Cited by 354Autophagy in Disease and TherapyAlzheimer's disease research and treatmentsCalcium signaling and nucleotide metabolism

The DOI matches its Crossref record; 98 of the 101 references it cites were found in a registry or an index.

Autophagy flux in CA1 neurons of Alzheimer hippocampus: Increased induction overburdens failing lysosomes to propel neuritic dystrophy

Open access

Bordi, Matteo, Berg, Martin J., Mohan, Panaiyur S., Peterhoff, Corrinne M., Alldred, Melissa J., Che, Shaoli, Ginsberg, Stephen D., Nixon, Ralph A.·2016·Autophagy

DOI 10.1080/15548627.2016.1239003PMC PMC5173282

Open this paper in CoChat — free account

Abstract

Defective autophagy contributes to Alzheimer disease (AD) pathogenesis although evidence is conflicting on whether multiple stages are impaired. Here, for the first time, we have comprehensively evaluated the entire autophagic process specifically in CA1 pyramidal neurons of hippocampus from early and late-stage AD subjects and nondemented controls. CA1 neurons aspirated by laser capture microdissection were analyzed using a custom-designed microarray comprising 578 neuropathology- and neuroscience-associated genes. Striking upregulation of autophagy-related genes, exceeding that of other gene ontology groups, reflected increases in autophagosome formation and lysosomal biogenesis beginning at early AD stages. Upregulated autophagosome formation was further indicated by elevated gene and protein expression levels for autophagosome components and increased LC3-positive puncta. Increased lysosomal biogenesis was evidenced by activation of MiTF/TFE family transcriptional regulators, particularly TFE3 (transcription factor binding to IGHM enhancer 3) and by elevated expression of their target genes and encoded proteins. Notably, TFEB (transcription factor EB) activation was associated more strongly with glia than neurons. These findings establish that autophagic sequestration is both competent and upregulated in AD. Autophagosome-lysosome fusion is not evidently altered. Despite this early disease response, however, autophagy flux is progressively impeded due to deficient substrate clearance, as reflected by autolysosomal accumulation of LC3-II and SQSTM1/p62 and expansion of autolysosomal size and total area. We propose that sustained induction of autophagy in the face of progressively declining lysosomal clearance of substrates explains the uncommonly robust autophagic pathology and neuritic dystrophy implicated in AD pathogenesis.

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 · 10.1080/15548627.2016.1239003

Cites

98 of 98 references verified0 citation errors · 0 not checkable

Statistics

Figure 1. Changes in expression of autophagy-related genes in hippocampal CA1 pyramidal neurons. (A) Autophagy-related genes showing differential regulation in CA1 neurons via custom-designed microarray analysis of 578 genes. Significantly (p ≤ 0.05) altered in both Br. III/IV and Br. V/VI shown in dark gray; others significantly altered in Br. V/VI only shown in black, no change in gray. (B) Pie chart indicating proportions of significantly upregulated and downregulated autophagy genes on the array platform. (C) Pie chart illustrating a relative paucity of genes upregulated in all 578 transcripts contrasting with the higher proportion that are downregulated. (D) GO analysis of all highly expressed genes in Br. III/IV and Br. V/VI when compared to control group. Autophagy, the most represented term, is highlighted in darker blue. p value cut off 0.05. (E) qPCR validation of selected autophagy/lysosomal genes assayed in the CA1 sector of the hippocampus. Statistical significance is denoted by asterisks with p-values shown determined by one-way ANOVA or for 2 column analysis by Student t test. *p ≤ 0.05; **p ≤ 0.01.CC BY-NC · PubMed Central

Figure 2. Evaluation of autophagy induction in AD. (A) Western blot analysis of indices of autophagic induction and autophagosome formation for ULK1, BECN1, PIK3C3/VPS34, ATG7, LC3, and SQSTM1/p62 and degradative products in AD hippocampus. (B) Histogram illustrating quantification of the findings in (A). (C–D) Western blot analysis of FOXO1 and FOXO3 levels in AD and control hippocampal tissue. Samples analyzed from patients as Control (n = 9), from AD Br. III (n = 10) and from AD Br. V (n = 10). Significance determined by one-way ANOVA with post-hoc Dunnett's Comparison to Control test. *p ≤ 0.05; **p ≤ 0.01. Western blots cropped as shown for purposes of clarity.CC BY-NC · PubMed Central

