Copper-Dependent Inhibition of Human Cytochrome c Oxidase by a Dimeric Conformer of Amyloid-β1-42

PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT

Lowry, O. H., Rosebrough, N., Farr, A. L., & Randall, R. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52451-6 · Cited by 315,771 · see citing works

A simplification of the protein assay method of Lowry et al. which is more generally applicable

Peterson, G. L. (1977) · Analytical Biochemistry · doi:10.1016/0003-2697(77)90043-4 · Cited by 8,531 · see citing works

Alzheimer's disease: the amyloid cascade hypothesis

Hardy, J. A., & Higgins, G. A. (1992) · Science · doi:10.1126/science.1566067 · Cited by 7,484 · see citing works

Alzheimer's Disease: Genes, Proteins, and Therapy

Selkoe, D. J. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.741 · Cited by 6,063 · see citing works

Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo

Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291 · see citing works

Correlative Memory Deficits, Aβ Elevation, and Amyloid Plaques in Transgenic Mice

Hsiao, K., Chapman, P., Nilsen, S., Eckman, C., Harigaya, Y., Younkin, S., Yang, F., & Cole, G. (1996) · Science · doi:10.1126/science.274.5284.99 · Cited by 4,210 · see citing works

Copper, iron and zinc in Alzheimer's disease senile plaques

Lovell, M. A., Robertson, J. D., Teesdale, W. J., Campbell, J. L., & Markesbery, W. R. (1998) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(98)00092-6 · Cited by 2,120 · see citing works

Mutation of the β-amyloid precursor protein in familial Alzheimer's disease increases β-protein production

Citron, M., Oltersdorf, T., Haass, C., McConlogue, L., Hung, A. Y., Seubert, P., Vigo-Pelfrey, C., Lieberburg, I., & Selkoe, D. J. (1992) · Nature · doi:10.1038/360672a0 · Cited by 1,757 · see citing works

Oligomeric and fibrillar species of amyloid-β peptides differentially affect neuronal viability

Dahlgren, K. N., Manelli, A. M., Stine, W. B., Baker, L. K., Krafft, G. A., & LaDu, M. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201750200 · Cited by 1,452 · see citing works

Mitochondrial abnormalities in Alzheimer's disease

Hirai, K., Aliev, G., Nunomura, A., Fujioka, H., Russell, R. L., Atwood, C. S., Johnson, A. B., Kress, Y., Vinters, H. V., Tabaton, M., et al. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-09-03017.2001 · Cited by 1,367 · see citing works

ABAD Directly Links Aß to Mitochondrial Toxicity in Alzheimer's Disease

Lustbader, J. W., Cirilli, M., Lin, C., Xu, H. W., Takuma, K., Wang, N., Caspersen, C., Chen, X., Pollak, S., Chaney, M., et al. (2004) · Science · doi:10.1126/science.1091230 · Cited by 1,303 · see citing works

Amyloid β-protein (Aβ) assembly: Aβ40 and Aβ42 oligomerize through distinct pathways

Bitan, G., Kirkitadze, M. D., Lomakin, A., Vollers, S. S., Benedek, G. B., & Teplow, D. B. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.222681699 · Cited by 1,280 · see citing works

Correlation Between Elevated Levels of Amyloid β-Peptide in the Brain and Cognitive Decline

Näslund, J. (2000) · JAMA · doi:10.1001/jama.283.12.1571 · Cited by 1,268 · see citing works

Dramatic Aggregation of Alzheimer Aβ by Cu(II) Is Induced by Conditions Representing Physiological Acidosis

Atwood, C. S., Moir, R. D., Huang, X., Scarpa, R. C., Bacarra, N. M. E., Romano, D. M., Hartshorn, M. A., Tanzi, R. E., & Bush, A. I. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.21.12817 · Cited by 1,009 · see citing works

Protofibrillar Intermediates of Amyloid β-Protein Induce Acute Electrophysiological Changes and Progressive Neurotoxicity in Cortical Neurons

Hartley, D. M., Walsh, D. M., Ye, C., Diehl, T. S., Vasquez, S., Vassilev, P., Teplow, D. B., & Selkoe, D. J. (1999) · Journal of Neuroscience · doi:10.1523/jneurosci.19-20-08876.1999 · Cited by 965 · see citing works

Immunization reverses memory deficits without reducing brain Aβ burden in Alzheimer's disease model

Dodart, J.-C., Bales, K. R., Gannon, K. S., Greene, S. J., DeMattos, R. B., Mathis, C., DeLong, C. A., Wu, S., Wu, X., Holtzman, D. M., et al. (2002) · Nature Neuroscience · doi:10.1038/nn842 · Cited by 858 · see citing works

Cu(II) Potentiation of Alzheimer Aβ Neurotoxicity

Huang, X., Cuajungco, M. P., Atwood, C. S., Hartshorn, M. A., Tyndall, J. D. A., Hanson, G. R., Stokes, K. C., Leopold, M., Multhaup, G., Goldstein, L. E., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.52.37111 · Cited by 762 · see citing works

[42]Assessment of mitochondrial oxidative phosphorylation in patient muscle biopsies, lymphoblasts, and transmitochondrial cell lines

Trounce, I. A., Kim, Y. L., Jun, A. S., & Wallace, D. C. (1996) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(96)64044-0 · Cited by 749 · see citing works

Alzheimer's Disease Amyloid-β Binds Copper and Zinc to Generate an Allosterically Ordered Membrane-penetrating Structure Containing Superoxide Dismutase-like Subunits

