Cited by 792Alzheimer's disease research and treatmentsMitochondrial Function and PathologyDementia and Cognitive Impairment Research

The DOI matches its Crossref record; 62 of the 62 references it cites were found in a registry or an index.

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

Open access

Devi, Latha, Prabhu, Badanavalu M., Galati, Domenico F., Avadhani, Narayan G., Anandatheerthavarada, Hindupur K.·2006·The Journal of Neuroscience

DOI 10.1523/jneurosci.1469-06.2006PMC PMC6675337

Open this paper in CoChat — free account Open PDF

Abstract

Mitochondrial dysfunction is one of the major intracellular lesions of Alzheimer's disease (AD). However, the causative factors involved in the mitochondrial dysfunction in human AD are not well understood. Here we report that nonglycosylated full-length and C-terminal truncated amyloid precursor protein (APP) accumulates exclusively in the protein import channels of mitochondria of human AD brains but not in age-matched controls. Furthermore, in AD brains, mitochondrially associated APP formed stable approximately 480 kDa complexes with the translocase of the outer mitochondrial membrane 40 (TOM40) import channel and a super complex of approximately 620 kDa with both mitochondrial TOM40 and the translocase of the inner mitochondrial membrane 23 (TIM23) import channel TIM23 in an "N(in mitochondria)-C(out cytoplasm)" orientation. Accumulation of APP across mitochondrial import channels, which varied with the severity of AD, inhibited the entry of nuclear-encoded cytochrome c oxidase subunits IV and Vb proteins, which was associated with decreased cytochrome c oxidase activity and increased levels of H2O2. Regional distribution of mitochondrial APP showed higher levels in AD-vulnerable brain regions, such as the frontal cortex, hippocampus, and amygdala. Mitochondrial accumulation of APP was also observed in the cholinergic, dopaminergic, GABAergic, and glutamatergic neuronal types in the category III AD brains. The levels of translocationally arrested mitochondrial APP directly correlated with mitochondrial dysfunction. Moreover, apolipoprotein genotype analysis revealed that AD subjects with the E3/E4 alleles had the highest content of mitochondrial APP. Collectively, these results suggest that abnormal accumulation of APP across mitochondrial import channels, causing mitochondrial dysfunction, is a hallmark of human AD pathology.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1523/jneurosci.1469-06.2006

Cites

62 of 62 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

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 316,394
Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
Schägger, H., & von JAGOW, G. (1991) · Analytical Biochemistry · doi:10.1016/0003-2697(91)90094-a · Cited by 2,267
The cholinergic hypothesis of Alzheimer’s disease: A review of progress
Francis, P. T., Palmer, A. M., Snape, M., & Wilcock, G. K. (1999) · Journal of Neurology, Neurosurgery & Psychiatry · doi:10.1136/jnnp.66.2.137 · Cited by 2,198 · cited 1×
“In addition to cholinergic neurons, several other neuronal types, such as dopaminergic, GABAergic, and glutamatergic neurons, have been shown to be affected in the later stages of the pathogenesis of AD (Francis et al., 1999; Francis, 2003).”
Background
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
Editorial on Consensus Recommendations for the Postmortem Diagnosis of Alzheimer Disease from the National Institute on Aging and the Reagan Institute Working Group on Diagnostic Criteria for the Neuropathological Assessment of Alzheimer Disease
HYMAN, B. T., & TROJANOWSKI, J. Q. (1997) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/00005072-199710000-00002 · Cited by 1,542
Treatment with a Copper-Zinc Chelator Markedly and Rapidly Inhibits β-Amyloid Accumulation in Alzheimer's Disease Transgenic Mice
Cherny, R. A., Atwood, C. S., Xilinas, M. E., Gray, D. N., Jones, W. D., McLean, C. A., Barnham, K. J., Volitakis, I., Fraser, F. W., Kim, Y.-S., et al. (2001) · Neuron · doi:10.1016/s0896-6273(01)00317-8 · Cited by 1,447
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
Translating cell biology into therapeutic advances in Alzheimer's disease
Selkoe, D. J. (1999) · Nature · doi:10.1038/399a023 · Cited by 1,166
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
Consensus Recommendations for the Postmortem Diagnosis of Alzheimer’s Disease
(1997) · Neurobiology of Aging · doi:10.1016/s0197-4580(97)00057-2 · Cited by 981

