Epac activation with 8CPT-AM induced RLC phosphorylation in the perfused hearts. by Yoshiki Ohnuki (576298)

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Epac activation increased MYPT phosphorylation via PLC/PKC. by Yoshiki Ohnuki (576298)

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Schematic summary of the proposed role of Epac1 in the regulation of myofilament function. by Yoshiki Ohnuki (576298)

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Functional characterization of skinned myocardium prepared from Epac1TG. by Yoshiki Ohnuki (576298)

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Epac activation increased RLC phosphorylation via PLC/PKC. by Yoshiki Ohnuki (576298)

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Phosphorylation status of myofilament proteins prepared from Epac1TG. by Yoshiki Ohnuki (576298)

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Effects of chronic ISO infusion on cardiac function in Epac1TG. by Yoshiki Ohnuki (576298)

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Epac1 expression in the hearts of NTG and Epac1TG. by Yoshiki Ohnuki (576298)

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Mutant p53 proteins have impaired DNA binding and transcriptional regulation. by Nathaniel C. Holcomb (22793595)

Synthesis and Preclinical Evaluation of Novel ^99mTc-Labeled FR-Targeting Agents with Satisfactory Imaging Contrast and Reduced Renal Uptake by Junhong Feng (11835903)

“…The results of both in vitro cell and in vivo normal mice biodistribution studies demonstrated specific binding of eight complexes to the FR. Among them, [^99mTc]Tc-DProFA-L1 exhibited lower off-target uptake and high tumor uptake in tumor-bearing mice, and significant inhibition in the biodistribution and SPECT/CT imaging study. …”

This Fig provides a comprehensive annotation of a AKT2 protein, depicting its domains, homologous superfamilies, active and binding sites, and other sites. by Sadia Afrin Runa (22504971)

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Measurement of Na⁺ ratio in the TE and blastocyst cross-sectional area in the ouabain-treated group. by Ayaka Fujishima (21221913)

Prediction of the effect of the 9 nsSNPs on AKT2 proteins’ structure and function by eight computational tools. by Sadia Afrin Runa (22504971)

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Distribution of SNPs and their frequencies based on mutation classes. by Sadia Afrin Runa (22504971)

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Hydrogen bond interactions between Capivasertib (red) and the AKT2 protein (blue) as predicted by molecular docking analyses. by Sadia Afrin Runa (22504971)

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Hydrogen bond interactions between Ipatasertib (red) and the AKT2 protein (blue) as predicted by molecular docking analyses. by Sadia Afrin Runa (22504971)

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Hydrogen bond interactions between Akt1/Akt2-IN-1 (red) and the AKT2 protein (blue) as predicted by molecular docking analyses. by Sadia Afrin Runa (22504971)

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Predicted pathogenicity of R274H, Y265N, and R467W substitutions and their molecular mechanisms. by Sadia Afrin Runa (22504971)

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The Fig illustrates the effects of mutations on the stability, flexibility, compactness, and interactions of the AKT2-Akt1/Akt2-IN-1 through molecular dynamics simulations. by Sadia Afrin Runa (22504971)

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Non-covalent interactions between Capivasertib (ball stick) and the AKT2 protein as predicted by molecular docking analyses. by Sadia Afrin Runa (22504971)

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