Cited by 233Alzheimer's disease research and treatmentsCell death mechanisms and regulationMicrotubule and mitosis dynamics

The DOI matches its Crossref record; 71 of the 71 references it cites were found in a registry or an index.

Tau Cleavage and Dephosphorylation in Cerebellar Granule Neurons Undergoing Apoptosis

Open access

Canu, Nadia, Dus, Laura, Barbato, Christian, Ciotti, Maria T., Brancolini, Claudio, Rinaldi, Anna M., Novak, Michal, Cattaneo, Antonino, Bradbury, Andrew, Calissano, Pietro·1998·The Journal of Neuroscience

DOI 10.1523/jneurosci.18-18-07061.1998PMC PMC6793249

Open this paper in CoChat — free account Open PDF

Abstract

Cerebellar granule cells undergo apoptosis in culture after deprivation of potassium and serum. During this process we found that tau, a neuronal microtubule-associated protein that plays a key role in the maintenance of neuronal architecture, and the pathology of which correlates with intellectual decline in Alzheimer’s disease, is cleaved. The final product of this cleavage is a soluble dephosphorylated tau fragment of 17 kDa that is unable to associate with microtubules and accumulates in the perikarya of dying cells. The appearance of this 17 kDa fragment is inhibited by both caspase and calpain inhibitors, suggesting that tau is an in vivo substrate for both of these proteases during apoptosis. Tau cleavage is correlated with disruption of the microtubule network, and experiments with colchicine and taxol show that this is likely to be a cause and not a consequence of tau cleavage. These data indicate that tau cleavage and change in phosphorylation are important early factors in the failure of the microtubule network that occurs during neuronal apoptosis. Furthermore, this study introduces new insights into the mechanism(s) that generate the truncated forms of tau present in Alzheimer’s disease.

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.18-18-07061.1998

Cites

71 of 71 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
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961
Short-Term Effects of Nose-Only Cigarette Smoke Exposure on Glutathione Redox Homeostasis, Cytochrome P450 1A1/2 and Respiratory Enzyme Activities in Mice Tissues
Raza, H., John, A., & Nemmar, A. (2013) · Cellular Physiology and Biochemistry · doi:10.1159/000350087 · Cited by 47,311
Apoptosis: A Basic Biological Phenomenon with Wideranging Implications in Tissue Kinetics
Kerr, J. F. R., Wyllie, A. H., & Currie, A. R. (1972) · British Journal of Cancer · doi:10.1038/bjc.1972.33 · Cited by 15,980
Apoptosis in the Pathogenesis and Treatment of Disease
Thompson, C. B. (1995) · Science · doi:10.1126/science.7878464 · Cited by 6,524
Caspases: the executioners of apoptosis
Cohen, G. M. (1997) · Biochemical Journal · doi:10.1042/bj3260001 · Cited by 4,737
Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology.
Grundke-Iqbal, I., Iqbal, K., Tung, Y. C., Quinlan, M., Wisniewski, H. M., & Binder, L. I. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.13.4913 · Cited by 3,676
Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease
Goedert, M., Spillantini, M. G., Jakes, R., Rutherford, D., & Crowther, R. A. (1989) · Neuron · doi:10.1016/0896-6273(89)90210-9 · Cited by 2,492
Mechanisms and Genes of Cellular Suicide
Steller, H. (1995) · Science · doi:10.1126/science.7878463 · Cited by 2,469
Microtubule-associated protein tau. A component of Alzheimer paired helical filaments.
Grundke, I., Iqbal, K., Quinlan, M., Tung, Y. C., Zaidi, M. S., & Wisniewski, H. M. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38495-8 · Cited by 1,780

Show all 71 references

Research works printed but not linked: 2

Fasulo, 1998, Tau truncation in Alzheimer’s disease: expression of a fragment encompassing PHF core tau induces apoptosis in COS cells., Alzheimer’s Rep, 1, 1
10.1128/MCB.9.4.1381 · DOI

