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238 results on '"Paul, Bindu D."'

1. Biliverdin Reductase-A integrates insulin signaling with mitochondrial metabolism through phosphorylation of GSK3β

Author

Lanzillotta, Chiara, Tramutola, Antonella, Lanzillotta, Simona, Greco, Viviana, Pagnotta, Sara, Sanchini, Caterina, Di Angelantonio, Silvia, Forte, Elena, Rinaldo, Serena, Paone, Alessio, Cutruzzolà, Francesca, Cimini, Flavia Agata, Barchetta, Ilaria, Cavallo, Maria Gisella, Urbani, Andrea, Butterfield, D. Allan, Di Domenico, Fabio, Paul, Bindu D., Perluigi, Marzia, Duarte, Joao M.N., and Barone, Eugenio

Published
2024
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5. Identification of a Novel Mechanism Fostering the Alterations of Brain Energy Metabolism: a Link Between AD and T2DM

Author

Lanzillotta, Chiara, primary, Lanzillotta, Simona, additional, Tramutola, Antonella, additional, Pagnotta, Sara, additional, Domenico, Fabio Di, additional, Paul, Bindu D, additional, Snyder, Solomon, additional, Butterfield, D Allan, additional, Perluigi, Marzia, additional, Duarte, Joao MN, additional, and Barone, Eugenio, additional

Published
2023
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8. Selective Persulfide Detection Reveals Evolutionarily Conserved Antiaging Effects of S-Sulfhydration

Author

Zivanovic, Jasmina, Kouroussis, Emilia, Kohl, Joshua B., Adhikari, Bikash, Bursac, Biljana, Schott-Roux, Sonia, Petrovic, Dunja, Miljkovic, Jan Lj., Thomas-Lopez, Daniel, Jung, Youngeun, Miler, Marko, Mitchell, Sarah, Milosevic, Verica, Gomes, Jose Eduardo, Benhar, Moran, Gonzalez-Zorn, Bruno, Ivanovic-Burmazovic, Ivana, Torregrossa, Roberta, Mitchell, James R., Whiteman, Matthew, Schwarz, Guenter, Snyder, Solomon H., Paul, Bindu D., Carroll, Kate S., and Filipovic, Milos R.

Published
2019
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9. Neuroprotective Roles of the Biliverdin Reductase-A/Bilirubin Axis in the Brain.

Author

Paul, Bindu D. and Pieper, Andrew A.

Subjects
*BILIVERDIN, *COGNITIVE aging, *NEUROPROTECTIVE agents, *BILIRUBIN, *COGNITIVE ability, *HOMEOSTASIS
Abstract

Biliverdin reductase-A (BVRA) is a multi-functional enzyme with a multitude of important roles in physiologic redox homeostasis. Classically, BVRA is well known for converting the heme metabolite biliverdin to bilirubin, which is a potent antioxidant in both the periphery and the brain. However, BVRA additionally participates in many neuroprotective signaling cascades in the brain that preserve cognition. Here, we review the neuroprotective roles of BVRA and bilirubin in the brain, which together constitute a BVRA/bilirubin axis that influences healthy aging and cognitive function. [ABSTRACT FROM AUTHOR]

Published
2024
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20. Identification of the NRF2 transcriptional network as a therapeutic target for trigeminal neuropathic pain

Author

Vasavda, Chirag, primary, Xu, Risheng, additional, Liew, Jason, additional, Kothari, Ruchita, additional, Dhindsa, Ryan S., additional, Semenza, Evan R., additional, Paul, Bindu D., additional, Green, Dustin P., additional, Sabbagh, Mark F., additional, Shin, Joseph Y., additional, Yang, Wuyang, additional, Snowman, Adele M., additional, Albacarys, Lauren K., additional, Moghekar, Abhay, additional, Pardo-Villamizar, Carlos A., additional, Luciano, Mark, additional, Huang, Judy, additional, Bettegowda, Chetan, additional, Kwatra, Shawn G., additional, Dong, Xinzhong, additional, Lim, Michael, additional, and Snyder, Solomon H., additional

Published
2022
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24. Cystathionine γ-lyase exacerbates Helicobacter pylori immunopathogenesis by promoting macrophage metabolic remodeling and activation

