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Thermostability-based binding assays reveal complex interplay of cation, substrate and lipid binding in the bacterial DASS transporter, VcINDY.

The Biochemical journal

Sampson CDD, Fàbregas Bellavista C, Stewart MJ, Mulligan C.
PMID: 34643224
Biochem J. 2021 Nov 12;478(21):3847-3867. doi: 10.1042/BCJ20210061.

The divalent anion sodium symporter (DASS) family of transporters (SLC13 family in humans) are key regulators of metabolic homeostasis, disruption of which results in protection from diabetes and obesity, and inhibition of liver cancer cell proliferation. Thus, DASS transporter...

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Sampson CDD, Fàbregas Bellavista C, Stewart MJ, et al. Thermostability-based binding assays reveal complex interplay of cation, substrate and lipid binding in the bacterial DASS transporter, VcINDY. Biochem J. 2021;478(21):3847-3867doi: 10.1042/BCJ20210061.
Sampson, C. D. D., Fàbregas Bellavista, C., Stewart, M. J., & Mulligan, C. (2021). Thermostability-based binding assays reveal complex interplay of cation, substrate and lipid binding in the bacterial DASS transporter, VcINDY. The Biochemical journal, 478(21), 3847-3867. https://doi.org/10.1042/BCJ20210061
Sampson, Connor D D, et al. "Thermostability-based binding assays reveal complex interplay of cation, substrate and lipid binding in the bacterial DASS transporter, VcINDY." The Biochemical journal vol. 478,21 (2021): 3847-3867. doi: https://doi.org/10.1042/BCJ20210061
Sampson CDD, Fàbregas Bellavista C, Stewart MJ, Mulligan C. Thermostability-based binding assays reveal complex interplay of cation, substrate and lipid binding in the bacterial DASS transporter, VcINDY. Biochem J. 2021 Nov 12;478(21):3847-3867. doi: 10.1042/BCJ20210061. PMID: 34643224; PMCID: PMC8652582.
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Revisiting the contribution of mitochondrial biology to the pathophysiology of skeletal muscle insulin resistance.

The Biochemical journal

Frangos SM, Bishop DJ, Holloway GP.
PMID: 34751699
Biochem J. 2021 Nov 12;478(21):3809-3826. doi: 10.1042/BCJ20210145.

While the etiology of type 2 diabetes is multifaceted, the induction of insulin resistance in skeletal muscle is a key phenomenon, and impairments in insulin signaling in this tissue directly contribute to hyperglycemia. Despite the lack of clarity regarding...

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Frangos SM, Bishop DJ, Holloway GP. Revisiting the contribution of mitochondrial biology to the pathophysiology of skeletal muscle insulin resistance. Biochem J. 2021;478(21):3809-3826doi: 10.1042/BCJ20210145.
Frangos, S. M., Bishop, D. J., & Holloway, G. P. (2021). Revisiting the contribution of mitochondrial biology to the pathophysiology of skeletal muscle insulin resistance. The Biochemical journal, 478(21), 3809-3826. https://doi.org/10.1042/BCJ20210145
Frangos, Sara M, et al. "Revisiting the contribution of mitochondrial biology to the pathophysiology of skeletal muscle insulin resistance." The Biochemical journal vol. 478,21 (2021): 3809-3826. doi: https://doi.org/10.1042/BCJ20210145
Frangos SM, Bishop DJ, Holloway GP. Revisiting the contribution of mitochondrial biology to the pathophysiology of skeletal muscle insulin resistance. Biochem J. 2021 Nov 12;478(21):3809-3826. doi: 10.1042/BCJ20210145. PMID: 34751699.
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N-terminal phosphorylation regulates the activity of Glycogen Synthase Kinase 3 from Plasmodium falciparum.

The Biochemical journal

Pazicky S, Alder A, Mertens H, Svergun DI, Gilberger T, Löw C.
PMID: 35023554
Biochem J. 2022 Jan 13; doi: 10.1042/BCJ20210829. Epub 2022 Jan 13.

As the decline of malaria cases stalled over the last five years, novel targets in Plasmodium falciparum are necessary for the development of new drugs. Glycogen Synthase Kinase (PfGSK3) has been identified as a potential target, since its selective...

