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Full-Text Articles in Physical Sciences and Mathematics
Mercury Metallation Of The Copper Protein Azurin And Structural Insight Into Possible Heavy Metal Reactivity., Anthony Zampino, Francesca Masters, Erika Bladholm, Matthew Panzner, Steven Berry, Thomas Leeper, Christopher Ziegler
Mercury Metallation Of The Copper Protein Azurin And Structural Insight Into Possible Heavy Metal Reactivity., Anthony Zampino, Francesca Masters, Erika Bladholm, Matthew Panzner, Steven Berry, Thomas Leeper, Christopher Ziegler
Thomas C Leeper
Mercury(II) metallation of Pseudomonas aeruginosa azurin has been characterized structurally and biochemically. The X-ray crystal structure at 1.5 Å of mercury(II) metallated azurin confirms the coordination of mercury at the copper binding active site and a second surface site. These findings are further validated by NMR, Matrix-assisted laser desorption/ionization spectrometry (MALDI), and UV–visible spectroscopic methods indicating copper displacement from the wild-type protein. Bioinformatic analysis has identified homologous human protein domains computationally, and compared them to the structure of azurin, providing a model for human mercury interactions. Study of the mercury–azurin adduct, in combination with other known examples of protein–heavy metal …
Mitoneet As A Novel Drug Target For Mitochondrial Dysfunction, Werner Geldenhuys, Thomas Leeper, Richard Carroll
Mitoneet As A Novel Drug Target For Mitochondrial Dysfunction, Werner Geldenhuys, Thomas Leeper, Richard Carroll
Thomas C Leeper
Mitochondrial dysfunction plays an important part in the pathology of several diseases, including Alzheimer's disease and Parkinson's disease. Targeting mitochondrial proteins shows promise in treating and attenuating the neurodegeneration seen in these diseases, especially considering their complex and pleiotropic origins. Recently, the mitochondrial protein mitoNEET [also referred to as CDGSH iron sulfur domain 1 (CISD1)] has emerged as the mitochondrial target of thiazolidinedione drugs such as the antidiabetic pioglitazone. In this review, we evaluate the current understanding regarding how mitoNEET regulates cellular bioenergetics as well as the structural requirements for drug compound association with mitoNEET. With a clear understanding of …
Structural Libraries Of Protein Models For Multiple Species To Understand Evolution Of The Renin-Angiotensin System, Jeremy Prokop, Victoria Petri, Mary Shimoyama, Ingrid Watanabe, Dulce Casarini, Thomas Peeper, Stephanie Bilinovich, Howard Jacob, Robson Santos, Almir Martins, Fabiano Araujo, Fernando Reis, Amy Milsted
Structural Libraries Of Protein Models For Multiple Species To Understand Evolution Of The Renin-Angiotensin System, Jeremy Prokop, Victoria Petri, Mary Shimoyama, Ingrid Watanabe, Dulce Casarini, Thomas Peeper, Stephanie Bilinovich, Howard Jacob, Robson Santos, Almir Martins, Fabiano Araujo, Fernando Reis, Amy Milsted
Thomas C Leeper
The details of protein pathways at a structural level provides a bridge between genetics/molecular biology and physiology. The renin-angiotensin system is involved in many physiological pathways with informative structural details in multiple components. Few studies have been performed assessing structural knowledge across the system. This assessment allows use of bioinformatics tools to fill in missing structural voids. In this paper we detail known structures of the renin-angiotensin system and use computational approaches to estimate and model components that do not have their protein structures defined. With the subsequent large library of protein structures, we then created a species specific protein …