Thiol isomerase ERp18 enhances platelet activation and arterial thrombosis

Authors: He, Chao ^{1, 2}, Yang, Aizhen ¹, Lv, Keyu ³, Zhang, Yuxin ², Zhao, Zhenzhen ¹, Lu, Yi ⁴, Fang, Chao ³, Han, Yue ⁵, Wu, Depei ⁵, Jiang, Miao ¹, Zhang, Jingyu ^{2, ∗}, Wu, Yi ^{1, 2, ∗}

Source: In Research and Practice in Thrombosis and Haemostasis February 2025 9(2)

Structural analyses of apolipoprotein A-IV polymorphisms Q360H and T347S elucidate the inhibitory effect against thrombosis

Authors: Shoara, Aron A. ^{1, 2, 3, 4, 5, 6}, Slavkovic, Sladjana ^{2, 3, 7}, Neves, Miguel A.D. ^{2, 3, 7}, Bhoria, Preeti ^{2, 6}, Prifti, Viktor ^{2, 6, 7}, Chen, Pingguo ^{2, 3, 6}, Donaldson, Logan W. ⁸, Beckett, Andrew N. ^{1, 2, 3, 4}, Johnson, Philip E. ^{9, ∗}, Ni, Heyu ^{1, 2, 3, 5, 6, 7, ∗}

Source: In Journal of Biological Chemistry

Platelet spreading and clot retraction are regulated by 2 distinct αIIbβ3 outside-in signaling pathways

Authors: Nigam, Arjit ¹, Manjuprasanna, Voddarahally N. ², Naik, Meghna U. ², Naik, Ulhas P. ^{2, ∗}

Source: In The Journal of Pharmacology and Experimental Therapeutics January 2025 392(1)

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

Authors: Zhenzhen Zhao, Yixin Cheng, Yaqiong Zhang, Meinan Peng, Yue Han, Depei Wu, Aizhen Yang, Yi Wu

Source: Research and Practice in Thrombosis and Haemostasis, Vol 8, Iss 5, Pp 102524- (2024)

Subject Terms: integrin αIIbβ3, platelet, redox, thiol isomerase, TMX1, Diseases of the blood and blood-forming organs, RC633-647.5

File Description: electronic resource

Relation: http://www.sciencedirect.com/science/article/pii/S247503792400219X; https://doaj.org/toc/2475-0379

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Platelet Activation Pathways Controlling Reversible Integrin αIIbβ3 Activation

Authors: Jinmi Zou, Siyu Sun, Ilaria De Simone, Hugo ten Cate, Philip G. de Groot, Bas de Laat, Mark Roest, Johan W.M. Heemskerk, Frauke Swieringa

Source: TH Open, Vol 08, Iss 02, Pp e232-e242 (2024)

Subject Terms: integrin αIIbβ3, glycoprotein VI, P-selectin, protease-activated receptors, protein kinase C, Diseases of the circulatory (Cardiovascular) system, RC666-701

File Description: electronic resource

Relation: https://doaj.org/toc/2512-9465

Access URL: https://doaj.org/article/a1a44a63b65c416f94bc44b92ad11959

Development of the Integrated Computer Simulation Model of the Intracellular, Transmembrane, and Extracellular Domain of Platelet Integrin αIIbβ3 (Platelet Membrane Glycoprotein: GPIIb–IIIa)

Authors: Masamitsu Nakayama, Shinichi Goto, Shinya Goto

Source: TH Open, Vol 08, Iss 01, Pp e96-e105 (2024)

Subject Terms: platelet, integrin αIIbβ3, molecular dynamic simulation, GPIIb/IIIa, Diseases of the circulatory (Cardiovascular) system, RC666-701

File Description: electronic resource

Relation: https://doaj.org/toc/2512-9465

Access URL: https://doaj.org/article/00de3a75164144a98be2428d0016e128

Myricetin as a promising inhibitor of platelet fibrinogen receptor in humans

Authors: Chang, Yi ^{a, b, c, 1}, Hsia, Chih-Wei ^{b, 1}, Huang, Wei-Chieh ^b, Jayakumar, Thanasekaran ^d, Hsia, Chih-Hsuan ^e, Yen, Ting-Lin ^f, Sheu, Joen-Rong ^{b, g, ∗}, Hou, Shaw-Min ^{b, c, h, ∗∗}

Source: In Heliyon October 2023 9(10)