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Pazicky S, Alder A, Mertens H, et al. N-terminal phosphorylation regulates the activity of Glycogen Synthase Kinase 3 from Plasmodium falciparum. Biochem J. 2022;doi: 10.1042/BCJ20210829.
Pazicky, S., Alder, A., Mertens, H., Svergun, D. I., Gilberger, T., & Löw, C. (2022). N-terminal phosphorylation regulates the activity of Glycogen Synthase Kinase 3 from Plasmodium falciparum. The Biochemical journal, . https://doi.org/10.1042/BCJ20210829
Pazicky, Samuel, et al. "N-terminal phosphorylation regulates the activity of Glycogen Synthase Kinase 3 from Plasmodium falciparum." The Biochemical journal vol. (2022). doi: https://doi.org/10.1042/BCJ20210829
Pazicky S, Alder A, Mertens H, Svergun DI, Gilberger T, Löw C. N-terminal phosphorylation regulates the activity of Glycogen Synthase Kinase 3 from Plasmodium falciparum. Biochem J. 2022 Jan 13; doi: 10.1042/BCJ20210829. Epub 2022 Jan 13. PMID: 35023554.
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Deep learning and generative methods in cheminformatics and chemical biology: navigating small molecule space intelligently.

The Biochemical journal

Kell DB, Samanta S, Swainston N.
PMID: 33290527
Biochem J. 2020 Dec 11;477(23):4559-4580. doi: 10.1042/BCJ20200781.

The number of 'small' molecules that may be of interest to chemical biologists - chemical space - is enormous, but the fraction that have ever been made is tiny. Most strategies are discriminative, i.e. have involved 'forward' problems (have...

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Kell DB, Samanta S, Swainston N. Deep learning and generative methods in cheminformatics and chemical biology: navigating small molecule space intelligently. Biochem J. 2020;477(23):4559-4580doi: 10.1042/BCJ20200781.
Kell, D. B., Samanta, S., & Swainston, N. (2020). Deep learning and generative methods in cheminformatics and chemical biology: navigating small molecule space intelligently. The Biochemical journal, 477(23), 4559-4580. https://doi.org/10.1042/BCJ20200781
Kell, Douglas B, et al. "Deep learning and generative methods in cheminformatics and chemical biology: navigating small molecule space intelligently." The Biochemical journal vol. 477,23 (2020): 4559-4580. doi: https://doi.org/10.1042/BCJ20200781
Kell DB, Samanta S, Swainston N. Deep learning and generative methods in cheminformatics and chemical biology: navigating small molecule space intelligently. Biochem J. 2020 Dec 11;477(23):4559-4580. doi: 10.1042/BCJ20200781. PMID: 33290527; PMCID: PMC7733676.
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Fetuin-A regulates adipose tissue macrophage content and activation in insulin resistant mice through MCP-1 and iNOS: involvement of IFNγ-JAK2-STAT1 pathway.

The Biochemical journal

Chattopadhyay D, Das S, Guria S, Basu S, Mukherjee S.
PMID: 34724561
Biochem J. 2021 Nov 26;478(22):4027-4043. doi: 10.1042/BCJ20210442.

In the context of obesity-induced adipose tissue (AT) inflammation, migration of macrophages and their polarization from predominantly anti-inflammatory to proinflammatory subtype is considered a pivotal event in the loss of adipose insulin sensitivity. Two major chemoattractants, monocyte chemoattractant protein-1...

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Chattopadhyay D, Das S, Guria S, et al. Fetuin-A regulates adipose tissue macrophage content and activation in insulin resistant mice through MCP-1 and iNOS: involvement of IFNγ-JAK2-STAT1 pathway. Biochem J. 2021;478(22):4027-4043doi: 10.1042/BCJ20210442.
Chattopadhyay, D., Das, S., Guria, S., Basu, S., & Mukherjee, S. (2021). Fetuin-A regulates adipose tissue macrophage content and activation in insulin resistant mice through MCP-1 and iNOS: involvement of IFNγ-JAK2-STAT1 pathway. The Biochemical journal, 478(22), 4027-4043. https://doi.org/10.1042/BCJ20210442
Chattopadhyay, Dipanjan, et al. "Fetuin-A regulates adipose tissue macrophage content and activation in insulin resistant mice through MCP-1 and iNOS: involvement of IFNγ-JAK2-STAT1 pathway." The Biochemical journal vol. 478,22 (2021): 4027-4043. doi: https://doi.org/10.1042/BCJ20210442
Chattopadhyay D, Das S, Guria S, Basu S, Mukherjee S. Fetuin-A regulates adipose tissue macrophage content and activation in insulin resistant mice through MCP-1 and iNOS: involvement of IFNγ-JAK2-STAT1 pathway. Biochem J. 2021 Nov 26;478(22):4027-4043. doi: 10.1042/BCJ20210442. PMID: 34724561.
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Accurate and rapid prediction of p.

