Cited by 571Alzheimer's disease research and treatmentsMitochondrial Function and PathologyAutophagy in Disease and Therapy

The DOI matches its Crossref record; 47 of the 47 references it cites were found in a registry or an index.

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

Open access

Anandatheerthavarada, Hindupur K., Biswas, Gopa, Robin, Marie-Anne, Avadhani, Narayan G.·2003·The Journal of Cell Biology

DOI 10.1083/jcb.200207030PMC PMC2172865

Open this paper in CoChat — free account

Abstract

Alzheimer's amyloid precursor protein 695 (APP) is a plasma membrane protein, which is known to be the source of the toxic amyloid beta (Abeta) peptide associated with the pathogenesis of Alzheimer's disease (AD). Here we demonstrate that by virtue of its chimeric NH2-terminal signal, APP is also targeted to mitochondria of cortical neuronal cells and select regions of the brain of a transgenic mouse model for AD. The positively charged residues at 40, 44, and 51 of APP are critical components of the mitochondrial-targeting signal. Chemical cross-linking together with immunoelectron microscopy show that the mitochondrial APP exists in NH2-terminal inside transmembrane orientation and in contact with mitochondrial translocase proteins. Mutational studies show that the acidic domain, which spans sequence 220-290 of APP, causes the transmembrane arrest with the COOH-terminal 73-kD portion of the protein facing the cytoplasmic side. Accumulation of full-length APP in the mitochondrial compartment in a transmembrane-arrested form, but not lacking the acidic domain, caused mitochondrial dysfunction and impaired energy metabolism. These results show, for the first time, that APP is targeted to neuronal mitochondria under some physiological and pathological conditions.

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 · 10.1083/jcb.200207030

Cites

47 of 47 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.

Translating cell biology into therapeutic advances in Alzheimer's disease
Selkoe, D. J. (1999) · Nature · doi:10.1038/399a023 · Cited by 1,166
Mitochondrial Dysfunction in Neurodegenerative Diseases
Johri, A., & Beal, M. F. (2012) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.112.192138 · Cited by 806
Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria
Eilers, M., & Schatz, G. (1986) · Nature · doi:10.1038/322228a0 · Cited by 725
Mitochondrial dysfunction in neurodegenerative diseases
Beal, M. F. (1998) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(98)00114-5 · Cited by 611
Cytochrome oxidase deficiency in Alzheimer’s disease
Parker, W. D., Filley, C. M., & Parks, J. K. (1990) · Neurology · doi:10.1212/wnl.40.8.1302 · Cited by 598 · cited 1×
“…$8.00 The Journal of Cell Biology, Volume 161, Number 1, April 14, 2003 41–54 http://www.jcb.org/cgi/doi/10.1083/jcb.200207030 JCB Article 41 Mitochondrial targeting and a novel transmembrane arrest of Alzheimer’s amyloid precursor protein impairs mitochondrial function in neuronal cells”
BackgroundInfluential
MUTANT GENES IN FAMILIAL ALZHEIMER'S DISEASE AND TRANSGENIC MODELS
Price, D. L., & Sisodia, S. S. (1998) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.21.1.479 · Cited by 581
γ-Secretase, notch, Aβ and alzheimer's disease: Where do the presenilins fit in?
Sisodia, S. S., & St George-Hyslop, P. H. (2002) · Nature Reviews Neuroscience · doi:10.1038/nrn785 · Cited by 512
Regulation of APP cleavage by α‐, β‐ and γ‐secretases
Nunan, J., & Small, D. H. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)02076-7 · Cited by 509
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
Untitled work
Selkoe (1999) · doi:10.1038/19866 · Cited by 468