Curtain, C. C., Ali, F. E. A., Volitakis, I., Cherny, R. A., Norton, R. S., Beyreuther, K. T., Barrow, C. J., Masters, C. L., Bush, A. I., & Barnham, K. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100175200 · Cited by 653 · see citing works

Chemistry for the analysis of protein–protein interactions: Rapid and efficient cross-linking triggered by long wavelength light

Fancy, D. A., & Kodadek, T. J. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.11.6020 · Cited by 585 · see citing works

Mitochondrial targeting and a novel transmembrane arrest of Alzheimer's amyloid precursor protein impairs mitochondrial function in neuronal cells

Anandatheerthavarada, H. K., Biswas, G., Robin, M.-A., & Avadhani, N. G. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200207030 · Cited by 571 · see citing works

Positron emission tomography in Alzheimer's disease

Duara, R., Grady, C., Haxby, J. V., Sundaram, M., Cutler, N. R., Heston, L. L., Moore, A., Schlageter, N. L., Larson, S., & Рапопорт, С. И. (1986) · Neurology · doi:10.1212/wnl.36.7.879 · Cited by 568 · see citing works

Soluble oligomers of β amyloid (1-42) inhibit long-term potentiation but not long-term depression in rat dentate gyrus

Wang, H.-W., Pasternak, J. F., Kuo, H., Ristic, H., Lambert, M. P., Chromy, B., Viola, K. L., Klein, W. L., Stine, W. B., Krafft, G. A., et al. (2002) · Brain Research · doi:10.1016/s0006-8993(01)03058-x · Cited by 527 · see citing works

β‐Amyloid inhibits integrated mitochondrial respiration and key enzyme activities

Casley, C. S., Canevari, L., Land, J. M., Clark, J. B., & Sharpe, M. A. (2001) · Journal of Neurochemistry · doi:10.1046/j.0022-3042.2001.00681.x · Cited by 485 · see citing works

Analysis of Heterogeneous βA4 Peptides in Human Cerebrospinal Fluid and Blood by a Newly Developed Sensitive Western Blot Assay

Ida, N., Hartmann, T., Pantel, J., Schrüder, J., Zerfaß, R., Fürstl, H., Sandbrink, R., Masters, C. L., & Beyreuther, K. T. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.37.22908 · Cited by 476 · see citing works

A selective defect of cytochrome c oxidase is present in brain of Alzheimer disease patients

Maurer, I. (2000) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00112-3 · Cited by 475 · see citing works

Amyloid β-Protein Oligomerization

Bitan, G., Lomakin, A., & Teplow, D. B. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102223200 · Cited by 387 · see citing works

Huntingtin aggregates may not predict neuronal death in Huntington's disease

Kuemmerle, S., Gutekunst, C., Klein, A., Li, X., Li, S.-H., Beal, M. F., Hersch, S. M., & Ferrante, R. J. (1999) · Annals of Neurology · doi:10.1002/1531-8249(199912)46:6 · Cited by 387 · see citing works

Copper Mediates Dityrosine Cross-Linking of Alzheimer's Amyloid-β

Atwood, C., Perry, G. L., Zeng, H., Kato, Y., Jones, W. D., Ling, K.-Q., Huang, X., Moir, R. D., Wang, D., Sayre, L. M., et al. (2003) · Biochemistry · doi:10.1021/bi0358824 · Cited by 371 · see citing works

Overexpression of Alzheimer's Disease Amyloid-β Opposes the Age-dependent Elevations of Brain Copper and Iron

Maynard, C. J., Cappai, R., Volitakis, I., Cherny, R. A., White, A. R., Beyreuther, K. T., Masters, C. L., Bush, A. I., & Li, Q. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204379200 · Cited by 352 · see citing works

Amyloid β-induced Changes in Nitric Oxide Production and Mitochondrial Activity Lead to Apoptosis

Keil, U., Bonert, A., Marques, C. A., Scherping, I., Weyermann, J., Strosznajder, J. B., Müller-Spahn, F., Haass, C., Czech, C., Pradier, L., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405600200 · Cited by 287 · see citing works

Elucidation of Primary Structure Elements Controlling Early Amyloid β-Protein Oligomerization

Bitan, G., Vollers, S. S., & Teplow, D. B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300825200 · Cited by 284 · see citing works

Aggregation-related toxicity of synthetic β-amyloid protein in hippocampal cultures

Pike, C. J., Walencewicz, A. J., Glabe, C. G., & Cotman, C. W. (1991) · European Journal of Pharmacology Molecular Pharmacology · doi:10.1016/0922-4106(91)90014-9 · Cited by 276 · see citing works

Neocortical Metabolic Abnormalities Precede Nonmemory Cognitive Defects in Early Alzheimer's-Type Dementia

Haxby, J. V., Grady, C. L., Duara, R., Schlageter, N. L., Berg, G., & Рапопорт, С. И. (1986) · Archives of Neurology · doi:10.1001/archneur.1986.00520090022010 · Cited by 270 · see citing works

Nicastrin, Presenilin, APH-1, and PEN-2 Form Active γ-Secretase Complexes in Mitochondria

Hansson, C. A., Frykman, S., Farmery, M. R., Tjernberg, L. O., Nilsberth, C., Pursglove, S. E., Ito, A., Winblad, B., Cowburn, R. F., Thyberg, J., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404500200 · Cited by 256 · see citing works

Increased Cerebral Glucose‐6‐Phosphate Dehydrogenase Activity in Alzheimer's Disease May Reflect Oxidative Stress

Martins, R. N., Harper, C. G., Stokes, G. B., & Masters, C. L. (1986) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1986.tb00615.x · Cited by 234 · see citing works

