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Proteomicsc-Abl Dependent Tyrosine Phosphorylation of theCo-chaperone Aha1 Regulates Interaction with Hsp90
The ability of Heat Shock Protein 90 (Hsp90) to hydrolyze ATP is essential for its chaperone function. The co-chaperone Aha1 stimulates Hsp90 ATPase activity tailoring the chaperone function to specific “client” proteins. The intracellular signaling mechanisms directly regulating Aha1 association wi...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-28 | MSV000080713 | MassIVE
UnknownCrystal structures of VAP1 reveal ADAMs' MDC domain architecture and its unique C-shaped scaffold.
Not available
S-EPMC1478178 | biostudies-literature
Proteomicsc-Abl Dependent Tyrosine Phosphorylation of theCo-chaperone Aha1 Regulates Interaction with Hsp90
The ability of Heat Shock Protein 90 (Hsp90) to hydrolyze ATP is essential for its chaperone function. The co-chaperone Aha1 stimulates Hsp90 ATPase activity tailoring the chaperone function to specific “client” proteins. The intracellular signaling mechanisms directly regulating Aha1 association wi...
ORGANISM(S): Homo sapiens (Human) 
2015-08-06 | PXD001737 | Pride
Molecular chaperone Q-exactive C-abl 18o labeling Aha1 Co-chaperone Heat shock protein 90 Quantative proteomics 
UnknownComplete sequences of mitochondrial genome of Hypselodoris festiva (A. Adams, 1861) (Mollusca, Gastropoda, Nudibranchia).
Not available
S-EPMC7871837 | biostudies-literature
ProteomicsEssential role of the Pax5 C-terminal domain in controlling B cell commitment and development
Pax5 controls B-cell commitment, development and immunity by repressing B-lineage-inappropriate genes and activating B-cell-specific genes. In addition to the N-terminal DNA-binding paired domain, Pax5 contains a conserved octapeptide, partial homeodomain and C-terminal sequences with transactivatin...
ORGANISM(S): Mus musculus (Mouse) 
2023-08-24 | PXD040424 | Pride
Co-repressors C-terminal regulatory domains Gene activation Co-activators Pax5 Gene repression 
UnknownSynthesis of complex allylic esters via C-H oxidation vs C-C bond formation.
Not available
S-EPMC3047454 | biostudies-literature
ProteomicsThe Effect of Temperature Conditioning (9°C and 20°C) on the Proteome of Steinernema carpocapsae and Heterorhabditis megidis Infective Juveniles
Entomopathogenic nematodes (Rhabditida; Steinernematidae and Heterorhabditidae) are insect parasites which are of economic importance due to their use as biocontrol agents. The third larval stage, infective juveniles (IJs) leave the natal host and move in the soil to locate a new insect host. Both f...
ORGANISM(S): Heterorhabditis megidis Escherichia coli Steinernema carpocapsae 
2022-03-27 | PXD027608 | Pride
Enomopathogenic nematodes Steinernema carpocapsae Heterorhabditis megidis Temperature conditioning 
UnknownSequential allylic C-H amination/vinylic C-H arylation: a strategy for unnatural amino acid synthesis from α-olefins.
Not available
S-EPMC4104998 | biostudies-literature
UnknownParacrine signals from liver sinusoidal endothelium regulate hepatitis C virus replication.
Not available
S-EPMC3992845 | biostudies-literature
UnknownCatalyst-controlled C-O versus C-N allylic functionalization of terminal olefins.
Not available
S-EPMC4124944 | biostudies-literature
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