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Full-Text Articles in Biochemistry
The Optimization Of Mitoneet Synthesis, Purification And Mutation Stability In The [2fe-2s] Cluster, Alexandria Defabio
The Optimization Of Mitoneet Synthesis, Purification And Mutation Stability In The [2fe-2s] Cluster, Alexandria Defabio
Williams Honors College, Honors Research Projects
MitoNEET, a mitochondrial membrane protein with an unsymmetrical Fe-S cluster coordination, was compared to similar proteins within the Rieske and Ferredoxin families. Point mutations were introduced via site-directed mutagenesis to induce stability, greater retention of the cluster, and to uncover structural limitations of the protein. Mutations were made within the cluster coordination and within the hydrophobic core of the protein. Some of the cluster mutations displayed a natural affinity for nickel during immobilized metal-ion affinity chromatography. It is possible that these mutations aid in the formation of a chelate when exposed to nickel. Spectroscopic monitoring of changes in cluster stability …
Identification Of Disufide Bond Formation Between Mitoneet And Glutamate Dehydrogenase 1, Morgan E. Roberts, Jacquelyn P. Crail, Megan M. Laffoon, William G. Fernandez, Michael A. Menze, Mary E. Konkle
Identification Of Disufide Bond Formation Between Mitoneet And Glutamate Dehydrogenase 1, Morgan E. Roberts, Jacquelyn P. Crail, Megan M. Laffoon, William G. Fernandez, Michael A. Menze, Mary E. Konkle
Michael Menze
MitoNEET is a protein that was identified as a drug target for diabetes, but its cellular function as well as its role in diabetes remains elusive. Protein pull-down experiments identified glutamate dehydrogenase 1 (GDH1) as a potential binding partner. GDH1 is a key metabolic enzyme with emerging roles in insulin regulation. MitoNEET forms a covalent complex with GDH1 through disulfide bond formation and acts as an activator. Proteomic analysis identified the specific cysteine residues that participate in the disulfide bond. This is the first report that effectively links mitoNEET to activation of the insulin regulator GDH1.
Identification Of Disufide Bond Formation Between Mitoneet And Glutamate Dehydrogenase 1, Morgan E. Roberts, Jacquelyn P. Crail, Megan M. Laffoon, William G. Fernandez, Michael A. Menze, Mary E. Konkle
Identification Of Disufide Bond Formation Between Mitoneet And Glutamate Dehydrogenase 1, Morgan E. Roberts, Jacquelyn P. Crail, Megan M. Laffoon, William G. Fernandez, Michael A. Menze, Mary E. Konkle
Faculty Research & Creative Activity
MitoNEET is a protein that was identified as a drug target for diabetes, but its cellular function as well as its role in diabetes remains elusive. Protein pull-down experiments identified glutamate dehydrogenase 1 (GDH1) as a potential binding partner. GDH1 is a key metabolic enzyme with emerging roles in insulin regulation. MitoNEET forms a covalent complex with GDH1 through disulfide bond formation and acts as an activator. Proteomic analysis identified the specific cysteine residues that participate in the disulfide bond. This is the first report that effectively links mitoNEET to activation of the insulin regulator GDH1.
Identification Of Disulfide Bond Formation Between Mitoneet And Glutamate Dehydrogenase 1, Morgan E. Roberts, Jacquelyn P. Crail, Megan M. Laffoon, William G. Fernandez, Michael A. Menze, Mary E. Konkle
Identification Of Disulfide Bond Formation Between Mitoneet And Glutamate Dehydrogenase 1, Morgan E. Roberts, Jacquelyn P. Crail, Megan M. Laffoon, William G. Fernandez, Michael A. Menze, Mary E. Konkle
Faculty Research & Creative Activity
MitoNEET is a protein that was identified as a drug target for diabetes, but its cellular function as well as its role in diabetes remains elusive. Protein pull-down experiments identified glutamate dehydrogenase 1 (GDH1) as a potential binding partner. GDH1 is a key metabolic enzyme with emerging roles in insulin regulation. MitoNEET forms a covalent complex with GDH1 through disulfide bond formation and acts as an activator. Proteomic analysis identified the specific cysteine residues that participate in the disulfide bond. This is the first report that effectively links mitoNEET to activation of the insulin regulator GDH1.
Identification Of Disufide Bond Formation Between Mitoneet And Glutamate Dehydrogenase 1., Morgan Roberts, Jacquelyn Crail, Megan Laffoon, William Fernandez, Michael Menze, Mary Konkle
Identification Of Disufide Bond Formation Between Mitoneet And Glutamate Dehydrogenase 1., Morgan Roberts, Jacquelyn Crail, Megan Laffoon, William Fernandez, Michael Menze, Mary Konkle
Faculty Scholarship
MitoNEET is a protein that was identified as a drug target for diabetes, but its cellular function as well as its role in diabetes remains elusive. Protein pull-down experiments identified glutamate dehydrogenase 1 (GDH1) as a potential binding partner. GDH1 is a key metabolic enzyme with emerging roles in insulin regulation. MitoNEET forms a covalent complex with GDH1 through disulfide bond formation and acts as an activator. Proteomic analysis identified the specific cysteine residues that participate in the disulfide bond. This is the first report that effectively links mitoNEET to activation of the insulin regulator GDH1.