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S-nitrosylation of the thioredoxin-like domains of protein disulfide isomerase and its role in neurodegenerative conditions (2015)
Journal Article
Conway, M. E., & Harris, M. (2015). S-nitrosylation of the thioredoxin-like domains of protein disulfide isomerase and its role in neurodegenerative conditions. Frontiers in Chemistry, 3(APR), https://doi.org/10.3389/fchem.2015.00027

© 2015 Conway and Harris. Correct protein folding and inhibition of protein aggregation is facilitated by a cellular "quality control system" that engages a network of protein interactions including molecular chaperones and the ubiquitin proteasome s... Read More about S-nitrosylation of the thioredoxin-like domains of protein disulfide isomerase and its role in neurodegenerative conditions.

The redox switch that regulates molecular chaperones (2015)
Journal Article
Conway, M. E., & Lee, C. (2015). The redox switch that regulates molecular chaperones. BioMolecular Concepts, 6(4), 269-284. https://doi.org/10.1515/bmc-2015-0015

© 2015 by De Gruyter. Modification of reactive cysteine residues plays an integral role in redox-regulated reactions. Oxidation of thiolate anions to sulphenic acid can result in disulphide bond formation, or overoxidation to sulphonic acid, represen... Read More about The redox switch that regulates molecular chaperones.

Regional Increase in the Expression of the BCAT Proteins in Alzheimer's Disease Brain: Implications in Glutamate Toxicity (2015)
Journal Article
Hull, J., Patel, V., El Hindy, M., Lee, C., Odeleye, E., Hezwani, M., …Conway, M. (2015). Regional Increase in the Expression of the BCAT Proteins in Alzheimer's Disease Brain: Implications in Glutamate Toxicity. Journal of Alzheimer's Disease, 45(3), 891-905. https://doi.org/10.3233/JAD-142970

© 2015 - IOS Press and the authors. All rights reserved. Background: The human branched chain aminotransferases (hBCATm, mitochondrial and hBCATc, cytosolic) are major contributors to brain glutamate production. This excitatory neurotransmitter is th... Read More about Regional Increase in the Expression of the BCAT Proteins in Alzheimer's Disease Brain: Implications in Glutamate Toxicity.

The branched-chain aminotransferase proteins: Novel redox chaperones for protein disulfide isomerase-implications in Alzheimer's disease (2014)
Journal Article
Patel, V. B., Lee, C., El Hindy, M., Hezwani, M., Corry, D., Hull, J., …Conway, M. E. (2014). The branched-chain aminotransferase proteins: Novel redox chaperones for protein disulfide isomerase-implications in Alzheimer's disease. Antioxidants and Redox Signaling, 20(16), 2497-2513. https://doi.org/10.1089/ars.2012.4869

Aims: The human branched-chain aminotransferase proteins (hBCATm and hBCATc) are regulated through oxidation and S-nitrosation. However, it remains unknown whether they share common redox characteristics to enzymes such as protein disulfide isomerase... Read More about The branched-chain aminotransferase proteins: Novel redox chaperones for protein disulfide isomerase-implications in Alzheimer's disease.

Investigation and verification of a bioluminescent biosensor for the quantitation of ara-CTP generation: A biomarker for cytosine arabinoside sensitivity in acute myeloid leukaemia (2014)
Journal Article
Graham Smith, J., Peter Fitzgerald, S., Martin, A., Ann Smith, M., Conway, M., Anderson, E., …Salisbury, V. (2014). Investigation and verification of a bioluminescent biosensor for the quantitation of ara-CTP generation: A biomarker for cytosine arabinoside sensitivity in acute myeloid leukaemia. Biosensors and Bioelectronics, 52, 345-353. https://doi.org/10.1016/j.bios.2013.09.014

A novel whole cell bacterial biosensor, which emits light in response to the active metabolite of cytosine arabinoside (ara-C, cytarabine), ara-CTP, has been investigated and verified. The biosensor has been formulated as an ex vivo assay, designed f... Read More about Investigation and verification of a bioluminescent biosensor for the quantitation of ara-CTP generation: A biomarker for cytosine arabinoside sensitivity in acute myeloid leukaemia.