β-Amyloid Fragment 25–35 Causes Mitochondrial Dysfunction in Primary Cortical Neurons

Casley, C. S., Land, J. M., Sharpe, M. A., Clark, J. B., Duchen, M. R., & Canevari, L. (2002) · Neurobiology of Disease · doi:10.1006/nbdi.2002.0516 · Cited by 205 · see citing works

Neurotoxic Aβ peptides increase oxidative stress in vivo through NMDA‐receptor and nitric‐oxide‐synthase mechanisms, and inhibit complex IV activity and induce a mitochondrial permeability transition in vitro

Parks, J. K., Smith, T. S., Trimmer, P. A., Bennett, J. P., & Parker, W. D. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00112.x · Cited by 198 · see citing works

β‐Amyloid fragment 25–35 selectively decreases complex IV activity in isolated mitochondria

Canevari, L., Clark, J. B., & Bates, T. E. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01028-5 · Cited by 196 · see citing works

Mitochondrial enzyme-deficient hippocampal neurons and choroidal cells in AD

Cottrell, D. A., Blakely, E. L., Johnson, M. A., Ince, P. G., & Turnbull, D. M. (2001) · Neurology · doi:10.1212/wnl.57.2.260 · Cited by 163 · see citing works

β‐Amyloid protein oligomers induced by metal ions and acid pH are distinct from those generated by slow spontaneous ageing at neutral pH

Klug, G. M., Lošić, D., Supundi, Subasinghe, S., Aguilar, M., Martin, L. L., & Small, D. H. (2003) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03815.x · Cited by 107 · see citing works

The role of cytochrome c oxidase deficient hippocampal neurones in Alzheimer's disease

Cottrell, D., Borthwick, G., Johnson, M., Ince, P. G., & Turnbull, D. (2002) · Neuropathology and Applied Neurobiology · doi:10.1046/j.1365-2990.2002.00414.x · Cited by 91 · see citing works

In vitro peroxidase oxidation induces stable dimers of β-amyloid (1-42) through dityrosine bridge formation

Galeazzi, L., Ronchi, P., Franceschi, C., & Giunta, S. (1999) · Amyloid · doi:10.3109/13506129908993282 · Cited by 87 · see citing works

Improved recovery of highly enriched mitochondrial fractions from small brain tissue samples

Anderson, M. F., & Sims, N. R. (2000) · Brain Research Protocols · doi:10.1016/s1385-299x(99)00060-4 · Cited by 66 · see citing works

The iron(III)-adriamycin complex inhibits cytochrome c oxidase before its inactivation

Hasinoff, B. B., & Davey, J. P. (1988) · Biochemical Journal · doi:10.1042/bj2500827 · Cited by 32 · see citing works

Computer prediction of peptide maps: assignment of polypeptides to human and mouse mitochondrial DNA genes by analysis of two-dimensional-proteolytic digest gels.

Wallace, D. C., Yang, J. H., Ye, J. H., Lott, M. T., Oliver, N., & McCarthy, J. (1986) · PubMed · Cited by 31 · see citing works

Mitochondrial Dysfunction and Oxidative Stress in Neurodegenerative Diseases

Lin, M. T., & Beal, M. F. (2006) · Nature · doi:10.1038/nature05292 · Cited by 6,455 · see citing works

A Mitochondrial Paradigm of Metabolic and Degenerative Diseases, Aging, and Cancer: A Dawn for Evolutionary Medicine

Wallace, D. C. (2005) · Annual Review of Genetics · doi:10.1146/annurev.genet.39.110304.095751 · Cited by 3,185 · see citing works

Mitochondria are a direct site of Aβ accumulation in Alzheimer's disease neurons: implications for free radical generation and oxidative damage in disease progression

Manczak, M., Anekonda, T. S., Henson, E., Park, B. S., Quinn, J., & Reddy, P. H. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl066 · Cited by 1,104 · see citing works

Mitochondrial fragmentation in neurodegeneration.

Knott, A. B., Perkins, G., Schwarzenbacher, R., & Bossy-Wetzel, E. (2008) · Nature Reviews Neuroscience · doi:10.1038/nrn2417 · Cited by 1,002 · see citing works

Amyloid beta, mitochondrial dysfunction and synaptic damage: Implications for cognitive decline in aging and Alzheimer’s disease

Reddy, P. H., & Beal, M. F. (2008) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2007.12.002 · Cited by 975 · see citing works

Mitochondria take center stage in aging and neurodegeneration

Beal, M. F. (2005) · Annals of Neurology · doi:10.1002/ana.20624 · Cited by 957 · see citing works

Cyclophilin D deficiency attenuates mitochondrial and neuronal perturbation and ameliorates learning and memory in Alzheimer's disease

Du, H., Guo, L., Fang, F., Chen, D., Sosunov, A. A., McKhann, G. M., Yan, Y., Wang, C., Zhang, H., Molkentin, J. D., et al. (2008) · Nature Medicine · doi:10.1038/nm.1868 · Cited by 935 · see citing works

Mitochondria and Mitochondrial Cascades in Alzheimer’s disease

Swerdlow, R. H. (2018) · Journal of Alzheimer’s Disease · doi:10.3233/jad-170585 · Cited by 850 · see citing works

Accumulation of amyloid precursor protein in the mitochondrial import channels of human Alzheimer's disease brain is associated with mitochondrial dysfunction

Devi, L., Prabhu, B. M., Galati, D. F., Avadhani, N. G., & Anandatheerthavarada, H. K. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.1469-06.2006 · Cited by 792 · see citing works