Figure 3. Analysis of lysosomal constituents in AD hippocampus. (A) Western blot analysis of structural and enzymatic constituents of lysosomes with quantification shown in (B). Samples analyzed from control patients (n = 9), from AD Br. III (n = 10) and from AD Br. V (n = 10). Significance determined by one-way ANOVA, with post-hoc Dunnett's Comparison to Control test. **p ≤ 0.01. Western blots cropped as shown for purposes of clarity.CC BY-NC · PubMed Central

Figure 4. Analysis of TFE3 and TFEB transcription factors in hippocampal CA1 pyramidal neurons and glia. (A) qPCR analysis of CA1 neurons for TFE3 and TFEB. (B) qPCR for both TFEB and TFE3 in hippocampal total RNA. (C) Amplification plots for TFE3 (red) and TFEB (green) showing a 1.2 cycle difference equivalent to a greater than 10-fold higher level of TFE3 mRNA in hippocampal tissue. (D–E) Western blot analysis for TFE3 and TFEB in hippocampal tissue and relative quantification showing higher levels of TFE3. Samples analyzed from control patients (n = 9), from AD Br. III (n = 10) and from AD Br. V (n = 10). (F) Immunocytochemical localization of TFE3 in the hippocampal CA1 region. Cells immunostained for TFE3 and counterstained with Nissl. Black arrowheads indicate translocation of TFE3 in neuronal nuclei; blue arrowheads point to negative TFE3 nuclear staining. Scale bar: 10 μm. (G) Quantification of TFE3 nuclear translocation in glia and neurons. (H) Fluorescent immunolocalization of TFEB (yellow arrowheads for neuronal, blue for glia) with Nissl staining shows neuronal or glial nuclei and with decreasing Nissl staining on nuclear translocation in hippocampal CA1 region. Scale bar: 10 μm. (I) Quantification of TFEB nuclear translocation in glia and neurons. A minimum of 50 fields were quantified per condition. Statistical significance denoted by asterisks with p-values shown determined by one-way ANOVA, with post-hoc Dunnett's Comparison to Control test, or for 2 columns analysis by Student t test. *p ≤ 0.05; **p ≤ 0.01; ***p ≤ 0.001; ****p ≤ 0.0001.CC BY-NC · PubMed Central

Figure 5. Double-immunofluorescent labeling of the CA1 region with LC3 and CTSD. (A) Immunofluorescent staining for LC3 (green channel) and CTSD (red) in CA1 hippocampal neurons from Control, Br. III and V. Scale bar: 20 μm. (B) Pearson's correlation coefficient of colocalization of CTSD with LC3 in hippocampal CA1 neurons. A minimum of 100 neurons were quantified per condition. (C–D) Characterization of vesicles in Control, Br. III and V CA1 neurons, identified as autophagosome (AP, LC3-positive, CTSD-negative vesicles), autolysosome (AL, LC3- and CTSD-positive vesicles) and lysosome (Ly, LC3-negative, CTSD-positive vesicles). Depicted is the total number and area covered per cell in (C) and (D) respectively. (E) Size distribution of autolysosomes in Control, Br. III and V CA1 neurons. Statistical significance denoted by asterisks with p-values shown determined by one-way ANOVA, with post-hoc Dunnett's Comparison to Control test for grouped analyses, and 2-way ANOVA for size distribution analyses. *p ≤ 0.05; **p ≤ 0.01; ***p ≤ 0.001.CC BY-NC · PubMed Central

Figure 6. Neuritic dystrophy adjacent to senile plaques in the CA1 region in AD brains. (A) The image of AD Br. V hippocampal CA1 depicts a population of putative dystrophic neurites (white arrowheads in the merged image) surrounding a weakly CTSD-positive senile plaque (P). (B) Z-stack images of consecutive optical slices through the single profile indicated by the box in (A) confirms the typical appearance of a dystrophic neurite, which is shown to contain mainly autophagic vacuoles including LC3-positive AP (green), LC3- and CTSD-positive AL, (yellow-orange vesicles) and less frequent CTSD-positive-only lysosomes (red). Scale bar: 10 μm.CC BY-NC · PubMed Central

Figure 7. Expression of cell-type markers in AD hippocampus shows alterations in neuronal and glial content. (A) Representative western blots illustrating neuronal ΤUBB3 and glial GFAP markers in AD and control hippocampus. (B) Relative quantification of markers in hippocampus indicates downregulation of neuronal-specific TUBB3 and upregulation of GFAP, consistent with neuronal cell loss and concomitant astrogliosis. Statistical significance denoted by asterisks with p-values shown determined by one-way ANOVA, Dunnett's test. *p ≤ 0.05; **p ≤ 0.01. Western blots cropped as shown for purposes of clarity.CC BY-NC · PubMed Central

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.