Sorted by citations

Apoptosis: controlled demolition at the cellular level
Taylor, R. C., Cullen, S. P., & Martin, S. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2312 · Cited by 2,708
Roles of tau protein in health and disease
Guo, T., Noble, W., & Hanger, D. P. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1707-9 · Cited by 1,003
Many cuts to ruin: a comprehensive update of caspase substrates
Fischer, U., Jänicke, R. U., & Schulze‐Osthoff, K. (2003) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401160 · Cited by 1,025
Degradation of misfolded proteins in neurodegenerative diseases: Therapeutic targets and strategies
Ciechanover, A., & Kwon, Y. T. (2015) · Experimental & Molecular Medicine · doi:10.1038/emm.2014.117 · Cited by 898
Calpain and caspase: can you tell the difference?
Wang, K. (2000) · Trends in Neurosciences · doi:10.1016/s0166-2236(99)01479-4 · Cited by 912
Caspase cleavage of tau: Linking amyloid and neurofibrillary tangles in Alzheimer's disease
Gamblin, T. C., Chen, F., Zambrano, A., Abraha, A., Lagalwar, S., Guillozet, A. L., Lu, M., Fu, Y., Garcia-Sierra, F., LaPointe, N., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1630428100 · Cited by 831
Post-translational modifications of tau protein: Implications for Alzheimer's disease
Martin, L., Latypova, X., & Terro, F. (2011) · Neurochemistry International · doi:10.1016/j.neuint.2010.12.023 · Cited by 683
Caspase-cleavage of tau is an early event in Alzheimer disease tangle pathology
Rissman, R. A., Poon, W. W., Blurton-Jones, M., Oddo, S., Torp, R., Vitek, M. P., LaFerla, F. M., Rohn, T. T., & Cotman, C. W. (2004) · Journal of Clinical Investigation · doi:10.1172/jci200420640 · Cited by 543
Structure and Pathology of Tau Protein in Alzheimer Disease
Kolarova, M., García‐Sierra, F., Bartoš, A., Říčný, J., & Řípová, D. (2012) · International Journal of Alzheimer s Disease · doi:10.1155/2012/731526 · Cited by 526
Synergistic Activation of Caspase-3 by m-Calpain after Neonatal Hypoxia-Ischemia
Blomgren, K., Zhu, C., Wang, X., Karlsson, J., Leverin, A., Bahr, B. A., Mallard, C. E., & Hagberg, H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007807200 · Cited by 447
Tau, tangles, and Alzheimer's disease
Binder, L. I., Guillozet-Bongaarts, A. L., García‐Sierra, F., & Berry, R. W. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.08.014 · Cited by 450
Implication of cysteine proteases calpain, cathepsin and caspase in ischemic neuronal death of primates
Yamashima, T. (2000) · Progress in Neurobiology · doi:10.1016/s0301-0082(00)00006-x · Cited by 346
Visualization of neurofibrillary tangle maturity in Alzheimer's disease: A clinicopathologic perspective for biomarker research
Moloney, C. M., Lowe, V. J., & Murray, M. E. (2021) · Alzheimer s & Dementia · doi:10.1002/alz.12321 · Cited by 358
Proteasomal degradation of tau protein
David, D. C., Layfield, R., Serpell, L., Narain, Y., Goedert, M., & Spillantini, M. G. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01137.x · Cited by 327
C-terminal inhibition of tau assembly in vitro and in Alzheimer’s disease
Abraha, A., Ghoshal, N., Gamblin, T. C., Cryns, V. L., Berry, R. W., Kuret, J., & Binder, L. I. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.21.3737 · Cited by 326
Tau gene alternative splicing: expression patterns, regulation and modulation of function in normal brain and neurodegenerative diseases
Andreadis, A. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.08.010 · Cited by 311
Active Caspase-6 and Caspase-6-Cleaved Tau in Neuropil Threads, Neuritic Plaques, and Neurofibrillary Tangles of Alzheimer's Disease
Guo, H., Albrecht, S., Bourdeau, M., Petzke, T., Bergeron, C., & LeBlanc, A. C. (2004) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)63317-2 · Cited by 287
The Generation of a 17 kDa Neurotoxic Fragment: An Alternative Mechanism by which Tau Mediates β-Amyloid-Induced Neurodegeneration
Park, S.-Y., & Ferreira, A. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.1125-05.2005 · Cited by 262