Flagged first, then by citations

Show all 47 references

Research works printed but not linked: 1

1996, Int. J. Dev. Neurosci., 14, 61

Sorted by citations

Items 201–300 of 570

The mitochondrial hypothesis: Dysfunction, bioenergetic defects, and the metabolic link to Alzheimer's disease
Swerdlow, R. H. (2020) · International review of neurobiology · doi:10.1016/bs.irn.2020.01.008 · Cited by 88
Modes of Aβ toxicity in Alzheimer’s disease
Götz, J., Eckert, A., Matamales, M., Ittner, L. M., & Liu, X. (2011) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-011-0750-2 · Cited by 87
Functions of amyloid precursor protein in metabolic diseases
Guo, Y., Wang, Q., Chen, S., & Xu, C. (2020) · Metabolism · doi:10.1016/j.metabol.2020.154454 · Cited by 89
Mitochondrial accumulation of APP and Aβ: significance for Alzheimer disease pathogenesis
Pavlov, P. F., Petersen, C. H., Glaser, E. G., & Ankarcrona, M. (2009) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2009.00892.x · Cited by 84
Alzheimer's Disease and Diabetes: An Integrative View of the Role of Mitochondria, Oxidative Stress, and Insulin
Moreira, P. I. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-111127 · Cited by 83
Eclipsed distribution: A phenomenon of dual targeting of protein and its significance
Regev‐Rudzki, N., & Pines, O. (2007) · BioEssays · doi:10.1002/bies.20609 · Cited by 82
Signal sequence insufficiency contributes to neurodegeneration caused by transmembrane prion protein
Rane, N. S., Chakrabarti, O., Feigenbaum, L., & Hegde, R. S. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.200911115 · Cited by 79
Proteinopathies and OXPHOS dysfunction in neurodegenerative diseases
Kawamata, H., & Manfredi, G. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201709172 · Cited by 86
The Alzheimer’s Disease Mitochondrial Cascade Hypothesis: A Current Overview
Swerdlow, R. H. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-221286 · Cited by 88
Alzheimer's Disease and Amyloid: Culprit or Coincidence?
Skaper, S. D. (2012) · International review of neurobiology · doi:10.1016/b978-0-12-386986-9.00011-9 · Cited by 82
Differentiated Alzheimer's Disease Transmitochondrial Cybrid Cell Lines Exhibit Reduced Organelle Movement
Trimmer, P. A., & Borland, M. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.1101 · Cited by 81
Association of hypometabolism and amyloid levels in aging, normal subjects
Lowe, V. J., Weigand, S. D., Senjem, M. L., Vemuri, P., Jordan, L. G., Kantarci, K., Boeve, B. F., Jack, C. R., Knopman, D. S., & Petersen, R. C. (2014) · Neurology · doi:10.1212/wnl.0000000000000467 · Cited by 83
Neurotoxic β-amyloid oligomers cause mitochondrial dysfunction—the trigger for PANoptosis in neurons
Meng, X., Song, Q., Liu, Z., Liu, X., Wang, Y., & Liu, J. (2024) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2024.1400544 · Cited by 84
Mitochondrial biology in Alzheimer’s disease pathogenesis
Galindo, M. F., Ikuta, I., Zhu, X., Casadesús, G., & Jordán, J. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06814.x · Cited by 79
Chronic exposure to sub‐lethal beta‐amyloid (Aβ) inhibits the import of nuclear‐encoded proteins to mitochondria in differentiated PC12 cells*
Sirk, D. P., Zhu, Z., Wadia, J. S., Shulyakova, N., Phan, N., Fong, J. C., & Mills, L. R. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04907.x · Cited by 81
Journal of Parkinson’s disease & Alzheimer’s disease
Gottschalk, W. K., Lutz, M. W., He, Y. T., Saunders, A. M., Burns, D. K., Roses, A. D., & Chiba‐Falek, O. (2014) · Journal of Parkinson’s Disease and Alzheimer’s Disease · doi:10.13188/2376-922x.1000003 · Cited by 80
Synaptic Mitochondria: An Early Target of Amyloid-β and Tau in Alzheimer’s Disease
Torres, A. K., Jara, C., Park-Kang, H. S., Polanco, C. M., Tapia, D., Alarcón, F., de la Peña, A., Llanquinao, J., Vargas-Mardones, G., Álvarez‐Indo, J., et al. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-215139 · Cited by 80
Neuronal response in Alzheimer’s and Parkinson’s disease: the effect of toxic proteins on intracellular pathways