Garcinol acts as a novel integrin αIIbβ3 inhibitor in human platelets

Authors: Hsia, Chih-Wei ^a, Huang, Wei-Chieh ^a, Jayakumar, Thanasekaran ^b, Hsia, Chih-Hsuan ^c, Hou, Shaw-Min ^{d, e}, Chang, Chao-Chien ^{a, d, e}, Yen, Ting-Lin ^d, Sheu, Joen-Rong ^{a, f, ⁎}

Source: In Life Sciences 1 August 2023 326

Novel homozygous silent mutation of ITGB3 gene caused Glanzmann thrombasthenia

Authors: Zhengrong Wang, Yuqing Xu, Yixi Sun, Shuang Wang, Minyue Dong

Source: Frontiers in Pediatrics, Vol 10 (2023)

Subject Terms: Glanzmann thrombasthenia, integrin αIIbβ3, ITGB3, silent mutation, whole exome sequencing, Pediatrics, RJ1-570

File Description: electronic resource

Relation: https://www.frontiersin.org/articles/10.3389/fped.2022.1062900/full; https://doaj.org/toc/2296-2360

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Unraveling the Mechanism of Platelet Aggregation Suppression by Thioterpenoids: Molecular Docking and In Vivo Antiaggregant Activity

Authors: Liliya E. Nikitina, Pavel S. Bocharov, Alexander A. Ksenofontov, Elena V. Antina, Ilmir R. Gilfanov, Roman S. Pavelyev, Olga V. Ostolopovskaya, Inna V. Fedyunina, Zulfiya R. Azizova, Svetlana V. Pestova, Evgeniy S. Izmest’ev, Svetlana A. Rubtsova, Sergei V. Boichuk, Aigul R. Galembikova, Elena A. Smolyarchuk, Ilshat G. Mustafin, Airat R. Kayumov, Aleksandr V. Samorodov

Source: Biomimetics, Vol 8, Iss 8, p 570 (2023)

Subject Terms: S-containing monoterpenoids, molecular docking, integrin αIIbβ3, antiaggregant activity, Technology

File Description: electronic resource

Relation: https://www.mdpi.com/2313-7673/8/8/570; https://doaj.org/toc/2313-7673

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Clot Retraction and Its Correlation with the Function of Platelet Integrin αIIbβ3

Authors: Daniel Gao, Caroline W. Sun, Angela B. Woodley, Jing-fei Dong

Source: Biomedicines, Vol 11, Iss 9, p 2345 (2023)

Subject Terms: clot retraction, integrin αIibβ3, PLA genotypes, Biology (General), QH301-705.5

File Description: electronic resource

Relation: https://www.mdpi.com/2227-9059/11/9/2345; https://doaj.org/toc/2227-9059

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Posttranslational modifications of platelet adhesion receptors

Authors: Shukun Sun, Bao Qiao, Yu Han, Bailu Wang, Shujian Wei, Yuguo Chen

Source: Pharmacological Research, Vol 183, Iss , Pp 106413- (2022)

Subject Terms: Platelets, Adhesion receptors, Glycoprotein Ib-IX-V, Glycoprotein VI, Integrin αIIbβ3, Posttranslational modification, Therapeutics. Pharmacology, RM1-950

File Description: electronic resource

Relation: http://www.sciencedirect.com/science/article/pii/S1043661822003589; https://doaj.org/toc/1096-1186

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Evaluation of blood collection methods and anticoagulants for platelet function analyses on C57BL/6J laboratory mice

Authors: Alexandra Grill, Klytaimnistra Kiouptsi, Cornelia Karwot, Kerstin Jurk, Christoph Reinhardt

Source: Platelets, Vol 31, Iss 8, Pp 981-988 (2020)

Subject Terms: blood collection, integrin αiibβ3, in vitro platelet assay, mice, platelet activation, pre-activation, p-selectin, thromboelastography, Diseases of the blood and blood-forming organs, RC633-647.5

File Description: electronic resource

Relation: https://doaj.org/toc/0953-7104; https://doaj.org/toc/1369-1635

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Modulation of human platelet activation and in vivo vascular thrombosis by columbianadin: regulation by integrin αIIbβ3 inside-out but not outside-in signals

Authors: Shaw-Min Hou, Chih-Wei Hsia, Cheng-Lin Tsai, Chih-Hsuan Hsia, Thanasekaran Jayakumar, Marappan Velusamy, Joen-Rong Sheu

Source: Journal of Biomedical Science, Vol 27, Iss 1, Pp 1-14 (2020)

Subject Terms: CBN, Coumarin derivative, Platelet aggregation, Arterial thrombosis, Integrin αIIbβ3, Medicine

File Description: electronic resource

Relation: http://link.springer.com/article/10.1186/s12929-020-0619-5; https://doaj.org/toc/1423-0127

