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 601–700 of 790

Pathological convergence of APP and SNCA deficiency in hippocampal degeneration of young rats
Wang, Y., Miao, Z., Xu, C., Cai, Y., Yang, Y., Hu, Y., Zhao, M., Shao, Y., Li, Z., Chen, J., et al. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-05846-5 · Cited by 12
The Importance of Being Connected
Lutz, M. W., Crenshaw, D. G., Saunders, A. M., & Roses, A. D. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-101765 · Cited by 11
Comparison of the glycopattern alterations of mitochondrial proteins in cerebral cortex between rat Alzheimer’s disease and the cerebral ischemia model
Yu, H., Yang, C., Chen, S., Huang, Y., Liu, C., Liu, J., & Yin, W. (2017) · Scientific Reports · doi:10.1038/srep39948 · Cited by 11
Promising molecular targets for pharmacological therapy of neurodegenerative pathologies
Неганова, М. Е., Aleksandrova, Y. R., Nebogatikov, V. O., Klochkov, S. G., & Ustyugov, A. A. (2020) · Acta Naturae · doi:10.32607/actanaturae.10925 · Cited by 11
Hydrogen Sulfide Selectively Inhibits γ-Secretase Activity and Decreases Mitochondrial Aβ Production in Neurons from APP/PS1 Transgenic Mice
Zhao, F., Qiao, P., Yan, N., Gao, D., Liu, M., & Yan, Y. P. (2015) · Neurochemical Research · doi:10.1007/s11064-015-1807-7 · Cited by 11
Deciphering ApoE Genotype-Driven Proteomic and Lipidomic Alterations in Alzheimer’s Disease Across Distinct Brain Regions
Odenkirk, M. T., Zheng, X., Kyle, J. E., Stratton, K. G., Nicora, C., Bloodsworth, K., McLean, C., Masters, C. L., Monroe, M. E., Doecke, J. D., et al. (2024) · Journal of Proteome Research · doi:10.1021/acs.jproteome.3c00604 · Cited by 10
A Paradigm Shift for Evaluating Pharmacotherapy for Alzheimer's Disease: The 10-Patient Screening Protocol
Weinstein, J. D., Gonzalez, E. R., Egleton, R. D., & Hunt, D. A. (2013) · The Consultant Pharmacist · doi:10.4140/tcp.n.2013.443 · Cited by 9
Influence of metformin on mitochondrial subproteome in the brain of apoE knockout mice
Suski, M., Olszanecki, R., Chmura, Ł., Stachowicz, A., Madej, J., Okoń, K., Adamek, D., & Korbut, R. (2015) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2015.12.036 · Cited by 10
Decoding mitochondrial quality control mechanisms: Identifying treatment targets for enhanced cellular health
Wankhede, N. L., Kopalli, S. R., Dhokne, M. D., Badnag, D. J., Chandurkar, P. A., Mangrulkar, S. V., Shende, P. V., Taksande, B. G., Upaganlawar, A. B., Umekar, M. J., et al. (2024) · Mitochondrion · doi:10.1016/j.mito.2024.101926 · Cited by 10
FLZ inhibited γ-secretase selectively and decreased Aβ mitochondrial production in APP-SH-SY5Y cells
Ye, X., Tai, W., Bao, X., Chen, X., & Zhang, D. (2013) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-013-0918-4 · Cited by 10
Tongluo Xingnao Effervescent Tablet preserves mitochondrial energy metabolism and attenuates cognition deficits in APPswe/PS1De9 mice
Dai, Y., Ma, T., Xiangyi, R., Wei, J., Fu, W., Ma, Y., Xu, S., & Zhang, Z. (2016) · Neuroscience Letters · doi:10.1016/j.neulet.2016.07.044 · Cited by 10
Genetic Editing and Pharmacogenetics in Current And Future Therapy Of Neurocognitive Disorders
Prendecki, M., Kowalska, M., Totoń, E., & Kozubski, W. P. (2020) · Current Alzheimer Research · doi:10.2174/1567205017666200422152440 · Cited by 10
Dimebon as a Potential Therapy for Alzheimer's Disease
Doody, R. S. (2009) · CNS Spectrums · doi:10.1017/s1092852900024913 · Cited by 10
Therapeutic Approaches to Delay the Onset of Alzheimer's Disease
Kumar, R., & Atamna, H. (2011) · Journal of Aging Research · doi:10.4061/2011/820903 · Cited by 10
Insights from Drosophila on Aβ- and tau-induced mitochondrial dysfunction: mechanisms and tools
Varte, V., Munkelwitz, J. W., & Rincón-Limas, D. E. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1184080 · Cited by 9
