Dr. Hani Atamna
Associate ProfessorThe Commonwealth Medical College, USA
Highest Degree
Ph.D. in Biochemistry from The Hebrew University of Jerusalem, Israel
Share this Profile
The Commonwealth Medical College, USA
Biography
Dr. Hani Atamna holds a position of Associate Professor of Neuroscience and Biochemistry at The Commonwealth Medical College, USA. He has completed his Ph.D. in Biochemistry from The Hebrew University of Jerusalem, Israel. His main area of interest focuses on Pharmacology and Toxicology, Biomedical Sciences, and Molecular Sciences. His area of expertise includes Alzheimer, Neurodegenration, Aging, Redox Metabolism, Mitochondria mtDNA, Iron, heme, Free radicals/Antioxidants, Amyloid beta, Energy Metabolism, Homeostasis, and Regulation, Intermediary Metabolism, Molecular Toxicology, and Neuroscience. He held a principal investigator position at Childrens Hospital and Research Center (Oakland, CA). He is engaged in advanced research on the Neurobiochemistry and Physiology at the Molecular and Translational levels. He is member of International Bioiron Society (IBIS), International Society for Free Radical Research (SFRRI). He also delivered number of invited lectures at different institutes. He is author and co-author of 43 journal papers. He is also serving as reviewer for many journals.
Area of Interest:
Pharmacology and Toxicology
100%
Alzheimer
62%
Free Radicals
90%
Metabolism
75%
Neurodegeneration
55%
Research Publications in Numbers
Books
0
0
Chapters
0
0
Articles
38
38
Abstracts
0
0
Selected Publications
- Dhahbi, J.M., S.R. Spindler, H. Atamna, A. Yamakawa, D. Boffelli, P. Mote and D.I.K. Martin, 2013. Deep sequencing identifies circulating mouse miRNAs that are functionally implicated in manifestations of aging and responsive to calorie restriction. Aging, 5: 130-141.
PubMed | Direct Link | - Dhahbi, J.M., R.S. Spindler, H. Atamna, A. Yamakawa, D. Boffelli, P. Mote and I.K.D. Martin, 2013. 5' tRNA halves are present as abundant complexes in serum, concentrated in blood cells, and modulated by aging and calorie restriction. BMC Genomics, (In Press). 10.1186/1471-2164-14-298.
CrossRef | PubMed | Direct Link | - Dhahbi, J.M., H. Atamna, D. Boffelli, D.I. Martin and S.R. Spindler, 2012. mRNA-Seq reveals complex patterns of gene regulation and expression in the mouse skeletal muscle transcriptome associated with calorie restriction. Physiol. Genomics, 44: 331-344.
CrossRef | PubMed | Direct Link | - Atamna, H., J. Mackey and J.M. Dhahbi, 2012. Mitochondrial pharmacology: Electron Transport Chain Bypass as Strategies to treat mitochondrial dysfunction. Biofactors, 38: 158-166.
CrossRef | PubMed | Direct Link | - Kumar, R., H. Atamna, M.N. Zakharov, S. Bhasin, S.H. Khan and R. Jasuja, 2011. Role of the androgen receptor CAG repeat polymorphism in prostate cancer, and spinal and bulbar muscular atrophy. Life Sci., 88: 565-571.
CrossRef | PubMed | Direct Link | - Kumar, R. and H. Atamna, 2011. Therapeutic approaches to Delay the Onset of Alzheimer's disease. J. Aging. Res., 10.4061/2011/820903.
CrossRef | PubMed | Direct Link | - Dhahbi, J.M., H. Atamna, D. Boffelli, W. Magis, S.R. Spindler and D.I.K. Martin, 2011. Deep sequencing reveals novel micrornas and regulation of microRNA expression during cell senescence. PLoS One, 10.1371/journal.pone.0020509.
CrossRef | Direct Link | - Atamna, H. and A. Gharib, 2011. Methylene Blue Induces Mitochondrial Complex IV and Improves the Cognitive Function and Grip Strength in Old Mice. In: Neurodegeneration: Theory, Disorders and Treatments, McNeill, A.S. (Ed.). Nova Publishers, New York, USA., pp: 63-86.
- Atamna, H. and R. Kumar, 2010. Protective role of methylene blue in Alzheimer's disease via mitochondria and cytochrome c oxidase. J. Alzheimer's Dis., 20: S439-S452.
CrossRef | PubMed | Direct Link | - Atamna, H., 2009. Amino acids variations in amyloid-β peptides, mitochondrial dysfunction, and new therapies for alzheimer's disease. J. Bioenerg. Biomemb., 41: 457-464.
CrossRef | PubMed | Direct Link | - Atamna, H. and W.H. Frey 2nd and N. Ko, 2009. Human and rodent amyloid-β peptides differentially bind heme: Relevance to the human susceptibility to Alzheimer's disease. Arch. Biochem. Biophys., 487: 59-65.
CrossRef | PubMed | Direct Link | - Lloret, A., M.C. Badia, N.J. Mora, A. Ortega and F.V. Pallardo et al., 2008. Gender and age-dependent differences in the mitochondrial apoptogenic pathway in Alzheimer's disease. Free Radic Biol. Med., 44: 2019-2025.
CrossRef | PubMed | Direct Link | - Atamna, H., A. Nguyen, C. Schultz, K. Boyle, J. Newberry, H. Kato and B.N. Ames, 2008. Methylene blue delays cellular senescence and enhances key mitochondrial biochemical pathways. Faseb. J., 22: 703-712.
CrossRef | PubMed | Direct Link | - Voloboueva, L.A., D.W. Killilea, H. Atamna and B.N. Ames, 2007. N-tert-butyl hydroxylamine, a mitochondrial antioxidant, protects human retinal pigment epithelial cells from iron overload: Relevance to macular degeneration. Faseb. J., 21: 4077-4086.
CrossRef | PubMed | Direct Link | - Atamna, H., J. Newberry, R. Erlitzki, C.S. Schultz and B.N. Ames, 2007. Biotin deficiency inhibits heme synthesis and impairs mitochondria in human lung fibroblasts. J. Nutr., 137: 25-30.
PubMed | Direct Link | - Atamna, H. and W.H. Frey II, 2007. Mechanisms of mitochondrial dysfunction and energy deficiency in Alzheimer's disease. Mitochondrion, 7: 297-310.
CrossRef | PubMed | Direct Link | - Atamna, H., 2006. Heme binding to amyloid-β peptide: Mechanistic role in Alzheimer's disease. J. Alzheimer's Dis., 10: 255-266.
PubMed | Direct Link | - Atamna, H. and K. Boyle, 2006. Amyloid-β peptide binds with heme to form a peroxidase: Relationship to the cytopathologies of Alzheimer's disease. Proc. Natl. Acad. Sci. USA., 103: 3381-3386.
CrossRef | PubMed | Direct Link | - Ames, B.N., H. Atamna and D.W. Killilea, 2005. Mineral and vitamin deficiencies can accelerate the mitochondrial decay of aging. Mol. Aspects Med., 26: 363-378.
CrossRef | PubMed | Direct Link | - Killilea, D.W., S.L. Wong, H.S. Cahaya, H. Atamna and B.N. Ames, 2004. Iron accumulation during cellular senescence. Ann. N. Y. Acad. Sci., 1019: 365-367.
CrossRef | PubMed | Direct Link | - Atamna, H., 2004. Heme, iron and the mitochondrial decay of ageing. Ageing Res. Rev., 3: 303-318.
CrossRef | PubMed | Direct Link | - Atamna, H. and W.H. Frey II, 2004. A role for heme in Alzheimer's disease: Heme binds amyloid β and has altered metabolism. Proc. Natl. Acad. Sci. USA., 101: 11153-11158.
CrossRef | PubMed | Direct Link | - Killilea, D.W., H. Atamna, C. Liao and B.N. Ames, 2003. Iron accumulation during cellular senescence in human fibroblasts in vitro. Antioxidant Redox Signaling, 5: 507-516.
CrossRef | PubMed | Direct Link | - Ames, B.N., J. Liu, H. Atamna and T. Hagen, 2003. Delaying the mitochondrial decay of aging in the brain. Clin. Neurosci. Res., 2: 331-338.