Activated caspase-3 expression in Alzheimer’s and aged control brain: correlation with Alzheimer pathology
Su, J. H., Zhao, M., Anderson, A. J., Srinivasan, A. N., & Cotman, C. W. (2001) · Brain Research · doi:10.1016/s0006-8993(01)02018-2 · Cited by 260
Tau truncation during neurofibrillary tangle evolution in Alzheimer’s disease
Guillozet-Bongaarts, A. L., Garcia-Sierra, F., Reynolds, M. R., Horowitz, P. M., Fu, Y., Wang, T., Cahill, M. E., Bigio, E. H., Berry, R. W., & Binder, L. I. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2004.09.019 · Cited by 256
Truncated tau from sporadic Alzheimer's disease suffices to drive neurofibrillary degeneration in vivo
Žilka, N., Filipčík, P., Koson, P., Fialová, Ľ., Škrabana, R., Žilková, M., Rolkova, G., Kontseková, E., & Novák, M. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.05.029 · Cited by 254
Rho GTPase signalling pathways in the morphological changes associated with apoptosis
Coleman, M. L., & Olson, M. F. (2002) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400987 · Cited by 250
NMDA receptor mediates tau-induced neurotoxicity by calpain and ERK/MAPK activation
Amadoro, G., Ciotti, M. T., Costanzi, M., Cestari, V., Calissano, P., & Canu, N. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0511065103 · Cited by 243
Self-citation
Caspase-9 Activation and Caspase Cleavage of tau in the Alzheimer's Disease Brain
Rohn, T. T., Rissman, R. A., Davis, M. C., Kim, Y., Cotman, C. W., & Head, E. (2002) · Neurobiology of Disease · doi:10.1006/nbdi.2002.0549 · Cited by 248
Tau clearance mechanisms and their possible role in the pathogenesis of Alzheimer disease.
Chesser, A. S., Pritchard, S. M., & Johnson, G. V. W. (2013) · Frontiers in Neurology · doi:10.3389/fneur.2013.00122 · Cited by 219
Early N-Terminal Changes and Caspase-6 Cleavage of Tau in Alzheimer's Disease
Horowitz, P. M., Patterson, K. R., Guillozet-Bongaarts, A. L., Reynolds, M. R., Carroll, C. A., Weintraub, S. T., Bennett, D. A., Cryns, V. L., Berry, R. W., & Binder, L. I. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.1988-04.2004 · Cited by 215
Cerebellar granule cells as a model to study mechanisms of neuronal apoptosis or survival in vivo and in vitro
Contestabile, A. (2002) · The Cerebellum · doi:10.1080/147342202753203087 · Cited by 221
Proapoptotic Effects of Tau Cleavage Product Generated by Caspase-3
Chung, C.-W., Song, Y.-H., Kim, I.-K., Yoon, W. J., Ryu, B. R., Jo, D., Woo, H., Kwon, Y.-K., Kim, H., Gwag, B.-J., et al. (2001) · Neurobiology of Disease · doi:10.1006/nbdi.2000.0335 · Cited by 211
Apoptotic mechanisms in Alzheimer neurofibrillary degeneration: cause or effect?
Dickson, D. W. (2004) · Journal of Clinical Investigation · doi:10.1172/jci22317 · Cited by 212
The Role of Caspase Cleavage of Tau in Alzheimer Disease Neuropathology
Cotman, C. W., Poon, W. W., Rissman, R. A., & Blurton-Jones, M. (2005) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/64.2.104 · Cited by 199
It’s all about tau
Tapia‐Rojas, C., Cabezas-Opazo, F., Deaton, C. A., Vergara, E. H., Johnson, G. V. W., & Quintanilla, R. A. (2018) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.12.005 · Cited by 207
The Neuronal Microtubule‐Associated Protein Tau Is a Substrate for Caspase‐3 and an Effector of Apoptosis
Fasulo, L., Ugolini, G., Visintin, M., Bradbury, A. M., Brancolini, C., Verzillo, V., Novák, M., & Cattaneo, A. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0750624.x · Cited by 195
Self-citation
Procaspase-3 and Poly(ADP)ribose Polymerase (PARP) Are Calpain Substrates
McGinnis, K., Gnegy, M. E., Park, Y. H., Mukerjee, N., & Wang, K. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.1315 · Cited by 179
Activation of Caspase-8 in the Alzheimer's Disease Brain
Rohn, T. T., Head, E., Nesse, W. H., Cotman, C. W., & Cribbs, D. H. (2001) · Neurobiology of Disease · doi:10.1006/nbdi.2001.0449 · Cited by 171
Pseudophosphorylation of tau at serine 422 inhibits caspase cleavage: in vitro evidence and implications for tangle formation in vivo