The Alzheimer’s disease mitochondrial cascade hypothesis: progress and perspectives

Swerdlow, R. H., Burns, J. M., & Khan, S. M. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.09.010 · Cited by 786 · see citing works

The amyloid β-peptide is imported into mitochondria via the TOM import machinery and localized to mitochondrial cristae

Hansson Petersen, C. A., Alikhani, N., Behbahani, H., Wiehager, B., Pavlov, P. F., Alafuzoff, I., Leinonen, V., Ito, A., Winblad, B., Glaser, E., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0806192105 · Cited by 693 · see citing works

Impaired mitochondrial biogenesis, defective axonal transport of mitochondria, abnormal mitochondrial dynamics and synaptic degeneration in a mouse model of Alzheimer's disease

Calkins, M. J., Manczak, M., Mao, P., Shirendeb, U., & Reddy, P. H. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr381 · Cited by 646 · see citing works

Early deficits in synaptic mitochondria in an Alzheimer's disease mouse model

Du, H., Guo, L., Yan, S., Sosunov, A. A., McKhann, G. M., & ShiDu Yan, S. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1006586107 · Cited by 704 · see citing works

The Alzheimer’s Disease Mitochondrial Cascade Hypothesis

Swerdlow, R. H., Burns, J. M., & Khan, S. M. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100339 · Cited by 562 · see citing works

Curcumin and its Derivatives: Their Application in Neuropharmacology and Neuroscience in the 21st Century

Lee, W., Loo, C., Bebawy, M., Luk, F., Mason, R. S., & Rohanizadeh, R. (2013) · Current Neuropharmacology · doi:10.2174/1570159x11311040002 · Cited by 539 · see citing works

Metabolism and functions of copper in brain

Scheiber, I. F., Mercer, J. F. B., & Dringen, R. (2014) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2014.01.002 · Cited by 511 · see citing works

How does diabetes accelerate Alzheimer disease pathology?

Sims-Robinson, C., Kim, B., Rosko, A., & Feldman, E. L. (2010) · Nature Reviews Neurology · doi:10.1038/nrneurol.2010.130 · Cited by 492 · see citing works

Modulation of the endoplasmic reticulum–mitochondria interface in Alzheimer’s disease and related models

Hedskog, L., Pinho, C. M., Filadi, R., Rönnbäck, A., Hertwig, L., Wiehager, B., Larssen, P., Gellhaar, S., Sandebring, A., Westerlund, M., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1300677110 · Cited by 478 · see citing works

Mitochondrial oxidative stress in aging and healthspan

Dai, D., Chiao, Y. A., Marcinek, D. J., Szeto, H. H., & Rabinovitch, P. S. (2014) · Longevity & Healthspan · doi:10.1186/2046-2395-3-6 · Cited by 481 · see citing works

Sirtuin Functions in Health and Disease

Yamamoto, H., Schoonjans, K., & Auwerx, J. (2007) · Molecular Endocrinology · doi:10.1210/me.2007-0079 · Cited by 480 · see citing works

Copper, iron, and zinc ions homeostasis and their role in neurodegenerative disorders (metal uptake, transport, distribution and regulation)

Kozłowski, H., Janicka-Kłos, A., Brasuń, J., Gaggelli, E., Valensin, D., & Valensin, G. (2009) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2009.05.011 · Cited by 467 · see citing works

Mitochondria-targeted antioxidants protect against amyloid-β toxicity in Alzheimer's disease neurons

Manczak, M., Mao, P., Calkins, M. J., Cornea, A., Reddy, A. P., Murphy, M. P., Szeto, H. H., Park, B., & Reddy, P. H. (2010) · Journal of Alzheimer's Disease · doi:10.3233/jad-2010-100564 · Cited by 469 · see citing works

Abnormal mitochondrial dynamics and synaptic degeneration as early events in Alzheimer’s disease: Implications to mitochondria-targeted antioxidant therapeutics

Reddy, P. H., Tripathi, R., Troung, Q., Tirumala, K., Reddy, T. P., Anekonda, V., Shirendeb, U. P., Calkins, M. J., Reddy, A. P., Mao, P., et al. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.10.011 · Cited by 394 · see citing works

Pharmacological approaches to restore mitochondrial function

Andreux, P. A., Houtkooper, R. H., & Auwerx, J. (2013) · Nature Reviews Drug Discovery · doi:10.1038/nrd4023 · Cited by 383 · see citing works

The Role of Mitochondria in Neurodegenerative Diseases: the Lesson from Alzheimer’s Disease and Parkinson’s Disease

Monzio Compagnoni, G., Di Fonzo, A., Corti, S., Comi, G. P., Bresolin, N., & Masliah, E. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-01926-1 · Cited by 378 · see citing works

Amyloid precursor protein‐mediated free radicals and oxidative damage: Implications for the development and progression of Alzheimer's disease

Reddy, P. H. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03530.x · Cited by 356 · see citing works

A mitochondrial bioenergetic etiology of disease

Wallace, D. C. (2013) · Journal of Clinical Investigation · doi:10.1172/jci61398 · Cited by 342 · see citing works

Metallostasis in Alzheimer's disease

Ayton, S., Lei, P., & Bush, A. I. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.10.558 · Cited by 354 · see citing works

Abnormal interaction of VDAC1 with amyloid beta and phosphorylated tau causes mitochondrial dysfunction in Alzheimer’s disease

Manczak, M., & Reddy, P. H. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds360 · Cited by 348 · see citing works

