Tag Archives: mitochondria

Recommended Readings: Hugo Bellen, Ph.D., D.V.M.

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Friday Lecture Series

Mitochondria and Neurodegeneration

Hugo Bellen, Ph.D., D.V.M., investigator, Howard Hughes Medical Institute;

professor, departments of molecular and human

genetics and neuroscience, director, Program in Developmental Biology,

Baylor College of Medicine

March 30, 2012

3:45 p.m.-5:00 p.m. (Refreshments, 3:15 p.m., Abby Lounge)

Caspary Auditorium

 

Recommended Readings:

Bibliography

Han, S. M., H. Tsuda, Y. Yang, J. Vibbert, P. Cottee, S. -J Lee, J. Winek, C. Haueter, H. J. Bellen, and M. A. Miller. 2012. “Secreted VAPB/ALS8 Major Sperm Protein Domains Modulate Mitochondrial Localization and Morphology Via Growth Cone Guidance Receptors.” Developmental Cell 22 (2): 348-362

Pesah, Y., T. Pham, H. Burgess, B. Middlebrooks, P. Verstreken, Y. Zhou, M. Harding, H. Bellen, and G. Mardon. 2004. “Drosophila Parkin Mutants have Decreased Mass and Cell Size and Increased Sensitivity to Oxygen Radical Stress.” Development 131 (9): 2183-2194

Romero, E., G. -H Cha, P. Verstreken, C. V. Ly, R. E. Hughes, H. J. Bellen, and J. Botas. 2008. “Suppression of Neurodegeneration and Increased Neurotransmission Caused by Expanded Full-Length Huntingtin Accumulating in the Cytoplasm.” Neuron 57 (1): 27-40

Venken, K. J. T., Y. He, R. A. Hoskins, and H. J. Bellen. 2006. “P[Acman]: A BAC Transgenic Platform for Targeted Insertion of Large DNA Fragments in D. Melanogaster.” Science 314 (5806): 1747-1751

Verstreken, P., C. V. Ly, K. J. T. Venken, T. -W Koh, Y. Zhou, and H. J. Bellen. 2005. “Synaptic Mitochondria are Critical for Mobilization of Reserve Pool Vesicles at Drosophila Neuromuscular Junctions.” Neuron 47 (3): 365-378


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Neuroglobin: Protection Against Alzheimer’s?

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ScienceDaily (Aug. 2, 2010) — A team of scientists at the University of California, Davis and the University of Auckland has discovered that neuroglobin may protect against Alzheimer’s disease by preventing brain neurons from dying in response to natural stress.   Neuroglobin protects cells from stroke damage, amyloid toxicity and injury due to lack of oxygen. Neuroglobin occurs in various regions of the brain and at particularly high levels in neurons.  Recent studies have hinted that neuroglobin protects cells by maintaining the function of mitochondria and regulating the concentration of important chemicals in the cell. However, the exact mechanisms by which neuroglobin protects cells from dying a natural death has, until now, remained unclear.  Click here for more on the research that resulted in these insights.

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Recommended Readings: Jerry Chipuk Ph.D. Oct 5, 2009

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Monday Lecture Series

Mitochondrial Outer Membrane Permeabilization and Apoptosis are Regulated by Collaborative Interactions between the BCL-2 Family and Mitochondrial Physiology

Jerry Chipuk, Ph.D.

Postdoctoral Fellow, Deptartment of Immunology, St. Jude Children’s Research Hospital

Monday, October 5, 2009

4:00 p.m.-5:00 p.m.

(Refreshments, 3:45 p.m.-4:00 p.m.)

Second Floor, Welch Hall

Recommended Review Article:

Chipuk JE, Green DR.  2008.  How do BCL-2 proteins induce mitochondrial outer membrane permeabilization?  TRENDS IN CELL BIOLOGY 18(4): 157-164

Recommended Articles:

Aslan JE, Thomas G.  2009.  Death by Committee: Organellar Trafficking and Communication in Apoptosis.  TRAFFIC 10(10): 1390-1404

Chipuk JE, Green DR.  2009.  PUMA cooperates with direct activator proteins to promote mitochondrial outer membrane permeabilization and apoptosis.  CELL CYCLE 8(17): 2692-2696

Chipuk JE, Bouchier-Hayes L, Green DR.  2006.  Mitochondrial outer membrane permeabilization during apoptosis: the innocent bystander scenario.  CELL DEATH AND DIFFERENTIATION 13(8): 1396-1402

Chipuk JE, Green DR.  2006.   Dissecting p53-dependent apoptosis.  CELL DEATH AND DIFFERENTIATION 13(6): 994-1002

Chipuk JE, Bouchier-Hayes L, Kuwana T, et al.  2005. PUMA couples the nuclear and cytoplasmic proapoptotic function of p53 .  SCIENCE 309(5741): 1732-1735

Kuwana T, Bouchier-Hayes L, Chipuk JE, et al.  2005.  BH3 domains of BH3-only proteins differentially regulate bax-mediated mitochondrial membrane permeabilization both directly and indirectly.  MOLECULAR CELL 17 (4): 525-535

Chipuk JE, Kuwana T, Bouchier-Hayes L, et al.  2004.   Direct activation of Bax by p53 mediates mitochondrial membrane permeabilization and apoptosis.  SCIENCE 303(5660): 1010-1014

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