Guillozet-Bongaarts, A. L., Cahill, M. E., Cryns, V. L., Reynolds, M. R., Berry, R. W., & Binder, L. I. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03784.x · Cited by 180
Proteins released from degenerating neurons are surrogate markers for acute brain damage
Siman, R., McIntosh, T. K., Soltesz, K., Chen, Z., Neumar, R. W., & Roberts, V. L. (2004) · Neurobiology of Disease · doi:10.1016/j.nbd.2004.03.016 · Cited by 164
Revisiting the grammar of Tau aggregation and pathology formation: how new insights from brain pathology are shaping how we study and target Tauopathies
Limorenko, G., & Lashuel, H. A. (2021) · Chemical Society Reviews · doi:10.1039/d1cs00127b · Cited by 168
Contribution of Tau Pathology to Mitochondrial Impairment in Neurodegeneration
Maria Jose Perez, J., Jara, C., & Quintanilla, R. A. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00441 · Cited by 157
Distinct Mechanistic Roles of Calpain and Caspase Activation in Neurodegeneration as Revealed in Mice Overexpressing Their Specific Inhibitors
Higuchi, M., Tomioka, M., Takano, J., Shirotani, K., Iwata, N., Masumoto, H., Maki, M., Itohara, S., & Saido, T. C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500939200 · Cited by 152
Lysine methylation is an endogenous post-translational modification of tau protein in human brain and a modulator of aggregation propensity
Funk, K. E., Thomas, S. N., Schafer, K. N., Cooper, G. L., Liao, Z., Clark, D. J., Yang, A. J., & Kuret, J. (2014) · Biochemical Journal · doi:10.1042/bj20140372 · Cited by 142
The Induction of the TNFα Death Domain Signaling Pathway in Alzheimer's Disease Brain
Zhao, M., Cribbs, D. H., Anderson, A. J., Cummings, B. J., Su, J. H., Wasserman, A., & Cotman, C. W. (2003) · Neurochemical Research · doi:10.1023/a:1022337519035 · Cited by 149
Stress in the brain: novel cellular mechanisms of injury linked to Alzheimer's disease
Chong, Z. Z., Li, F., & Maiese, K. (2005) · Brain Research Reviews · doi:10.1016/j.brainresrev.2004.11.005 · Cited by 152
Accumulation of Aspartic Acid 421 - and Glutamic Acid 391 -Cleaved Tau in Neurofibrillary Tangles Correlates With Progression in Alzheimer Disease
Basurto‐Islas, G., Luna‐Muñoz, J., Guillozet-Bongaarts, A. L., Binder, L. I., Mena, R., & García‐Sierra, F. (2008) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e31817275c7 · Cited by 163
From Alzheimer to Huntington: why is a structural understanding so difficult?
Temussi, P. A., Masino, L., & Pastore, A. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg044 · Cited by 147
Proteasome Involvement and Accumulation of Ubiquitinated Proteins in Cerebellar Granule Neurons Undergoing Apoptosis
Canu, N., Barbato, C., Ciotti, M. T., Serafino, A., Dus, L., & Calissano, P. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-02-00589.2000 · Cited by 144
Self-citation
Molecular mechanisms of ionizing radiation‐induced apoptosis
Watters, D. J. (1999) · Immunology and Cell Biology · doi:10.1046/j.1440-1711.1999.00824.x · Cited by 138
Proteolytic processing of tau
Wang, Y., Garg, S., Mandelkow, E., & Mandelkow�, E. (2010) · Biochemical Society Transactions · doi:10.1042/bst0380955 · Cited by 145
Clathrin adaptor CALM/PICALM is associated with neurofibrillary tangles and is cleaved in Alzheimer’s brains
Ando, K., Brion, J.-P., Stygelbout, V., Suain, V., Authelet, M., Dedecker, R., Chanut, A., Lacor, P., Lavaur, J., Sazdovitch, V., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1111-z · Cited by 136
Quantitative proteomics reveals distinct composition of amyloid plaques in Alzheimer’s disease
Xiong, F., Ge, W., & Ma, C. (2019) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2018.10.006 · Cited by 133
and Alzheimer's disease
Brioni, J. D., Esbenshade, T. A., Garrison, T. R., Bitner, S. R., & Cowart, M. (2010) · Cited by 125
Mutations in the tau gene that cause an increase in three repeat tau and frontotemporal dementia
Stanford, P. M. (2003) · Brain · doi:10.1093/brain/awg090 · Cited by 125