Fiji: an open-source platform for biological-image analysis
Schindelin, J., Arganda-Carreras, I., Frise, E., Kaynig, V., Longair, M., Pietzsch, T., Preibisch, S., Rueden, C., Saalfeld, S., Schmid, B., et al. (2012) · Nature Methods · doi:10.1038/nmeth.2019 · Cited by 66,890
Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
Huang, D. W., Sherman, B. T., & Lempicki, R. A. (2009) · Nature Protocols · doi:10.1038/nprot.2008.211 · Cited by 35,890
Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes
Vandesompele, J., De Preter, K., Pattyn, F., Poppe, B., Van Roy, N., De Paepe, A., & Speleman, F. (2002) · Genome Biology · doi:10.1186/gb-2002-3-7-research0034 · Cited by 20,038
Measurement of protein using bicinchoninic acid
Smith, P. K., Krohn, R. I., Hermanson, G. T., Mallia, A. K., Gartner, F. H., Provenzano, M. D., Fujimoto, E. K., Goeke, N. M., Olson, B. J., & Klenk, D. C. (1985) · Analytical Biochemistry · doi:10.1016/0003-2697(85)90442-7 · Cited by 18,482
Neuropathological stageing of Alzheimer-related changes.
Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123 · cited 3×
“V/VI, n D 15).79 Based on results from these analyses, subsequent studies were typed solely on the basis of the primary neuropathological assessment as described by Braak and Braak.79 For qPCR and western blot analyses, fresh-frozen postmortem human brain tissue was obtained from the Harvard Brain Tissue Resource Cent…”
MethodInfluential
Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition).
Klionsky, D. J., Abdelmohsen, K., Abe, A., Abedin, M. J., Abeliovich, H., Acevedo Arozena, A., Adachi, H., Adams, C. M., Adams, P. D., Adeli, K., et al. (2016) · Autophagy · doi:10.1080/15548627.2015.1100356 · Cited by 5,894
Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
Glenner, G. G., & Wong, C. W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(84)80190-4 · Cited by 5,404
The Consortium to Establish a Registry for Alzheimer's Disease (CERAD): Part II. Standardization of the neuropathologic assessment of Alzheimer's disease
Mirra, S. S., Heyman, A., McKeel, D., Sumi, S. M., Crain, B. J., Brownlee, L. M., Vogel, F. S., Hughes, J. P., Belle, G. V., Berg, L., et al. (1991) · Neurology · doi:10.1212/wnl.41.4.479 · Cited by 4,961
Autophagy and the Integrated Stress Response
Kroemer, G., Mariño, G., & Levine, B. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.023 · Cited by 3,506
TFEB Links Autophagy to Lysosomal Biogenesis
Settembre, C., Di Malta, C., Polito, V. A., Arencibia, M. G., Vetrini, F., Erdin, S., Erdin, S. U., Huynh, T., Medina, D., Colella, P., et al. (2011) · Science · doi:10.1126/science.1204592 · Cited by 3,365

Show all 101 references

Research works printed but not linked: 4

Kawai M, 1992, Am J Pathol, 140, 947
Pickford F, 2008, J Clin Invest, 118, 2190
Kim S, 2015, Mol Psychiatry
Schmidt SD, 2005, Methods Mol Biol, 299, 267