Mitochondria-targeted peptide antioxidants: Novel neuroprotective agents

Szeto, H. H. (2006) · The AAPS Journal · doi:10.1208/aapsj080362 · Cited by 332 · see citing works

Mitochondria-Associated Membranes: Composition, Molecular Mechanisms, and Physiopathological Implications

Giorgi, C., Missiroli, S., Patergnani, S., Duszyński, J., Wieckowski, M. R., & Pinton, P. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.6223 · Cited by 332 · see citing works

Mitochondria, calcium and cell death: A deadly triad in neurodegeneration

Celsi, F., Pizzo, P., Brini, M., Leo, S., Fotino, C., Pinton, P., & Rizzuto, R. (2009) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.02.021 · Cited by 321 · see citing works

Aging and amyloid beta-induced oxidative DNA damage and mitochondrial dysfunction in Alzheimer's disease: Implications for early intervention and therapeutics

Mao, P., & Reddy, P. H. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.08.005 · Cited by 311 · see citing works

PINK1 signalling rescues amyloid pathology and mitochondrial dysfunction in Alzheimer’s disease

Du, F., Yu, Q., Yan, S., Hu, G., Lue, L., Walker, D., Wu, L., Yan, S. F., Tieu, K., & Yan, S. S. (2017) · Brain · doi:10.1093/brain/awx258 · Cited by 307 · see citing works

A mitochondrial etiology of Alzheimer and Parkinson disease

Coskun, P. E., Wyrembak, J., Schriner, S. E., Chen, H.-W., Marciniack, C., LaFerla, F. M., & Wallace, D. C. (2011) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2011.08.008 · Cited by 297 · see citing works

Mitochondrial dynamics in cell death and neurodegeneration

Cho, D., Nakamura, T., & Lipton, S. A. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0435-2 · Cited by 299 · see citing works

RAGE-mediated signaling contributes to intraneuronal transport of amyloid-β and neuronal dysfunction

Takuma, K., Fang, F., Zhang, W., Yan, S., Fukuzaki, E., Du, H., Sosunov, A., McKhann, G., Funatsu, Y., Nakamichi, N., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0905686106 · Cited by 290 · see citing works

Are mitochondria critical in the pathogenesis of Alzheimer's disease?

Reddy, P. H., & Beal, M. F. (2005) · Brain Research Reviews · doi:10.1016/j.brainresrev.2005.03.004 · Cited by 289 · see citing works

Increasing Cu bioavailability inhibits Aβ oligomers and tau phosphorylation

Crouch, P. J., Hung, L. W., Adlard, P. A., Cortés, M., Lal, V., Filiz, G., Perez, K. A., Nurjono, M., Caragounis, A., Du, T., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809057106 · Cited by 280 · see citing works

Intraneuronal amyloid β oligomers cause cell death via endoplasmic reticulum stress, endosomal/lysosomal leakage, and mitochondrial dysfunction in vivo

Umeda, T., Tomiyama, T., Sakama, N., Tanaka, S., Lambert, M. P., Klein, W. L., & Mori, H. (2011) · Journal of Neuroscience Research · doi:10.1002/jnr.22640 · Cited by 264 · see citing works

Amyloid beta, mitochondrial structural and functional dynamics in Alzheimer's disease

Reddy, P. H. (2009) · Experimental Neurology · doi:10.1016/j.expneurol.2009.03.042 · Cited by 262 · see citing works

Vascular dysfunction in the pathogenesis of Alzheimer's disease — A review of endothelium-mediated mechanisms and ensuing vicious circles

Marco, L. Y. D., Venneri, A., Farkas, E., Evans, P. C., Marzo, A., & Frangi, A. F. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.08.014 · Cited by 258 · see citing works

Diabetes and Alzheimer’s disease crosstalk

Baglietto‐Vargas, D., Shi, J. J., Yaeger, D. M., Ager, R. R., & LaFerla, F. M. (2016) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2016.03.005 · Cited by 254 · see citing works

Reduction in mitochondrial superoxide dismutase modulates Alzheimer’s disease-like pathology and accelerates the onset of behavioral changes in human amyloid precursor protein transgenic mice

Esposito, L., Raber, J., Kekonius, L., Yan, F., Yu, G.-Q., Bien-Ly, N., Puoliväli, J., Scearce-Levie, K., Masliah, E., & Mucke, L. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.0482-06.2006 · Cited by 254 · see citing works

Impairing the Mitochondrial Fission and Fusion Balance: A New Mechanism of Neurodegeneration

Knott, A. B., & Bossy‐Wetzel, E. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1427.030 · Cited by 258 · see citing works

The transition metals copper and iron in neurodegenerative diseases

Rivera-Mancía, S., Pérez‐Neri, I., Rı́os, C., Tristán-López, L. A., Rivera-Espinosa, L., & Montes, S. (2010) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2010.04.010 · Cited by 243 · see citing works

Mechanisms of Aβ mediated neurodegeneration in Alzheimer's disease

Crouch, P. J., Harding, S.-M. E., White, A. R., Camakaris, J., Bush, A. I., & Masters, C. L. (2007) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.07.013 · Cited by 244 · see citing works

Pathogenesis of Alzheimer's disease.

