Results 41 to 50 of about 1,158,143 (284)
Therapeutic Apheresis and Dialysis, EarlyView.ABSTRACT Introduction This final analysis of a multicenter, prospective postmarketing surveillance study evaluated the safety of daprodustat in patients with chronic kidney disease anemia in routine clinical practice in Japan. Methods Patients who initiated daprodustat between September 2020 and July 2022 were registered.
Tadao Akizawa +7 more
wiley +1 more source
Comprehensive Approach to Developing Baseline Reference Ranges for Platelet Function
Педиатрическая фармакология, 2023 Background. Thrombocytopathies are topical issues of pediatrics. Platelet dysfunction clinically manifests as thrombotic and hemorrhagic events of various severity and location. Platelet function can be evaluated via aggregatometry.
Olga B. Gordeeva +7 more
doaj +1 more source
An isoform of 14‐3‐3 protein regulates transbilayer lipid movement at the plasma membrane
FEBS Letters, EarlyView.Loss of 14‐3‐3ζ in CHO cells confers resistance to exogenous phosphatidylserine (PS) and impairs endocytosis‐independent inward flip‐flop of fluorescent PS at the plasma membrane. RNAi‐mediated knockdown reproduces this defect, while no additive effect is seen in ATP11C‐deficient cells.
Akiko Yamaji‐Hasegawa +3 more
wiley +1 more source
Platelets, 2018 αIIbβ3, the major platelet integrin, plays a central role in hemostasis and thrombosis. Upon platelet activation, conformation of αIIbβ3 changes and allows fibrinogen binding and, subsequently, platelet aggregation.
Alexia V. Gkourogianni +6 more
doaj +1 more source
Inhibition of platelet aggregation by protease inhibitors. Possible involvement of proteases in platelet aggregation [PDF]
Blood, 1978 Abstract The possible participation of proteases in human platelet aggregation was explored using various protease inhibitors and substrates. Protease inhibitors used included naturally occurring inhibitors of serine proteases and synthetic inhibitors that modify the active site of protease.
N, Aoki, K, Naito, N, Yoshida
openaire +3 more sources
Degradation mechanism of the von Willebrand factor A2 domain by nattokinase
FEBS Letters, EarlyView.Nattokinase, a natto‐derived protease, exhibits potent antithrombotic effects. This study demonstrates that nattokinase directly cleaves the von Willebrand factor (vWF) A2 domain in vitro. Unlike the native regulator ADAMTS13, nattokinase degrades folded vWF independently of shear stress.
Ryuichi Hyakumoto +3 more
wiley +1 more source
AZAPROSTANOIC ACIDS AS INHIBITORS OF PLATELET AGGREGATION.
, 1978 AZAPROSTANOIC ACIDS AS INHIBITORS OF PLATELET ...
STEVEN EDWARD. ENKE (7993676)
core +6 more sources
Journal of Clinical and Translational ScienceOBJECTIVES/GOALS: The research objectives of this project are to elucidate the effects of Bruton’s tyrosine kinase inhibitors (BTKi) of varying target specificity on platelet function with regard to platelet aggregation, adhesion, spreading, and ...
Thomas Kartika +3 more
doaj +1 more source
FEBS Letters, EarlyView.CT10 regulator of kinase (CRK) and CRK‐Like (CRKL) are signaling adaptors driving cell adhesion, motility, differentiation, and proliferation. SH2‐domain containing (SH) proteins are enriched in YXXP motifs which when phosphorylated create preferred binding sites for CRK family SH2 domains.
Phoebe M. Cousens +8 more
wiley +1 more source
A novel role of sesamol in inhibiting NF-κB-mediated signaling in platelet activation
Journal of Biomedical Science, 2011 Background Platelet activation is relevant to a variety of coronary heart diseases. Our previous studies revealed that sesamol possesses potent antiplatelet activity through increasing cyclic AMP formation.
Chang Chao-Chien +6 more
doaj +1 more source