y. takada

FGF2 binds to the allosteric site (site 2) and activates integrin αIIbβ3 and FGF1 binds to site 2 but suppresses integrin activation by FGF2: A potential mechanism of anti-thrombotic action of FGF1.

This study shows FGF2 activates integrin αIIbβ3 via site 2, while FGF1 binds site 2 but inhibits FGF2-induced activation, suggesting FGF1's anti-thrombotic mechanism.

FGF2 binds to the allosteric site (site 2) and activates αvβ3 integrin and FGF1 binds to site 2 but suppresses integrin activation by FGF2: a potential mechanism of anti-inflammatory action of FGF1

This study shows FGF2 activates αvβ3 integrin via site 2, while FGF1 binds site 2 but suppresses integrin activation, suggesting FGF1's anti-inflammatory action is through blocking site 2.

FGF9, a potent mitogen, is a new ligand for integrin αvβ3, and the FGF9 mutant defective in integrin binding acts as an antagonist.

This study identifies FGF9 as a new ligand for integrin αvβ3 and shows that a mutant defective in integrin binding acts as an antagonist by suppressing FGF9 signaling.

The heparin-binding domain of VEGF165 directly binds to integrin αvβ3 and plays a critical role in signaling.

This study identifies the heparin-binding domain of VEGF165 as critical for integrin αvβ3 binding and signaling, showing its role in mitogenic activity.

Pro-inflammatory chemokines CCL5, CXCL12, and CX3CL1 bind to and activate platelet integrin αIIbβ3 in an allosteric manner.

This study identifies CCL5, CXCL12, and CX3CL1 as novel ligands for platelet integrin αIIbβ3 that allosterically activate it, linking inflammation to thrombosis.

Anti-PF4 (heparin-independent)/PF4 complex induces allosteric activation of integrins αIIbβ3 and αvβ3, a potential mechanism of vaccine-induced thrombotic thrombocytopenia (VITT) and autoimmune diseases

This paper shows that the PF4/anti-PF4 complex activates integrins αIIbβ3 and αvβ3 through site 2 binding, suggesting a mechanism for VITT and autoimmune diseases.

The C-type lectin domain of CD62P (P-selectin) is an integrin ligand.

This study identifies the C-type lectin domain of CD62P as a potential integrin ligand through docking simulations and experimental validation, showing distinct binding sites from glycan recognition.

Changes in subcellular structures and states of Pumilio1 regulate the translation of target Mad2 and Cyclin B1 mRNAs

The paper shows that changes in Pumilio1 structures and states regulate the translation of Mad2 and Cyclin B1 mRNAs in mouse oocytes through an aggregation-dissolution mechanism.

Cross-talks of glycosylphosphatidylinositol biosynthesis with glycosphingolipid biosynthesis and ER-associated degradation

The paper identifies B3GALT4's dual role in GPI and glycosphingolipid biosynthesis and shows ER-associated degradation suppresses GPI biosynthesis when GPI transfer to proteins is defective.