Sorted by citations

Items 301–354 of 354

Mitochondrial response to axonal injury
Kedra, J. (2020) · TUScholarShare (Temple University)
Selective Disruption of Drp1-Independent Mitophagy and Mitolysosome Trafficking by an Alzheimer’s Disease Relevant Tau Modification in a Novel C. elegans ModelPreprint
Guha, S. K., Cheng, A., Carroll, T., King, D. P., Koren, S. A., Swords, S., Nehrke, K. W., & Johnson, G. V. W. (2021) · Research Square · doi:10.21203/rs.3.rs-1096882/v1
Design and Analysis of a Nanosatellite Platform for Orbital Debris Mitigation through Launch of Space Tether in Low Earth Orbits
Asundi, S. (2013)
Faculty Opinions recommendation of Characterization of LAMP1-labeled nondegradative lysosomal and endocytic compartments in neurons.
Chapman, E. R., & Vevea, J. (2018) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.733114368.793553076
Lysosomal Dysfunction in Down Syndrome and Alzheimer Mouse Models is Caused by Selective V-Atpase Inhibition by Tyr 682 Phosphorylated APP βCTFPreprint
Im, E., Jiang, Y., Stavrides, P. H., Darji, S., Erdjument‐Bromage, H., Thomas, N. A., Bordi, M., Choi, J. Y., Lee, J., & Nixon, R. A. (2022) · SSRN Electronic Journal · doi:10.2139/ssrn.4106838
Self-citation
Effekte einer pharmakologischen Inhibition der ULK1-Kinase auf die akute axonalen Degeneration in vivo
Sundermeyer, J. (2022) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-9423
Nodweddu effaith signalu ghrelin-GHS-R ar awtoffagi niwronaidd
Roberts, L. D. (2022) · Cronfa (Swansea University) · doi:10.23889/suthesis.62285
Rooibos tea—in the cross fire of ROS, mitochondrial dysfunction and loss of proteostasis—positioned for healthy aging
Smit, C., de Wet, S., van Blerk, T. B., & Loos, B. (2023) · Biogerontology · doi:10.1007/s10522-022-10012-z
Sex differences in response to obesity and caloric restriction on cognition and hippocampal markers of autophagic-lysosomal pathway functionPreprint
Baer, S. B., Dorn, A. D., & Osborne, D. M. (2023) · Research Square · doi:10.21203/rs.3.rs-2724928/v1
Alternative Hypotheses and Observations that Were Somehow Lost on the Way
Behl, C. (2023) · Springer eBooks · doi:10.1007/978-3-031-31570-1_17
The role of Banf1 in mechanisms of cellular ageing and cancer prognosis
Plowman, J. (2024) · Queensland University of Technology · doi:10.5204/thesis.eprints.247163
Additional file 2 of TNEA therapy promotes the autophagic degradation of NLRP3 inflammasome in a transgenic mouse model of Alzheimer’s disease via TFEB/TFE3 activation
Lin, W., Zhao, L., Liang, G., Zhou, R., Zheng, X., Tao, R., Huo, Q., Su, C.-F., Li, M., Xu, N., et al. (2023) · Figshare · doi:10.6084/m9.figshare.22612913
Lysosomal pH Homeostasis and Parkinson’s Disease
温, 娜. (2024) · Advances in Clinical Medicine · doi:10.12677/acm.2024.1451672
Inhibition of miR-4763-3p expression in the brains of AD-MCI mice activates the PI3K/mTOR/Bcl2 autophagy signaling pathway to reverse neuronal loss and ameliorate cognitive declinePreprint
Qi, W., Dong, N., Peiru, W. U., Fu, W., Liu, Q., Zhang, X., Wu, H., He, X., Wu, L., Ward, N., et al. (2024) · Research Square · doi:10.21203/rs.3.rs-4458094/v1
Sertad1 is elevated and plays a necessary role in synaptic loss, neuron death and cognitive impairment in a model of Alzheimer’s diseasePreprint
Ambareen, N., Gharami, K., & Biswas, S. C. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.08.06.606751
TFEB and TFE3 have cell-type specific expression in the brain and divergent roles in neuronsPreprint
McGuinness, W., Ryan, B. J., Guardado, C. L., Carling, P., Vallin, B., Caiazza, M. C., Heon‐Roberts, R., Kilfeather, P., Wantling, J., Hoffmann, J., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.04.22.649949 · Cited by 3
Relationship between p62 and learning behavior in male and female mice deficient in hippocampal folliculin
Guvenir, A., & Osborne, D. M. (2025) · Journal of Emerging Investigators · doi:10.59720/23-206
Regulated cell death: Discovery, features, and implications for neurodegenerative diseases
Pandey, S. K., Nanda, A., Singh, S., & Singh, R. K. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-32852-7.00001-2
Therapeutic approaches targeting regulated cell death in neurodegenerative diseases: Current understanding and recent advances in combating neuronal loss
Bakkar, N. Z., Arida, R. E., Soliman, A. Y., & EL‐Yazbi, A. F. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-32852-7.00016-4
