Phosphatidylserine Allows Observation of the Calcium–Myristoyl Switch of Recoverin and Its Preferential Binding

2016 ◽  
Vol 138 (41) ◽  
pp. 13533-13540 ◽  
Author(s):  
Philippe Calvez ◽  
Thaís F. Schmidt ◽  
Line Cantin ◽  
Kristina Klinker ◽  
Christian Salesse
Keyword(s):  
Preferential Binding ◽  
Myristoyl Switch

Ca2+-Myristoyl Switch in Neuronal Calcium Sensor-1: A Role of C-Terminal Segment

2015 ◽  
Vol 14 (4) ◽  
pp. 437-451 ◽  
Author(s):  
Viktoriia Baksheeva ◽  
Aliya Nazipova ◽  
Dmitry Zinchenko ◽  
Marina Serebryakova ◽  
Ivan Senin ◽  
...  
Keyword(s):  
Terminal Segment ◽  
Calcium Sensor ◽  
Neuronal Calcium Sensor ◽  
Myristoyl Switch

scholarly journals A bispecific antibody agonist of the IL-2 heterodimeric receptor preferentially promotes in vivo expansion of CD8 and NK cells

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Katherine E. Harris ◽  
Kyle J. Lorentsen ◽  
Harbani K. Malik-Chaudhry ◽  
Kaitlyn Loughlin ◽  
Harish Medlari Basappa ◽  
...  
Keyword(s):  
T Cells ◽  
Nk Cells ◽  
Bispecific Antibody ◽  
T Regulatory Cells ◽  
Tumor Regression ◽  
Interleukin 2 ◽  
In Vivo Studies ◽  
Preferential Binding

AbstractThe use of recombinant interleukin-2 (IL-2) as a therapeutic protein has been limited by significant toxicities despite its demonstrated ability to induce durable tumor-regression in cancer patients. The adverse events and limited efficacy of IL-2 treatment are due to the preferential binding of IL-2 to cells that express the high-affinity, trimeric receptor, IL-2Rαβγ such as endothelial cells and T-regulatory cells, respectively. Here, we describe a novel bispecific heavy-chain only antibody which binds to and activates signaling through the heterodimeric IL-2Rβγ receptor complex that is expressed on resting T-cells and NK cells. By avoiding binding to IL-2Rα, this molecule circumvents the preferential T-reg activation of native IL-2, while maintaining the robust stimulatory effects on T-cells and NK-cells in vitro. In vivo studies in both mice and cynomolgus monkeys confirm the molecule’s in vivo biological activity, extended pharmacodynamics due to the Fc portion of the molecule, and enhanced safety profile. Together, these results demonstrate that the bispecific antibody is a safe and effective IL-2R agonist that harnesses the benefits of the IL-2 signaling pathway as a potential anti-cancer therapy.

Penetration and preferential binding of charged nanoparticles to mixed lipid monolayers: interplay of lipid packing and charge density

Soft Matter ◽  
2020 ◽  
Author(s):  
Anurag Chaudhury ◽  
Koushik Debnath ◽  
Wei Bu ◽  
Nikhil R. Jana ◽  
Jaydeep Kumar Basu
Keyword(s):  
Charge Density ◽  
Biomedical Applications ◽  
Cell Membranes ◽  
Lipid Monolayers ◽  
Cytotoxic Effects ◽  
Lipid Packing ◽  
Preferential Binding ◽  
Charged Nanoparticles

Designing of nanoparticles (NPs) for biomedical applications or mitigating their cytotoxic effects require microscopic understanding of their interactions with cell membranes. Such insight is best obtained by studying model biomembranes...

Conformational effect on the preferential binding of alkali metal cation with crown ether: A molecular level investigation

2009 ◽  
Vol 12 (1-3) ◽  
pp. 93-99 ◽  
Author(s):  
Sulagna De ◽  
Sk. Musharaf Ali ◽  
M.R.K. Shenoi ◽  
Sandip K. Ghosh ◽  
Dilip K. Maity
Keyword(s):  
Crown Ether ◽  
Alkali Metal ◽  
Metal Cation ◽  
Molecular Level ◽  
Alkali Metal Cation ◽  
Conformational Effect ◽  
Preferential Binding

scholarly journals Preferential Binding and Orientation of Recoverin to Phospholipid Monolayers

2009 ◽  
Vol 96 (3) ◽  
pp. 117a-118a
Author(s):  
Philippe Calvez ◽  
Julie Boucher ◽  
Philippe Desmeules ◽  
Christian Salesse
Keyword(s):  
Phospholipid Monolayers ◽  
Preferential Binding

scholarly journals Preferential Binding of E7010 to Murine β3-Tubulin and Decreased β3-Tubulin in E7010-resistant Cell Lines

1998 ◽  
Vol 89 (9) ◽  
pp. 954-962 ◽  
Author(s):  
Yasuo Iwamoto ◽  
Kazuto Nishio ◽  
Hisao Fukumoto ◽  
Kentaro Yoshimatsu ◽  
Michio Yamakido ◽  
...  
Keyword(s):  
Cell Lines ◽  
Resistant Cell ◽  
Preferential Binding

scholarly journals More than redox, biological organic ligands control iron isotope fractionation in the riparian wetland

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Elaheh Lotfi-Kalahroodi ◽  
Anne-Catherine Pierson-Wickmann ◽  
Olivier Rouxel ◽  
Rémi Marsac ◽  
Martine Bouhnik-Le Coz ◽  
...  
Keyword(s):  
Redox Reactions ◽  
Isotope Fractionation ◽  
Isotopic Fractionation ◽  
Isotopic Signature ◽  
Organic Ligands ◽  
Riparian Wetland ◽  
Fe Isotopes ◽  
Preferential Binding ◽  
Isotope Systematics

AbstractAlthough redox reactions are recognized to fractionate iron (Fe) isotopes, the dominant mechanisms controlling the Fe isotope fractionation and notably the role of organic matter (OM) are still debated. Here, we demonstrate how binding to organic ligands governs Fe isotope fractionation beyond that arising from redox reactions. The reductive biodissolution of soil Fe(III) enriched the solution in light Fe isotopes, whereas, with the extended reduction, the preferential binding of heavy Fe isotopes to large biological organic ligands enriched the solution in heavy Fe isotopes. Under oxic conditions, the aggregation/sedimentation of Fe(III) nano-oxides with OM resulted in an initial enrichment of the solution in light Fe isotopes. However, heavy Fe isotopes progressively dominate the solution composition in response to their binding with large biologically-derived organic ligands. Confronted with field data, these results demonstrate that Fe isotope systematics in wetlands are controlled by the OM flux, masking Fe isotope fractionation arising from redox reactions. This work sheds light on an overseen aspect of Fe isotopic fractionation and calls for a reevaluation of the parameters controlling the Fe isotopes fractionation to clarify the interpretation of the Fe isotopic signature.

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