Targeting mitochondrial dysfunction in Alzheimer's disease: New findings and perspectives
Hroudová, J., & Fišar, Z. (2025) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2025.111491 · Cited by 9
Unfolding is the driving force for mitochondrial import and degradation of the Parkinson's disease-related protein DJ-1
Queliconi, B. B., Kojima, W., Kimura, M., Imai, K., Udagawa, C., Motono, C., Hirokawa, T., Tashiro, S., Caaveiro, J. M. M., Tsumoto, K., et al. (2021) · Journal of Cell Science · doi:10.1242/jcs.258653 · Cited by 10
Early Chronic Stress Induced Changes within the Locus Coeruleus in Sporadic Alzheimer’s Disease
Minné, D., Marnewick, J. L., & Engel-Hills, P. C. (2023) · Current Alzheimer Research · doi:10.2174/1567205020666230811092956 · Cited by 10
Revisiting the Mitochondrial Function and Communication in Neurodegenerative Diseases
Wankhede, N. L., Kale, M. B., Umare, M. D., Lokhande, S., Upaganlawar, A. B., Wal, P., Taksande, B. G., Umekar, M. J., Khandige, P. S., Singh, B., et al. (2024) · Current Pharmaceutical Design · doi:10.2174/0113816128286655240304070740 · Cited by 9
TOMM40 gene polymorphisms association with lipid profile
Ринатович, С. Р., Goncharova, I. A., Makeeva, O. A., Golubenko, M. V., Кулиш, Е. В., Кашталап, В. В., Барбараш, О. Л., & Puzyrev, V. P. (2014) · Russian Journal of Genetics · doi:10.1134/s1022795413120090 · Cited by 9
Molecular Determinants of Alzheimer’s Disease Aβ Peptide Neurotoxicity
Cappai, R., & Barnham, K. J. (2007) · Future Neurology · doi:10.2217/14796708.2.4.397 · Cited by 9
RACK1 and IRE1 participate in the translational quality control of amyloid precursor protein in Drosophila models of Alzheimer’s disease
Li, Y., Liu, D., Zhang, X., Rimal, S., Lu, B., & Li, S. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.105719 · Cited by 9
Beyond Conventional Therapies: Molecular Dynamics of Alzheimer's Treatment through CLOCK/BMAL1 Interactions
Haskologlu, I. C., Erdağ, E., Şehirli, A. Ö., Uludağ, M. O., & Abacıoğlu, N. (2023) · Current Alzheimer Research · doi:10.2174/0115672050301014240315065235 · Cited by 8
Multimodal investigation of neuropathology and neurometabolites in mild cognitive impairment and late-life depression with 11C-PiB beta-amyloid PET and 7T magnetic resonance spectroscopy
Davies‐Jenkins, C. W., Workman, C. I., Hupfeld, K. E., Zöllner, H. J., Leoutsakos, J., Kraut, M. A., Barker, P. B., Smith, G. S., & Oeltzschner, G. (2024) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2024.06.003 · Cited by 8
Aging Promotes Amyloid-β Peptide Induced Mitochondrial Dysfunctions in Rat Brain: A Molecular Link Between Aging and Alzheimer's Disease
Sinha, M. S., Behera, P., Bhowmick, P., Banerjee, K., Basu, S., & Chakrabarti, S. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-110686 · Cited by 8
The APP swe/ PS 1A246E mutations in an astrocytic cell line leads to increased vulnerability to oxygen and glucose deprivation, Ca2+ dysregulation, and mitochondrial abnormalities
Martin‐de‐Saavedra, M. D., Navarro, E., Moreno‐Ortega, A. J., Cunha, M. P., Buendía, I., Hernansanz‐Agustín, P., Leon, R. M., Cano‐Abad, M. F., Martínez-Ruiz, A., Martínez‐Murillo, R., et al. (2018) · Journal of Neurochemistry · doi:10.1111/jnc.14293 · Cited by 8
Metal Binding by GMP-1 and Its Pyrimido [1, 2]benzimidazole Analogs Confirms Protection Against Amyloid-β Associated Neurotoxicity
Kumar, R., Pavlov, P. F., & Winblad, B. G. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190695 · Cited by 8
The Molecular and Functional Interaction Between Membrane-Bound Organelles and Membrane-Less Condensates
Zhou, C. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.896305 · Cited by 8