A novel bioluminescent bacterial biosensor for measurement of Ara-CTP and cytarabine potentiation by fludarabine in seven leukaemic cell lines (2013)
Journal Article
Conway, M., Anderson, E., Smith, M. A., Martin, A., Ruddock, M., Lamont, J., …Salisbury, V. (2013). A novel bioluminescent bacterial biosensor for measurement of Ara-CTP and cytarabine potentiation by fludarabine in seven leukaemic cell lines. Leukemia Research, 37(6), 690-696. https://doi.org/10.1016/j.leukres.2013.02.012

This study evaluates an in vitro biosensor assay capable of detecting the intracellular levels of the tri-phosphorylated form of cytarabine (Ara-CTP) within one working day. The biosensor predicted the response of seven leukaemic cell lines with vary... Read More about A novel bioluminescent bacterial biosensor for measurement of Ara-CTP and cytarabine potentiation by fludarabine in seven leukaemic cell lines.

Distribution of the branched chain aminotransferase proteins in the human brain and their role in glutamate regulation (2012)
Journal Article
Hull, J., Hindy, M. E., Kehoe, P. G., Chalmers, K., Love, S., & Conway, M. E. (2012). Distribution of the branched chain aminotransferase proteins in the human brain and their role in glutamate regulation. Journal of Neurochemistry, 123(6), 997-1009. https://doi.org/10.1111/jnc.12044

The branched chain aminotransferase enzymes (BCAT) serve as nitrogen donors for the production of 30% of de novo glutamate synthesis in rat brain. Despite the importance of this major metabolite and excitatory neurotransmitter, the distribution of BC... Read More about Distribution of the branched chain aminotransferase proteins in the human brain and their role in glutamate regulation.

Differential redox potential between the human cytosolic and mitochondrial branched-chain aminotransferase (2012)
Journal Article
Coles, S. J., Hancock, J. T., & Conway, M. E. (2012). Differential redox potential between the human cytosolic and mitochondrial branched-chain aminotransferase. Acta Biochimica et Biophysica Sinica, 44(2), 172-176. https://doi.org/10.1093/abbs/gmr103

The human branched-chain aminotransferase (hBCAT) isoenzymes are CXXC motif redox sensitive homodimers central to glutamate metabolism in the central nervous system. These proteins respond differently to oxidation by H 2O 2, NO, and S-glutathionylati... Read More about Differential redox potential between the human cytosolic and mitochondrial branched-chain aminotransferase.

Aminotransferases (2011)
Book Chapter
Conway, M. E. (2011). Aminotransferases. In J. D'Mello (Ed.), Amino Acids in Human Nutrition and Health (24-41). CABI

The aminotransferases are PLP dependent proteins which catalyze the transfer of an amino group from the donor amino acid to α-ketoglutarate, forming glutamate and the respective keto acids. Several key aminotransferase proteins have been identified a... Read More about Aminotransferases.

S-Nitrosoglutathione inactivation of the mitochondrial and cytosolic BCAT proteins: S-nitrosation and S-thiolation (2009)
Journal Article
Coles, S. J., Easton, P., Sharrod, H., Hutson, S. M., Hancock, J. T., Patel, V., & Conway, M. E. (2009). S-Nitrosoglutathione inactivation of the mitochondrial and cytosolic BCAT proteins: S-nitrosation and S-thiolation. Biochemistry, 48(3), 645-656. https://doi.org/10.1021/bi801805h

Specific proteins with reactive thiol(ate) groups are susceptible to nitric oxide (NO) modification, which can result in S-nitrosation, S-thiolation, or disulfide bond formation. In the present study the effect of NO modification on the functionality... Read More about S-Nitrosoglutathione inactivation of the mitochondrial and cytosolic BCAT proteins: S-nitrosation and S-thiolation.

