Evaluation of a Novel Antiplatelet Therapy Strategy in Patients Undergoing Elective Percutaneous Coronary Intervention.

Background: Ticagrelor presents less thrombotic risk compared to clopidogrel in acute coronary syndromes. However, its role in dual antiplatelet therapy (DAPT)-naive patients with stable ischemic heart disease (SIHD) undergoing elective percutaneous intervention (PCI) remains unclear, including uncertainty in the method of conversion to clopidogrel for adequate coverage without increased bleeding risk.

Objective: Determine the safety and efficacy of ticagrelor loading and transitioning to clopidogrel in patients with SIHD undergoing elective PCI.

Microtubule-associated protein 1 light chain 3 (LC3) interacts with Bnip3 protein to selectively remove endoplasmic reticulum and mitochondria via autophagy.

Autophagy plays an important role in cellular quality control and is responsible for removing protein aggregates and dysfunctional organelles. Bnip3 is an atypical BH3-only protein that is known to cause mitochondrial dysfunction and cell death. Interestingly, Bnip3 can also protect against cell death by inducing mitochondrial autophagy.

A sliding docking interaction is essential for sequential and processive phosphorylation of an SR protein by SRPK1.

The 2.9 A crystal structure of the core SRPK1:ASF/SF2 complex reveals that the N-terminal half of the basic RS domain of ASF/SF2, which is destined to be phosphorylated, is bound to an acidic docking groove of SRPK1 distal to the active site. Phosphorylation of ASF/SF2 at a single site in the C-terminal end of the RS domain generates a primed phosphoserine that binds to a basic site in the kinase.

SR protein kinase 1 is resilient to inactivation.

SR protein kinase 1 (SRPK1) is a constitutively active kinase, which processively phosphorylates multiple serines within its substrates, ASF/SF2. We describe crystallographic, molecular dynamics, and biochemical results that shed light on how SRPK1 preserves its constitutive active conformation. Our structure reveals that unlike other known active kinase structures, the activation loop remains in an active state without any specific intraprotein interactions.