Quantitative Proteomic Analysis of the Orbital Frontal Cortex in Rats Following Extended Exposure to Caffeine Reveals Extensive Changes to Protein Expression: Implications for Neurological Disease
Franklin, J. L., Mirzaei, M., Wearne, T. A., Homewood, J., Goodchild, A. K., Haynes, P. A., & Cornish, J. L. (2016) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5b01043 · Cited by 8
Evidence for early identification of Alzheimer's diseasePreprint
Alexiou, A. T., & Vlamos, P. (2012) · arXiv (Cornell University) · doi:10.48550/arxiv.1209.4223 · Cited by 9
Unclogging of the TOM complex under import stress
Jackson, J., & Becker, T. (2025) · Biological Chemistry · doi:10.1515/hsz-2025-0110 · Cited by 7
Protein quality control systems in neurodegeneration – culprits, mitigators, and solutions?
Ciechanover, A. J., & Livneh, I. (2025) · Frontiers in Neurology · doi:10.3389/fneur.2025.1604076 · Cited by 8
Readdressing the Localization of Apolipoprotein E (APOE) in Mitochondria-Associated Endoplasmic Reticulum (ER) Membranes (MAMs): An Investigation of the Hepatic Protein–Protein Interactions of APOE with the Mitochondrial Proteins Lon Protease (LONP1), Mitochondrial Import Receptor Subunit TOM40 (TOMM40) and Voltage-Dependent Anion-Selective Channel 1 (VDAC1)
Rueter, J., Rimbach, G. H., Bilke, S., Tholey, A., & Huebbe, P. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms251910597 · Cited by 7
Investigating the Impact of Sorghum on Tau Protein Phosphorylation and Mitochondrial Dysfunction Modulation in Alzheimer’s Disease: An In Vitro Study
Rezaee, N., Hone, E., Sohrabi, H. R., Adisa, A. R., Johnson, S. K., Gunzburg, S. T., Martins, R. N., & Fernando, W. M. A. D. B. (2025) · Nutrients · doi:10.3390/nu17030516 · Cited by 7
Trends of mitochondrial changes in AD: a bibliometric study
Song, R., Guo, Y., Fu, Y., Ren, H., Wang, H., Yan, H., & Ge, Y. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1136400 · Cited by 7
Conserved quality control mechanisms of mitochondrial protein import
Borgert, L., Becker, T., & den Brave, F. (2024) · Journal of Inherited Metabolic Disease · doi:10.1002/jimd.12756 · Cited by 9
The Effect of TOMM40 Poly-T Repeat Lengths on Age of Onset and Cerebrospinal Fluid Biomarkers in Finnish Alzheimer's Disease Patients
Helisalmi, S., Hall, A., Meriläinen, E.-H., Väisänen, V., Koivisto, A. M., Herukka, S., Laitinen, M. H., Soininen, H. S., & Hiltunen, M. O. (2014) · Neurodegenerative Diseases · doi:10.1159/000367994 · Cited by 7
A promising structural magnetic resonance imaging assessment in patients with preclinical cognitive decline and diabetes mellitus
Dong, Y., Wang, Q., Yao, H., Xiao, Y., Wei, J., Xie, P., Hu, J., Chen, W., Tang, Y., Zhou, H., et al. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.28359 · Cited by 6
Mitochondria in Neurodegeneration
Swerdlow, R. H. (2011) · Advances in neurobiology · doi:10.1007/978-1-4614-1788-0_30 · Cited by 7
Análisis de desempeños cognitivos y polimorfismos en SORL, PVRL2, CR1, TOMM40, APOE, PICALM, GWAS_14q, CLU y BIN1 en pacientes con trastorno neurocognitivo leve y en sujetos cognitivamente sanos
Sanabria, F. C., Bonilla-Vargas, K. J., Estrada, K., Páez, O. M., Vega, E., Guerrero, E., Ortega-Rojas, J., Mahecha, M. F., Romero, A., Montañés, P., et al. (2018) · Neurología · doi:10.1016/j.nrl.2018.07.002 · Cited by 7
Molecular genetics of early-onset Alzheimer's disease and frontotemporal lobar degeneration
Krüger, J. (2010) · Cited by 7
Lipid Peroxidation and Mitochondrial Dysfunction in Alzheimer's and Parkinson's Diseases: Role of Natural Products as Cytoprotective Agents
Fernández‐Moriano, C., González‐Burgos, E., & Gómez-Serranillos, M. P. (2017) · Wiley eBooks · doi:10.1002/9783527803781.ch6 · Cited by 7
Organelle perturbation in Alzheimer’s disease: do intracellular amyloid-ß and the fragmented Golgi mediate early intracellular neurotoxicity?