Flagged first, then by citations

Show all 62 references

Research works printed but not linked: 2

Dasso M (1998) in Current protocols in cell biology, In vitro reconstitution, eds Bonifacino JS Dasso M Harford JB Lippincot-Schawartz J Yamada KM (Wiley, New York), pp 11.0.1–11.0.2.
Jagannatha Rao, 1999, Trace elements in the cerebrospinal fluid of Alzheimer’s disease, Alzheimers Rep, 2, 333

Sorted by citations

Items 101–200 of 790

Mitochondrial cholesterol: Metabolism and impact on redox biology and disease
Goicoechea, L., de la Rosa, L. C., Torres, S., García‐Ruiz, C., & Fernández-Checa, J. C. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102643 · Cited by 196
Axonal Degeneration during Aging and Its Functional Role in Neurodegenerative Disorders
Salvadores, N., Sanhueza, M., Manque, P., & Court, F. A. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00451 · Cited by 182
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 182
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 180
Current Concepts of Neurodegenerative Mechanisms in Alzheimer’s Disease
Magalingam, K. B., Radhakrishnan, A., Ping, N. S., & Haleagrahara, N. (2018) · BioMed Research International · doi:10.1155/2018/3740461 · Cited by 178
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
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 183
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 176
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
Defective mitophagy and synaptic degeneration in Alzheimer's disease: Focus on aging, mitochondria and synapse
Morton, H., Kshirsagar, S., Orlov, E., Bunquin, L. E., Sawant, N. A., Boleng, L., George, M., Basu, T., Ramasubramanian, B., Pradeepkiran, J. A., et al. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.07.013 · Cited by 172
Dissection of Regulatory Networks that Are Altered in Disease via Differential Co-expression
Amar, D., Safer, H., & Shamir, R. (2013) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1002955 · Cited by 169
Roles of mitochondria in human disease
Duchen, M. R., & Szabadkai, G. (2010) · Essays in Biochemistry · doi:10.1042/bse0470115 · Cited by 171
ALS-linked mutant superoxide dismutase 1 (SOD1) alters mitochondrial protein composition and decreases protein import
Li, Q., Vande Velde, C., Israelson, A., Xie, J., Bailey, A. O., Dong, M.-Q., Chun, S.-J., Roy, T., Winer, L., Yates, J. R., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1014862107 · Cited by 169
Biology of Mitochondria in Neurodegenerative Diseases
Martin, L. J. (2012) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-385883-2.00005-9 · Cited by 164
Nature and cause of mitochondrial dysfunction in Huntington’s disease: focusing on huntingtin and the striatum
Oliveira, J. M. A. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06741.x · Cited by 163
Mitochondrial respiratory chain dysfunction: Implications in neurodegeneration
Morán, M., Moreno-Lastres, D., Marín-Buera, L., Arenas, J., Martín, M. A., & Ugalde, C. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.05.009 · Cited by 168
Defective Autophagy and Mitophagy in Aging and Alzheimer’s Disease
Tran, M., & Reddy, P. H. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.612757 · Cited by 167
A Synergistic Dysfunction of Mitochondrial Fission/Fusion Dynamics and Mitophagy in Alzheimer's Disease
Santos, R. X., Correia, S. C., Wang, X., Perry, G. L., Smith, M. A., Moreira, P. I., & Zhu, X. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100666 · Cited by 162
Localization and Processing of the Amyloid-β Protein Precursor in Mitochondria-Associated Membranes
Prete, D. D., Suski, J. M., Oulès, B., Debayle, D., Gay, A.-S., Lacas‐Gervais, S., Bussiere, R., Bauer, C., Pinton, P., Paterlini-Bréchot, P., et al. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160953 · Cited by 167
Mitochondrial biology, targets, and drug delivery
Milane, L. S., Trivedi, M. S., Singh, A., Talekar, M., & Amiji, M. M. (2015) · Journal of Controlled Release · doi:10.1016/j.jconrel.2015.03.036 · Cited by 163
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 161
The role of mitophagy in the regulation of mitochondrial energetic status in neurons
Han, S., Zhang, M., Jeong, Y. Y., Margolis, D. J., & Cai, Q. (2021) · Autophagy · doi:10.1080/15548627.2021.1907167 · Cited by 151
Mitochondrial Cholesterol Loading Exacerbates Amyloid β Peptide-Induced Inflammation and Neurotoxicity