Swerdlow, R. H. (2007) · PubMed Central · Cited by 236 · see citing works

Mitochondrial Medicine for Aging and Neurodegenerative Diseases

Reddy, P. H. (2008) · NeuroMolecular Medicine · doi:10.1007/s12017-008-8044-z · Cited by 230 · see citing works

Mechanisms of mitochondrial dysfunction and energy deficiency in Alzheimer’s disease

Atamna, H., & Frey, W. H. (2007) · Mitochondrion · doi:10.1016/j.mito.2007.06.001 · Cited by 278 · see citing works

Mitochondria as a Therapeutic Target for Aging and Neurodegenerative Diseases

Reddy, P. H., & Reddy, T. P. (2011) · Current Alzheimer Research · doi:10.2174/156720511795745401 · Cited by 227 · see citing works

Alterations in Mitochondrial Quality Control in Alzheimer’s Disease

Cai, Q., & Tammineni, P. (2016) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2016.00024 · Cited by 215 · see citing works

The Alzheimer's disease mitochondrial cascade hypothesis: an update

Swerdlow, R. H., & Khan, S. M. (2009) · Experimental Neurology · doi:10.1016/j.expneurol.2009.01.011 · Cited by 206 · see citing works

Mitochondria and Cell Bioenergetics: Increasingly Recognized Components and a Possible Etiologic Cause of Alzheimer's Disease

Swerdlow, R. H. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4149 · Cited by 203 · see citing works

Mitochondria in Neurodegeneration

Lezi, E., & Swerdlow, R. H. (2011) · Advances in experimental medicine and biology · doi:10.1007/978-94-007-2869-1_12 · Cited by 204 · see citing works

Oxidized cholesterol as the driving force behind the development of Alzheimer’s disease

Gamba, P., Testa, G., Gargiulo, S., Staurenghi, E., Poli, G., & Leonarduzzi, G. (2015) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2015.00119 · Cited by 202 · see citing works

Molecular links between Alzheimer’s disease and diabetes mellitus

Yang, Y., & Song, W. (2013) · Neuroscience · doi:10.1016/j.neuroscience.2013.07.009 · Cited by 201 · see citing works

Redox Reactions of Copper Complexes Formed with Different β-Amyloid Peptides and Their Neuropathalogical Relevance

Jiang, D., Men, L., Wang, J., Zhang, Y., Chickenyen, S., Wang, Y., & Zhou, F. (2007) · Biochemistry · doi:10.1021/bi700508n · Cited by 202 · see citing works

Concentration Dependent Cu2+Induced Aggregation and Dityrosine Formation of the Alzheimer's Disease Amyloid-β Peptide

Smith, D. P., Ciccotosto, G. D., Tew, D. J., Fodero‐Tavoletti, M. T., Johanssen, T., Masters, C. L., Barnham, K. J., & Cappai, R. (2007) · Biochemistry · doi:10.1021/bi0620961 · Cited by 193 · see citing works

Insulin signaling, glucose metabolism and mitochondria: Major players in Alzheimer's disease and diabetes interrelation

Correia, S. C., Santos, R. X., Carvalho, C., Cardoso, S., Candeias, E., Santos, M. S., Oliveira, C. R., & Moreira, P. I. (2012) · Brain Research · doi:10.1016/j.brainres.2011.12.063 · Cited by 195 · see citing works

Mitochondrial Dysfunction: The First Domino in Brain Aging and Alzheimer's Disease?

Leuner, K., Hauptmann, S., Abdel-Kader, R. M., Scherping, I., Keil, U., Strosznajder, J. B., Eckert, A., & Müller, W. E. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1763 · Cited by 194 · see citing works

Mitochondrial Amyloid-β Levels are Associated with the Extent of Mitochondrial Dysfunction in Different Brain Regions and the Degree of Cognitive Impairment in Alzheimer's Transgenic Mice

Dragicevic, N., Mamcarz, M. B., Zhu, Y., Buzzeo, R. W., Tan, J., Arendash, G. W., & Bradshaw, P. C. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100342 · Cited by 193 · see citing works

Brain mitochondrial dysfunction as a link between Alzheimer's disease and diabetes

Moreira, P. I., Santos, M. S., Seiça, R. M. F., & Oliveira, C. R. (2007) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2007.01.017 · Cited by 187 · see citing works

Mitochondrial Dysfunction in Aging and Alzheimer's Disease: Strategies to Protect Neurons

Reddy, P. H. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1754 · Cited by 187 · see citing works

Role of Mitochondria in Neurodegenerative Diseases: Mitochondria as a Therapeutic Target in Alzheimer's Disease

Reddy, P. H. (2009) · CNS Spectrums · doi:10.1017/s1092852900024901 · Cited by 186 · see citing works

Melatonin treatment restores mitochondrial function in Alzheimer’s mice: a mitochondrial protective role of melatonin membrane receptor signaling

Dragicevic, N., Copes, N., O’Neal-Moffitt, G., Jin, J., Buzzeo, R. W., Mamcarz, M., Tan, J., Cao, C., Olcese, J., Arendash, G. W., et al. (2011) · Journal of Pineal Research · doi:10.1111/j.1600-079x.2011.00864.x · Cited by 185 · see citing works

The Alzheimer’s therapeutic PBT2 promotes amyloid‐β degradation and GSK3 phosphorylation via a metal chaperone activity

Crouch, P. J., Savva, M. S., Hung, L. W., Donnelly, P. S., Mot, A. I., Parker, S. J., Greenough, M. A., Volitakis, I., Adlard, P. A., Cherny, R. A., et al. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07402.x · Cited by 183 · see citing works

Role of Mitochondrial Amyloid-β in Alzheimer's Disease

Chen, J. X., & Yan, S. S. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100357 · Cited by 181 · see citing works

Three Histidine Residues of Amyloid-β Peptide Control the Redox Activity of Copper and Iron