Majd, S., Power, J. H. T., & Grantham, H. J. M. (2015) · BMC Neuroscience · doi:10.1186/s12868-015-0211-1 · Cited by 79
Intracellular Dynamics of Synucleins
Surguchov, A. P. (2015) · International review of cytology · doi:10.1016/bs.ircmb.2015.07.007 · Cited by 77
Enhanced apoptosis, oxidative stress and mitochondrial dysfunction in lymphocytes as potential biomarkers for Alzheimer’s disease
Leuner, K., Pantel, J., Frey, C., Schindowski, K., Schulz, K. L., Wegat, T., Maurer, K., Eckert, A., & Müller, W. E. G. (2007) · Springer eBooks · doi:10.1007/978-3-211-73574-9_27 · Cited by 74
HIV-1 Tat protein directly induces mitochondrial membrane permeabilization and inactivates cytochrome c oxidase
Lecoeur, H., Borgne‐Sanchez, A., Chaloin, O., El‐Khoury, R., Brabant, M., Langonné, A., Porceddu, M., Brière, J.-J., Buron, N., Rebouillat, D., et al. (2012) · Cell Death and Disease · doi:10.1038/cddis.2012.21 · Cited by 74
Genetic variation in APOE cluster region and Alzheimer's disease risk
Cervantes, S., Samaranch, L., Vidal-Taboada, J. M., Lamet, I., Bullido, M. J., Frank-García, A., Coria, F., Lleó, A., Clarimón, J., Lorenzo, E., et al. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.05.023 · Cited by 62
Clinical effects of chemical exposures on mitochondrial function
Zolkipli‐Cunningham, Z., & Falk, M. J. (2017) · Toxicology · doi:10.1016/j.tox.2017.07.009 · Cited by 74
Epoxyeicosatrienoic acids pretreatment improves amyloid β-induced mitochondrial dysfunction in cultured rat hippocampal astrocytes
Sarkar, P., Žaja, I., Bienengraeber, M., Rarick, K. R., Terashvili, M., Canfield, S. G., Falck, J. R., & Harder, D. R. (2013) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00001.2013 · Cited by 72
Dystrophic neurites of senile plaques in Alzheimer’s disease are deficient in cytochrome c oxidase
Pérez-Gracia, E., Torrejón-Escribano, B., & Ferrer, I. (2008) · Acta Neuropathologica · doi:10.1007/s00401-008-0370-6 · Cited by 71
HtrA2 Regulates β-Amyloid Precursor Protein (APP) Metabolism through Endoplasmic Reticulum-associated Degradation
Huttunen, H. J., Guénette, S. Y., Peach, C., Greco, C., Xia, W., Kim, D. Y., Barren, C., Tanzi, R. E., & Kovacs, D. M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702951200 · Cited by 72
Understanding the genetics of APOE and TOMM40 and role of mitochondrial structure and function in clinical pharmacology of Alzheimer's disease
Roses, A., Sundseth, S., Saunders, A., Gottschalk, W., Burns, D., & Lutz, M. (2016) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2016.03.015 · Cited by 70
Clinical Features and Pathogenesis of Alzheimer’s Disease: Involvement of Mitochondria and Mitochondrial DNA
Mancuso, M., Orsucci, D., LoGerfo, A., Calsolaro, V., & Siciliano, G. (2010) · Advances in experimental medicine and biology · doi:10.1007/978-1-4419-6448-9_4 · Cited by 69
Mechanisms Linking Mitochondrial Dysfunction and Proteostasis Failure
Lu, B., & Guo, S. (2020) · Trends in Cell Biology · doi:10.1016/j.tcb.2020.01.008 · Cited by 69
Mitochondrial trafficking and morphology in neuronal injury
Rintoul, G. L., & Reynolds, I. J. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.09.005 · Cited by 70
Appoptosin is a Novel Pro-Apoptotic Protein and Mediates Cell Death in Neurodegeneration
Zhang, H., Zhang, Y.-W., Chen, Y., Huang, X., Zhou, F., Wang, W., Xian, B., Zhang, X., Masliah, E., Chen, Q., et al. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.3668-12.2012 · Cited by 68
Dysregulation of amyloid precursor protein impairs adipose tissue mitochondrial function and promotes obesity
An, Y., Crewe, C., Asterholm, I. W., Sun, K., Chen, S., Zhang, F., Shao, M., Funcke, J., Zhang, Z., Straub, L. G., et al. (2019) · Nature Metabolism · doi:10.1038/s42255-019-0149-1 · Cited by 64
Structural characterization of a polysaccharide from Lycium barbarum and its neuroprotective effect against β-amyloid peptide neurotoxicity