Fernández, A., Llacuna, L., Fernández-Checa, J. C., & Colell, A. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.4909-08.2009 · Cited by 154
A review on mitochondrial restorative mechanism of antioxidants in Alzheimer’s disease and other neurological conditions
Kumar, A., & Singh, A. (2015) · Frontiers in Pharmacology · doi:10.3389/fphar.2015.00206 · Cited by 157
TOM40 Mediates Mitochondrial Dysfunction Induced by α-Synuclein Accumulation in Parkinson’s Disease
Bender, A., Desplats, P., Spencer, B. J., Rockenstein, E. M., Adame, A., Elstner, M., Laub, C., Mueller, S. K., Koob, A. O., Mante, M., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0062277 · Cited by 151
Retracted
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
Synaptic Mitochondrial Pathology in Alzheimer's Disease
Du, H., Guo, L., & Yan, S. S. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4277 · Cited by 154
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
Hyperoside protects primary rat cortical neurons from neurotoxicity induced by amyloid β-protein via the PI3K/Akt/Bad/BclXL-regulated mitochondrial apoptotic pathway
Zeng, K., Wang, X., Ko, H., Kwon, H. C., Cha, J. W., & Yang, H. O. (2011) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2011.09.177 · Cited by 147
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 148
Physiology and pharmacology of amyloid precursor protein
Cho, Y., Bae, H., Okun, E., Arumugam, T. V., & Jo, D. (2022) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2022.108122 · Cited by 150
Alzheimer's APP mangles mitochondria
Lin, M. T., & Beal, M. F. (2006) · Nature Medicine · doi:10.1038/nm1106-1241 · Cited by 143
Role of increased expression of the proteasome in the protective effects of sulforaphane against hydrogen peroxide-mediated cytotoxicity in murine neuroblastoma cells
Kwak, M.-K., Cho, J.-M., Huang, B., Shin, S., & Kensler, T. W. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.05.029 · Cited by 143
Mechanisms of protein toxicity in neurodegenerative diseases
Chung, C. G., Lee, H., & Lee, S. B. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-018-2854-4 · Cited by 142
Neuroketotherapeutics: A modern review of a century-old therapy
Koppel, S. J., & Swerdlow, R. H. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.05.019 · Cited by 142
Genetic association study on in and around the APOE in late-onset Alzheimer disease in Japanese
Takei, N., Miyashita, A., Tsukie, T., Arai, H., Asada, T., Imagawa, M., Shoji, M., Higuchi, S., Urakami, K., Kimura, H., et al. (2009) · Genomics · doi:10.1016/j.ygeno.2009.01.003 · Cited by 143
Amyloid‐beta ( A β1–42)‐induced paralysis in C aenorhabditis elegans is inhibited by the polyphenol quercetin through activation of protein degradation pathways
Regitz, C., Dußling, L. M., & Wenzel, U. (2014) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201400014 · Cited by 142
Neuroprotective Secreted Amyloid Precursor Protein Acts by Disrupting Amyloid Precursor Protein Dimers
Gralle, M., Caarls, M. B., & Wouters, F. S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808755200 · Cited by 148
Cognitive and non-cognitive behaviors in the triple transgenic mouse model of Alzheimer's disease expressing mutated APP, PS1, and Mapt (3xTg-AD)
Filali, M., Lalonde, R., Thériault, P., Julien, C., Calon, F., & Planel, E. (2012) · Behavioural Brain Research · doi:10.1016/j.bbr.2012.07.004 · Cited by 139
Glutathione peroxidase activity is neuroprotective in models of Huntington's disease
Mason, R. P., Casu, M., Butler, N. J., Breda, C., Campesan, S., Clapp, J., Green, E. W., Dhulkhed, D., Kyriacou, C. P., & Giorgini, F. (2013) · Nature Genetics · doi:10.1038/ng.2732 · Cited by 138
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 137
Roles of sigma-1 receptors on mitochondrial functions relevant to neurodegenerative diseases
Weng, T.-Y., Tsai, S., & Su, T. (2017) · Journal of Biomedical Science · doi:10.1186/s12929-017-0380-6 · Cited by 142
Intracellular Sources of ROS/H2O2 in Health and Neurodegeneration: Spotlight on Endoplasmic Reticulum
Konno, T., Melo, E. P., Chambers, J. E., & Avezov, E. (2021) · Cells · doi:10.3390/cells10020233 · Cited by 143
Protective Role of Methylene Blue in Alzheimer's Disease via Mitochondria and Cytochrome c Oxidase
Atamna, H., & Kumar, R. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100414 · Cited by 142
