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ProteomicsTripartite interactions of PKA catalytic subunit and C-terminal domains of cardiac Ca2+ channel may modulate its β-adrenergic regulation
The β-adrenergic augmentation of cardiac contraction, by increasing the conductivity of L-type voltage-gated CaV1.2 channels, is of great physiological and pathophysiological importance. Stimulation of β-adrenergic receptors (βAR) activates protein kinase A (PKA) through separation of regulatory (PK...
ORGANISM(S): Homo sapiens (Human) 
2024-11-22 | PXD057841 | Pride
Calcium channel  protein‐protein interaction  adrenergic regulation  cardiac  protein kinase a (pka)  heterologous expression 
UnknownNathan H. Azrin: A Case Study in Research Translation in Behavior Science.
Not available
S-EPMC8076359 | biostudies-literature
MetabolomicsExtreme genome diversity and cryptic speciation in a harmful algal bloom forming eukaryote

Harmful algal blooms (HABs) of the toxic haptophyte Prymnesium parvum are a recurrent problem in many inland and estuarine waters around the world. Strains of P. parvum vary in the toxins they produce and in other physiological traits associated with HABs, but the genetic basis ...

2023-04-26 | MTBLS5893 | MetaboLights
UnknownSteering CO2 hydrogenation toward C-C coupling to hydrocarbons using porous organic polymer/metal interfaces.
Not available
S-EPMC8851537 | biostudies-literature
UnknownAbsence of DNA polymerase eta reveals targeting of C mutations on the nontranscribed strand in immunoglobulin switch regions.
Not available
S-EPMC2211872 | biostudies-literature
UnknownNeuroprotection mediated by cystatin C-loaded extracellular vesicles.
Not available
S-EPMC6668451 | biostudies-literature
MetabolomicsGut Bacteroides act in a microbial consortium to cause susceptibility to severe malaria

Malaria, caused by Plasmodium species, remains a significant cause of morbidity and mortality globally. Gut bacteria can influence the severity of malaria, but the contribution of specific bacteria to the risk of severe malaria is unknown. Here, multiomics approaches demonstrate specific...

2023-09-13 | MTBLS3449 | MetaboLights
UnknownStructural Basis for the Species-Selective Binding of N,C-Capped Dipeptides to the Mycobacterium tuberculosis Proteasome.
Not available
S-EPMC5745808 | biostudies-literature
Unknownc-FLIP regulates autophagy by interacting with Beclin-1 and influencing its stability.
Not available
S-EPMC8266807 | biostudies-literature
UnknownN,C-Capped dipeptides with selectivity for mycobacterial proteasome over human proteasomes: role of S3 and S1 binding pockets.
Not available
S-EPMC3773049 | biostudies-literature
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