Fourrière, L., & Gleeson, P. A. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2025.1550211 · Cited by 6
Structures and functions of the MICOS: Pathogenesis and therapeutic implications in Alzheimer's disease
Wang, Z., Zhang, K., Huang, M., Shang, D., He, X., Wu, Z., Xu, Y., & Zhang, X. (2025) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2025.04.019 · Cited by 6
Impact prediction of translocation of the mitochondrial outer membrane 70 as biomarker in Alzheimer's disease
Cao, X., Chen, Y., Sang, X., Xu, S., Xie, Z., Zhu, Z., Wang, P., Bi, J., & Xu, L. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.1013943 · Cited by 6
Genotypic Effects of the TOMM40'523 Variant and APOE on Longitudinal Cognitive Change over 4 Years: The TOMMORROW Study
Zou, H., Luo, S., Liu, H., Lutz, M. W., Bennett, D. A., Plassman, B. L., & Welsh-Bohmer, K. A. (2023) · The Journal of Prevention of Alzheimer s Disease · doi:10.14283/jpad.2023.115 · Cited by 6
Effects and mechanisms of APP and its cleavage product Aβ in the comorbidity of sarcopenia and Alzheimer’s disease
Wu, J., Tang, J., Huang, D., Wang, Y., Zhou, E., Ru, Q., Xu, G., Chen, L., & Wu, Y. (2024) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2024.1482947 · Cited by 7
Quality control of un-imported mitochondrial proteins at a glance
Balzarini, M., Kim, J., & Weidberg, H. (2025) · Journal of Cell Science · doi:10.1242/jcs.263757 · Cited by 7
Mitochondrial Dysfunction in Neurodegenerative Disease: Protein Aggregation, Autophagy, and Oxidative Stress
Zhang, J., & Darley-Usmar, V. M. (2011) · Springer eBooks · doi:10.1007/978-0-85729-701-3_6 · Cited by 7
Mitochondrial Dysregulation in Skeletal Muscle from Patients Diagnosed with Alzheimer’s Disease and Sporadic Inclusion Body Myositis
Shabrokh, E., Kavanaugh, J., McMillan, R. P., Pittman, J., Hulver, M. W., & Frisard, M. I. (2014) · Open Journal of Molecular and Integrative Physiology · doi:10.4236/ojmip.2014.42002 · Cited by 6
Evolution of Alzheimer’s disease pathogenesis conception
Stefanova, N. A., & Kolosova, N. G. (2016) · Moscow University Biological Sciences Bulletin · doi:10.3103/s0096392516010119 · Cited by 6
Mitochondrial Precursor Overaccumulation Stress
Coyne, L. P., & Chen, X. J. (2026) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-051424-061016 · Cited by 7
Sesamol: A Phenolic Compound of Health Benefits and Therapeutic Promise in Neurodegenerative Diseases
Javed, H., Meeran, M. F. N., Jha, N. K., Ashraf, G. M., & Ojha, S. K. (2023) · Current Topics in Medicinal Chemistry · doi:10.2174/0115680266273944231213070916 · Cited by 6
MitoCPR: a novel protective mechanism in response to mitochondrial protein import stress
Tang, M., Luo, X., Huang, Z., & Chen, L. (2018) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmy098 · Cited by 5
Chemical Stimulation of Rodent and Human Cortical Synaptosomes: Implications in Neurodegeneration