Wu, J., Chen, T., Wan, F., Wang, J., Li, X., Li, W., & Ma, L. (2021) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2021.02.016 · Cited by 68
Surface Plasmon Resonance and Nuclear Magnetic Resonance Studies of ABAD−Aβ Interaction
Yan, Y., Liu, Y., Sorci, M., Belfort, G., Lustbader, J. W., Yan, S. S., & Wang, C. (2007) · Biochemistry · doi:10.1021/bi061314n · Cited by 67
The consequences of mitochondrial amyloid β-peptide in Alzheimer's disease
Muirhead, K. E. A., Borger, E., Aitken, L., Conway, S. J., & Gunn‐Moore, F. J. (2010) · Biochemical Journal · doi:10.1042/bj20091941 · Cited by 68
Heterogeneity of nervous system mitochondria: Location, location, location!
Dubinsky, J. M. (2009) · Experimental Neurology · doi:10.1016/j.expneurol.2009.05.020 · Cited by 67
Mitochondrial dysfunction in Alzheimer's disease: Guiding the path to targeted therapies
Percy, K. C. M., Liu, Z., & Qi, X. (2025) · Neurotherapeutics · doi:10.1016/j.neurot.2025.e00525 · Cited by 70
Controlling Protein Compartmentalization to Overcome Disease
Davis, J. R., Kakar, M., & Lim, C. S. (2006) · Pharmaceutical Research · doi:10.1007/s11095-006-9133-z · Cited by 65
Mitochondrial Importance in Alzheimer’s, Huntington’s and Parkinson’s Diseases
Correia, S. C., Santos, R. X., Perry, G. L., Zhu, X., Moreira, P. I., & Smith, M. A. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-0653-2_16 · Cited by 65
Reassessment of Pioglitazone for Alzheimer’s Disease
Saunders, A. M., Burns, D. K., & Gottschalk, W. K. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.666958 · Cited by 71
Synaptic mitochondrial dysfunction and septin accumulation are linked to complement-mediated synapse loss in an Alzheimer’s disease animal model
Györffy, B. A., Tóth, V., Török, G., Gulyássy, P., Kovács, R. Á., Vadászi, H., Micsonai, A., Tóth, M. E., Sántha, M., Homolya, L., et al. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03468-0 · Cited by 65
Mitochondrial Microheteroplasmy and a Theory of Aging and Age-Related Disease
Smigrodzki, R. M., & Khan, S. M. (2005) · Rejuvenation Research · doi:10.1089/rej.2005.8.172 · Cited by 62
APOE mRNA and protein expression in postmortem brain are modulated by an extended haplotype structure
Bekris, L. M., Galloway, N. M., Montine, T. J., Schellenberg, G. D., & Yu, C. (2009) · American Journal of Medical Genetics Part B Neuropsychiatric Genetics · doi:10.1002/ajmg.b.30993 · Cited by 63
Nuclear Gene Expression Changes Due to Mitochondrial Dysfunction in ARPE-19 Cells: Implications for Age-Related Macular Degeneration
Miceli, M. V., & Jazwinski, S. M. (2005) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.04-1327 · Cited by 62
Overexpression of Amyloid-β Protein Precursor Induces Mitochondrial Oxidative Stress and Activates the Intrinsic Apoptotic Cascade
Bartley, M. G., Marquardt, K., Kirchhof, D., Wilkins, H., Patterson, D. W., & Linseman, D. A. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-111172 · Cited by 61
Amyloid-β-Induced Mitochondrial Dysfunction Impairs the Autophagic Lysosomal Pathway in a Tubulin Dependent Pathway
Silva, D. F., Esteves, A. R., Arduíno, D. M., Oliveira, C. R., & Cardoso, S. M. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-110423 · Cited by 61
Molecular Dysfunctions of Mitochondria-Associated Membranes (MAMs) in Alzheimer’s Disease
Eysert, F., Kinoshita, P. F., Mary, A., Vaillant-Beuchot, L., Checler, F., & Chami, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21249521 · Cited by 63
Blood–Brain Barrier and Neurovascular Unit In Vitro Models for Studying Mitochondria-Driven Molecular Mechanisms of Neurodegeneration
Salmina, A. B., Kharitonova, E. V., Gorina, Y. V., Тепляшина, Е. А., Malinovskaya, N. A., Хилажева, Е. Д., Mosiagina, A. I., Morgun, A. V., Shuvaev, А. N., Salmin, V. V., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094661 · Cited by 63
Rethinking Alzheimer's Disease Therapy: Are Mitochondria the Key?
Ankarcrona, M., Mangialasche, F., & Winblad, B. G. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100327 · Cited by 60