Mitochondrial dysfunction and accumulation of the β-secretase-cleaved C-terminal fragment of APP in Alzheimer's disease transgenic mice
Devi, L., & Ohno, M. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.09.001 · Cited by 133
Alleviation of neuronal energy deficiency by mTOR inhibition as a treatment for mitochondria-related neurodegeneration
Zheng, X., Boyer, L. F., Jin, M., Kim, Y., Fan, W., Bardy, C., Berggren, W. T., Evans, R. M., Gage, F. H., & Hunter, T. R. (2016) · eLife · doi:10.7554/elife.13378 · Cited by 139
Melatonin in Alzheimer’s Disease: A Latent Endogenous Regulator of Neurogenesis to Mitigate Alzheimer’s Neuropathology
Hossain, M. F., Uddin, M. S., Uddin, G. M. S., Sumsuzzman, D. M., Islam, M. S., Barreto, G. E., Mathew, B., & Ashraf, G. M. (2019) · Molecular Neurobiology · doi:10.1007/s12035-019-01660-3 · Cited by 136
Molecular mechanisms linking amyloid β toxicity and Tau hyperphosphorylation in Alzheimer׳s disease
Lloret, A., Fuchsberger, T., Giraldo, E., & Viña, J. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.02.028 · Cited by 135
Linking Oxidative Stress and Proteinopathy in Alzheimer’s Disease
Sharma, C., & Kim, S. R. (2021) · Antioxidants · doi:10.3390/antiox10081231 · Cited by 145
Metabolic Risk Factors of Sporadic Alzheimer's Disease: Implications in the Pathology, Pathogenesis and Treatment
Chakrabarti, S., Kumar Khemka, V., Banerjee, A., Chatterjee, G., Ganguly, A., & Biswas, A. (2015) · Aging and disease · doi:10.14336/ad.2014.002 · Cited by 134
Enhanced Expression of the Voltage-Dependent Anion Channel 1 (VDAC1) in Alzheimer's Disease Transgenic Mice: An Insight into the Pathogenic Effects of Amyloid-β
Cuadrado‐Tejedor, M., Vilariño, M., Cabodevilla, F., Río, J. D., Frechilla, D., & Pérez‐Mediavilla, A. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100966 · Cited by 134
Contribution of the Nrf2 Pathway on Oxidative Damage and Mitochondrial Failure in Parkinson and Alzheimer’s Disease
Villavicencio-Tejo, F., & Quintanilla, R. A. (2021) · Antioxidants · doi:10.3390/antiox10071069 · Cited by 143
The role of amyloid-beta in the regulation of memory
Morley, J. E., & Farr, S. A. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2013.12.018 · Cited by 140
Amyloid Precursor Protein and Alzheimer’s Disease
Orobets, K. S., & Karamyshev, A. L. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241914794 · Cited by 141
Anatomically-distinct genetic associations of APOE ɛ4 allele load with regional cortical atrophy in Alzheimer's disease
Filippini, N., Rao, A., Wetten, S., Gibson, R. A., Borrie, M., Guzman, D., Kertesz, A., Loy-English, I., Williams, J., Nichols, T., et al. (2009) · NeuroImage · doi:10.1016/j.neuroimage.2008.10.003 · Cited by 143
High-dose of vitamin C supplementation reduces amyloid plaque burden and ameliorates pathological changes in the brain of 5XFAD mice
Kook, S.-Y., Lee, K.-M., Kim, Y., Cha, M.-Y., Kang, S., Baik, S., Lee, H., Park, R., & Mook‐Jung, I. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.26 · Cited by 129
Early dysregulation of the mitochondrial proteome in a mouse model of Alzheimer's disease
Chou, J. L., Shenoy, D. V., Thomas, N., Choudhary, P. K., LaFerla, F. M., Goodman, S. R., & Breen, G. A. M. (2011) · Journal of Proteomics · doi:10.1016/j.jprot.2010.12.012 · Cited by 123
Mitochondrial dysfunction and Alzheimer's disease
Maruszak, A., & Żekanowski, C. (2010) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2010.07.004 · Cited by 124
Metformin activation of AMPK-dependent pathways is neuroprotective in human neural stem cells against Amyloid-beta-induced mitochondrial dysfunction
Chiang, M., Cheng, Y., Chen, S., Yen, C., & Huang, R. (2016) · Experimental Cell Research · doi:10.1016/j.yexcr.2016.08.013 · Cited by 126
The concept of translocational regulation
Hegde, R. S., & Kang, S. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200804157 · Cited by 119
Amyloid precursor protein transgenic mouse models and Alzheimer's disease: Understanding the paradigms, limitations, and contributions
Kokjohn, T. A., & Roher, A. E. (2009) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2009.03.002 · Cited by 126
Relationships between Mitochondrial Dysfunction and Neurotransmission Failure in Alzheimer’s Disease
Wong, K. Y., Roy, J., Fung, M., Heng, B. C., Zhang, C., & Lim, L. W. (2020) · Aging and Disease · doi:10.14336/ad.2019.1125 · Cited by 122
Genome instability in Alzheimer disease