Ahmad, F., Yu, J. H., Lladó, A., & Liu, P. (2021) · Cells · doi:10.3390/cells10051174 · Cited by 6
Uncovering the Localization and Function of a Novel Read-Through Transcript ‘TOMM40-APOE’
Chang, S., Torii, S., Inamo, J., Ishikawa, K., Kochi, Y., & Shimizu, S. (2023) · Cells · doi:10.3390/cells13010069 · Cited by 5
Molecular Genetics and Metabolism
Fu, R., Yanjanin, N. M., Bianconi, S. E., Pavan, W. J., & Porter, F. D. (2010) · Cited by 5
The transferred translocases: An old wine in a new bottle
Balaji, S. (2021) · Biotechnology and Applied Biochemistry · doi:10.1002/bab.2230 · Cited by 5
Adult-Onset Deficiency of Mitochondrial Complex III in a Mouse Model of Alzheimer’s Disease Decreases Amyloid Beta Plaque Formation
Pinto, M., Díaz, F., Nissanka, N., Guastucci, C. S., Illiano, P., Brambilla, R., & Moraes, C. T. (2022) · Molecular Neurobiology · doi:10.1007/s12035-022-02992-3 · Cited by 5
Role of Mitochondria in Neurodegenerative Diseases: The Dark Side of the “Energy Factory”
Correia, S. C., & Moreira, P. I. (2018) · Springer eBooks · doi:10.1007/978-3-319-73344-9_11 · Cited by 5
Effects of Novel Tacrine Derivatives on Mitochondrial Energy Metabolism and Monoamine Oxidase Activity—In Vitro Study
Hroudová, J., Nováková, T., Korábečný, J., Maliňák, D., Górecki, L., & Fišar, Z. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-02172-1 · Cited by 5
Targeting cellular batteries for the therapy of neurological diseases
Arora, A., Behl, T., Sehgal, A., Singh, S., Sharma, N., Mathew, B., & BUNGAU, S. G. (2021) · Environmental Science and Pollution Research · doi:10.1007/s11356-021-14665-0 · Cited by 5
Protein Degradation: BAGging Up the Trash
Ast, T., & Schuldiner, M. (2011) · Current Biology · doi:10.1016/j.cub.2011.08.018 · Cited by 5
Genetics of Alzheimer's Disease
Bekris, L. M., Yu, C., Bird, T. D., & Tsuang, D. W. (2010) · Wiley eBooks · doi:10.1002/9780470669600.ch43 · Cited by 6
A synapse perspective on the function of the amyloid precursor protein
Kruse, P., Eichler, A., Klukas, L., & Lenz, M. (2025) · Science Progress · doi:10.1177/00368504251360728 · Cited by 5
Passive Immunotherapy in Alzheimer’s Disease
Dolan, P. J., & Zago, W. M. (2018) · InTech eBooks · doi:10.5772/intechopen.76299 · Cited by 4
Insights into the promising prospect of medicinal chemistry studies against neurodegenerative disorders
Rahman, M. M., Islam, M. R., Tumpa, M. A. A., Shohag, S., shuvo, S. K., Ferdous, J., Kajol, S. A., Aljohani, A. S. M., Abdulmonem, W. A., Rauf, A., et al. (2023) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2023.110375 · Cited by 4
Isolated Mitochondrial Preparations andIn organelloAssays: A Powerful and RelevantEx vivoTool for Assessment of Brain (Patho)physiology
Ahmad, F., Ramamoorthy, S., Areeshi, M. Y., Ashraf, G. M., & Haque, S. (2023) · Current Neuropharmacology · doi:10.2174/1570159x21666230303123555 · Cited by 4
Does an Alzheimer's disease susceptibility gene influence the cognitive effects of cancer therapy?