S-nitrosoglutathione inactivation of the mitochondrial and cytosolic BCAT proteins: S-nitrosation and s-thiolation (2009)
Journal Article
Coles, S. J., Easton, P., Sharrod, H., Hutson, S. M., Hancock, J. T., Patel, V. B., & Conway, M. E. (2009). S-nitrosoglutathione inactivation of the mitochondrial and cytosolic BCAT proteins: S-nitrosation and s-thiolation. Biochemistry, 48(3), 645-656. https://doi.org/10.1021/bi801805h

Specific proteins with reactive thiol(ate) groups are susceptible to nitric oxide (NO) modification, which can result in S-nitrosation, S-thiolation, or disulfide bond formation. In the present study the effect of NO modification on the functionality... Read More about S-nitrosoglutathione inactivation of the mitochondrial and cytosolic BCAT proteins: S-nitrosation and s-thiolation.

Redox regulation and trapping sulfenic acid in the peroxide-sensitive human mitochondrial branched chain aminotransferase (2009)
Book Chapter
Hutson, S. M., Poole, L. B., Coles, S., & Conway, M. E. (2009). Redox regulation and trapping sulfenic acid in the peroxide-sensitive human mitochondrial branched chain aminotransferase. In J. T. Hancock (Ed.), Redox-Mediated Signal Transduction (135-148). Humana Press (Springer Imprint). https://doi.org/10.1007/978-1-59745-129-1_10

The human branched chain aminotransferase enzymes are key regulators of glutamate metabolism in the brain and are among a growing number of redox-sensitive proteins. Studies that use thiol-specific reagents and electrospray ionization mass spectromet... Read More about Redox regulation and trapping sulfenic acid in the peroxide-sensitive human mitochondrial branched chain aminotransferase.

Redox regulation and trapping sulphenic acid in the peroxide sensitive human mitochondrial branched chain aminotransferase (2008)
Journal Article
Coles, S., Hutson, S. M., Poole, L. B., & Conway, M. E. (2008). Redox regulation and trapping sulphenic acid in the peroxide sensitive human mitochondrial branched chain aminotransferase. Methods in Molecular Biology, 476, 139-152. https://doi.org/10.1007/978-1-59745-129-1_10

The human branched chain aminotransferase enzymes are key regulators of glutamate metabolism in the brain and are among a growing number of redox-sensitive proteins. Studies that use thiol-specific reagents and electrospray ionization mass spectromet... Read More about Redox regulation and trapping sulphenic acid in the peroxide sensitive human mitochondrial branched chain aminotransferase.

Regulatory control of human cytosolic branched-chain aminotransferase by oxidation and S-glutathionylation and its interactions with redox sensitive neuronal proteins (2008)
Journal Article
Conway, M. E., Coles, S. J., Islam, M. M., & Hutson, S. M. (2008). Regulatory control of human cytosolic branched-chain aminotransferase by oxidation and S-glutathionylation and its interactions with redox sensitive neuronal proteins. Biochemistry, 47(19), 5465-5479. https://doi.org/10.1021/bi800303h

Redox regulation of proteins through oxidation and S-thiolation are important regulatory processes, acting in both a protective and adaptive role in the cell. In the current study, we investigated the sensitivity of the neuronal human cytosolic branc... Read More about Regulatory control of human cytosolic branched-chain aminotransferase by oxidation and S-glutathionylation and its interactions with redox sensitive neuronal proteins.

A novel branched-chain amino acid metabolon: Protein-protein interactions in a supramolecular complex (2007)
Journal Article
Islam, M. M., Wallin, R., Wynn, R. M., Conway, M., Fujii, H., Mobley, J. A., …Hutson, S. M. (2007). A novel branched-chain amino acid metabolon: Protein-protein interactions in a supramolecular complex. Journal of Biological Chemistry, 282(16), 11893-11903. https://doi.org/10.1074/jbc.M700198200

The catabolic pathways of branched-chain amino acids have two common steps. The first step is deamination catalyzed by the vitamin B6-dependent branched-chain aminotransferase isozymes (BCATs) to produce branched-chain α-keto acids (BCKAs). The secon... Read More about A novel branched-chain amino acid metabolon: Protein-protein interactions in a supramolecular complex.