Author

Latour, Yvonne L., primary, Sierra, Johanna C., additional, Finley, Jordan L., additional, Asim, Mohammad, additional, Barry, Daniel P., additional, Allaman, Margaret M., additional, Smith, Thaddeus M., additional, McNamara, Kara M., additional, Luis, Paula B., additional, Schneider, Claus, additional, Jacobse, Justin, additional, Goettel, Jeremy A., additional, Calcutt, M. Wade, additional, Rose, Kristie L., additional, Schey, Kevin L., additional, Milne, Ginger L., additional, Delgado, Alberto G., additional, Piazuelo, M. Blanca, additional, Paul, Bindu D., additional, Snyder, Solomon H., additional, Gobert, Alain P., additional, and Wilson, Keith T., additional

Published
2022
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27. Biliverdin reductase bridges focal adhesion kinase to Src to modulate synaptic signaling

Author

Vasavda, Chirag, primary, Semenza, Evan R., additional, Liew, Jason, additional, Kothari, Ruchita, additional, Dhindsa, Ryan S., additional, Shanmukha, Shruthi, additional, Lin, Anthony, additional, Tokhunts, Robert, additional, Ricco, Cristina, additional, Snowman, Adele M., additional, Albacarys, Lauren, additional, Pastore, Francesco, additional, Ripoli, Cristian, additional, Grassi, Claudio, additional, Barone, Eugenio, additional, Kornberg, Michael D., additional, Dong, Xinzhong, additional, Paul, Bindu D., additional, and Snyder, Solomon H., additional

Published
2022
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29. Cystathionine γ-lyase deficiency mediates neurodegeneration in huntington's disease

Author

Paul, Bindu D., Sbodio, Juan I., Xu, Risheng, Vandiver, M. Scott, Cha, Jiyoung Y., Snowman, Adele M., and Snyder, Solomon H.

Subjects
Cysteine proteinases -- Physiological aspects, Huntington's chorea -- Risk factors -- Development and progression, Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

Huntington's disease is an autosomal dominant disease associated with a mutation in the gene encoding huntingtin (Htt) leading to expanded polyglutamine repeats of mutant Htt (mHtt) that elicit oxidative stress, neurotoxicity, and motor and behavioural changes (1). Huntington's disease is characterized by highly selective and profound damage to the corpus striatum, which regulates motor function. Striatal selectivity of Huntington's disease may reflect the striatally selective small G protein Rhes binding to mHtt and enhancing its neurotoxicity (2). Specific molecular mechanisms by which mHtt elicits neurodegeneration have been hard to determine. Here we show a major depletion of cystathionine γ-lyase (CSE), the biosynthetic enzyme for cysteine, in Huntington's disease tissues, which may mediate Huntington's disease pathophysiology. The defect occurs at the transcriptional level and seems to reflect influences of mHtt on specificity protein 1, a transcriptional activator for CSE. Consistent with the notion of loss of CSE as a pathogenic mechanism, supplementation with cysteine reverses abnormalities in cultures of Huntington's disease tissues and in intact mouse models of Huntington's disease, suggesting therapeutic potential., CSE is a principal generator of cysteine from cystathionine (3,4). Cystathionine is formed by cystathionine β-synthase (CBS) by condensing homocysteine and serine. CSE, CBS and 3-mercaptopyruvate sulphurtransferase use cysteine to [...]

Published
2014
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36. Biliverdin reductase bridges focal adhesion kinase to Src to modulate synaptic signaling

Author

Vasavda, Chirag, primary, Semenza, Evan R., additional, Liew, Jason, additional, Kothari, Ruchita, additional, Dhindsa, Ryan S., additional, Shanmukha, Shruthi, additional, Ricco, Cristina, additional, Tokhunts, Robert, additional, Snowman, Adele M., additional, Albacarys, Lauren, additional, Paul, Bindu D., additional, and Snyder, Solomon H., additional

Published
2020
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37. Loss of biliverdin reductase‐a (BVR‐A) impairs beneficial effects of CNS insulin on brain energy metabolism favoring the development of Alzheimer's disease (AD) neuropathology

Author

Lanzillotta, Chiara, primary, Tramutola, Antonella, additional, Di Domenico, Fabio, additional, Vasavda, Chirag, additional, Paul, Bindu D., additional, Snyder, Solomon, additional, Butterfield, D. Allan, additional, Perluigi, Marzia, additional, Duarte, Joao M.N., additional, and Barone, Eugenio, additional