Current status of fluid biomarkers in mild traumatic brain injury
Kulbe, J. R., & Geddes, J. W. (2015) · Experimental Neurology · doi:10.1016/j.expneurol.2015.05.004 · Cited by 128
Analysis of Tau Phosphorylation and Truncation in a Mouse Model of Human Tauopathy
Delobel, P., Lavenir, I., Fraser, G. M., Ingram, E., Holzer, M., Ghetti, B. F., Spillantini, M. G., Crowther, R. A., & Goedert, M. (2007) · American Journal Of Pathology · doi:10.2353/ajpath.2008.070627 · Cited by 124
Anti-Apoptotic Effects of Carotenoids in Neurodegeneration
Park, H., Hayden, M. M., Bannerman, S., Jansen, J., & Crowe-White, K. M. (2020) · Molecules · doi:10.3390/molecules25153453 · Cited by 127
Microtubule-associated Protein MAP1A, MAP1B, and MAP2 Proteolysis during Soluble Amyloid β-Peptide-induced Neuronal Apoptosis
Fifre, A., Sponne, I., Koziel, V., Kriem, B., Yen, F. T., Bihain, B. E., Olivier, J. L., Oster, T., & Pillot, T. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m507378200 · Cited by 124
Transgenic zebrafish model of neurodegeneration
Tomasiewicz, H. G., Flaherty, D. B., Soria, J., & Wood, J. G. (2002) · Journal of Neuroscience Research · doi:10.1002/jnr.10451 · Cited by 117
μ-Calpain activation, DNA fragmentation, and synergistic effects of caspase and calpain inhibitors in protecting hippocampal neurons from ischemic damage
Rami, A., Agarwal, R., Botez, G., & Winckler, J. (2000) · Brain Research · doi:10.1016/s0006-8993(00)02301-5 · Cited by 115
Functional genomic screen and network analysis reveal novel modifiers of tauopathy dissociated from tau phosphorylation
Ambegaokar, S. S., & Jackson, G. R. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr432 · Cited by 113
“Indeed, calpain A has been shown to cleave tau and is reported to be responsible for producing a 17 kDa fragment that may be a highly toxic tau derivative (211,212).”
Background
The role of caspases in Alzheimer’s disease; potential novel therapeutic opportunities
Rohn, T. T. (2010) · APOPTOSIS · doi:10.1007/s10495-010-0463-2 · Cited by 112
Apoptosis and in vitro Alzheimer’s disease neuronal models
Calissano, P., Matrone, C., & Amadoro, G. (2009) · Communicative & Integrative Biology · doi:10.4161/cib.7704 · Cited by 111
Self-citation
Early induction of secondary injury factors causing activation of calpain and mitochondria‐mediated neuronal apoptosis following spinal cord injury in rats
Wingrave, J. M., Schaecher, K. E., Sribnick, E. A., Wilford, G. G., Ray, S. K., Hazen‐Martin, D. J., Hogan, E. L., & Banik, N. L. (2003) · Journal of Neuroscience Research · doi:10.1002/jnr.10607 · Cited by 110
Recent advances on neuronal caspases in development and neurodegeneration
Marks, N., & Berg, M. J. (1999) · Neurochemistry International · doi:10.1016/s0197-0186(99)00061-3 · Cited by 109
Cleavage of Tau by calpain in Alzheimer's disease: the quest for the toxic 17 kD fragment
Garg, S., Timm, T., Mandelkow, E.-M., Mandelkow, E., & Wang, Y. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2010.09.008 · Cited by 103
Caspases as Targets for Anti-Inflammatory and Anti-Apoptotic Drug Discovery
Talanian, R. V., Brady, K. D., & Cryns, V. L. (2000) · Journal of Medicinal Chemistry · doi:10.1021/jm000060f · Cited by 102
Truncation of Tau Protein and its Pathological Significance in Alzheimer's Disease
García‐Sierra, F., Mondragón‐Rodríguez, S., & Basurto‐Islas, G. (2008) · Journal of Alzheimer s Disease · doi:10.3233/jad-2008-14407 · Cited by 109
The Peptidylprolyl cis/trans-Isomerase Pin1 Modulates Stress-induced Dephosphorylation of Tau in Neurons
Galas, M.-C., Dourlen, P., Bégard, S., Ando, K., Blum, D., Hamdane, M., & Buée, L. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601849200 · Cited by 97
Accumulation of caspase cleaved amyloid precursor protein represents an early neurodegenerative event in aging and in Alzheimer's disease
Zhao, M., Su, J. H., Head, E., & Cotman, C. W. (2003) · Neurobiology of Disease · doi:10.1016/j.nbd.2003.07.006 · Cited by 97
