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Stimulation of the steady state ATPase kinetics of the ABC exporter NaAtm1 by a transported substrate GSSG.

Protein science : a publication of the Protein Society

Fan C, Rees DC.
PMID: 34878193
Protein Sci. 2021 Dec 08; doi: 10.1002/pro.4250. Epub 2021 Dec 08.

We report the steady state ATPase activities of the ATP Binding Cassette (ABC) exporter NaAtm1 in the absence and presence of a transported substrate, oxidized glutathione (GSSG), in detergent, nanodiscs and proteoliposomes. The steady state kinetic data were fit...

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Fan C, Rees DC. Stimulation of the steady state ATPase kinetics of the ABC exporter NaAtm1 by a transported substrate GSSG. Protein Sci. 2021;doi: 10.1002/pro.4250.
Fan, C., & Rees, D. C. (2021). Stimulation of the steady state ATPase kinetics of the ABC exporter NaAtm1 by a transported substrate GSSG. Protein science : a publication of the Protein Society, . https://doi.org/10.1002/pro.4250
Fan, Chengcheng, and Rees, Douglas C. "Stimulation of the steady state ATPase kinetics of the ABC exporter NaAtm1 by a transported substrate GSSG." Protein science : a publication of the Protein Society vol. (2021). doi: https://doi.org/10.1002/pro.4250
Fan C, Rees DC. Stimulation of the steady state ATPase kinetics of the ABC exporter NaAtm1 by a transported substrate GSSG. Protein Sci. 2021 Dec 08; doi: 10.1002/pro.4250. Epub 2021 Dec 08. PMID: 34878193.
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High-resolution structure of the membrane-embedded skeletal muscle ryanodine receptor.

Structure (London, England : 1993)

Melville Z, Kim K, Clarke OB, Marks AR.
PMID: 34469755
Structure. 2022 Jan 06;30(1):172-180.e3. doi: 10.1016/j.str.2021.08.001. Epub 2021 Aug 31.

The type 1 ryanodine receptor (RyR)/calcium release channel on the sarcoplasmic reticulum (SR) is required for skeletal muscle excitation-contraction coupling and is the largest known ion channel, composed of four 565-kDa protomers. Cryogenic electron microscopy (cryo-EM) studies of the...

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Melville Z, Kim K, Clarke OB, et al. High-resolution structure of the membrane-embedded skeletal muscle ryanodine receptor. Structure. 2021;30(1):172-180.e3doi: 10.1016/j.str.2021.08.001.
Melville, Z., Kim, K., Clarke, O. B., & Marks, A. R. (2022). High-resolution structure of the membrane-embedded skeletal muscle ryanodine receptor. Structure (London, England : 1993), 30(1), 172-180.e3. https://doi.org/10.1016/j.str.2021.08.001
Melville, Zephan, et al. "High-resolution structure of the membrane-embedded skeletal muscle ryanodine receptor." Structure (London, England : 1993) vol. 30,1 (2022): 172-180.e3. doi: https://doi.org/10.1016/j.str.2021.08.001
Melville Z, Kim K, Clarke OB, Marks AR. High-resolution structure of the membrane-embedded skeletal muscle ryanodine receptor. Structure. 2022 Jan 06;30(1):172-180.e3. doi: 10.1016/j.str.2021.08.001. Epub 2021 Aug 31. PMID: 34469755; PMCID: PMC8741649.
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High-resolution structure of the membrane-embedded skeletal muscle ryanodine receptor.

Structure (London, England : 1993)

Melville Z, Kim K, Clarke OB, Marks AR.
PMID: 34469755
Structure. 2022 Jan 06;30(1):172-180.e3. doi: 10.1016/j.str.2021.08.001. Epub 2021 Aug 31.

The type 1 ryanodine receptor (RyR)/calcium release channel on the sarcoplasmic reticulum (SR) is required for skeletal muscle excitation-contraction coupling and is the largest known ion channel, composed of four 565-kDa protomers. Cryogenic electron microscopy (cryo-EM) studies of the...