Caselli, R. J. (2013) · Pediatric Blood & Cancer · doi:10.1002/pbc.24768 · Cited by 4
Mitochondrial Membrane Potential and Dynamics
Oliveira, J. M. A. (2011) · Springer eBooks · doi:10.1007/978-0-85729-701-3_8 · Cited by 4
Metal Metabolic Homeostasis Disruption and Early Initiation of Mechanism for Alzheimer′s Disease*
Zhao, B., & Wan, L. (2012) · PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS · doi:10.3724/sp.j.1206.2012.00297 · Cited by 4
Genetic Risk Factors for Dementia
Hollingworth, P., & Williams, J. H. (2011) · Wiley eBooks · doi:10.1002/9781444344110.ch6 · Cited by 4
Mitochondrial accumulation and lysosomal dysfunction result in mitochondrial plaques in Alzheimer’s disease
Dan, X., Croteau, D. L., Liu, W., Chu, X., McDevitt, R. A., Robbins, P. D., & Bohr, V. A. (2026) · Nature Neuroscience · doi:10.1038/s41593-026-02390-1 · Cited by 3
Retracted: Mitochondria, the missing link between body and soul: Proteomic prospective evidence
Warda, M., & Han, J. (2008) · PROTEOMICS · doi:10.1002/pmic.200700695 · Cited by 3
Retracted
Recent Progress of Mitochondrial Dysfunction Induced by β-Amyloid Protein*
Xu, S., & Gui-Lan, L. I. U. (2010) · PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS · doi:10.3724/sp.j.1206.2010.00073 · Cited by 3
Clogging the mitochondrial protein-entry gate promotes obesity
Song, J., & Becker, T. (2019) · Nature Metabolism · doi:10.1038/s42255-019-0155-3 · Cited by 3
Molecular linkages among Aβ, tau, impaired mitophagy, and mitochondrial dysfunction in Alzheimer’s disease
Schmauck‐Medina, T., Patrick-Brown, T. D. J. H., Zhang, S., Gilbert, A., & Fang, E. F. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-89906-2.00007-1 · Cited by 3
Immature Persimmon Suppresses Amyloid Beta (Aβ) Mediated Cognitive Dysfunction via Tau Pathology in ICR Mice
Yoo, S. K., Kim, J. M., Lee, U., Kang, J.-Y., Park, S.-K., Han, H.-J., Park, H.-W., Kim, H., Kim, C. W., Kim, M.-J., et al. (2021) · Current Issues in Molecular Biology · doi:10.3390/cimb43010033 · Cited by 3
The Impact of HAART on Advanced Brain Aging: Implications for Mitochondrial Dysfunction and APP Processing
Campos, J. (2013) · Journal of Antivirals & Antiretrovirals · doi:10.4172/jaa.s10-003 · Cited by 3
Cerebral lactate metabolism and memory: Implications for Alzheimer's disease
Harris, R. A. (2017) · Scholarship@Western (Western University) · Cited by 3
Aβ 42 oligomers impair the bioenergetic activity in hippocampal synaptosomes derived from APP-KO mice
Beckert, B., Acker‐Palmer, A., & Volknandt, W. (2018) · Biological Chemistry · doi:10.1515/hsz-2017-0238 · Cited by 3
Warning SINEs: Alu elements, evolution of the human brain, and the spectrum of neurological diseasePreprint
Larsen, P. A., Hunnicutt, K. E., Larsen, R. J., Yoder, A. D., & Saunders, A. M. (2017) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/230367 · Cited by 2
Intercellular Mitochondrial Transfer as a Rescue Mechanism in Response to Protein Import FailurePreprint
Needs, H. I., Pereira, G. C., Glover, E., Witt, A., Hübner, W., Dodding, M. P., Henley, J. M., & Collinson, I. R. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.11.30.518494 · Cited by 3
OMA1 protease eliminates arrested protein import intermediates upon depolarization of the inner mitochondrial membranePreprint
Krakowczyk, M., Lenkiewicz, A. M., Sitarz, T., Mussulini, B. H. M., Linke, V., Malińska, D., Szczepankiewicz, A. A., Wydrych, A., Nieznańska, H., Serwa, R. A., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.06.08.543713 · Cited by 3
Mitochondrial Function and Neurodegenerative Diseases
Wilkins, H. M., Weidling, I., Koppel, S., Wang, X., von Schulze, A., & Swerdlow, R. H. (2018) · The Molecular and Cellular Basis of Neurodegenerative Diseases · doi:10.1016/b978-0-12-811304-2.00013-4 · Cited by 2
Ayurveda: Ayurvedic herbs against neurological disorders: are they golden nuggets?