The Role of Tau in Neurodegenerative Diseases and Its Potential as a Therapeutic Target
Wolfe, M. S. (2012) · Scientifica · doi:10.6064/2012/796024 · Cited by 105
Blockade of HMG‐CoA reductase activity causes changes in microtubule‐stabilizing protein tau via suppression of geranylgeranylpyrophosphate formation: implications for Alzheimer's disease
Meske, V., Albert, F., Richter, D., Schwarze, J., & Ohm, T. G. (2003) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.2003.02433.x · Cited by 94
Upstream Signaling Pathways Leading to the Activation of Double-stranded RNA-dependent Serine/Threonine Protein Kinase in β-Amyloid Peptide Neurotoxicity
Suen, K.-C., Yu, M.-S., So, K.-F., Chang, R. C.-C., & Hugon, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306503200 · Cited by 95
Neurodegeneration in Alzheimer's disease: caspases and synaptic element interdependence
Bredesen, D. E. (2009) · Molecular Neurodegeneration · doi:10.1186/1750-1326-4-27 · Cited by 103
A peptide containing residues 26–44 of tau protein impairs mitochondrial oxidative phosphorylation acting at the level of the adenine nucleotide translocator
Atlante, A., Amadoro, G., Bobba, A., Lidia de, B. A. R. I., Corsetti, V., Pappalardo, G., Marra, E., Calissano, P., & Passarella, S. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.07.004 · Cited by 93
Self-citation
Molecular basis of Alzheimer's disease
Drouet, B., Pinçon‐Raymond, M., Chambaz, J., & Pillot, T. (2000) · Cellular and Molecular Life Sciences · doi:10.1007/s000180050035 · Cited by 96
Nerve Growth Factor and Alzheimer's Disease: New Facts for an Old Hypothesis
Cattaneo, A., & Calissano, P. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8310-9 · Cited by 93
Self-citation
Cell-based Models To Investigate Tau Aggregation
Lim, S., Haque, M. M., Kim, D., Kim, D. J., & Kim, Y. K. (2014) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2014.09.011 · Cited by 91
Discovering New Treatments for Alzheimer's Disease by Repurposing Approved Medications
Appleby, B. S., & Cummings, J. L. (2013) · Current Topics in Medicinal Chemistry · doi:10.2174/15680266113136660162 · Cited by 78
In vivo activation and nuclear translocation of phosphorylated glycogen synthase kinase‐3β in neuronal apoptosis: links to tau phosphorylation
Elyaman, W., Terro, F., Wong, N. S., & Hugon, J. (2002) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.2002.01899.x · Cited by 79
Tau, where are we now?
Johnson, G. V. W., & Bailey, C. D. C. (2002) · Journal of Alzheimer's Disease · doi:10.3233/jad-2002-4505 · Cited by 61
Microtubule-associated protein tau as a therapeutic target in Alzheimer's disease
Iqbal, K., Gong, C., & Liu, F. (2014) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2014.870156 · Cited by 76
Beyond the Signal Sequence: Protein Routing in Health and Disease
Castro-Fernández, C., Maya‐Núñez, G., & Conn, P. M. (2004) · Endocrine Reviews · doi:10.1210/er.2004-0010 · Cited by 73
Misregulation of Tau Alternative Splicing in Neurodegeneration and Dementia
Andreadis, A. (2006) · Progress in molecular and subcellular biology · doi:10.1007/978-3-540-34449-0_5 · Cited by 72
Tau Phosphorylation and Cleavage in Ethanol-Induced Neurodegeneration in the Developing Mouse Brain
Saito, M., Chakraborty, G., Mao, R.-F., Paik, S.-M., Vadász, C., & Saito, M. (2010) · Neurochemical Research · doi:10.1007/s11064-009-0116-4 · Cited by 72
Understanding molecular mechanisms of proteolysis in Alzheimer's disease: Progress toward therapeutic interventions
Higuchi, M., Iwata, N., & Saido, T. C. (2005) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2005.02.013 · Cited by 73
Hyperglycemia-Induced Tau Cleavage in vitro and in vivo: A Possible Link Between Diabetes and Alzheimer's Disease
Kim, B., Backus, C., Oh, S., & Feldman, E. L. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-121669 · Cited by 74
Accumulation of C-terminally truncated tau protein associated with vulnerability of the perforant pathway in early stages of neurofibrillary pathology in Alzheimer's disease