CrossRef | Direct Link | - Liu, J., H. Atamna, H. Kuratsune and B.N. Ames, 2002. Delaying brain mitochondrial decay and aging with mitochondrial antioxidants and metabolites. Ann. New York Acad. Sci., 959: 133-166.
CrossRef | PubMed | Direct Link | - Atamna, H., P.B. Walter and B.N. Ames, 2002. The role of heme and iron-sulfur clusters in mitochondrial biogenesis, maintenance, and decay with age. Arch. Biochem. Biophys, 397: 345-353.
CrossRef | PubMed | Direct Link | - Atamna, H., D.W. Killilea, A.N. Killilea and B.N. Ames, 2002. Heme deficiency may be a factor in the mitochondrial and neuronal decay of aging. Proc. Natl. Acad. Sci. USA., 99: 14807-14812.
CrossRef | Direct Link | - Atamna, H., J. Liu and B.N. Ames, 2001. Heme deficiency selectively interrupts assembly of mitochondrial complex IV in human fibroblasts: Relevance to aging. J. Biol. Chem., 276: 48410-48416.
CrossRef | PubMed | Direct Link | - Atamna, H., C. Robinson, R. Ingersoll, H. Elliott and B.N. Ames, 2001. N-t-Butyl hydroxylamine is an antioxidant that reverses age-related changes in mitochondria In vivo and in vitro. Faseb. J., 15: 2196-2204.
CrossRef | PubMed | Direct Link | - Atamna, H., I. Cheung and B.N. Ames, 2000. A method for detecting abasic sites in living cells: Age-dependent changes in base excision repair. Proc. Natl. Acad. Sci. USA., 97: 686-691.
CrossRef | PubMed | Direct Link | - Atamna, H., A. Paler-Martı́nez and B.N. Ames, 2000. N-t-butyl hydroxylamine, a hydrolysis product of α-phenyl-N-t-butyl nitrone, is more potent in delaying senescence in human lung fibroblasts. J. Biol. Chem., 275: 6741-6748.
CrossRef | PubMed | Direct Link | - Atamna, H. and H. Ginsburg, 1997. The malaria parasite supplies glutathione to its host cell-invasion to glutathione transport and metabolism in human erythrocytes infected with Plasmodium falciparum. Eur. J. Biochem., 250: 670-679.
- Ginsburg, H., H. Atamna, G. Shalmiev, J. Kanaani and M. Krugliak, 1996. Resistance of glucose-6-phosphate dehydrogenase deficiency to malaria: Effects of fava bean hydroxypyrimidine glucosides on Plasmodium falciparum growth in culture and on the phagocytosis of infected cells. Parasitology, 113: 7-18.
CrossRef | PubMed | Direct Link | - Atamna, H., M. Krugliak, G. Shalmiev, E. Deharo, G. Pescarmona and H. Ginsburg, 1996. Mode of antimalarial effect of methylene blue and some of its analogues on Plasmodium falciparum in culture and their inhibition of P. vinckei petteri and P. yoelii nigeriensis in vivo. Biochem. Pharmacol., 51: 693-700.
CrossRef | PubMed | Direct Link | - Atamna, H. and H. Ginsburg, 1995. Heme degradation in the presence of glutathione: A proposed mechanism to account for the high levels of non-heme iron found in the membranes of hemoglobinopathic red blood cells. J. Biol. Chem., 270: 24876-24883.
CrossRef | PubMed | Direct Link | - Ginsburg, H. and H. Atamna, 1994. The redox status of malaria-infected erythrocytes: An overview with an emphasis on unresolved problems. Parasite, 1: 5-13.
PubMed | - Atamna, H., G. Pascarmona and H. Ginsburg, 1994. Hexose-monophosphate shunt activity in intact Plasmodium falciparum-infected erythrocytes and in free parasites. Mol. Biochem. Parasitol., 67: 79-89.
CrossRef | PubMed | Direct Link | - Atamna, H. and H. Ginsburg, 1993. Origin of reactive oxygen species in erythrocytes infected with Plasmodium falciparum. Mol. Biochem. Parasitol., 61: 231-241.
PubMed |