Human mitochondrial branched chain aminotransferase isozyme: Structural role of the CXXC center in catalysis (2006)
Journal Article
Conway, M., Islam, M. M., Yennawar, N. H., Islam, M. M., Conway, M. E., Wallin, R., & Hutson, S. M. (2006). Human mitochondrial branched chain aminotransferase isozyme: Structural role of the CXXC center in catalysis. Journal of Biological Chemistry, 281(51), 39660-39671. https://doi.org/10.1074/jbc.M607552200

Mammalian branched chain aminotransferases (BCATs) have a unique CXXC center. Kinetic and structural studies of three CXXC center mutants (C315A, C318A, and C315A/C318A) of human mitochondrial (hBCATm) isozyme and the oxidized hBCATm enzyme (hBCATm-O... Read More about Human mitochondrial branched chain aminotransferase isozyme: Structural role of the CXXC center in catalysis.

Structural determinants for branched-chain aminotransferase isozyme-specific inhibition by the anticonvulsant drug gabapentin (2005)
Journal Article
Yennawar, N., Goto, M., Miyahara, I., Hirotsu, K., Conway, M., Islam, M. M., & Hutson, S. M. (2005). Structural determinants for branched-chain aminotransferase isozyme-specific inhibition by the anticonvulsant drug gabapentin. Journal of Biological Chemistry, 280(44), 37246-37256. https://doi.org/10.1074/jbc.M506486200

This study presents the first three-dimensional structures of human cytosolic branched-chain aminotransferase (hBCATc) isozyme complexed with the neuroactive drug gabapentin, the hBCATc Michaelis complex with the substrate analog, 4-methylvalerate, a... Read More about Structural determinants for branched-chain aminotransferase isozyme-specific inhibition by the anticonvulsant drug gabapentin.

Roles for cysteine residues in the regulatory CXXC motif of human mitochondrial branched chain aminotransferase enzyme (2004)
Journal Article
Conway, M. E., Poole, L. B., & Hutson, S. M. (2004). Roles for cysteine residues in the regulatory CXXC motif of human mitochondrial branched chain aminotransferase enzyme. Biochemistry, 43(23), 7356-7364. https://doi.org/10.1021/bi0498050

The redox-active dithiol/disulfide C315-Xaa-Xaa-C318 center has been implicated in the regulation of the human mitochondrial branched chain aminotransferase isozyme (hBCATm) [Conway, M. E., Yennawar, N., Wallin, R., Poole, L. B., and Hutson, S. M. (2... Read More about Roles for cysteine residues in the regulatory CXXC motif of human mitochondrial branched chain aminotransferase enzyme.

Human mitochondrial branched chain aminotransferase: Structural basis for substrate specificity and role of redox active cysteines (2003)
Journal Article
Yennawar, N., Conway, M. E., Wallin, R., Poole, L. B., & Hutson, S. M. (2003). Human mitochondrial branched chain aminotransferase: Structural basis for substrate specificity and role of redox active cysteines. BBA - Proteins and Proteomics, 1647(1-2), 61-65. https://doi.org/10.1016/S1570-9639%2803%2900051-7

Crystal structures of the fold type IV pyridoxal phosphate (PLP)-dependent human mitochondrial branched chain aminotransferase (hBCATm) reaction intermediates have provided a structural explanation for the kinetically determined substrate specificity... Read More about Human mitochondrial branched chain aminotransferase: Structural basis for substrate specificity and role of redox active cysteines.

Human mitochondrial and cytosolic branched-chain aminotransferases are cysteine S-conjugate β-lyases, but turnover leads to inactivation (2003)
Journal Article
Cooper, A. J. L., Bruschi, S. A., Conway, M., & Hutson, S. M. (2003). Human mitochondrial and cytosolic branched-chain aminotransferases are cysteine S-conjugate β-lyases, but turnover leads to inactivation. Biochemical Pharmacology, 65(2), 181-192. https://doi.org/10.1016/S0006-2952%2802%2901513-7

The mitochondrial and cytosolic branched-chain aminotransferases (BCATm and BCATc) are homodimers in the fold type IV class of pyridoxal 5′-phosphate-containing enzymes that also contains D-amino acid aminotransferase and 4-amino-4-deoxychorismate ly... Read More about Human mitochondrial and cytosolic branched-chain aminotransferases are cysteine S-conjugate β-lyases, but turnover leads to inactivation.