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Medical Microbiology

Department of Biochemistry and Molecular Biology Faculty Papers

Department of Biochemistry and Molecular Biology

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Full-Text Articles in Medicine and Health Sciences

Deacetylation Of Hsd17b10 By Sirt3 Regulates Cell Growth And Cell Resistance Under Oxidative And Starvation Stresses., Lu Liu, Shuaiyi Chen, Miao Yu, Chenxu Ge, Mengmeng Ren, Boya Liu, Xin Yang, Thomas W Christian, Ya-Ming Hou, Junhua Zou, Wei-Guo Zhu, Jianyuan Luo Jul 2020

Deacetylation Of Hsd17b10 By Sirt3 Regulates Cell Growth And Cell Resistance Under Oxidative And Starvation Stresses., Lu Liu, Shuaiyi Chen, Miao Yu, Chenxu Ge, Mengmeng Ren, Boya Liu, Xin Yang, Thomas W Christian, Ya-Ming Hou, Junhua Zou, Wei-Guo Zhu, Jianyuan Luo

Department of Biochemistry and Molecular Biology Faculty Papers

17-beta-hydroxysteroid dehydrogenase 10 (HSD17B10) plays an important role in mitochondrial fatty acid metabolism and is also involved in mitochondrial tRNA maturation. HSD17B10 missense mutations cause HSD10 mitochondrial disease (HSD10MD). HSD17B10 with mutations identified from cases of HSD10MD show loss of function in dehydrogenase activity and mitochondrial tRNA maturation, resulting in mitochondrial dysfunction. It has also been implicated to play roles in the development of Alzheimer disease (AD) and tumorigenesis. Here, we found that HSD17B10 is a new substrate of NAD-dependent deacetylase Sirtuin 3 (SIRT3). HSD17B10 is acetylated at lysine residues K79, K99 and K105 by the acetyltransferase CBP, and the …


Neutralization Of Botulinum Neurotoxin By A Human Monoclonal Antibody Specific For The Catalytic Light Chain., Sharad P Adekar, Tsuyoshi Takahashi, R Mark Jones, Fetweh H Al-Saleem, Denise M Ancharski, Michael J Root, B P Kapadnis, Lance L Simpson, Scott K Dessain Aug 2008

Neutralization Of Botulinum Neurotoxin By A Human Monoclonal Antibody Specific For The Catalytic Light Chain., Sharad P Adekar, Tsuyoshi Takahashi, R Mark Jones, Fetweh H Al-Saleem, Denise M Ancharski, Michael J Root, B P Kapadnis, Lance L Simpson, Scott K Dessain

Department of Biochemistry and Molecular Biology Faculty Papers

BACKGROUND: Botulinum neurotoxins (BoNT) are a family of category A select bioterror agents and the most potent biological toxins known. Cloned antibody therapeutics hold considerable promise as BoNT therapeutics, but the therapeutic utility of antibodies that bind the BoNT light chain domain (LC), a metalloprotease that functions in the cytosol of cholinergic neurons, has not been thoroughly explored.

METHODS AND FINDINGS: We used an optimized hybridoma method to clone a fully human antibody specific for the LC of serotype A BoNT (BoNT/A). The 4LCA antibody demonstrated potent in vivo neutralization when administered alone and collaborated with an antibody specific for …