Nakamura, M., Shishido, N., Nunomura, A., Smith, M. A., Perry, G. L., Hayashi, Y., Nakayama, K., & Hayashi, T. (2007) · Biochemistry · doi:10.1021/bi701079z · Cited by 184 · see citing works

Mitochondrial dysfunction: the missing link between aging and sporadic Alzheimer’s disease

Grimm, A., Friedland, K., & Eckert, A. (2015) · Biogerontology · doi:10.1007/s10522-015-9618-4 · Cited by 182 · see citing works

Copper in Alzheimer's Disease: A Meta-Analysis of Serum, Plasma, and Cerebrospinal Fluid Studies

Bucossi, S., Ventriglia, M., Panetta, V., Salustri, C., Pasqualetti, P., Mariani, S., Siotto, M., Rossini, P. M., & Squitti, R. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-101473 · Cited by 183 · see citing works

The role of mitochondria in inherited neurodegenerative diseases

Kwong, J. Q., Beal, M. F., & Manfredi, G. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03990.x · Cited by 180 · see citing works

Reduced dynamin-related protein 1 protects against phosphorylated Tau-induced mitochondrial dysfunction and synaptic damage in Alzheimer’s disease

Kandimalla, R. J. L., Mańczak, M., Fry, D., Yeguvapalli, S., Sesaki, H., & Reddy, P. H. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw312 · Cited by 180 · see citing works

Protective effects of reduced dynamin-related protein 1 against amyloid beta-induced mitochondrial dysfunction and synaptic damage in Alzheimer’s disease

Mańczak, M., Kandimalla, R. J. L., Fry, D., Sesaki, H., & Reddy, P. H. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw330 · Cited by 176 · see citing works

Mitochondrial dysfunction - the beginning of the end in Alzheimer's disease? Separate and synergistic modes of tau and amyloid-β toxicity

Eckert, A., Schmitt, K., & Götz, J. (2011) · Alzheimer's Research & Therapy · doi:10.1186/alzrt74 · Cited by 177 · see citing works

Multiple Defects in Energy Metabolism in Alzheimers Disease

Ferreira, I. L., Resende, R., Ferreiro, E. B., Rego, A. C., & Pereira, C. (2010) · Current Drug Targets · doi:10.2174/1389450111007011193 · Cited by 181 · see citing works

Quantitative profiling brain proteomes revealed mitochondrial dysfunction in Alzheimer’s disease

Adav, S. S., Park, J. E., & Sze, S. K. (2019) · Molecular Brain · doi:10.1186/s13041-019-0430-y · Cited by 175 · see citing works

Defining Alzheimer as a common age-related neurodegenerative process not inevitably leading to dementia

Ferrer, I. (2012) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2012.03.005 · Cited by 174 · see citing works

Mitochondria-targeted catalase reduces abnormal APP processing, amyloid production and BACE1 in a mouse model of Alzheimer's disease: implications for neuroprotection and lifespan extension

Mao, P., Mańczak, M., Calkins, M. J., Truong, Q., Reddy, T. P., Reddy, A. P., Shirendeb, U. P., Lo, H., Rabinovitch, P. S., & Reddy, P. H. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds128 · Cited by 174 · see citing works

Role of mitochondrial homeostasis and dynamics in Alzheimer's disease

Selfridge, J. E., E, L., Lu, J., & Swerdlow, R. H. (2013) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.12.057 · Cited by 175 · see citing works

Altered mitochondria, energy metabolism, voltage-dependent anion channel, and lipid rafts converge to exhaust neurons in Alzheimer’s disease

Ferrer, I. (2009) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-009-9243-5 · Cited by 172 · see citing works

Mitochondrial membrane permeabilisation by amyloid aggregates and protection by polyphenols

Camilleri, A., Zarb, C., Caruana, M., Ostermeier, U., Ghio, S., Högen, T., Schmidt, F., Giese, A., & Vassallo, N. (2013) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2013.06.026 · Cited by 161 · see citing works

S-Nitrosylation of DRP1 Does Not Affect Enzymatic Activity and is Not Specific to Alzheimer's Disease

Bossy, B., Petrilli, A. M., Klinglmayr, E., Chen, J., Lütz‐Meindl, U., Knott, A. B., Masliah, E., Schwarzenbacher, R., & Bossy‐Wetzel, E. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100552 · Cited by 162 · see citing works

Coenzyme Q10 Decreases Amyloid Pathology and Improves Behavior in a Transgenic Mouse Model of Alzheimer's Disease

Dumont, M., Kipiani, K., Yu, F., Wille, E. J., Katz, M., Calingasan, N. Y., Gouras, G. K., Lin, M. T. S., & Beal, M. F. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-110209 · Cited by 161 · see citing works

Impaired platelet mitochondrial activity in Alzheimer's disease and mild cognitive impairment

Valla, J., Schneider, L., Niedzielko, T., Coon, K. D., Caselli, R., Sabbagh, M. N., Ahern, G. L., Baxter, L., Alexander, G., Walker, D. G., et al. (2006) · Mitochondrion · doi:10.1016/j.mito.2006.10.004 · Cited by 159 · see citing works

Redox Control of the Survival of Healthy and Diseased Cells

Zhang, Y., Du, Y., Le, W., Wang, K., Kieffer, N., & Zhang, J. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3685 · Cited by 156 · see citing works

Mitochondrial Oxidative Damage in Aging and Alzheimer′s Disease: Implications for Mitochondrially Targeted Antioxidant Therapeutics

Reddy, P. H. (2006) · BioMed Research International · doi:10.1155/jbb/2006/31372 · Cited by 153 · see citing works