Hou, Y., Song, H., Croteau, D. L., Akbari, M., & Bohr, V. A. (2017) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2016.04.005 · Cited by 120
Alzheimer's disease: diverse aspects of mitochondrial malfunctioning.
Santos, R. X., Correia, S. C., Wang, X., Perry, G. L., Smith, M. A., Moreira, P. I., & Zhu, X. (2010) · Europe PMC (PubMed Central) · Cited by 120
Mitochondria and reactive oxygen and nitrogen species in neurological disorders and stroke: Therapeutic implications☆
Bolaños, J. P., Moro, M. Á., Lizasoaín, I., & Almeida, Á. (2009) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2009.05.009 · Cited by 120
An inherited variable poly-T repeat genotype in TOMM40 in Alzheimer disease
Roses, A. D. (2010) · Archives of Neurology · doi:10.1001/archneurol.2010.88 · Cited by 118
New Insights in the Amyloid-Beta Interaction with Mitochondria
Spuch, C., Ortolano, S., & Fernández-Balbuena, C. N. (2012) · Journal of Aging Research · doi:10.1155/2012/324968 · Cited by 121
Deconstructing Mitochondrial Dysfunction in Alzheimer Disease
García‐Escudero, V., Martín-Maestro, P., Perry, G. L., & Ávila, J. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/162152 · Cited by 120
Mitochondrial protein import dysfunction: mitochondrial disease, neurodegenerative disease and cancer
Palmer, C. S., Anderson, A. J., & Stojanovski, D. (2020) · FEBS Letters · doi:10.1002/1873-3468.14022 · Cited by 126
Decreased Proteolytic Activity of the Mitochondrial Amyloid-β Degrading Enzyme, PreP Peptidasome, in Alzheimer's Disease Brain Mitochondria
Alikhani, N., Guo, L., Yan, S., Du, H., Pinho, C. M., Chen, J. X., Glaser, E. G., & Yan, S. S. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-101716 · Cited by 119
Oxidative stress in Niemann–Pick disease, type C
Fu, R., Yanjanin, N. M., Bianconi, S. E., Pavan, W. J., & Porter, F. D. (2010) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2010.06.018 · Cited by 117
Mitochondria-Division Inhibitor 1 Protects Against Amyloid-β induced Mitochondrial Fragmentation and Synaptic Damage in Alzheimer’s Disease
Reddy, P. H., Manczak, M., & Yin, X. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170051 · Cited by 116
Mitochondrial γ‐secretase participates in the metabolism of mitochondria‐associated amyloid precursor protein
Pavlov, P. F., Wiehager, B., Sakai, J., Frykman, S., Behbahani, H., Winblad, B. G., & Ankarcrona, M. (2010) · The FASEB Journal · doi:10.1096/fj.10-157230 · Cited by 115
Amyloid-β-Induced Ion Flux in Artificial Lipid Bilayers and Neuronal Cells: Resolving a Controversy
Capone, R. F., Quiroz, F. G., Prangkio, P., Saluja, I., Sauer, A., Bautista, M. R., Turner, R. S., Yang, J., & Mayer, M. (2009) · Neurotoxicity Research · doi:10.1007/s12640-009-9033-1 · Cited by 114
Mitochondrial and Nuclear DNA Oxidative Damage in Physiological and Pathological Aging
Kowalska, M., Piekut, T., Prendecki, M., Sodel, A., Kozubski, W. P., & Dorszewska, J. (2020) · DNA and Cell Biology · doi:10.1089/dna.2019.5347 · Cited by 114
The Neurodegenerative Mitochondriopathies
Swerdlow, R. H. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-1095 · Cited by 115
Inhibitors of Catalase-Amyloid Interactions Protect Cells from β-Amyloid-Induced Oxidative Stress and Toxicity
Habib, L. K., Lee, M. T. C., & Yang, J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.132860 · Cited by 114
Characterization of mitochondrial DNA quantity and quality in the human aged and Alzheimer’s disease brain
Klein, H., Trumpff, C., Yang, H., Lee, A., Picard, M. A., Bennett, D. A., & Jager, P. L. D. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00495-8 · Cited by 110
Characterizing the Preclinical Stages of Alzheimer's Disease and the Prospect of Presymptomatic Intervention
Caselli, R. J., & Reiman, E. M. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-129026 · Cited by 111
When It Comes to an End: Oxidative Stress Crosstalk with Protein Aggregation and Neuroinflammation Induce Neurodegeneration
Michalska, P., & Leon, R. M. (2020) · Antioxidants · doi:10.3390/antiox9080740 · Cited by 119
Delineating the Mechanism of Alzheimer’s Disease Aβ Peptide Neurotoxicity
Cappai, R., & Barnham, K. J. (2008) · Neurochemical Research · doi:10.1007/s11064-007-9469-8 · Cited by 108
Alzheimer’s Disease: Recent Concepts on the Relation of Mitochondrial Disturbances, Excitotoxicity, Neuroinflammation, and Kynurenines