APP promotes osteoblast survival and bone formation by regulating mitochondrial function and preventing oxidative stress
Pan, J.-X., Tang, F., Xiong, F., Xiong, L., Zeng, P., Wang, B., Zhao, K., Guo, H., Shun, C., Xia, W.-F., et al. (2018) · Cell Death & Disease · doi:10.1038/s41419-018-1123-7 · Cited by 59
Amyloid-β precursor protein: Multiple fragments, numerous transport routes and mechanisms
Mureşan, V., & Muresan, Z. L. (2015) · Experimental Cell Research · doi:10.1016/j.yexcr.2014.12.014 · Cited by 61
Mitochondrial preconditioning: a potential neuroprotective strategy
Correia, S. C. (2010) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2010.00138 · Cited by 58
Superoxide Anion, Uncoupling Proteins and Alzheimer’s Disease
Wu, Z., Zhao, Y., & Zhao, B. (2010) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.09-104-2 · Cited by 60
Unraveling the complexity of neurodegeneration in brains of subjects with Down syndrome: Insights from proteomics
Marzia Perluigi, A., Domenico, F. D., & Butterfield, D. A. (2013) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.201300066 · Cited by 59
Mitochondria, Cognitive Impairment, and Alzheimer's Disease
Mancuso, M., Calsolaro, V., Orsucci, D., Carlesi, C., Choub, A., Piazza, S., & Siciliano, G. (2009) · International Journal of Alzheimer s Disease · doi:10.4061/2009/951548 · Cited by 58
Mortal engines: Mitochondrial bioenergetics and dysfunction in neurodegenerative diseases
Joshi, A. U., & Mochly‐Rosen, D. (2018) · Pharmacological Research · doi:10.1016/j.phrs.2018.08.010 · Cited by 57
Mitochondrial Cascade Hypothesis of Alzheimer's Disease: Myth or Reality?
Mancuso, M., Coppedè, F., Murri, L., & Siciliano, G. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1761 · Cited by 56
Mitochondria Are Related to Synaptic Pathology in Alzheimer′s Disease
Balogiannis, S. (2011) · International Journal of Alzheimer s Disease · doi:10.4061/2011/305395 · Cited by 58
Mitochondria and Alzheimer’s disease: amyloid-β peptide uptake and degradation by the presequence protease, hPreP
Alikhani, N., Ankarcrona, M., & Glaser, E. G. (2009) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-009-9244-4 · Cited by 55
HNE-modified proteins in Down syndrome: Involvement in development of Alzheimer disease neuropathology
Barone, E., Head, E., Butterfield, D. A., & Perluigi, M. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.10.508 · Cited by 53
Oxidative stress caused by ozone exposure induces β-amyloid 1–42 overproduction and mitochondrial accumulation by activating the amyloidogenic pathway
Hernández-Zimbrón, L. F., & Rivas-Arancibia, S. (2015) · Neuroscience · doi:10.1016/j.neuroscience.2015.07.011 · Cited by 54
Structural and Functional Alterations in Mitochondria-Associated Membranes (MAMs) and in Mitochondria Activate Stress Response Mechanisms in an In Vitro Model of Alzheimer’s Disease
Fernandes, T., Resende, R., Silva, D. F., Marques, A. P., Santos, A. E., Cardoso, S. M., Domingues, M. R., Moreira, P. I., & Pereira, C. (2021) · Biomedicines · doi:10.3390/biomedicines9080881 · Cited by 56
Possible association of mitochondrial transcription factor A (TFAM) genotype with sporadic Alzheimer disease
Günther, C., Hadeln, K. V., Müller-Thomsen, T., Alberici, A., Binetti, G., Hock, C., Nitsch, R. M., Stoppe, G., Reiss, J., Gal, A., et al. (2004) · Neuroscience Letters · doi:10.1016/j.neulet.2004.07.070 · Cited by 53
Mitochondria in Aging and Alzheimer's Disease
Crouch, P. J., Cimdins, K., Duce, J. A., Bush, A. I., & Trounce, I. A. (2007) · Rejuvenation Research · doi:10.1089/rej.2007.0592 · Cited by 54
Bimodal targeting of microsomal cytochrome P450s to mitochondria: implications in drug metabolism and toxicity
Sangar, M. C., Bansal, S., & Avadhani, N. G. (2010) · Expert Opinion on Drug Metabolism & Toxicology · doi:10.1517/17425255.2010.503955 · Cited by 53
Mitochondrial links between brain aging and Alzheimer’s disease
Wilkins, H., & Swerdlow, R. H. (2021) · Translational Neurodegeneration · doi:10.1186/s40035-021-00261-2 · Cited by 53
The Potentials of Methylene Blue as an Anti-Aging Drug