Access URL: https://doaj.org/article/a95805c688424ed388ae9b7600b23f2f

Pharmacological actions of dieckol on modulation of platelet functions and thrombus formation via integrin αIIbβ3 and cAMP signaling

Authors: Muhammad Irfan, Tae-Hyung Kwon, Hyuk-Woo Kwon, Man Hee Rhee

Source: Pharmacological Research, Vol 177, Iss , Pp 106088- (2022)

Subject Terms: Anti-platelet, Cyclic-AMP, Dieckol, Integrin αIIbβ3, Thrombosis, VASPSer−157, Therapeutics. Pharmacology, RM1-950

File Description: electronic resource

Relation: http://www.sciencedirect.com/science/article/pii/S1043661822000330; https://doaj.org/toc/1096-1186

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Platelet Phenotype Analysis of COVID-19 Patients Reveals Progressive Changes in the Activation of Integrin αIIbβ3, F13A1, the SARS-CoV-2 Target EIF4A1 and Annexin A5

Authors: Huriye Ercan, Waltraud Cornelia Schrottmaier, Anita Pirabe, Anna Schmuckenschlager, David Pereyra, Jonas Santol, Erich Pawelka, Marianna T. Traugott, Christian Schörgenhofer, Tamara Seitz, Mario Karolyi, Jae-Won Yang, Bernd Jilma, Alexander Zoufaly, Alice Assinger, Maria Zellner

Source: Frontiers in Cardiovascular Medicine, Vol 8 (2021)

Subject Terms: COVID-19, thrombosis, platelets, integrin αIIbβ3, coagulation factor XIII (FXIII, F13A1), antiphospholipid syndrome, Diseases of the circulatory (Cardiovascular) system, RC666-701

File Description: electronic resource

Relation: https://www.frontiersin.org/articles/10.3389/fcvm.2021.779073/full; https://doaj.org/toc/2297-055X

Access URL: https://doaj.org/article/3b745cc794fd43db9f5982030c9086d2

A handshake between platelets and neutrophils might fuel deep vein thrombosis

Authors: Martin Kenny, Ingmar Schoen

Source: Platelets, Vol 31, Iss 5, Pp 624-626 (2020)

Subject Terms: choline transporter-like protein 2, slc44a2, inflammation, netosis, integrin αiibβ3, mechanotransduction, Diseases of the blood and blood-forming organs, RC633-647.5

File Description: electronic resource

Relation: https://doaj.org/toc/0953-7104; https://doaj.org/toc/1369-1635

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Rumex acetosa modulates platelet function and inhibits thrombus formation in rats

Authors: Dahye Jeong, Muhammad Irfan, Dong-Ha Lee, Seung-Bok Hong, Jae-Wook Oh, Man Hee Rhee

Source: BMC Complementary Medicine and Therapies, Vol 20, Iss 1, Pp 1-9 (2020)

Subject Terms: Antiplatelet agent, Integrin αIIbβ3, MAPK, Platelets, Rumex acetosa, Thrombosis, Other systems of medicine, RZ201-999

File Description: electronic resource

Relation: http://link.springer.com/article/10.1186/s12906-020-02889-5; https://doaj.org/toc/2662-7671

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Blood platelet research in autism spectrum disorders: In search of biomarkers

Authors: Manisha Padmakumar, Eveline Van Raes, Chris Van Geet, Kathleen Freson

Source: Research and Practice in Thrombosis and Haemostasis, Vol 3, Iss 4, Pp 566-577 (2019)

Subject Terms: autism spectrum disorders, blood platelets, gamma‐aminobutyric acid, integrin αIIbβ3, melatonin, neurotransmitter agents, Diseases of the blood and blood-forming organs, RC633-647.5

File Description: electronic resource

Relation: https://doaj.org/toc/2475-0379

Access URL: https://doaj.org/article/7cf875eacf8e4a6285b3871d84c30ed2

Maximum likelihood approach suggests positive selection in platelet integrin αIIbβ3 in mammalian species

Authors: Luís Bernardo Pina-Cabral, Miguel Carneiro, Begoña Criado, Pedro José Esteves

Source: Platelets, Vol 30, Iss 4, Pp 460-466 (2019)

Subject Terms: platelet integrin αiibβ3, positive selection, Diseases of the blood and blood-forming organs, RC633-647.5

File Description: electronic resource

Relation: https://doaj.org/toc/0953-7104; https://doaj.org/toc/1369-1635

Access URL: https://doaj.org/article/8c9a6141717643c0ba50be255161bd5e