Zádori, D., Veres, G., Szalárdy, L., Klivènyi, P., & Vécsei, L. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-170929 · Cited by 108
Physical Exercise and Brain Mitochondrial Fitness: The Possible Role Against Alzheimer's Disease
Bernardo, T. C., Marques‐Aleixo, I., Beleza, J., Oliveira, P. J., Ascensão, A., & Magalhães, J. (2016) · Brain Pathology · doi:10.1111/bpa.12403 · Cited by 108
Central and Peripheral Metabolic Defects Contribute to the Pathogenesis of Alzheimer's Disease: Targeting Mitochondria for Diagnosis and Prevention
Peng, Y., Gao, P., Shi, L., Chen, L., Liu, J., & Long, J. (2020) · Antioxidants & Redox Signaling · doi:10.1089/ars.2019.7763 · Cited by 110
Are oxidative stress and mitochondrial dysfunction the key players in the neurodegenerative diseases?
Carlo, M. D., Giacomazza, D., Picone, P., Nuzzo, D., & Biagio, P. L. S. (2012) · Free Radical Research · doi:10.3109/10715762.2012.714466 · Cited by 106
Quantitative Interaction Proteomics of Neurodegenerative Disease Proteins
Hosp, F., Voßfeldt, H., Heinig, M., Vasiljević, D., Arumughan, A., Wyler, E., Landthaler, M., Hübner, N., Wanker, E. E., Lannfelt, L., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.04.030 · Cited by 106
Long-term electromagnetic field treatment enhances brain mitochondrial function of both Alzheimer's transgenic mice and normal mice: a mechanism for electromagnetic field-induced cognitive benefit?
Dragicevic, N., Bradshaw, P. C., Mamcarz, M. B., Lin, X., Wang, L., Cao, C., & Arendash, G. W. (2011) · Neuroscience · doi:10.1016/j.neuroscience.2011.04.012 · Cited by 104
Genetic variation at a single locus and age of onset for Alzheimer's disease
Lutz, M. W., Crenshaw, D. G., Saunders, A. M., & Roses, A. D. (2010) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2010.01.011 · Cited by 101
Identification of Alzheimer's disease–associated long noncoding RNAs
Zhou, X., & Xu, J. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.07.015 · Cited by 102
Insights into amyloid-β-induced mitochondrial dysfunction in Alzheimer disease
Wang, X., Su, B., Perry, G. L., Smith, M. A., & Zhu, X. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.09.007 · Cited by 102
Mitochondria in Alzheimer's disease and their potential role in Alzheimer's proteostasis
Weidling, I. W., & Swerdlow, R. H. (2020) · Experimental Neurology · doi:10.1016/j.expneurol.2020.113321 · Cited by 104
The neuroimmune nexus: unraveling the role of the mtDNA-cGAS-STING signal pathway in Alzheimer’s disease
Quan, S., Fu, X., Cai, H., Ren, Z., Xu, Y., & Jia, L. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00815-2 · Cited by 110
Mitochondrial cholesterol in health and disease.
García‐Ruiz, C., Marí, M., Colell, A., Morales, A., Caballero, F. G., Montero, J., Terrones, O., Basáñez, G., & Fernández-Checa, J. C. (2009) · PubMed · doi:10.14670/hh-24.117 · Cited by 101
US-China Education Review B
Santos, L. I. R., Alcoforado, L., & Cordeiro, A. M. R. (2024) · 美中教育评论：B · doi:10.17265/2161-6248 · Cited by 100
Mitochondria, Cybrids, Aging, and Alzheimer's Disease
Swerdlow, R. H., Koppel, S., Weidling, I., Hayley, C., Ji, Y., & Wilkins, H. M. (2017) · Progress in Molecular Biology and Translational Science · doi:10.1016/bs.pmbts.2016.12.017 · Cited by 106
Association between mitochondrial DNA variations and Alzheimer's disease in the ADNI cohort
Lakatos, A., Derbeneva, O. A., Younes, D., Keator, D. B., Bakken, T. E., Lvova, M., Brandon, M. C., Guffanti, G., Reglődi, D., Saykin, A. J., et al. (2010) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2010.04.031 · Cited by 97
Mechanisms of amyloid plaque pathogenesis
Fiala, J. C. (2007) · Acta Neuropathologica · doi:10.1007/s00401-007-0284-8 · Cited by 99
How the Mitoprotein-Induced Stress Response Safeguards the Cytosol: A Unified View
Boos, F., Labbadia, J. P., & Herrmann, J. M. (2020) · Trends in Cell Biology · doi:10.1016/j.tcb.2019.12.003 · Cited by 91
Interplay Between Mitochondrial Oxidative Disorders and Proteostasis in Alzheimer’s Disease
Llanos-González, E., Henares-Chavarino, Á. A., Pedrero-Prieto, C. M., García‐Carpintero, S., Frontiñán-Rubio, J., Sancho-Bielsa, F. J., Alcain, F. J., Peinado, J. R., Rabanal‐Ruiz, Y., & Durán‐Prado, M. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.01444 · Cited by 99
Sensing, signaling and surviving mitochondrial stress
Eckl, E.-M., Ziegemann, O., Krumwiede, L., Fessler, E., & Jae, L. T. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03887-7 · Cited by 93