Ferulic acid inhibits oxidative stress and cell death induced by Ab oligomers: Improved delivery by solid lipid nanoparticles

Picone, P., Bondı̀, M. L., Picone, P., Bondı̀, M. L., Montana, G., Bruno, A., Pitarresi, G. L., Giammona, G., & Carlo, M. D. (2009) · Free Radical Research · doi:10.1080/10715760903214454 · Cited by 154 · see citing works

Mitochondrial respiratory chain Complexes I and IV are impaired by β-amyloid via direct interaction and through Complex I-dependent ROS production, respectively

Bobba, A., Amadoro, G., Valenti, D., Corsetti, V., Lassandro, R., & Atlante, A. (2013) · Mitochondrion · doi:10.1016/j.mito.2013.03.008 · Cited by 150 · see citing works

Mitoenergetic failure in Alzheimer disease

Parihar, M. S., & Brewer, G. J. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00232.2006 · Cited by 149 · see citing works

Mitochondrial trafficking of APP and alpha synuclein: Relevance to mitochondrial dysfunction in Alzheimer's and Parkinson's diseases

Devi, L., & Anandatheerthavarada, H. K. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.07.007 · Cited by 149 · see citing works

Mitochondrial Dysfunction Contributes to the Pathogenesis of Alzheimer’s Disease

Cabezas-Opazo, F., Vergara-Pulgar, K., Maria Jose Perez, J., Jara, C., Osorio‐Fuentealba, C., & Quintanilla, R. A. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/509654 · Cited by 150 · see citing works

Multi-Target Directed Donepezil-Like Ligands for Alzheimer's Disease

Unzeta, M., Esteban, G., Bolea, I., Fogel, W. A., Ramsay, R. R., Youdim, M. B. H., Tipton, K. F., & Marco, J. L. (2016) · Frontiers in Neuroscience · doi:10.3389/fnins.2016.00205 · Cited by 151 · see citing works

Amyloid beta-induced glycogen synthase kinase 3β phosphorylated VDAC1 in Alzheimer's disease: Implications for synaptic dysfunction and neuronal damage

Reddy, P. H. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.06.012 · Cited by 147 · see citing works

Multiple faces of dynamin-related protein 1 and its role in Alzheimer's disease pathogenesis

Kandimalla, R. J. L., & Reddy, P. H. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.12.018 · Cited by 144 · see citing works

Alzheimer's APP mangles mitochondria

Lin, M. T., & Beal, M. F. (2006) · Nature Medicine · doi:10.1038/nm1106-1241 · Cited by 143 · see citing works

Adiponectin is Protective against Oxidative Stress Induced Cytotoxicity in Amyloid-Beta Neurotoxicity

Chan, K., Lam, K. S. L., Cheng, O.-Y., Kwan, J., Ho, P. W., Cheng, K. K. Y., Chung, S. K., Ho, J. W.-M., Guo, V. Y., & Xu, A. (2012) · PLoS ONE · doi:10.1371/journal.pone.0052354 · Cited by 140 · see citing works

The role of mitochondria in neurodegenerative diseases

Filosto, M., Scarpelli, M., Cotelli, M. S., Vielmi, V., Todeschini, A., Gregorelli, V., Tonin, P., Tomelleri, G., & Padovani, A. (2011) · Journal of Neurology · doi:10.1007/s00415-011-6104-z · Cited by 140 · see citing works

Mitochondria and Neurodegeneration

Petrozzi, L., Ricci, G., Giglioli, N. J., Siciliano, G., & Mancuso, M. (2007) · Bioscience Reports · doi:10.1007/s10540-007-9038-z · Cited by 139 · see citing works

Mitochondria-targeted small molecule SS31: a potential candidate for the treatment of Alzheimer’s disease

Reddy, P. H., Mańczak, M., & Kandimalla, R. J. L. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx052 · Cited by 134 · see citing works

Copper‐dependent inhibition of cytochrome c oxidase by Aβ1−42 requires reduced methionine at residue 35 of the Aβ peptide

Crouch, P. J., Barnham, K. J., Duce, J. A., Blake, R. E., Masters, C. L., & Trounce, I. A. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04050.x · Cited by 46 · see citing works

Amyloid-b Peptide Binds to Cytochrome C Oxidase Subunit 1

Fern, L., Hern, O., Mena, R., Vazquez-ramirez, R., Kubli‐Garfias, C., Cribbs, D. H., Manoutcharian, K., & Gevorkian, G. (2012)

P2‐130: Beta‐amyloid peptide 1‐42 binds to N‐terminal fragment of cytochrome C oxidase subunit 1 (COX1)

Hernandez, L. G., Luna‐Muñoz, J., Acero, G., Vázquez‐Ramírez, R., & Gevorkian, G. (2012) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2012.05.835

Amyloid-β Peptide Binds to Cytochrome C Oxidase Subunit 1

Hernández-Zimbrón, L. F., Luna‐Muñoz, J., Mena, R., Vázquez‐Ramírez, R., Kubli‐Garfias, C., Cribbs, D. H., Manoutcharian, K., & Gevorkian, G. (2012) · PLoS ONE · doi:10.1371/journal.pone.0042344 · Cited by 93 · see citing works

Amyloid-beta Peptide Binds to Cytochrome C Oxidase Subunit 1

Hernandez-Zimbron, L. F., Luna-Muoz, J., Mena, R., Vazquez-Ramirez, R., Kubli‐Garfias, C., Cribbs, D. H., Manoutcharian, K., & Gevorkian, G. (2012) · eScholarship (California Digital Library)