Muralidhara, M. (2023) · Elsevier eBooks · doi:10.1016/b978-0-443-19084-1.00022-3 · Cited by 2
Integrative gene co-expression network analysis reveals protein-coding and LncRNA genes associated with Alzheimer’s disease pathology
Zebardast, F., Riethmueller, M. P. S., & Nowick, K. (2025) · Scientific Reports · doi:10.1038/s41598-025-30392-9 · Cited by 2
Alzheimer’s Disease Pathogenic Mechanisms: Linking Redox Homeostasis and Mitochondria-Associated Metabolic Pathways Through Nuclear Factor Erythroid 2-Related Factor 2 (Nrf2)
Rostagno, A. A., & Ghiso, J. A. (2025) · Antioxidants · doi:10.3390/antiox14070812 · Cited by 3
Lobetyolin, an anti-AD factor from the diet campanulaceae source, metabolism regulation and target exploration
Huang, W. C., Liu, Y., Jiang, H., Guo, D., Song, Y., Wang, J., Li, L., & Zhang, Q. (2025) · Natural Products and Bioprospecting · doi:10.1007/s13659-025-00549-0 · Cited by 2
Free Cholesterol — A Double-Edge Sword in Alzheimer Disease
Fernández-Checa, J. C. (2015) · InTech eBooks · doi:10.5772/59935 · Cited by 3
The Amyloid _-Protein and Alzheimer's Disease
Teplow, D. B., Yang, M., Roychaudhuri, R., Pang, E. S., Huynh, T. V., Chen, M., & Beroukhim, S. (2012) · Frontiers in neuroscience · doi:10.1201/b11986-2 · Cited by 2
Nitric Oxide Biochemistry: Pathophysiology of Nitric Oxide-Mediated Protein Modifications
Rossi‐George, A., & Gow, A. J. (2009) · Contemporary clinical neuroscience · doi:10.1007/978-1-60327-342-8_2 · Cited by 2
Mitochondria in Alzheimer disease : regulatory mechanisms and cell death
Hedskog, L. (2012) · Figshare · Cited by 2
Mitochondrial Involvement in Neurodegenerative Dementia
Bonanni, L., Frazzini, V., Thomas, A., & ONOFRJ, M. C. (2015) · Wiley eBooks · doi:10.1002/9781119017127.ch13 · Cited by 2
Amyloid, Protein Misfolding Defects, and Inclusions
Cheville, N. F. (2009) · Wiley eBooks · doi:10.1002/9780813810379.ch26 · Cited by 2
The NanoLuc Assay System for Accurate Real-Time Monitoring of Mitochondrial Protein Import within Intact Mammalian CellsPreprint
Needs, H. I., Pereira, G. C., Henley, J. M., & Collinson, I. R. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.09.23.509159 · Cited by 2
Perturbation of the mitochondrial import machinery by aggregation prone Tau affects organelle morphology and reduces neuronal complexityPreprint
Needs, H. I., Wilkinson, K. A., Henley, J. M., & Collinson, I. R. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.11.30.518502 · Cited by 2
Investigation of Cytotoxicity and Ion Flux Induced by Various Aggregation States of Amyloid-Beta Peptides.
Prangkio, P. (2011) · Deep Blue (University of Michigan) · Cited by 2
Amyloid-β protein precursor modulates mitophagy and mitochondrial function through its cellular localization
Strope, T. A., Troutwine, B., Hauger, B. M., Smith, K. P., Swerdlow, R. H., & Wilkins, H. (2025) · Journal of Alzheimer s Disease · doi:10.1177/13872877251360243 · Cited by 2
PTEN-L dephosphorylates Parkin and Ub Ser65 to aggravate mitophagy dysfunction in prion disease cell models
Li, X., Li, J., Gou, F., Dai, Y., Zhao, M., Wang, D., Sun, Z., Wen, P., Wang, J., Fan, Q., et al. (2025) · Life Sciences · doi:10.1016/j.lfs.2025.123860 · Cited by 1

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