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Free Energy Profile of APOBEC3G Protein Calculated by a Molecular Dynamics Simulation.

Biology

Fukunishi Y, Hongo S, Lintuluoto M, Matsuo H.
PMID: 24832225
Biology (Basel). 2012 Jul 26;1(2):245-59. doi: 10.3390/biology1020245.

The human APOBEC3G protein (A3G) is a single-stranded DNA deaminase that inhibits the replication of retrotransposons and retroviruses, including HIV-1. Atomic details of A3G's catalytic mechanism have started to emerge, as the structure of its catalytic domain (A3Gctd) has...

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Fukunishi Y, Hongo S, Lintuluoto M, et al. Free Energy Profile of APOBEC3G Protein Calculated by a Molecular Dynamics Simulation. Biology (Basel). 2012;1(2):245-59doi: 10.3390/biology1020245.
Fukunishi, Y., Hongo, S., Lintuluoto, M., & Matsuo, H. (2012). Free Energy Profile of APOBEC3G Protein Calculated by a Molecular Dynamics Simulation. Biology, 1(2), 245-59. https://doi.org/10.3390/biology1020245
Fukunishi, Yoshifumi, et al. "Free Energy Profile of APOBEC3G Protein Calculated by a Molecular Dynamics Simulation." Biology vol. 1,2 (2012): 245-59. doi: https://doi.org/10.3390/biology1020245
Fukunishi Y, Hongo S, Lintuluoto M, Matsuo H. Free Energy Profile of APOBEC3G Protein Calculated by a Molecular Dynamics Simulation. Biology (Basel). 2012 Jul 26;1(2):245-59. doi: 10.3390/biology1020245. PMID: 24832225; PMCID: PMC4009775.
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Size-dependent structures of NanI+n-1 cluster ions with a methanol adsorbate: a combined study by photodissociation spectroscopy and density-functional theory calculation.

The Journal of chemical physics

Misaizu F, Tsuruta M, Tsunoyama H, Furuya A, Ohno K, Lintuluoto M.
PMID: 16268670
J Chem Phys. 2005 Oct 22;123(16):161101. doi: 10.1063/1.2102909.

Methanol adsorption sites on NanI+n-1 ions were investigated. Photoexcitation to charge-transfer states of NanI+n-1 (methanol) predominantly produces two fragment ions: Nan-1I+n-2 (methanol) (neutral NaI loss) and Nan-1I+n-2(neutral NaI and methanol loss), without forming NanI+n-1 (methanol loss). The relative intensities...

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Misaizu F, Tsuruta M, Tsunoyama H, et al. Size-dependent structures of NanI+n-1 cluster ions with a methanol adsorbate: a combined study by photodissociation spectroscopy and density-functional theory calculation. J Chem Phys. 2005;123(16):161101doi: 10.1063/1.2102909.
Misaizu, F., Tsuruta, M., Tsunoyama, H., Furuya, A., Ohno, K., & Lintuluoto, M. (2005). Size-dependent structures of NanI+n-1 cluster ions with a methanol adsorbate: a combined study by photodissociation spectroscopy and density-functional theory calculation. The Journal of chemical physics, 123(16), 161101. https://doi.org/10.1063/1.2102909
Misaizu, Fuminori, et al. "Size-dependent structures of NanI+n-1 cluster ions with a methanol adsorbate: a combined study by photodissociation spectroscopy and density-functional theory calculation." The Journal of chemical physics vol. 123,16 (2005): 161101. doi: https://doi.org/10.1063/1.2102909
Misaizu F, Tsuruta M, Tsunoyama H, Furuya A, Ohno K, Lintuluoto M. Size-dependent structures of NanI+n-1 cluster ions with a methanol adsorbate: a combined study by photodissociation spectroscopy and density-functional theory calculation. J Chem Phys. 2005 Oct 22;123(16):161101. doi: 10.1063/1.2102909. PMID: 16268670.
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Adsorption of small molecules with the hydroxyl group on sodium halide cluster ions.

The journal of physical chemistry. A

Tsuruta M, Furuya A, Ohno K, Lintuluoto M, Misaizu F.
PMID: 20020720
J Phys Chem A. 2010 Jan 28;114(3):1432-6. doi: 10.1021/jp9072312.

We have investigated adsorption of molecules with hydroxyl group, ROH, on sodium halide cluster ions, Na(n)X(n-1)(+) (X = F and I, n = 10-17) by mass spectrometry and by theoretical calculations. From analysis of the cluster ion intensities, the...

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Tsuruta M, Furuya A, Ohno K, et al. Adsorption of small molecules with the hydroxyl group on sodium halide cluster ions. J Phys Chem A. 2010;114(3):1432-6doi: 10.1021/jp9072312.
Tsuruta, M., Furuya, A., Ohno, K., Lintuluoto, M., & Misaizu, F. (2010). Adsorption of small molecules with the hydroxyl group on sodium halide cluster ions. The journal of physical chemistry. A, 114(3), 1432-6. https://doi.org/10.1021/jp9072312
Tsuruta, Mamoru, et al. "Adsorption of small molecules with the hydroxyl group on sodium halide cluster ions." The journal of physical chemistry. A vol. 114,3 (2010): 1432-6. doi: https://doi.org/10.1021/jp9072312
Tsuruta M, Furuya A, Ohno K, Lintuluoto M, Misaizu F. Adsorption of small molecules with the hydroxyl group on sodium halide cluster ions. J Phys Chem A. 2010 Jan 28;114(3):1432-6. doi: 10.1021/jp9072312. PMID: 20020720.
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Molecular Dynamics Simulation Study on Allosteric Regulation of CD44-Hyaluronan Binding as a Force Sensing Mechanism.

ACS omega

Lintuluoto M, Horioka Y, Hongo S, Lintuluoto JM, Fukunishi Y.
PMID: 33817464
ACS Omega. 2021 Mar 16;6(12):8045-8055. doi: 10.1021/acsomega.0c05502. eCollection 2021 Mar 30.

CD44 protein exists on surfaces of a variety of human cells, acts as a receptor for the hyaluronan (HA) molecule, and mediates cell adhesion via the HA binding in leukocyte trafficking, cell rolling, and so on. The molecular structures...

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Lintuluoto M, Horioka Y, Hongo S, et al. Molecular Dynamics Simulation Study on Allosteric Regulation of CD44-Hyaluronan Binding as a Force Sensing Mechanism. ACS Omega. 2021;6(12):8045-8055doi: 10.1021/acsomega.0c05502.
Lintuluoto, M., Horioka, Y., Hongo, S., Lintuluoto, J. M., & Fukunishi, Y. (2021). Molecular Dynamics Simulation Study on Allosteric Regulation of CD44-Hyaluronan Binding as a Force Sensing Mechanism. ACS omega, 6(12), 8045-8055. https://doi.org/10.1021/acsomega.0c05502
Lintuluoto, Masami, et al. "Molecular Dynamics Simulation Study on Allosteric Regulation of CD44-Hyaluronan Binding as a Force Sensing Mechanism." ACS omega vol. 6,12 (2021): 8045-8055. doi: https://doi.org/10.1021/acsomega.0c05502
Lintuluoto M, Horioka Y, Hongo S, Lintuluoto JM, Fukunishi Y. Molecular Dynamics Simulation Study on Allosteric Regulation of CD44-Hyaluronan Binding as a Force Sensing Mechanism. ACS Omega. 2021 Mar 16;6(12):8045-8055. doi: 10.1021/acsomega.0c05502. eCollection 2021 Mar 30. PMID: 33817464; PMCID: PMC8014924.
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