Xue, H., Thaivalappil, A., & Cao, K. (2021) · Cells · doi:10.3390/cells10123379 · Cited by 56
Genetic association of the cytochrome c oxidase-related genes with Alzheimer’s disease in Han Chinese
Bi, R., Zhang, W., Zhang, D., Xu, M., Fan, Y., Hu, Q.-X., Jiang, H., Tan, L., Li, T., Fang, Y., et al. (2018) · Neuropsychopharmacology · doi:10.1038/s41386-018-0144-3 · Cited by 54
Mitochondrial function and Aβ in Alzheimer's disease postmortem brain
Troutwine, B. R., Strope, T. A., Franczak, E., Lysaker, C. R., Hamid, L., Mansel, C., Stopperan, J. A., Gouvion, C. M., Haeri, M., Swerdlow, R. H., et al. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105781 · Cited by 51
Quinones Facilitate the Self-Assembly of the Phosphorylated Tubulin Binding Region of Tau into Fibrillar Polymers
Santa‐María, I., Hernández, F., Martín, C. P., Ávila, J., & Moreno, F. J. (2004) · Biochemistry · doi:10.1021/bi035345j · Cited by 51
Genome-wide pathway analysis implicates intracellular transmembrane protein transport in Alzheimer disease
Hong, M., Alexeyenko, A., Lambert, J., Amouyel, P., & Prince, J. A. (2010) · Journal of Human Genetics · doi:10.1038/jhg.2010.92 · Cited by 50
Therapeutic Potential of Multifunctional Tacrine Analogues
Przybyłowska, M., Kowalski, S., Dzierzbicka, K., & Inkielewicz‐Stępniak, I. (2018) · Current Neuropharmacology · doi:10.2174/1570159x16666180412091908 · Cited by 51
Molecular and biochemical trajectories from diabetes to Alzheimer’s disease: A critical appraisal
Sandhir, R., & Gupta, S. N. (2015) · World Journal of Diabetes · doi:10.4239/wjd.v6.i12.1223 · Cited by 49
Role of mitochondrial ion channels in cell death
Ryu, S., Peixoto, P. M. V., Teijido, Ó., Dejean, L. M., & Kinnally, K. W. (2010) · BioFactors · doi:10.1002/biof.101 · Cited by 49
Stimulation of SIRT1 Attenuates the Level of Oxidative Stress in the Brains of APP/PS1 Double Transgenic Mice and in Primary Neurons Exposed to Oligomers of the Amyloid-β Peptide
Dong, Y., Cao, K., Tan, L.-C., Wang, X., Qi, X., Xiao, Y. C., & Guan, Z.-Z. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-171020 · Cited by 48
Mitochondrial DNA damage in a mouse model of Alzheimer's disease decreases amyloid beta plaque formation
Pinto, M., Pickrell, A. M., Fukui, H., & Moraes, C. T. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.04.014 · Cited by 47
Key Role of Mitochondria in Alzheimer’s Disease Synaptic Dysfunction
Cavallucci, V., Ferraina, C., & D’Amelio, M. (2013) · Current Pharmaceutical Design · doi:10.2174/1381612811319360005 · Cited by 47
HIG1, a novel regulator of mitochondrial γ‐secretase, maintains normal mitochondrial function
Hayashi, H., Nakagami, H., Takeichi, M., Shimamura, M., Koibuchi, N., Oiki, E., Sato, N., Koriyama, H., Mori, M., Araujo, R. G., et al. (2012) · The FASEB Journal · doi:10.1096/fj.11-196063 · Cited by 46
The role of mitochondrial defects and oxidative stress in Alzheimer’s disease
Islam, B. U., Jabir, N. R., & Tabrez, S. S. M. (2019) · Journal of drug targeting · doi:10.1080/1061186x.2019.1584808 · Cited by 48
The role of cytochrome c oxidase deficiency in ROS and amyloid plaque formation
Pickrell, A. M., Fukui, H., & Moraes, C. T. (2009) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-009-9245-3 · Cited by 47
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
The multi-faceted impact of methamphetamine on Alzheimer’s disease: From a triggering role to a possible therapeutic use
Shukla, M., & Vincent, B. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101062 · Cited by 52
Understanding the neuronal synapse and challenges associated with the mitochondrial dysfunction in mild cognitive impairment and Alzheimer’s disease
Verma, H., Gangwar, P., Yadav, A., Yadav, B., Rao, R., Kaur, S., Kumar, P., Dhiman, M., Taglialatela, G., & Mantha, A. K. (2023) · Mitochondrion · doi:10.1016/j.mito.2023.09.003 · Cited by 46
Strategic Role for Mitochondria in Alzheimer's Disease and Cancer
Hedskog, L., Zhang, S., & Ankarcrona, M. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4259 · Cited by 45