Cite
Melville Z, Kim K, Clarke OB, et al. High-resolution structure of the membrane-embedded skeletal muscle ryanodine receptor. Structure. 2021;30(1):172-180.e3doi: 10.1016/j.str.2021.08.001.
Melville, Z., Kim, K., Clarke, O. B., & Marks, A. R. (2022). High-resolution structure of the membrane-embedded skeletal muscle ryanodine receptor. Structure (London, England : 1993), 30(1), 172-180.e3. https://doi.org/10.1016/j.str.2021.08.001
Melville, Zephan, et al. "High-resolution structure of the membrane-embedded skeletal muscle ryanodine receptor." Structure (London, England : 1993) vol. 30,1 (2022): 172-180.e3. doi: https://doi.org/10.1016/j.str.2021.08.001
Melville Z, Kim K, Clarke OB, Marks AR. High-resolution structure of the membrane-embedded skeletal muscle ryanodine receptor. Structure. 2022 Jan 06;30(1):172-180.e3. doi: 10.1016/j.str.2021.08.001. Epub 2021 Aug 31. PMID: 34469755; PMCID: PMC8741649.
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Energetics of lipid transport by the ABC transporter MsbA is lipid dependent.

Communications biology

Guo D, Singh H, Shimoyama A, Guffick C, Tang Y, Rowe SM, Noel T, Spring DR, Fukase K, van Veen HW.
PMID: 34887543
Commun Biol. 2021 Dec 09;4(1):1379. doi: 10.1038/s42003-021-02902-8.

The ABC multidrug exporter MsbA mediates the translocation of lipopolysaccharides and phospholipids across the plasma membrane in Gram-negative bacteria. Although MsbA is structurally well characterised, the energetic requirements of lipid transport remain unknown. Here, we report that, similar to...

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Guo D, Singh H, Shimoyama A, et al. Energetics of lipid transport by the ABC transporter MsbA is lipid dependent. Commun Biol. 2021;4(1):1379doi: 10.1038/s42003-021-02902-8.
Guo, D., Singh, H., Shimoyama, A., Guffick, C., Tang, Y., Rowe, S. M., Noel, T., Spring, D. R., Fukase, K., & van Veen, H. W. (2021). Energetics of lipid transport by the ABC transporter MsbA is lipid dependent. Communications biology, 4(1), 1379. https://doi.org/10.1038/s42003-021-02902-8
Guo, Dawei, et al. "Energetics of lipid transport by the ABC transporter MsbA is lipid dependent." Communications biology vol. 4,1 (2021): 1379. doi: https://doi.org/10.1038/s42003-021-02902-8
Guo D, Singh H, Shimoyama A, Guffick C, Tang Y, Rowe SM, Noel T, Spring DR, Fukase K, van Veen HW. Energetics of lipid transport by the ABC transporter MsbA is lipid dependent. Commun Biol. 2021 Dec 09;4(1):1379. doi: 10.1038/s42003-021-02902-8. PMID: 34887543.
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Tissue factor-loaded collagen/alginate hydrogel beads as a hemostatic agent.

Journal of biomedical materials research. Part B, Applied biomaterials

Liu C, Shi Z, Sun H, Zhao L, Wang X, Huang F.
PMID: 33369080
J Biomed Mater Res B Appl Biomater. 2021 Aug;109(8):1116-1123. doi: 10.1002/jbm.b.34774. Epub 2020 Dec 23.

Uncontrolled hemorrhage accounts for a significant proportion of annual mortality worldwide. The development of bioinspired hemostatic composites can effectively reduce hemorrhage and related deaths. This work aims to develop an efficient hemostatic agent by incorporating tissue factor (TF) integrated...

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Liu C, Shi Z, Sun H, et al. Tissue factor-loaded collagen/alginate hydrogel beads as a hemostatic agent. J Biomed Mater Res B Appl Biomater. 2020;109(8):1116-1123doi: 10.1002/jbm.b.34774.
Liu, C., Shi, Z., Sun, H., Zhao, L., Wang, X., & Huang, F. (2021). Tissue factor-loaded collagen/alginate hydrogel beads as a hemostatic agent. Journal of biomedical materials research. Part B, Applied biomaterials, 109(8), 1116-1123. https://doi.org/10.1002/jbm.b.34774
Liu, Chengkun, et al. "Tissue factor-loaded collagen/alginate hydrogel beads as a hemostatic agent." Journal of biomedical materials research. Part B, Applied biomaterials vol. 109,8 (2021): 1116-1123. doi: https://doi.org/10.1002/jbm.b.34774
Liu C, Shi Z, Sun H, Zhao L, Wang X, Huang F. Tissue factor-loaded collagen/alginate hydrogel beads as a hemostatic agent. J Biomed Mater Res B Appl Biomater. 2021 Aug;109(8):1116-1123. doi: 10.1002/jbm.b.34774. Epub 2020 Dec 23. PMID: 33369080.
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Showing 97 to 101 of 101 entries