Published
2020
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39. Selective Persulfide Detection Reveals Evolutionarily Conserved Antiaging Effects of S-Sulfhydration

Author

Zivanovic, Jasmina, primary, Kouroussis, Emilia, additional, Kohl, Joshua B., additional, Adhikari, Bikash, additional, Bursac, Biljana, additional, Schott-Roux, Sonia, additional, Petrovic, Dunja, additional, Miljkovic, Jan Lj., additional, Thomas-Lopez, Daniel, additional, Jung, Youngeun, additional, Miler, Marko, additional, Mitchell, Sarah, additional, Milosevic, Verica, additional, Gomes, Jose Eduardo, additional, Benhar, Moran, additional, Gonzalez-Zorn, Bruno, additional, Ivanovic-Burmazovic, Ivana, additional, Torregrossa, Roberta, additional, Mitchell, James R., additional, Whiteman, Matthew, additional, Schwarz, Guenter, additional, Snyder, Solomon H., additional, Paul, Bindu D., additional, Carroll, Kate S., additional, and Filipovic, Milos R., additional

Published
2020
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42. Regulators of the transsulfuration pathway

Author

Sbodio, Juan I, Snyder, Solomon H, and Paul, Bindu D

Subjects
Sulfur Compounds, Transcription, Genetic, Animals, Humans, Protein Processing, Post-Translational, Themed Section: Review Article, Signal Transduction
Abstract

The transsulfuration pathway is a metabolic pathway where transfer of sulfur from homocysteine to cysteine occurs. The pathway leads to the generation of several sulfur metabolites, which include cysteine, GSH and the gaseous signalling molecule hydrogen sulfide (H(2)S). Precise control of this pathway is critical for maintenance of optimal cellular function and, therefore, the key enzymes of the pathway, cystathionine β‐synthase and cystathionine γ‐lyase, are regulated at multiple levels. Disruption of the transsulfuration pathway contributes to the pathology of several conditions such as vascular dysfunction, Huntington's disease and during ageing. Treatment with donors of hydrogen sulfide and/or stimulation of this pathway have proved beneficial in several of these disorders. In this review, we focus on the regulation of the transsulfuration pathway pertaining to cysteine and H(2)S, which could be targeted to develop novel therapeutics. LINKED ARTICLES: This article is part of a themed section on Chemical Biology of Reactive Sulfur Species. To view the other articles in this section visit http://onlinelibrary.wiley.com/doi/10.1111/bph.v176.4/issuetoc

Published
2018

50. Regulators of the transsulfuration pathway.

Author

Sbodio, Juan I, Snyder, Solomon H, and Paul, Bindu D

Subjects
SULFURATION, CHEMICAL reactions, HOMOCYSTEINE, CYSTEINE metabolism, HYDROGEN sulfide, CYSTATHIONINE beta-synthase, CYSTATHIONINE beta-lyase, HUNTINGTON disease, ANIMALS, CELLULAR signal transduction, PROTEINS, RNA, SULFUR compounds
Abstract

The transsulfuration pathway is a metabolic pathway where transfer of sulfur from homocysteine to cysteine occurs. The pathway leads to the generation of several sulfur metabolites, which include cysteine, GSH and the gaseous signalling molecule hydrogen sulfide (H2 S). Precise control of this pathway is critical for maintenance of optimal cellular function and, therefore, the key enzymes of the pathway, cystathionine β-synthase and cystathionine γ-lyase, are regulated at multiple levels. Disruption of the transsulfuration pathway contributes to the pathology of several conditions such as vascular dysfunction, Huntington's disease and during ageing. Treatment with donors of hydrogen sulfide and/or stimulation of this pathway have proved beneficial in several of these disorders. In this review, we focus on the regulation of the transsulfuration pathway pertaining to cysteine and H2 S, which could be targeted to develop novel therapeutics. LINKED ARTICLES: This article is part of a themed section on Chemical Biology of Reactive Sulfur Species. To view the other articles in this section visit http://onlinelibrary.wiley.com/doi/10.1111/bph.v176.4/issuetoc. [ABSTRACT FROM AUTHOR]

Published
2019
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