García‐Sierra, F., Wischik, C. M., Harrington, C. R., Luna‐Muñoz, J., & Mena, R. (2001) · Journal of Chemical Neuroanatomy · doi:10.1016/s0891-0618(01)00096-5 · Cited by 72
Role of N-terminal tau domain integrity on the survival of cerebellar granule neurons
Amadoro, G., Serafino, A., Barbato, C., Ciotti, M. T., Sacco, A., Calissano, P., & Canu, N. (2003) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401314 · Cited by 69
Self-citation
Chronic traumatic encephalopathy-integration of canonical traumatic brain injury secondary injury mechanisms with tau pathology
Kulbe, J. R., & Hall, E. D. (2017) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2017.08.003 · Cited by 70
Tau phosphorylation and proteolysis: Insights and perspectives
Johnson, G. V. W. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-9s326 · Cited by 69
Early release and subsequent caspase‐mediated degradation of cytochrome c in apoptotic cerebellar granule cells
Bobba, A., Atlante, A., Giannattasio, S., Sgaramella, G., Calissano, P., & Marra, E. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01018-2 · Cited by 68
Self-citation
Linking Alterations in Tau Phosphorylation and Cleavage during Neuronal Apoptosis
Rametti‐Lacroux, A., Esclaire, F., Yardin, C., & Terro, F. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408186200 · Cited by 64
Identification of a caspase-derived N-terminal tau fragment in cellular and animal Alzheimer's disease models
Corsetti, V., Amadoro, G., Gentile, A., Capsoni, S., Ciotti, M. T., Cencioni, M. T., Atlante, A., Canu, N., Rohn, T. T., Cattaneo, A., et al. (2008) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2008.03.011 · Cited by 68
Self-citation
Concurrent calpain and caspase-3 mediated proteolysis of αII-spectrin and tau in rat brain after methamphetamine exposure: A similar profile to traumatic brain injury
Warren, M. W., Kobeissy, F. H., Liu, M. C., Hayes, R. L., Gold, M. S., & Wang, K. (2005) · Life Sciences · doi:10.1016/j.lfs.2005.04.058 · Cited by 64
Intracellular and Extracellular Roles for Tau in Neurodegenerative Disease
Hanger, D. P., Lau, D. H. W., Phillips, E. C., Bondulich, M. K., Guo, T., Woodward, B. W., Pooler, A. M., & Noble, W. J. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-132054 · Cited by 66
Caspase activation independent of cell death is required for proper cell dispersal and correct morphology in PC12 cells
Rohn, T. T., Cusack, S. M., Kessinger, S. R., & Oxford, J. T. (2004) · Experimental Cell Research · doi:10.1016/j.yexcr.2003.12.029 · Cited by 62
Active c‐jun N‐terminal kinase induces caspase cleavage of tau and additional phosphorylation by GSK‐3β is required for tau aggregation
Sahara, N., Murayama, M., Lee, B., Park, J., Lagalwar, S., Binder, L. I., & Takashima, A. (2008) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2008.06258.x · Cited by 63
Tau Filament Self-Assembly and Structure: Tau as a Therapeutic Target
Oakley, S. S., Maina, M. B., Marshall, K. E., Al‐Hilaly, Y. K., Harrington, C., Wischik, C. M., & Serpell, L. C. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.590754 · Cited by 59
Tau cleavage and tau aggregation in neurodegenerative disease
Hanger, D. P., & Wray, S. (2010) · Biochemical Society Transactions · doi:10.1042/bst0381016 · Cited by 60
Tau Function and Dysfunction in Neurons
Ávila, J., Lim, F., Moreno, F. J., Belmonte, C., & Cuello, A. C. (2002) · Molecular Neurobiology · doi:10.1385/mn:25:3:213 · Cited by 63
Dual Vulnerability of Tau to Calpains and Caspase-3 Proteolysis Under Neurotoxic and Neurodegenerative Conditions
Liu, M. C., Kobeissy, F. H., Zheng, W., Zhang, Z., Hayes, R. L., & Wang, K. (2010) · ASN NEURO · doi:10.1042/an20100012 · Cited by 59
Conformational changes and cleavage of tau in Pick bodies parallel the early processing of tau found in Alzheimer pathology
Mondragón‐Rodríguez, S., Mena, R., Binder, L. I., Smith, M. A., Perry, G. L., & García‐Sierra, F. (2007) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2007.00853.x · Cited by 60

