Results 11 to 20 of about 9,490 (159)

αIIbβ3 binding to a fibrinogen fragment lacking the γ-chain dodecapeptide is activation dependent and EDTA inducible

Blood Advances, 2017
: Platelet integrin receptor αIIbβ3 supports platelet aggregation by binding fibrinogen. The interaction between the fibrinogen C-terminal γ-chain peptide composed of residues γ-404-411 (GAKQAGDV) and the Arg-Gly-Asp (RGD) binding pocket on αIIbβ3 is ...
Hina Zafar, Yi Shang, Jihong Li, George A. David, III, Joseph P. Fernandez, Henrik Molina, Marta Filizola, Barry S. Coller   +7 more
doaj   +2 more sources

Migfilin supports hemostasis and thrombosis through regulating platelet αIIbβ3 outside-in signaling. [PDF]

Haematologica, 2019
Elucidating the regulation mechanism of integrin αIIbβ3 is key to understand platelet biology and thrombotic diseases. Previous in vitro studies have implicated a role of migfilin in the support of platelet αIIbβ3 activation, however, contribution of ...
Yangfan Zhou, Mengjiao Hu, Xiaoyan Chen, Shuai Wang, Jingke Li, Lina Sa, Li Li, Jiaqi Huang, Hongqiang Cheng, Hu Hu   +9 more
doaj   +2 more sources

Mechanistic Basis for the Binding of RGD- and AGDV-Peptides to the Platelet Integrin αIIbβ3 [PDF]

, 2017
© 2017 American Chemical Society.Binding of soluble fibrinogen to the activated conformation of the integrin αIIbβ3 is required for platelet aggregation and is mediated exclusively by the C-terminal AGDV-containing dodecapeptide (γC-12) sequence of the ...
Weisel J., Klochkov V., Litvinov R., Barsegov V., Kononova O., Bennett J., Blokhin D.   +6 more
core   +3 more sources

High-resolution cryo-EM structure of integrin αIIbβ3 bound to disease-causing maternal HPA-1a antibody that blocks integrin activation. [PDF]

Sci Adv
Integrins promote immunity, embryonic development, wound healing, and hemostasis, and are activated by ‘bent/closed’ to ‘extended/open’ conformational changes.
de Pereda JM, Stam W, Gragera M, van der Meer F, Chichón FJ, Zarkadas E, van der Schoot E, Vidarsson G, Takagi J, Margadant C.   +9 more
europepmc   +2 more sources

Strong Binding of Platelet Integrin αIIbβ3 to Fibrin Clots: Potential Target to Destabilize Thrombi [PDF]

, 2017
The formation of platelet thrombi is determined by the integrin αIIbβ3-mediated interactions of platelets with fibrinogen and fibrin. Blood clotting in vivo is catalyzed by thrombin, which simultaneously induces fibrinogen binding to αIIbβ3 and converts ...
Mark S. Alber, Zhiliang Xu, Weisel, John W, Weisel, John W., Kim, Oleg V., Shixin Xu, John W. Weisel, Oleg V. Kim, Bennett, Joel S, Xu, Shixin, Litvinov, Rustem I., Litvinov, Rustem I, Kim, Oleg V, Xu, Zhiliang, Peter Höök, Joel S. Bennett, Alber, Mark S, Alber, Mark S., Höök, Peter, Rustem I. Litvinov, Bennett, Joel S.   +20 more
core   +4 more sources

Directly Activating the Integrin αIIbβ3 Initiates Outside-In Signaling by Causing αIIbβ3 Clustering [PDF]

, 2016
αIIbβ3 activation in platelets is followed by activation of the tyrosine kinase c-Src associated with the carboxyl terminus of the β3 cytosolic tail. Exogenous peptides designed to interact with the αIIb transmembrane (TM) domain activate single αIIbβ3 ...
Bennett, Joel S, Tamura, Ryo, Yoon, Kyungchul, Moore, David T, Yin, Hang, Fong, Karen P, Zhu, Hua, Span, Lisa M, DeGrado, William F   +8 more
core   +1 more source

Wdr1-Dependent Actin Reorganization in Platelet Activation. [PDF]

PLoS ONE, 2016
In resting platelets, the integrin αIIbβ3 is present in a low-affinity "bent" state. During platelet aggregation, intracytoplasmic signals induce conformational changes (inside-out signaling) that result in a "swung-out" conformation competent to bind ...
Swapan K Dasgupta, Anhquyen Le, Qi Da, Miguel Cruz, Rolando E Rumbaut, Perumal Thiagarajan   +5 more
doaj   +1 more source

Platelet integrin αIIbβ3: signal transduction, regulation, and its therapeutic targeting

Journal of Hematology & Oncology, 2019
Integrins are a family of transmembrane glycoprotein signaling receptors that can transmit bioinformation bidirectionally across the plasma membrane.
Jiansong Huang, Xia Li, Xiaofeng Shi, Mark Zhu, Jinghan Wang, Shujuan Huang, Xin Huang, Huafeng Wang, Ling Li, Huan Deng, Yulan Zhou, Jianhua Mao, Zhangbiao Long, Zhixin Ma, Wenle Ye, Jiajia Pan, Xiaodong Xi, Jie Jin   +17 more
doaj   +1 more source

Cryo-EM structures of full-length integrin αIIbβ3 in native lipids

Nature Communications, 2023
Platelet integrin αIIbβ3 is maintained in a bent inactive state (low affinity to physiologic ligand), but can rapidly switch to a ligand-competent (high-affinity) state in response to intracellular signals (“inside-out” activation).
Brian D. Adair, Jian-Ping Xiong, Mark Yeager, M. Amin Arnaout   +3 more
doaj   +1 more source

New αIIbβ3 variants in 28 Turkish Glanzmann patients; structural hypothesis for complex activation by residues variations in I-EGF domains

Platelets, 2022
Glanzmann thrombasthenia (GT) is a rare autosomal recessive bleeding disorder characterized by impaired platelet aggregation due to defects in integrin αIIbβ3, a fibrinogen receptor.
M Y Koker, N Sarper, C Albayrak, B Zulfikar, E Zengin, B Saraymen, D Albayrak, B Koc, H Avcilar, M Karakükcü, C Chenet, F Bianchi, A G de Brevern, R Petermann, V Jallu   +14 more
doaj   +1 more source