Results 31 to 40 of about 62,112 (126)

Transmembrane thiol isomerase TMX1 counterbalances the effect of ERp46 to inhibit platelet activation and integrin αIIbβ3 function

Research and Practice in Thrombosis and Haemostasis
Background: Previous studies have shown that thiol isomerases such as ERp46 positively regulate platelet function by reducing integrin αIIbβ3 disulfides, and the transmembrane thiol isomerase TMX1 negatively regulates integrin αIIbβ3 activation. However,
Zhenzhen Zhao, Yixin Cheng, Yaqiong Zhang, Meinan Peng, Yue Han, Depei Wu, Aizhen Yang, Yi Wu   +7 more
doaj   +1 more source

New insights into regulation of αIIbβ3 integrin signaling by filamin A

Research and Practice in Thrombosis and Haemostasis, 2022
Background Filamin (FLN) regulates many cell functions through its scaffolding activity cross‐linking cytoskeleton and integrins. FLN was shown to inhibit integrin activity, but the exact mechanism remains unclear. Objectives The aim of this study was to
Lamia Lamrani, Frédéric Adam, Christelle Soukaseum, Cécile V. Denis, Hana Raslova, Jean‐Philippe Rosa, Marijke Bryckaert   +6 more
doaj   +1 more source

Heterodimeric Protein Surface‐Coupling Platform: Immobilization of Conformation Switchable and Functional αIIbβ3 Integrin

Advanced Materials Interfaces, 2023
Many biotechnologies require direct contact between biomolecules and (semi)solid substrates. However, little information is available regarding site‐directed covalent surface immobilization of heterodimeric proteins.
Miguel A. D. Neves, Sladjana Slavkovic, Yiming Wang, Yfke Pasman, Aron A. Shoara, Reid C. Gallant, Guangheng Zhu, Pasquale Benvenuto, Philip E. Johnson, Michael Thompson, Heyu Ni   +10 more
doaj   +1 more source

Integrin Priming Dynamics: Mechanisms of Integrin Antagonist-Promoted αIIbβ3:PAC-1 Molecular Recognition

, 2016
This investigation addressed the paradox that disintegrins and small RGD-ligands readily bind to the resting αIIbβ3 integrin, while macromolecules with similar integrin recognition motifs require an activated, or primed, receptor.
Mary C. Stahle (2255554), Roy R. Hantgan (202202)   +1 more
core   +1 more source

Structural basis for distinctive recognition of fibrinogen γC peptide by the platelet integrin αIIbβ3 [PDF]

, 2008
Hemostasis and thrombosis (blood clotting) involve fibrinogen binding to integrin αIIbβ3 on platelets, resulting in platelet aggregation. αvβ3 binds fibrinogen via an Arg-Asp-Gly (RGD) motif in fibrinogen's α subunit.
Timothy A. Springer, Zhu, Jianghai, Xiao, Tsan, Tsan Xiao, Springer, Timothy, Jianghai Zhu   +5 more
core   +1 more source

Halogenated Tryptophans Improve Integrin αVβ6 Affinity of Cyclic RGD Peptides and Provide Handles for Late‐Stage Derivatization

Chemistry – A European Journal, EarlyView.
Lighting up αVβ6: Halotryptophan engineering converts an RGD scaffold into a modular αVβ6 ligand platform, enabling picomolar affinity and late‐stage functionalization. The resulting probes combine high selectivity with fluorescence for FACS and tumor imaging.
Beate Nachtigall, Caroline Brinkmann, Jana Langosch, Anke Nieß, Norbert Sewald   +4 more
wiley   +1 more source

Integrin αIIbβ3 outside-in signaling

, 2017
Integrin αIIbβ3 is a highly abundant heterodimeric platelet receptor that can transmit information bidirectionally across the plasma membrane, and plays a critical role in hemostasis and thrombosis. Upon platelet activation, inside-out signaling pathways
Marion T. van den Bosch, Tom N. Durrant, Ingeborg Hers   +2 more
core   +1 more source

The β integrin modulates serotonin sensitivity via NPxY motifs to regulate egg laying and mechanosensation behaviors in Caenorhabditis elegans

Developmental Dynamics, EarlyView.
Abstract Background Integrin is an αβ heterodimeric receptor to the extracellular matrix; its binding to the matrix recruits focal adhesions to two NPxY motifs, the tyrosine phosphorylation sites in the cytoplasmic domain. Studies found that replacing tyrosines (Y) with phenylalanines (F) in the motif of β1 integrin displayed little developmental or ...
Josh Haram Bumm, Daniel Dogeon Lee, Zhongqiang Qiu, Angela Haeun Choi, Meghana Kolluri, Michael J. Olsen, Lianzijun Wang, Myeongwoo Lee   +7 more
wiley   +1 more source

Structure-guided design of pure orthosteric inhibitors of αIIbβ3 that prevent thrombosis but preserve hemostasis

Nature Communications, 2020
Current inhibitors of platelet integrin αIIbβ3 cause excessive bleeding, which limited their clinical use in cardiac patients. Here the authors design pure orthosteric αIIbβ3 inhibitors that prevent platelet aggregation and thrombosis without causing ...
Brian D. Adair, José L. Alonso, Johannes van Agthoven, Vincent Hayes, Hyun Sook Ahn, I-Shing Yu, Shu-Wha Lin, Jian-Ping Xiong, Mortimer Poncz, M. Amin Arnaout   +9 more
doaj   +1 more source

Commonalities of platelet dysfunction in heart failure with preserved ejection fraction and underlying comorbidities

ESC Heart Failure, Volume 12, Issue 2, Page 1013-1028, April 2025.
Abstract Heart failure with preserved ejection fraction (HFpEF) is characterized by a lack of a specific targeted treatment and a complex, partially unexplored pathophysiology. Common comorbidities associated with HFpEF are hypertension, atrial fibrillation, obesity and diabetes.
Giorgia D'Italia, Blanche Schroen, Judith M.E.M. Cosemans   +2 more
wiley   +1 more source