Authors: Canu, N., Dus, L., Barbato, C., Ciotti, M. T., Brancolini, C., Rinaldi, A. M., Novak, M., Cattaneo, A., Bradbury, A., & Calissano, P.
Affiliations: University of Rome Tor Vergata (IT)
Institute of Neurobiology and Molecular Medicine (IT)
AREA Science Park (IT)
Scuola Internazionale Superiore di Studi Avanzati (IT)
ORCID: Barbato, Christian
Brancolini, Claudio
Rinaldi, Anna M.
Cattaneo, Antonino
Bradbury, Andrew
Venue: The Journal of Neuroscience
Publisher: Society for Neuroscience
Published: 1998-09-15
Volume: 18
Issue: 18
Pages: 7061-7074
ISSN: 0270-6474 (ISSN-L)
1529-2401
DOI: 10.1523/jneurosci.18-18-07061.1998
PMC: PMC6793249
OpenAlex: W2122437043
Cited by: 232
References: 71
Citations by year: 2026: 1 · 2024: 1 · 2023: 1 · 2022: 4 · 2021: 3 · 2020: 6 · 2019: 6 · 2018: 13 · 2017: 7 · 2016: 3 · 2015: 7 · 2014: 13 · 2013: 9 · 2012: 6
FWCI: 8.40
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by-nc-sa
creativecommons.org/licenses/by-nc-sa/4.0/ (vor, 181 d)
Locations: Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Cineca Institutional Research Information System (Tor Vergata University) (submittedVersion, other-oa)
Institutional Research Information System (University of Udine) (submittedVersion)
Scuola Normale Superiore di Pisa (submittedVersion)
Funders: Consiglio Nazionale delle Ricerche
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
Keywords: tau protein, tau cleavage, tau dephosphorylation, cerebellar granule cells, neuronal apoptosis, caspases, calpain, microtubule-associated proteins, Alzheimer's disease
MeSH terms: Alzheimer Disease, Animals, Antineoplastic Agents, Phytogenic, Calpain, Cerebellum, Colchicine, Cysteine Endopeptidases, Cytoskeleton, Enzyme Precursors, Microtubules, Neurons, Oligopeptides, Peptide Fragments, Phosphorylation, Solubility, Cysteine Proteinase Inhibitors, tau Proteins, Rats, Wistar, Apoptosis, Paclitaxel, Caspases, Rats, Caspase 3

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

Tau Cleavage and Dephosphorylation in Cerebellar Granule Neurons Undergoing Apoptosis

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