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Shp1/p47 is a cofactor of the Cdc48/p97 complex involved in the energy-dependent segregation of intracellular aggregates and multiprotein complexes. We identified two serine residues (S108 and S315) in the S. Cerevisiae protein Shp1 which increase in phosphorylation upon various cell stresses such a...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2023-01-30 | PXD035819 | Pride
KDM3B inhibition suppresses SHP1 expression by modulating the epigenetic landscape of the Shp1 promoter.
The Cdc48 AAA+ ATPase is an abundant and essential enzyme that unfolds substrates in multiple protein quality control pathways. The enzyme includes two conserved AAA+ ATPase cassettes, D1 and D2, that assemble as hexameric rings with D1 stacked above D2. Here, we report an ensemble of structures of ...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2024-10-17 | PXD048280 | Pride
The protein tyrosine phosphatases (PTPs) TCPTP, PTPN22, and SHP1 are critical regulators of the activating phophotyrosine (pY) site on the initiating T cell kinase, LckY394, but the broader implications of these phophatases in T cell receptor (TCR) signalling and T cell biology remain unclear. By co...
ORGANISM(S): Homo sapiens (Human) 
2025-08-01 | PXD058624 | Pride
Immunological proteins are major disease targets, and the majority remain undrugged. Post-translational redox modification of protein cysteine residues has emerged as a mode of immune cell regulation, especially in the context of the macrophage cytokine response. Here, we develop a strategy for syst...
ORGANISM(S): Mus musculus (Mouse) Homo sapiens (Human) 
2026-03-17 | PXD072062 | Pride
Immunological proteins are major disease targets and the majority remain undrugged. Post-translational redox modification of protein cysteine residues has emerged as a mode of immune cell regulation, especially in the context of the macrophage cytokine response.1 Here, we develop a strategy for syst...
ORGANISM(S): Homo sapiens (Human) 
2026-02-24 | PXD055006 | Pride
By combining strategies of substrate trapping for PTPs and pupylation-based interaction tagging (PUP-IT) for protein-protein interaction, we develop a systematic proximity labeling methodology PEPSI in identifying novel substrate for PTPs. We apply this approach to SHP1 and surprisingly, identified ...
ORGANISM(S): Homo Sapiens 
Immunotherapy has emerged as a promising therapeutic option for cancer management, but its applicability in patients with triple–negative breast cancer (TNBC) is limited by the low efficacy due to the immunosuppressive tumor microenvironment (TME). Here, we identify lysine demethylase 3B (KDM3B) as ...
ORGANISM(S): Mus musculus 
2026-07-15 | GSE329777 | GEO
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