Impaired MAPT/tau-secretory lysosomes are linked to cognitive vulnerability in Alzheimer patients
Sharma, P., Pallavi, A., Chatterjee, A., Prasad, V. M., Gandasi, N. R., & Saroja, S. R. (2025) · Autophagy · doi:10.1080/15548627.2025.2552905
Utility of biological aging acceleration in capturing transitions of atrial fibrillation and dementia: a population-based study
Liu, Y., & Li, C. (2025) · npj Aging · doi:10.1038/s41514-025-00274-5
Sertad1 is elevated and plays a necessary role in neuron loss and cognitive impairment in a mouse model of Alzheimer's disease
Ambareen, N., Gharami, K., Mondal, A., Sarkar, U. A., & Biswas, S. C. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110875
Chronic Overexpression of Neuronal NRG1-III in Mice Causes Long-Term Detrimental Changes in Lower Motor Neurons, Neuromuscular Synapses and Motor Behaviour
Salvany, S., Hernández, S., Garcia-Casanovas, A., Gras, S., Piedrafita, L., Bosch-Queralt, M., Schwab, M. H., Calderó, J., Esquerda, J. E., & Tarabal, O. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262311421
Ultra-large stokes shift probe enables SIM super-resolution tracking of lysosomal acidification impairment in Aβ trafficking dysregulation during Alzheimer's disease
Liu, Y., Zhang, C., Wang, X., Shao, Y., Cai, X., Liu, H., Zhu, H., Liu, X., Qian, Y., & Wang, X. (2025) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2025.118284
Additional file 1 of Cathepsin B abundance, activity and microglial localisation in Alzheimer’s disease-Down syndrome and early onset Alzheimer’s disease; the role of elevated cystatin B
Wu, Y., Mumford, P., Noy, S., Cleverley, K., Mrzyglod, A., Luo, D., van Dalen, F., Verdoes, M., Fisher, E., & Wiseman, F. K. (2023) · Figshare · doi:10.6084/m9.figshare.23949660
Additional file 2 of Sex differences in response to obesity and caloric restriction on cognition and hippocampal measures of autophagic-lysosomal transcripts and signaling pathways
Baer, S. B., Dorn, A. D., & Osborne, D. M. (2024) · Figshare · doi:10.6084/m9.figshare.26658469
Additional file 3 of Sex differences in response to obesity and caloric restriction on cognition and hippocampal measures of autophagic-lysosomal transcripts and signaling pathways
Baer, S. B., Dorn, A. D., & Osborne, D. M. (2024) · Figshare · doi:10.6084/m9.figshare.26658472
Additional file 1 of Sex differences in response to obesity and caloric restriction on cognition and hippocampal measures of autophagic-lysosomal transcripts and signaling pathways
Baer, S. B., Dorn, A. D., & Osborne, D. M. (2024) · Figshare · doi:10.6084/m9.figshare.26658466
Additional file 1 of TNEA therapy promotes the autophagic degradation of NLRP3 inflammasome in a transgenic mouse model of Alzheimer’s disease via TFEB/TFE3 activation
Lin, W., Li, Z., Liang, G., Zhou, R., Zheng, X., Tao, R., Huo, Q., Su, C., Li, M., Xu, N., et al. (2023) · Figshare · doi:10.6084/m9.figshare.22612910
Tubuloside B Alleviates Aβ25-35 Induced PC12 Cell Injury by Attenuating Pyroptosis, Apoptosis and Excessive Autophagy
Yang, H., Fu, R., DUAN, Y., Hua, Y., Wei, T., Li, G., Gu, X., Li, M., Yu, X., Li, L., et al. (2026) · Neurotoxicity Research · doi:10.1007/s12640-026-00791-5
Intervention of ginseng-derived macromolecular drugs in Alzheimer’s disease: exploring mechanisms and assessing potential
Liu, W., Bai, Y., Qu, W., Zhang, X., Zhou, S., Luo, H., Zhu, M., Li, D., & Fang, X. (2026) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2026.1752446
The role of MicroRNAs in Alzheimer’s disease: from pathogenesis to therapeutic potential
Zhou, Y., Li, S., & Xiang, J. (2026) · Molecular Biology Reports · doi:10.1007/s11033-026-11746-6
Drug Discovery for Alzheimer’s Disease: Current Status
Wolfe, M. S. (2026) · Topics in medicinal chemistry · doi:10.1007/7355_2026_186
Generation of oxidative stress as an anticancer therapeutic strategy : Investigating the mechanism of action of vitamin C, auranofin and their combination
Banna, N. E. (2019) · theses.fr (ABES) · doi:10.70675/0a905f67zf870z4c60z8f5czada3b7341188
LRRK2 et fonction mitochondriale dans la maladie de Parkinson : rôle dans la régulation de la mitophagie dépendante de la voie PINK1/Parkine
Bonello, F. (2018) · theses.fr (ABES) · doi:10.70675/e43ece04z57d0z4e13z96dez05a00e151822
Mécanismes de régulation de l’ecto-F1-ATPase par la mitophagie