Physical chemistry chemical physics : PCCP

Sinha V, Laan JJ, Pidko EA.
PMID: 33325474
Phys Chem Chem Phys. 2021 Feb 04;23(4):2557-2567. doi: 10.1039/d0cp05281g.

Rapid and accurate prediction of reactivity descriptors of transition metal (TM) complexes is a major challenge for contemporary quantum chemistry. The recently-developed GFN2-xTB method based on the density functional tight-binding theory (DFT-B) is suitable for high-throughput calculation of geometries...

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Sinha V, Laan JJ, Pidko EA. Accurate and rapid prediction of p. Phys Chem Chem Phys. 2021;23(4):2557-2567doi: 10.1039/d0cp05281g.
Sinha, V., Laan, J. J., & Pidko, E. A. (2021). Accurate and rapid prediction of p. Physical chemistry chemical physics : PCCP, 23(4), 2557-2567. https://doi.org/10.1039/d0cp05281g
Sinha, Vivek, et al. "Accurate and rapid prediction of p." Physical chemistry chemical physics : PCCP vol. 23,4 (2021): 2557-2567. doi: https://doi.org/10.1039/d0cp05281g
Sinha V, Laan JJ, Pidko EA. Accurate and rapid prediction of p. Phys Chem Chem Phys. 2021 Feb 04;23(4):2557-2567. doi: 10.1039/d0cp05281g. PMID: 33325474.
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Interactions between insulin and exercise.

The Biochemical journal

Richter EA, Sylow L, Hargreaves M.
PMID: 34751700
Biochem J. 2021 Nov 12;478(21):3827-3846. doi: 10.1042/BCJ20210185.

The interaction between insulin and exercise is an example of balancing and modifying the effects of two opposing metabolic regulatory forces under varying conditions. While insulin is secreted after food intake and is the primary hormone increasing glucose storage...

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Richter EA, Sylow L, Hargreaves M. Interactions between insulin and exercise. Biochem J. 2021;478(21):3827-3846doi: 10.1042/BCJ20210185.
Richter, E. A., Sylow, L., & Hargreaves, M. (2021). Interactions between insulin and exercise. The Biochemical journal, 478(21), 3827-3846. https://doi.org/10.1042/BCJ20210185
Richter, Erik A, et al. "Interactions between insulin and exercise." The Biochemical journal vol. 478,21 (2021): 3827-3846. doi: https://doi.org/10.1042/BCJ20210185
Richter EA, Sylow L, Hargreaves M. Interactions between insulin and exercise. Biochem J. 2021 Nov 12;478(21):3827-3846. doi: 10.1042/BCJ20210185. PMID: 34751700.
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Insight into the function of active site residues in the catalytic mechanism of human ferrochelatase.

The Biochemical journal

Medlock AE, Najahi-Missaoui W, Shiferaw MT, Albetel AN, Lanzilotta WN, Dailey HA.
PMID: 34402499
Biochem J. 2021 Sep 17;478(17):3239-3252. doi: 10.1042/BCJ20210460.

Ferrochelatase catalyzes the insertion of ferrous iron into a porphyrin macrocycle to produce the essential cofactor, heme. In humans this enzyme not only catalyzes the terminal step, but also serves a regulatory step in the heme synthesis pathway. Over...

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Medlock AE, Najahi-Missaoui W, Shiferaw MT, et al. Insight into the function of active site residues in the catalytic mechanism of human ferrochelatase. Biochem J. 2021;478(17):3239-3252doi: 10.1042/BCJ20210460.
Medlock, A. E., Najahi-Missaoui, W., Shiferaw, M. T., Albetel, A. N., Lanzilotta, W. N., & Dailey, H. A. (2021). Insight into the function of active site residues in the catalytic mechanism of human ferrochelatase. The Biochemical journal, 478(17), 3239-3252. https://doi.org/10.1042/BCJ20210460
Medlock, Amy E, et al. "Insight into the function of active site residues in the catalytic mechanism of human ferrochelatase." The Biochemical journal vol. 478,17 (2021): 3239-3252. doi: https://doi.org/10.1042/BCJ20210460
Medlock AE, Najahi-Missaoui W, Shiferaw MT, Albetel AN, Lanzilotta WN, Dailey HA. Insight into the function of active site residues in the catalytic mechanism of human ferrochelatase. Biochem J. 2021 Sep 17;478(17):3239-3252. doi: 10.1042/BCJ20210460. PMID: 34402499.
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Showing 7261 to 7268 of 7268 entries