Authors: Devi, L., Prabhu, B. M., Galati, D. F., Avadhani, N. G., & Anandatheerthavarada, H. K.
Affiliations: University of Pennsylvania (US)
ORCID: Galati, Domenico F.
Avadhani, Narayan G.
Venue: The Journal of Neuroscience
Publisher: Society for Neuroscience
Published: 2006-08-30
Volume: 26
Issue: 35
Pages: 9057-9068
ISSN: 0270-6474 (ISSN-L)
1529-2401
DOI: 10.1523/jneurosci.1469-06.2006
PMC: PMC6675337
OpenAlex: W2076241970
Cited by: 792
References: 62
Citations by year: 2026: 21 · 2025: 21 · 2024: 36 · 2023: 47 · 2022: 53 · 2021: 60 · 2020: 50 · 2019: 37 · 2018: 44 · 2017: 39 · 2016: 36 · 2015: 35 · 2014: 34 · 2013: 40 · 2012: 50
FWCI: 19.78
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by-nc-sa
creativecommons.org/licenses/by-nc-sa/4.0/ (vor, 182 d)
Locations: Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
National Institute on Aging (R01AG021920, AG 021920)
National Institute of General Medical Sciences (GM-49683, R01GM049683)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Keywords: amyloid precursor protein, Alzheimer's disease, mitochondrial dysfunction, Tom40, Tim23, cytochrome c oxidase, hydrogen peroxide, neuronal cell types
MeSH terms: Alzheimer Disease, Apolipoproteins E, Biological Transport, Brain, Cadaver, Electron Transport Complex IV, Glycosylation, Humans, Hydrogen Peroxide, Mitochondria, Neurons, Tissue Distribution, Case-Control Studies, Amyloid beta-Protein Precursor, Mitochondrial Proteins, Mitochondrial Membrane Transport Proteins, Mitochondrial Membranes, Apolipoprotein E3, Apolipoprotein E4

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

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

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks