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Exploring the cellular network of metabolic flexibility in the adipose tissue.

Genes & nutrition

Tareen SHK, Kutmon M, Adriaens ME, Mariman ECM, de Kok TM, Arts ICW, Evelo CT.
PMID: 30002738
Genes Nutr. 2018 Jul 05;13:17. doi: 10.1186/s12263-018-0609-3. eCollection 2018.

BACKGROUND: Metabolic flexibility is the ability of cells to change substrates for energy production based on the nutrient availability and energy requirement. It has been shown that metabolic flexibility is impaired in obesity and chronic diseases such as type...

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Tareen SHK, Kutmon M, Adriaens ME, et al. Exploring the cellular network of metabolic flexibility in the adipose tissue. Genes Nutr. 2018;13:17doi: 10.1186/s12263-018-0609-3.
Tareen, S. H. K., Kutmon, M., Adriaens, M. E., Mariman, E. C. M., de Kok, T. M., Arts, I. C. W., & Evelo, C. T. (2018). Exploring the cellular network of metabolic flexibility in the adipose tissue. Genes & nutrition, 1317. https://doi.org/10.1186/s12263-018-0609-3
Tareen, Samar H K, et al. "Exploring the cellular network of metabolic flexibility in the adipose tissue." Genes & nutrition vol. 13 (2018): 17. doi: https://doi.org/10.1186/s12263-018-0609-3
Tareen SHK, Kutmon M, Adriaens ME, Mariman ECM, de Kok TM, Arts ICW, Evelo CT. Exploring the cellular network of metabolic flexibility in the adipose tissue. Genes Nutr. 2018 Jul 05;13:17. doi: 10.1186/s12263-018-0609-3. eCollection 2018. PMID: 30002738; PMCID: PMC6034334.
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Monitoring checkpoints of metabolism and protein biogenesis in mitochondria by Phos-tag technology.

Journal of proteomics

Walter C, Marada A, Meisinger C.
PMID: 34813945
J Proteomics. 2021 Nov 20;252:104430. doi: 10.1016/j.jprot.2021.104430. Epub 2021 Nov 20.

A role for reversible phosphorylation in regulation of mitochondrial proteins has been neglected for a long time. Particularly, the import machineries that mediate influx of more than 1000 different precursor proteins into the organelle were considered as predominantly constitutively...

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Walter C, Marada A, Meisinger C. Monitoring checkpoints of metabolism and protein biogenesis in mitochondria by Phos-tag technology. J Proteomics. 2021;252:104430doi: 10.1016/j.jprot.2021.104430.
Walter, C., Marada, A., & Meisinger, C. (2021). Monitoring checkpoints of metabolism and protein biogenesis in mitochondria by Phos-tag technology. Journal of proteomics, 252104430. https://doi.org/10.1016/j.jprot.2021.104430
Walter, Corvin, et al. "Monitoring checkpoints of metabolism and protein biogenesis in mitochondria by Phos-tag technology." Journal of proteomics vol. 252 (2021): 104430. doi: https://doi.org/10.1016/j.jprot.2021.104430
Walter C, Marada A, Meisinger C. Monitoring checkpoints of metabolism and protein biogenesis in mitochondria by Phos-tag technology. J Proteomics. 2021 Nov 20;252:104430. doi: 10.1016/j.jprot.2021.104430. Epub 2021 Nov 20. PMID: 34813945.
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Oxidative phosphorylation enhances the leukemogenic capacity and resistance to chemotherapy of B cell acute lymphoblastic leukemia.

Science advances

Chen C, Hao X, Lai X, Liu L, Zhu J, Shao H, Huang D, Gu H, Zhang T, Yu Z, Xie L, Zhang X, Yang Y, Xu J, Zhao Y, Lu Z, Zheng J.
PMID: 33692103
Sci Adv. 2021 Mar 10;7(11). doi: 10.1126/sciadv.abd6280. Print 2021 Mar.

How metabolic status controls the fates of different types of leukemia cells remains elusive. Using a SoNar-transgenic mouse line, we demonstrated that B cell acute lymphoblastic leukemia (B-ALL) cells had a preference in using oxidative phosphorylation. B-ALL cells with...

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Chen C, Hao X, Lai X, et al. Oxidative phosphorylation enhances the leukemogenic capacity and resistance to chemotherapy of B cell acute lymphoblastic leukemia. Sci Adv. 2021;7(11)doi: 10.1126/sciadv.abd6280.
Chen, C., Hao, X., Lai, X., Liu, L., Zhu, J., Shao, H., Huang, D., Gu, H., Zhang, T., Yu, Z., Xie, L., Zhang, X., Yang, Y., Xu, J., Zhao, Y., Lu, Z., & Zheng, J. (2021). Oxidative phosphorylation enhances the leukemogenic capacity and resistance to chemotherapy of B cell acute lymphoblastic leukemia. Science advances, 7(11), . https://doi.org/10.1126/sciadv.abd6280
Chen, Chiqi, et al. "Oxidative phosphorylation enhances the leukemogenic capacity and resistance to chemotherapy of B cell acute lymphoblastic leukemia." Science advances vol. 7,11 (2021). doi: https://doi.org/10.1126/sciadv.abd6280
Chen C, Hao X, Lai X, Liu L, Zhu J, Shao H, Huang D, Gu H, Zhang T, Yu Z, Xie L, Zhang X, Yang Y, Xu J, Zhao Y, Lu Z, Zheng J. Oxidative phosphorylation enhances the leukemogenic capacity and resistance to chemotherapy of B cell acute lymphoblastic leukemia. Sci Adv. 2021 Mar 10;7(11). doi: 10.1126/sciadv.abd6280. Print 2021 Mar. PMID: 33692103; PMCID: PMC7946372.
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Hsp40 Affinity to Identify Proteins Destabilized by Cellular Toxicant Exposure.

Analytical chemistry

Quanrud GM, Montoya MR, Mei L, Awad MR, Genereux JC.
PMID: 34874156
Anal Chem. 2021 Dec 07; doi: 10.1021/acs.analchem.1c04230. Epub 2021 Dec 07.

Environmental toxins and toxicants can damage proteins and threaten cellular proteostasis. Most current methodologies to identify misfolded proteins in cells survey the entire proteome for sites of changed reactivity. We describe and apply a quantitative proteomics methodology to identify...

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Quanrud GM, Montoya MR, Mei L, et al. Hsp40 Affinity to Identify Proteins Destabilized by Cellular Toxicant Exposure. Anal Chem. 2021;doi: 10.1021/acs.analchem.1c04230.
Quanrud, G. M., Montoya, M. R., Mei, L., Awad, M. R., & Genereux, J. C. (2021). Hsp40 Affinity to Identify Proteins Destabilized by Cellular Toxicant Exposure. Analytical chemistry, . https://doi.org/10.1021/acs.analchem.1c04230
Quanrud, Guy M, et al. "Hsp40 Affinity to Identify Proteins Destabilized by Cellular Toxicant Exposure." Analytical chemistry vol. (2021). doi: https://doi.org/10.1021/acs.analchem.1c04230
Quanrud GM, Montoya MR, Mei L, Awad MR, Genereux JC. Hsp40 Affinity to Identify Proteins Destabilized by Cellular Toxicant Exposure. Anal Chem. 2021 Dec 07; doi: 10.1021/acs.analchem.1c04230. Epub 2021 Dec 07. PMID: 34874156.
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The phenotypic spectrum of dihydrolipoamide dehydrogenase deficiency in Saudi Arabia.

Molecular genetics and metabolism reports

Alfarsi A, Alfadhel M, Alameer S, Alhashem A, Tabarki B, Ababneh F, Al Fares A, Al Mutairi F.
PMID: 34745891
Mol Genet Metab Rep. 2021 Oct 23;29:100817. doi: 10.1016/j.ymgmr.2021.100817. eCollection 2021 Dec.

BACKGROUND: Dihydrolipoamide dehydrogenase deficiency (DLDD) is a rare metabolic disorder inherited in an autosomal recessive manner. This heterogeneous disease has a variable clinical presentation, onset, and biochemical markers.MATERIALS AND METHODS: We retrospectively reviewed the clinical and molecular diagnosis of...

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Alfarsi A, Alfadhel M, Alameer S, et al. The phenotypic spectrum of dihydrolipoamide dehydrogenase deficiency in Saudi Arabia. Mol Genet Metab Rep. 2021;29:100817doi: 10.1016/j.ymgmr.2021.100817.
Alfarsi, A., Alfadhel, M., Alameer, S., Alhashem, A., Tabarki, B., Ababneh, F., Al Fares, A., & Al Mutairi, F. (2021). The phenotypic spectrum of dihydrolipoamide dehydrogenase deficiency in Saudi Arabia. Molecular genetics and metabolism reports, 29100817. https://doi.org/10.1016/j.ymgmr.2021.100817
Alfarsi, Anar, et al. "The phenotypic spectrum of dihydrolipoamide dehydrogenase deficiency in Saudi Arabia." Molecular genetics and metabolism reports vol. 29 (2021): 100817. doi: https://doi.org/10.1016/j.ymgmr.2021.100817
Alfarsi A, Alfadhel M, Alameer S, Alhashem A, Tabarki B, Ababneh F, Al Fares A, Al Mutairi F. The phenotypic spectrum of dihydrolipoamide dehydrogenase deficiency in Saudi Arabia. Mol Genet Metab Rep. 2021 Oct 23;29:100817. doi: 10.1016/j.ymgmr.2021.100817. eCollection 2021 Dec. PMID: 34745891; PMCID: PMC8554626.
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The Pyruvate Dehydrogenase Complex in Sepsis: Metabolic Regulation and Targeted Therapy.

Frontiers in nutrition

Zeng Z, Huang Q, Mao L, Wu J, An S, Chen Z, Zhang W.
PMID: 34970577
Front Nutr. 2021 Dec 14;8:783164. doi: 10.3389/fnut.2021.783164. eCollection 2021.

Anaerobic glycolysis is the process by which glucose is broken down into pyruvate and lactate and is the primary metabolic pathway in sepsis. The pyruvate dehydrogenase complex (PDHC) is a multienzyme complex that serves as a critical hub in...

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Zeng Z, Huang Q, Mao L, et al. The Pyruvate Dehydrogenase Complex in Sepsis: Metabolic Regulation and Targeted Therapy. Front Nutr. 2021;8:783164doi: 10.3389/fnut.2021.783164.
Zeng, Z., Huang, Q., Mao, L., Wu, J., An, S., Chen, Z., & Zhang, W. (2021). The Pyruvate Dehydrogenase Complex in Sepsis: Metabolic Regulation and Targeted Therapy. Frontiers in nutrition, 8783164. https://doi.org/10.3389/fnut.2021.783164
Zeng, Zhenhua, et al. "The Pyruvate Dehydrogenase Complex in Sepsis: Metabolic Regulation and Targeted Therapy." Frontiers in nutrition vol. 8 (2021): 783164. doi: https://doi.org/10.3389/fnut.2021.783164
Zeng Z, Huang Q, Mao L, Wu J, An S, Chen Z, Zhang W. The Pyruvate Dehydrogenase Complex in Sepsis: Metabolic Regulation and Targeted Therapy. Front Nutr. 2021 Dec 14;8:783164. doi: 10.3389/fnut.2021.783164. eCollection 2021. PMID: 34970577; PMCID: PMC8712327.
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PKM1 Exerts Critical Roles in Cardiac Remodeling Under Pressure Overload in the Heart.

Circulation

Li Q, Li C, Elnwasany A, Sharma G, An YA, Zhang G, Elhelaly WM, Lin J, Gong Y, Chen G, Wang M, Zhao S, Dai C, Smart CD, Liu J, Luo X, Deng Y, Tan L, Lv SJ, Davidson SM, Locasale JW, Lorenzi PL, Malloy CR, Gillette TG, Vander Heiden MG, Scherer PE, Szweda LI, Fu G, Wang ZV.
PMID: 34102853
Circulation. 2021 Aug 31;144(9):712-727. doi: 10.1161/CIRCULATIONAHA.121.054885. Epub 2021 Jun 09.

BACKGROUND: Metabolic remodeling precedes most alterations during cardiac hypertrophic growth under hemodynamic stress. The elevation of glucose utilization has been recognized as a hallmark of metabolic remodeling. However, its role in cardiac hypertrophic growth and heart failure in response...

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Li Q, Li C, Elnwasany A, et al. PKM1 Exerts Critical Roles in Cardiac Remodeling Under Pressure Overload in the Heart. Circulation. 2021;144(9):712-727doi: 10.1161/CIRCULATIONAHA.121.054885.
Li, Q., Li, C., Elnwasany, A., Sharma, G., An, Y. A., Zhang, G., Elhelaly, W. M., Lin, J., Gong, Y., Chen, G., Wang, M., Zhao, S., Dai, C., Smart, C. D., Liu, J., Luo, X., Deng, Y., Tan, L., Lv, S. J., Davidson, S. M., Locasale, J. W., Lorenzi, P. L., Malloy, C. R., Gillette, T. G., Vander Heiden, M. G., Scherer, P. E., Szweda, L. I., Fu, G., & Wang, Z. V. (2021). PKM1 Exerts Critical Roles in Cardiac Remodeling Under Pressure Overload in the Heart. Circulation, 144(9), 712-727. https://doi.org/10.1161/CIRCULATIONAHA.121.054885
Li, Qinfeng, et al. "PKM1 Exerts Critical Roles in Cardiac Remodeling Under Pressure Overload in the Heart." Circulation vol. 144,9 (2021): 712-727. doi: https://doi.org/10.1161/CIRCULATIONAHA.121.054885
Li Q, Li C, Elnwasany A, Sharma G, An YA, Zhang G, Elhelaly WM, Lin J, Gong Y, Chen G, Wang M, Zhao S, Dai C, Smart CD, Liu J, Luo X, Deng Y, Tan L, Lv SJ, Davidson SM, Locasale JW, Lorenzi PL, Malloy CR, Gillette TG, Vander Heiden MG, Scherer PE, Szweda LI, Fu G, Wang ZV. PKM1 Exerts Critical Roles in Cardiac Remodeling Under Pressure Overload in the Heart. Circulation. 2021 Aug 31;144(9):712-727. doi: 10.1161/CIRCULATIONAHA.121.054885. Epub 2021 Jun 09. PMID: 34102853; PMCID: PMC8405569.
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Deciphering the Probiotic Potential of Bacillus amyloliquefaciens COFCAU_P1 Isolated from the Intestine of Labeo rohita Through In Vitro and Genetic Assessment.

Probiotics and antimicrobial proteins

Khan MIR, Kamilya D, Choudhury TG, Tripathy PS, Rathore G.
PMID: 33900565
Probiotics Antimicrob Proteins. 2021 Dec;13(6):1572-1584. doi: 10.1007/s12602-021-09788-2. Epub 2021 Apr 26.

In this study, a bacterial strain COFCAU_P1, isolated from the digestive tract of a freshwater teleost rohu (Labeo rohita), was identified as Bacillus amyloliquefaciens using 16S rRNA gene sequence analysis combined with amplification of species-specific BamHI and barnase genes....

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Khan MIR, Kamilya D, Choudhury TG, et al. Deciphering the Probiotic Potential of Bacillus amyloliquefaciens COFCAU_P1 Isolated from the Intestine of Labeo rohita Through In Vitro and Genetic Assessment. Probiotics Antimicrob Proteins. 2021;13(6):1572-1584doi: 10.1007/s12602-021-09788-2.
Khan, M. I. R., Kamilya, D., Choudhury, T. G., Tripathy, P. S., & Rathore, G. (2021). Deciphering the Probiotic Potential of Bacillus amyloliquefaciens COFCAU_P1 Isolated from the Intestine of Labeo rohita Through In Vitro and Genetic Assessment. Probiotics and antimicrobial proteins, 13(6), 1572-1584. https://doi.org/10.1007/s12602-021-09788-2
Khan, Md Idrish Raja, et al. "Deciphering the Probiotic Potential of Bacillus amyloliquefaciens COFCAU_P1 Isolated from the Intestine of Labeo rohita Through In Vitro and Genetic Assessment." Probiotics and antimicrobial proteins vol. 13,6 (2021): 1572-1584. doi: https://doi.org/10.1007/s12602-021-09788-2
Khan MIR, Kamilya D, Choudhury TG, Tripathy PS, Rathore G. Deciphering the Probiotic Potential of Bacillus amyloliquefaciens COFCAU_P1 Isolated from the Intestine of Labeo rohita Through In Vitro and Genetic Assessment. Probiotics Antimicrob Proteins. 2021 Dec;13(6):1572-1584. doi: 10.1007/s12602-021-09788-2. Epub 2021 Apr 26. PMID: 33900565.
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Dihydrolipoamide dehydrogenase moonlighting activity as a DNA chelating agent.

Proteins

Dayan A, Yeheskel A, Lamed R, Fleminger G, Ashur-Fabian O.
PMID: 32761961
Proteins. 2020 Aug 06; doi: 10.1002/prot.25991. Epub 2020 Aug 06.

Dihydrolipoamide dehydrogenase (DLDH) is a mitochondrial enzyme that comprises an essential component of the pyruvate dehydrogenase complex. Lines of evidence have shown that many dehydrogenases possess unrelated actions known as moonlightings in addition to their oxidoreductase activity. As part...

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Dayan A, Yeheskel A, Lamed R, et al. Dihydrolipoamide dehydrogenase moonlighting activity as a DNA chelating agent. Proteins. 2020;doi: 10.1002/prot.25991.
Dayan, A., Yeheskel, A., Lamed, R., Fleminger, G., & Ashur-Fabian, O. (2020). Dihydrolipoamide dehydrogenase moonlighting activity as a DNA chelating agent. Proteins, . https://doi.org/10.1002/prot.25991
Dayan, Avraham, et al. "Dihydrolipoamide dehydrogenase moonlighting activity as a DNA chelating agent." Proteins vol. (2020). doi: https://doi.org/10.1002/prot.25991
Dayan A, Yeheskel A, Lamed R, Fleminger G, Ashur-Fabian O. Dihydrolipoamide dehydrogenase moonlighting activity as a DNA chelating agent. Proteins. 2020 Aug 06; doi: 10.1002/prot.25991. Epub 2020 Aug 06. PMID: 32761961.
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Solvent accessibility of E1α and E1β residues with known missense mutations causing pyruvate dehydrogenase complex (PDC) deficiency: Impact on PDC-E1 structure and function.

Journal of inherited metabolic disease

Ducich NH, Mears JA, Bedoyan JK.
PMID: 35038180
J Inherit Metab Dis. 2022 Jan 17; doi: 10.1002/jimd.12477. Epub 2022 Jan 17.

Pyruvate dehydrogenase complex deficiency (PDCD) is a major cause of primary lactic acidemia resulting in high morbidity and mortality, with limited therapeutic options. PDHA1 mutations are responsible for >82% of cases. The E1 component of PDC is a symmetric...

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Ducich NH, Mears JA, Bedoyan JK. Solvent accessibility of E1α and E1β residues with known missense mutations causing pyruvate dehydrogenase complex (PDC) deficiency: Impact on PDC-E1 structure and function. J Inherit Metab Dis. 2022;doi: 10.1002/jimd.12477.
Ducich, N. H., Mears, J. A., & Bedoyan, J. K. (2022). Solvent accessibility of E1α and E1β residues with known missense mutations causing pyruvate dehydrogenase complex (PDC) deficiency: Impact on PDC-E1 structure and function. Journal of inherited metabolic disease, . https://doi.org/10.1002/jimd.12477
Ducich, Nicole H, et al. "Solvent accessibility of E1α and E1β residues with known missense mutations causing pyruvate dehydrogenase complex (PDC) deficiency: Impact on PDC-E1 structure and function." Journal of inherited metabolic disease vol. (2022). doi: https://doi.org/10.1002/jimd.12477
Ducich NH, Mears JA, Bedoyan JK. Solvent accessibility of E1α and E1β residues with known missense mutations causing pyruvate dehydrogenase complex (PDC) deficiency: Impact on PDC-E1 structure and function. J Inherit Metab Dis. 2022 Jan 17; doi: 10.1002/jimd.12477. Epub 2022 Jan 17. PMID: 35038180.
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Monitoring checkpoints of metabolism and protein biogenesis in mitochondria by Phos-tag technology.

Journal of proteomics

Walter C, Marada A, Meisinger C.
PMID: 34813945
J Proteomics. 2021 Nov 20;252:104430. doi: 10.1016/j.jprot.2021.104430. Epub 2021 Nov 20.

A role for reversible phosphorylation in regulation of mitochondrial proteins has been neglected for a long time. Particularly, the import machineries that mediate influx of more than 1000 different precursor proteins into the organelle were considered as predominantly constitutively...

Cite
Walter C, Marada A, Meisinger C. Monitoring checkpoints of metabolism and protein biogenesis in mitochondria by Phos-tag technology. J Proteomics. 2021;252:104430doi: 10.1016/j.jprot.2021.104430.
Walter, C., Marada, A., & Meisinger, C. (2021). Monitoring checkpoints of metabolism and protein biogenesis in mitochondria by Phos-tag technology. Journal of proteomics, 252104430. https://doi.org/10.1016/j.jprot.2021.104430
Walter, Corvin, et al. "Monitoring checkpoints of metabolism and protein biogenesis in mitochondria by Phos-tag technology." Journal of proteomics vol. 252 (2021): 104430. doi: https://doi.org/10.1016/j.jprot.2021.104430
Walter C, Marada A, Meisinger C. Monitoring checkpoints of metabolism and protein biogenesis in mitochondria by Phos-tag technology. J Proteomics. 2021 Nov 20;252:104430. doi: 10.1016/j.jprot.2021.104430. Epub 2021 Nov 20. PMID: 34813945.
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E. coli and the etiology of human PBC: Antimitochondrial antibodies and spreading determinants.

Hepatology (Baltimore, Md.)

Yang Y, Choi J, Chen Y, Invernizzi P, Yang G, Zhang W, Shao TH, Jordan F, Nemeria NS, Coppel RL, Ridgway WM, Kurth M, Ansari AA, Leung PSC, Gershwin ME.
PMID: 34608663
Hepatology. 2022 Feb;75(2):266-279. doi: 10.1002/hep.32172. Epub 2021 Dec 12.

BACKGROUND AND AIMS: The increased frequency of urinary tract infections in patients with primary biliary cholangitis (PBC) and the cross-reactivity between the lipoyl domains (LD) of human pyruvate dehydrogenase complex (hPDC-E2) and Escherichia coli PDC-E2 (ePDC-E2) have long suggested...

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Yang Y, Choi J, Chen Y, et al. E. coli and the etiology of human PBC: Antimitochondrial antibodies and spreading determinants. Hepatology. 2021;75(2):266-279doi: 10.1002/hep.32172.
Yang, Y., Choi, J., Chen, Y., Invernizzi, P., Yang, G., Zhang, W., Shao, T. H., Jordan, F., Nemeria, N. S., Coppel, R. L., Ridgway, W. M., Kurth, M., Ansari, A. A., Leung, P. S. C., & Gershwin, M. E. (2022). E. coli and the etiology of human PBC: Antimitochondrial antibodies and spreading determinants. Hepatology (Baltimore, Md.), 75(2), 266-279. https://doi.org/10.1002/hep.32172
Yang, Yao, et al. "E. coli and the etiology of human PBC: Antimitochondrial antibodies and spreading determinants." Hepatology (Baltimore, Md.) vol. 75,2 (2022): 266-279. doi: https://doi.org/10.1002/hep.32172
Yang Y, Choi J, Chen Y, Invernizzi P, Yang G, Zhang W, Shao TH, Jordan F, Nemeria NS, Coppel RL, Ridgway WM, Kurth M, Ansari AA, Leung PSC, Gershwin ME. E. coli and the etiology of human PBC: Antimitochondrial antibodies and spreading determinants. Hepatology. 2022 Feb;75(2):266-279. doi: 10.1002/hep.32172. Epub 2021 Dec 12. PMID: 34608663.
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Showing 25 to 36 of 185 entries