Fried, S. (2018) · theses.fr (ABES) · doi:10.70675/f53f2ce5z6e85z479bz9bbbz68e1878cc5bc
Les APP-CTFs au cœur du processus pathologique de la maladie d’Alzheimer : contribution du système lysosomal-autophagique et de la sécrétion exosomale
Bécot, A. (2019) · theses.fr (ABES) · doi:10.70675/21765754zb9e7z40f9zb951z367e5fa4bcac
Maladies neurodégénératives et stress oxydant
Lévy, E. (2020) · theses.fr (ABES) · doi:10.70675/75371581z194fz4cb4zb457z91bf72dc0320 · Cited by 4
Implications de la signalisation de la protéine kinase activée par l’AMP (AMPK) dans les dysfonctions mitochondriales, la pathologie amyloïde et Tau, et la neuroinflammation dans la maladie d’Alzheimer
Mary, A. (2022) · theses.fr (ABES) · doi:10.70675/868e288ezd237z49c1z866fzf618e1462aab
Role of PTH and PTHrP in the central regulation of energy metabolism
Galerne, M. (2024) · theses.fr (ABES) · doi:10.70675/31092b82za087z48dczb698z1409347feb21
Gibt es mehr als dreißig Jahre nach Einführung der Amyloid-Kaskaden-Hypothese endlich den Paradigmenwechsel?
Behl, C. (2026) · Springer eBooks · doi:10.1007/978-3-662-72210-7_20
Alternative Hypothesen und Beobachtungen, die verloren gingen
Behl, C. (2026) · Springer eBooks · doi:10.1007/978-3-662-72210-7_17
Integrative genomic and functional analyses reveal NINL as a modulator of tau aggregation
Swift, S. K., Huang, G., Cochran, J. N., Albanus, R. D., Minaya, M., Castruita, P. A., Zhang, R., Miller, K. J., Starr, E., Galasso, G., et al. (2026) · Alzheimer s & Dementia · doi:10.1002/alz.71352 · Cited by 1
KBN2201 attenuates Aβ pathology and neuroinflammation while promoting neuroprotective and neurogenesis-related changes in a late-stage 5xFAD mouse model of Alzheimer's disease
Lee, S., Kim, J. C., Song, J., Lee, Y., Kim, M., Chang, S.-H., Kim, J. S., Park, J.-S., Choi, M., & Lee, S. (2026) · Neuropharmacology · doi:10.1016/j.neuropharm.2026.110970 · Cited by 1
Small Molecule Guided Photocatalytic Proteomics Profiling of Amyloid Deposits in Hippocampal and Cortical Alzheimer’s Disease Tissues
Yan, J., Feng, H., Xia, Q., Shen, D., Jin, H. K., Sun, R., Sun, J. F., Tang, W., Yu, X., Guo, F., et al. (2026) · Analytical Chemistry · doi:10.1021/acs.analchem.5c08045
The modifier matrix: emerging roles of ubiquitin-like proteins in Alzheimer’s disease
颜亭祥, Vaquer, J., Springer, W., & Fiesel, F. C. (2026) · Molecular Neurodegeneration Advances · doi:10.1186/s44477-026-00031-2
TFE3 Regulates Microglial Phagocytosis and Inflammation in MPTP-induced Parkinson’s Disease
Liu, Q., Xie, W., Tian, X., Su, Z., Wang, Z., Zhang, Y., Wang, H., Zuo, D., Du, H., Gao, J., et al. (2026) · Molecular Neurobiology · doi:10.1007/s12035-026-06012-6
Di(2-ethylhexyl) phthalate exposure aggravates amyloid-beta-induced toxicity in transgenic AD Caenorhabditis elegans via exacerbating lysosomal dysfunction and oxidative stress
Yang, F., & Zhao, Y. (2026) · Food and Chemical Toxicology · doi:10.1016/j.fct.2026.116276
Astrocytic lactate shuttle disruption and the energy-starved lysosome in Alzheimer's diseasePreprint
Kim¹, Y., Heo, W., Park, S. J., Kim, Y., & Cho², Y. E. (2026) · Research Square · doi:10.21203/rs.3.rs-10057949/v1
Endoplasmic Reticulum Stress Drives Copper-Induced Reticulophagy in Porcine Hepatocytes
Yang, S., Chen, W., Xi, H., Qiu, W., Huang, H., Wang, S., Liao, J., & Tang, Z. (2026) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.5c16689
Aβ-induced CaMKII hyperactivation is associated with impaired lysosomal maturation and mitophagy
Suh, E. C., Kim, Y. A., Lee, K. E., & Park, E. (2026) · Neurochemistry International · doi:10.1016/j.neuint.2026.106252
Autophagy Stimulation by Intermittent Fasting and Its Potential Neuroprotective Role in Alzheimer’s Disease
Corrales, N., Vallejo-Bedia, F., Olivares-Raya, I., Ávila, J., & García‐Escudero, V. (2026) · Applied Sciences · doi:10.3390/app16199488
NEFL contributes to DJ-1-mediated neuroprotection and autophagic flux regulation in Alzheimer’s disease-like injury
Liu, Y., Li, X., Wang, M., Fan, X., Liu, W., Wang, Y., Li, W., Miao, Y., & Li, X. (2026) · Experimental Neurology · doi:10.1016/j.expneurol.2026.116092
The pathological roles of intrinsically disordered proteins in lysosomal acidification dysfunction in neurodegenerative diseases
Abd-Elraouf, K., Murphy, D. T., Cheong, L. Y. T., Zeng, J., & Lo, C. H. (2026) · Translational Neurodegeneration · doi:10.1186/s40035-026-00591-z