Genetic basis of Alzheimer's dementia: role of mtDNA mutations
Grazina, M. M., Pratas, J., Silva, F., Oliveira, S. A., Santana, I. J., & Oliveira, C. R. (2006) · Genes Brain & Behavior · doi:10.1111/j.1601-183x.2006.00225.x · Cited by 47
Compartment-Restricted Biotinylation Reveals Novel Features of Prion Protein Metabolism in Vivo
Emerman, A. B., Zhang, Z.-R., Chakrabarti, O., & Hegde, R. S. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-09-0742 · Cited by 45
Amyloid precursor protein drives down-regulation of mitochondrial oxidative phosphorylation independent of amyloid beta
Lopez Sanchez, M. I. G., Waugh, H. S., Tsatsanis, A., Wong, B. X., Crowston, J. G., Duce, J. A., & Trounce, I. A. (2017) · Scientific Reports · doi:10.1038/s41598-017-10233-0 · Cited by 45
Amyloid precursor protein‐mediated mitochondrial regulation and Alzheimer's disease
Lopez Sanchez, M. I. G., van Wijngaarden, P., & Trounce, I. A. (2019) · British Journal of Pharmacology · doi:10.1111/bph.14554 · Cited by 45
Mitochondria as a Therapeutic Target in Alzheimers Disease and Diabetes
Moreira, P. I., Cardoso, S. M., Pereira, C., Santos, M. S., & Oliveira, C. R. (2009) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/187152709789824651 · Cited by 44
Amyloidosis in Retinal Neurodegenerative Diseases
Masuzzo, A., Dinet, V., Cavanagh, C., Mascarelli, F., & Krantic, S. M. (2016) · Frontiers in Neurology · doi:10.3389/fneur.2016.00127 · Cited by 45
Role of ketone bodies in diabetes-induced dementia: sirtuins, insulin resistance, synaptic plasticity, mitochondrial dysfunction, and neurotransmitter
Chung, J. Y., Kim, O. Y., & Song, J. (2021) · Nutrition Reviews · doi:10.1093/nutrit/nuab118 · Cited by 47
Regulation of mitochondrial dysfunction induced cell apoptosis is a potential therapeutic strategy for herbal medicine to treat neurodegenerative diseases
Li, R., Wang, L., Duan, H., Zhang, Q., Guo, X., Wu, C., & Peng, W. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.937289 · Cited by 48
Inhibition of Poly(ADP-ribose) Polymerase-1 Enhances Gene Expression of Selected Sirtuins and APP Cleaving Enzymes in Amyloid Beta Cytotoxicity
Wencel, P. L., Lukiw, W. J., Strosznajder, J. B., & Strosznajder, R. P. (2017) · Molecular Neurobiology · doi:10.1007/s12035-017-0646-8 · Cited by 43
The BACH1/Nrf2 Axis in Brain in Down Syndrome and Transition to Alzheimer Disease-Like Neuropathology and Dementia
Marzia Perluigi, A., Tramutola, A., Pagnotta, S. E., Barone, E., & Butterfield, D. A. (2020) · Antioxidants · doi:10.3390/antiox9090779 · Cited by 44
A New Function of Human HtrA2 as an Amyloid-β Oligomerization Inhibitor
Kooistra, J., Milojevic, J., Melacini, G., & Ortega, J. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-1037 · Cited by 45
Mitochondrial DAMPs: Key mediators in neuroinflammation and neurodegenerative disease pathogenesis
Yu, H., Ren, K., Jin, Y., Zhang, L., Liu, H., Huang, Z., Zhang, Z., Chen, X., Yang, Y., & Wei, Z. (2024) · Neuropharmacology · doi:10.1016/j.neuropharm.2024.110217 · Cited by 46
Mitochondria and neuroprotection in stroke: Cationic arginine-rich peptides (CARPs) as a novel class of mitochondria-targeted neuroprotective therapeutics
MacDougall, G., Anderton, R. S., Mastaglia, F. L., Knuckey, N. W., & Meloni, B. P. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.09.010 · Cited by 41
Alzheimer’s Pathogenesis and Its Link to the Mitochondrion
Simoncini, C., Orsucci, D., Ienco, E. C., Siciliano, G., Bonuccelli, U., & Mancuso, M. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/803942 · Cited by 45
Neuroprotective effect of emodin against Alzheimer's disease via Nrf2 signaling in U251 cells and APP/PS1 mice
Li, Z., Bi, H. C., Jiang, H., Song, J., Meng, Q., Zhang, Y., & Fei, X. (2020) · Molecular Medicine Reports · doi:10.3892/mmr.2020.11747 · Cited by 40
An update on the toxicity of Aβ in Alzheimer’s disease
Götz, J. (2008) · Neuropsychiatric Disease and Treatment · doi:10.2147/ndt.s3016 · Cited by 40

Authors: Anandatheerthavarada, H. K., Biswas, G., Robin, M.-A., & Avadhani, N. G.
Affiliations: University of Pennsylvania (US)
ORCID: Avadhani, Narayan G.
Venue: The Journal of Cell Biology
Publisher: Rockefeller University Press
Published: 2003-04-14
Volume: 161
Issue: 1
Pages: 41-54
ISSN: 0021-9525 (ISSN-L)
1540-8140
DOI: 10.1083/jcb.200207030
PMC: PMC2172865
OpenAlex: W2132988134
Cited by: 571
References: 47
Citations by year: 2026: 11 · 2025: 12 · 2024: 18 · 2023: 22 · 2022: 16 · 2021: 24 · 2020: 23 · 2019: 18 · 2018: 35 · 2017: 14 · 2016: 27 · 2015: 24 · 2014: 17 · 2013: 24 · 2012: 31
FWCI: 13.60
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: cc-by-nc-sa
Locations: The Journal of Cell Biology (publishedVersion)
PubMed Central (publishedVersion, cc-by-nc-sa)
PubMed (publishedVersion)
Funders: National Institutes of Health (1r01gm034483-01a3)
National Institute of General Medical Sciences (GM34483)
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
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Keywords: amyloid precursor protein, APP695, mitochondrial targeting, mitochondrial dysfunction, energy metabolism, Alzheimer's disease, amyloid-beta, mitochondrial translocase, acidic domain, cortical neurons, transgenic mouse model, crosslinking, immunoelectron microscopy
MeSH terms: Alzheimer Disease, Amino Acid Sequence, Animals, Brain, Cell Compartmentation, Cells, Cultured, Disease Models, Animal, Energy Metabolism, Humans, Immunohistochemistry, Intracellular Membranes, Mice, Transgenic, Microscopy, Electron, Mitochondria, Molecular Conformation, Neurons, Recombinant Fusion Proteins, Amyloid beta-Protein Precursor, Protein Structure, Tertiary, Protein Transport, Cytochrome-c Oxidase Deficiency, Mice

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

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

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