small-molecule inhibitor Hect e3 Mass spectrometry Enzymology Click chemistry Non-protein ubiquitination 
ProteomicsMass spectrometric analysis of proteolytic cleavage related to ArtA and PssA from Haloferax volcanii
The S-layer glycoprotein (SLG) of Haloferax volcanii has been shown to be processed and C-terminally linked to a lipid in an archaeosortase A (ArtA)-dependent manner. A C-terminal tripartite structure including a PGF motif is required for the processing of SLG as well as other substrates (Abdul Hali...
ORGANISM(S): Haloferax volcanii (Halobacterium volcanii) 
2020-05-11 | PXD011050 | Pride
Haloferax volcanii Lipid anchoring Archaeosortase S-layer glycoprotein 
UnknownCritical assessment of LC3/GABARAP ligands used for degrader development and ligandability of LC3/GABARAP binding pockets.
Not available
S-EPMC11589570 | biostudies-literature
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