Authors: Bordi, M., Berg, M. J., Mohan, P. S., Peterhoff, C. M., Alldred, M. J., Che, S., Ginsberg, S. D., & Nixon, R. A.
Affiliations: Nathan Kline Institute for Psychiatric Research (US)
Corresponding author: Nixon, Ralph A.
ORCID: Bordi, Matteo
Berg, Martin J.
Alldred, Melissa J.
Ginsberg, Stephen D.
Nixon, Ralph A.
Venue: Autophagy
Publisher: Informa UK Limited
Published: 2016-11-04
Volume: 12
Issue: 12
Pages: 2467-2483
ISSN: 1554-8627 (ISSN-L)
1554-8635
DOI: 10.1080/15548627.2016.1239003
PMC: PMC5173282
OpenAlex: W2547593615
Cited by: 353
References: 101
Citations by year: 2026: 23 · 2025: 37 · 2024: 41 · 2023: 38 · 2022: 37 · 2021: 42 · 2020: 48 · 2019: 34 · 2018: 30 · 2017: 22
FWCI: 26.84
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by-nc
creativecommons.org/licenses/by-nc/3.0/ (vor)
Locations: Autophagy (publishedVersion, cc-by-nc)
PubMed Central (publishedVersion, cc-by-nc)
PubMed (publishedVersion)
Funders: Emory University
National Institute on Aging (P01AG014449, R01AG043375, P50AG025688, P01AG017617)
National Institute of Neurological Disorders and Stroke (P30NS055077)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
Keywords: Alzheimer's disease, autophagic flux, CA1 pyramidal neurons, hippocampus, autophagosome formation, lysosomal biogenesis, TFE3, TFEB, p62, LC3-II, neuritic dystrophy, autophagosome-lysosome fusion
MeSH terms: Autophagosomes, Aged, Aged, 80 and over, Alzheimer Disease, Autophagy, Cathepsin D, Demography, Female, Gene Expression Regulation, Humans, Lysosomes, Male, Microtubule-Associated Proteins, Middle Aged, Neurites, Basic Helix-Loop-Helix Leucine Zipper Transcription Factors, CA1 Region, Hippocampal

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

Autophagy flux in CA1 neurons of Alzheimer hippocampus: Increased induction overburdens failing lysosomes to propel neuritic dystrophy

Abstract

Overview

Integrity signals

Figures

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks