Tau Cleavage and Dephosphorylation in Cerebellar Granule Neurons Undergoing Apoptosis

Canu, Nadia; Dus, Laura; Barbato, Christian; Ciotti, Maria T.; Brancolini, Claudio; Rinaldi, Anna M.; Novak, Michal; Cattaneo, Antonino; Bradbury, Andrew; Calissano, Pietro

doi:10.1523/jneurosci.18-18-07061.1998

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

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 +2 more·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?

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.
“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).”
From Functional genomic screen and network analysis reveal novel modifiers of tauopathy dissociated from tau phosphorylation (2011) · cites this paper as [212]
The section 'Identification of the proteases responsible for producing the 17 kDa fragment' reports that purified calpain cleaves tau to produce a 17 kDa band matching the one seen during neuronal apoptosis (page not indexed). Our copy does not identify the protease specifically as 'calpain A' or describe the fragment as highly toxic; the Discussion instead suggests a possible role for tau cleavage in cytoskeletal breakdown. (LLM, conf=0.88)
Experimental — accuracy not yet measured

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 315,771 · see citing works
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 · see citing works
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 · see citing works
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 15,673 · see citing works
Apoptosis in the Pathogenesis and Treatment of Disease
Thompson, C. B. (1995) · Science · doi:10.1126/science.7878464 · Cited by 6,524 · see citing works
Caspases: the executioners of apoptosis
Cohen, G. M. (1997) · Biochemical Journal · doi:10.1042/bj3260001 · Cited by 4,720 · see citing works
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 · see citing works
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 · see citing works
Mechanisms and Genes of Cellular Suicide
Steller, H. (1995) · Science · doi:10.1126/science.7878463 · Cited by 2,465 · see citing works
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 · see citing works
A68: a Major Subunit of Paired Helical Filaments and Derivatized Forms of Normal Tau
Lee, V. M.-Y., Balin, B. J., Otvos, L., & Trojanowski, J. Q. (1991) · Science · doi:10.1126/science.1899488 · Cited by 1,418 · cited 2× · see citing works
“This is reminiscent of the A68 fragment found in AD (Lee et al., 1991).”
BackgroundResult
Tau proteins of alzheimer paired helical filaments: Abnormal phosphorylation of all six brain isoforms
Goedert, M., Spillantini, M. G., Cairns, N. J., & Crowther, R. A. (1992) · Neuron · doi:10.1016/0896-6273(92)90117-v · Cited by 1,114 · see citing works
Apoptosis
Cohen, J. (1993) · Immunology Today · doi:10.1016/0167-5699(93)90214-6 · Cited by 986 · see citing works
Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau.
Drechsel, D. N., Hyman, A. A., Cobb, M. H., & Kirschner, M. W. (1992) · Molecular Biology of the Cell · doi:10.1091/mbc.3.10.1141 · Cited by 971 · see citing works
Rat monoclonal antitubulin antibodies derived by using a new nonsecreting rat cell line.
Kilmartin, J. V., Wright, B., & Milstein, C. (1982) · The Journal of Cell Biology · doi:10.1083/jcb.93.3.576 · Cited by 942 · see citing works
Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease.
Wischik, C. M., Novak, M., Thøgersen, H. C., Edwards, P. C., Runswick, M. J., Jakes, R., Walker, J. E., Milstein, C., Roth, M., & Klug, A. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.12.4506 · Cited by 939 · see citing works
Expression of separate isoforms of human tau protein: correlation with the tau pattern in brain and effects on tubulin polymerization.
Goedert, M., & Jakes, R. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb07870.x · Cited by 929 · cited 2× · see citing works
“binding repeats (Goedert and Jakes, 1990), (2) the proline-rich”
Background
Phosphorylation affects the ability of tau protein to promote microtubule assembly.
Lindwall, G., & Cole, R. D. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42989-9 · Cited by 901 · see citing works
Induction of apoptosis in cerebellar granule neurons by low potassium: inhibition of death by insulin-like growth factor I and cAMP.
D'Mello, S. R., Galli, C., Ciotti, T., & Calissano, P. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.23.10989 · Cited by 892 · see citing works
Self-citation
Phosphorylation of Ser262 strongly reduces binding of tau to microtubules: Distinction between PHF-like immunoreactivity and microtubule binding
Biernat, J., Gustke, N., Drewes, G., Mandelkow, E., & Mandelkow, E. (1993) · Neuron · doi:10.1016/0896-6273(93)90279-z · Cited by 796 · see citing works
Tau protein function in living cells.
Drubin, D. G., & Kirschner, M. W. (1986) · The Journal of Cell Biology · doi:10.1083/jcb.103.6.2739 · Cited by 745 · see citing works
Calpain: new perspectives in molecular diversity and physiological‐pathological involvement
Saido, T. C., Sorimachi, H., & Suzuki, K. (1994) · The FASEB Journal · doi:10.1096/fasebj.8.11.8070630 · Cited by 669 · see citing works
Domains of tau Protein and Interactions with Microtubules
Gustke, N., Trinczek, B., Biernat, J., Mandelkow, E.-M., & Mandelkow, E. (1994) · Biochemistry · doi:10.1021/bi00198a017 · Cited by 655 · see citing works
Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain.
Brandt, R., Léger, J. G., & Lee, G. S. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.131.5.1327 · Cited by 624 · see citing works
Immunohistochemical evidence for apoptosis in Alzheimer's disease.
Su, J., Anderson, A., Cummings, B. J., & Cotman, C. (1994) · NeuroReport · doi:10.1097/00001756-199412000-00031 · Cited by 607 · see citing works
Widespread activation of calcium-activated neutral proteinase (calpain) in the brain in Alzheimer disease: a potential molecular basis for neuronal degeneration.
Saito, K., Elce, J. S., Hamos, J. E., & Nixon, R. A. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.7.2628 · Cited by 579 · see citing works
Hydrofluoric acid-treated tau PHF proteins display the same biochemical properties as normal tau.
Greenberg, S. G., Davies, P., Schein, J., & Binder, L. I. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48531-6 · Cited by 542 · see citing works
Tau Consists of a Set of Proteins with Repeated C-Terminal Microtubule-Binding Domains and Variable N-Terminal Domains
Himmler, A., Drechsel, D. N., Kirschner, M. W., & Martin, D. W. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.4.1381-1388.1989 · Cited by 535 · see citing works
Glycogen synthase kinase‐3 and the Alzheimer‐like state of microtubule‐associated protein tau
Mandelkow, E.-M., Drewes, G., Biernat, J., Gustke, N., Van Lint, J., Vandenheede, J. R., & Mandelkow, E. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)81496-9 · Cited by 515 · see citing works
Evidence for Apoptotic Cell Death in Alzheimer's Disease
Smale, G., Nichols, N. R., Brady, D. R., Finch, C. E., & Horton, W. E. (1995) · Experimental Neurology · doi:10.1006/exnr.1995.1025 · Cited by 488 · see citing works
Calpain activation in apoptosis
Squier, M. K. T., Miller, A. C. K., Malkinson, A. M., & Cohen, J. (1994) · Journal of Cellular Physiology · doi:10.1002/jcp.1041590206 · Cited by 431 · see citing works
Non-erythroid α-spectrin breakdown by calpain and interleukin 1 β-converting-enzyme-like protease(s) in apoptotic cells: contributory roles of both protease families in neuronal apoptosis
Nath, R., Raser, K. J., STAFFORD, D., Hajimohammadreza, I., Posner, A., Allen, H., Talanian, R. V., Yuen, P., Gilbertsen, R. B., & Wang, K. (1996) · Biochemical Journal · doi:10.1042/bj3190683 · Cited by 425 · see citing works
Microtubule organization and dynamics dependent on microtubule-associated proteins
Hirokawa, N. (1994) · Current Opinion in Cell Biology · doi:10.1016/0955-0674(94)90119-8 · Cited by 412 · see citing works
Autoradiographic localization and depolarization-induced release of acidic amino acids in differentiating cerebellar granule cell cultures
Levi, G., Aloisi, F., Ciotti, M. T., & Gallo, V. (1984) · Brain Research · doi:10.1016/0006-8993(84)90737-6 · Cited by 402 · see citing works
Self-citation
Apoptosis in cerebellar granule cells is blocked by high KCl, forskolin, and IGF-1 through distinct mechanisms of action: the involvement of intracellular calcium and RNA synthesis
Galli, C., Meucci, O., Scorziello, A., Werge, T., Calissano, P., & Schettini, G. (1995) · Journal of Neuroscience · doi:10.1523/jneurosci.15-02-01172.1995 · Cited by 400 · see citing works
Self-citation
Molecular characterization of the minimal protease resistant tau unit of the Alzheimer's disease paired helical filament
Novak, M., Kabat, J., & Wischik, C. M. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05665.x · Cited by 398 · see citing works
Glycosylation of microtubule–associated protein tau: An abnormal posttranslational modification in Alzheimer's disease
Wang, J.-Z., Grundke-Iqbal, I., & Iqbal, K. (1996) · Nature Medicine · doi:10.1038/nm0896-871 · Cited by 360 · see citing works
Monoclonal antibodies with selective specificity for Alzheimer Tau are directed against phosphatase-sensitive epitopes
Mercken, M. H., Vandermeeren, M., Lübke, U., Six, J., Boons, J., VOORDE, A. V. D., Martin, J., & Gheuens, J. (1992) · Acta Neuropathologica · doi:10.1007/bf00227819 · Cited by 356 · see citing works
Detection of Phosphorylated Ser262 in Fetal Tau, Adult Tau, and Paired Helical Filament Tau
Seubert, P., Mawal-Dewan, M., Barbour, R., Jakes, R., Goedert, M., Johnson, G. V. W., Litersky, J. M., Schenk, D., Lieberburg, I., Trojanowski, J. Q., et al. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.32.18917 · Cited by 345 · see citing works
Pituitary Adenylate Cyclase-Activating Polypeptide (PACAP-38) Protects Cerebellar Granule Neurons from Apoptosis by Activating the Mitogen-Activated Protein Kinase (MAP Kinase) Pathway
Villalba, M., Bockaert, J., & Journot, L. (1997) · Journal of Neuroscience · doi:10.1523/jneurosci.17-01-00083.1997 · Cited by 334 · see citing works
Analysis of microtubule-associated protein tau glycation in paired helical filaments.
Ledesma, M. D., Bonay, P., Colaço, C., & Avila, J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31849-5 · Cited by 333 · cited 1× · see citing works
“…posttranslational changes, including physiological phosphorylation and glycosylation (Lovestone and Reynolds, 1997), as well as pathological phosphorylation (Grundke-Iqbal et al., 1986a), glycosylation (Wang et al., 1996), glycation (Ledesma et al., 1994), and truncation (Novak et al., 1993) in AD.”
Background
Molecular characterization of microtubule-associated proteins tau and map2
Goedert, M., Crowther, R. A., & Garner, C. C. (1991) · Trends in Neurosciences · doi:10.1016/0166-2236(91)90105-4 · Cited by 315 · see citing works
Proteasomes play an essential role in thymocyte apoptosis.
Grimm, L. M., Goldberg, A. L., Poirier, G. G., Schwartz, L. M., & Osborne, B. A. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00757.x · Cited by 309 · see citing works
Correlates of p53- and Fas (CD95)-mediated apoptosis in Alzheimer's disease
de la Monte, S. M., Sohn, Y. K., & Wands, J. R. (1997) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(97)00131-7 · Cited by 307 · see citing works
A novel pool of protein phosphatase 2A is associated with microtubules and is regulated during the cell cycle.
Sontag, E., Nunbhakdi‐Craig, V., Bloom, G. S., & Mumby, M. C. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.128.6.1131 · Cited by 301 · see citing works
Discussion
Lovestone, S., & Reynolds, C. H. (1997) · Neuroscience · doi:10.1016/s0306-4522(96)00577-5 · Cited by 278 · see citing works
Dephosphorylation of Alzheimer paired helical filaments by protein phosphatase-2A and -2B
Wang, J.-Z., Gong, C.-X., Zaidi, T., Grundke-Iqbal, I., & Iqbal, K. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.9.4854 · Cited by 269 · see citing works
Involvement of the proteasome in the programmed cell death of NGF‐deprived sympathetic neurons.
Sadoul, R., Fernandez, P.-A., Quiquerez, A., Martinou, I., Maki, M., Schröter, M., Becherer, J. D., Irmler, M., Tschopp, J. F., & Martinou, J. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00758.x · Cited by 260 · see citing works
The role of estrogens on the proliferation of human breast tumor cells (MCF-7)
Soto, A. M., & Sonnenschein, C. (1985) · Journal of Steroid Biochemistry · doi:10.1016/0022-4731(85)90265-1 · Cited by 254 · see citing works
Dismantling Cell–Cell Contacts during Apoptosis Is Coupled to a Caspase-dependent Proteolytic Cleavage of β-Catenin
Brancolini, C., Lazarević, D., Rodriguez, J., & Schneider, C. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.139.3.759 · Cited by 236 · see citing works
Self-citation
Difference between the tau protein of Alzheimer paired helical filament core and normal tau revealed by epitope analysis of monoclonal antibodies 423 and 7.51.
Novak, M., Jakes, R., Edwards, P. C., Milstein, C., & Wischik, C. (1991) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.88.13.5837 · Cited by 217 · see citing works
Self-citation
Specific Cleavage of α-Fodrin during Fas- and Tumor Necrosis Factor-induced Apoptosis Is Mediated by an Interleukin-1β-converting Enzyme/Ced-3 Protease Distinct from the Poly(ADP-ribose) Polymerase Protease
Cryns, V. L., Bergeron, L., Zhu, H., Li, H., & Yuan, J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.49.31277 · Cited by 209 · see citing works
Recognition of the minimal epitope of monoclonal antibody Tau‐1 depends upon the presence of a phosphate group but not its location
Szendrei, G., Lee, V. M. Y., & Otvos, L. (1993) · Journal of Neuroscience Research · doi:10.1002/jnr.490340212 · Cited by 204 · see citing works
Phosphorylation by cAMP-dependent protein kinase inhibits the degradation of tau by calpain.
Litersky, J. M., & Johnson, G. V. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45982-0 · Cited by 201 · see citing works
Tau in Alzheimer neurofibrillary tangles. N- and C-terminal regions are differentially associated with paired helical filaments and the location of a putative abnormal phosphorylation site
Brion, J., Hanger, D. P., Bruce, M. T., Couck, A. M., Flament-Durand, J., & Anderton, B. H. (1991) · Biochemical Journal · doi:10.1042/bj2730127 · Cited by 168 · see citing works
Calpain inhibitors, but not caspase inhibitors, prevent actin proteolysis and DNA fragmentation during apoptosis
Villa, P., Henzel, W. J., Sensenbrenner, M., Henderson, C. E., & Pettmann, B. (1998) · Journal of Cell Science · doi:10.1242/jcs.111.6.713 · Cited by 157 · see citing works
Dephosphorylation of Alzheimer's disease abnormally phosphorylated tau by protein phosphatase-2A
Gong, C., Grundke, I., & Iqbal, K. (1994) · Neuroscience · doi:10.1016/0306-4522(94)90400-6 · Cited by 156 · see citing works
Alzheimer paired helical filaments Restoration of the biological activity by dephosphorylation
Iqbal, K., Zaidi, T., Bancher, C., & Grundke, I. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00650-4 · Cited by 150 · see citing works
Alzheimer's Disease Abnormally Phosphorylated τ Is Dephosphorylated by Protein Phosphatase‐2B (Calcineurin)
Gong, C., Singh, T. J., Grundke, I., & Iqbal, K. (1994) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1994.62020803.x · Cited by 145 · see citing works
The tubulin-binding sequence of brain microtubule-associated proteins, tau and MAP-2, is also involved in actin binding
Correas, I., Padilla, R., & Avila, J. (1990) · Biochemical Journal · doi:10.1042/bj2690061 · Cited by 144 · see citing works
Colchicine Induces Apoptosis in Cerebellar Granule Cells
Bonfoco, E., Ceccatelli, S., Manzo, L., & Nicotera, P. (1995) · Experimental Cell Research · doi:10.1006/excr.1995.1147 · Cited by 143 · see citing works
The phosphorylation state of tau in the developing rat brain is regulated by phosphoprotein phosphatases.
Mawal-Dewan, M., Henley, J., VOORDE, A. V. D., Trojanowski, J. Q., & Lee, V. M. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47378-4 · Cited by 140 · see citing works
Inhibition of activation-induced programmed cell death and restoration of defective immune responses of HIV+ donors by cysteine protease inhibitors.
Sarin, A., Clerici, M., Blatt, S. P., Hendrix, C. W., Shearer, G. M., & Henkart, P. A. (1994) · The Journal of Immunology · doi:10.4049/jimmunol.153.2.862 · Cited by 130 · see citing works
Development of a method for measuring cell number: Application to CNS primary neuronal cultures
Volonté, C., Ciotti, M. T., & Battistini, L. (1994) · Cytometry · doi:10.1002/cyto.990170311 · Cited by 86 · see citing works
Self-citation
Brain μ‐Calpain Autolysis During Global Cerebral Ischemia
Neumar, R. W., Hagle, S. M., DeGracia, D. J., Krause, G. S., & White, B. C. (1996) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1996.66010421.x · Cited by 73 · see citing works
Interaction between microtubule-associated protein tau and spectrin
Carlier, M., Simon, C., Cassoly, R., & Pradel, L. (1984) · Biochimie · doi:10.1016/0300-9084(84)90007-5 · Cited by 63 · see citing works
The role of growth factors in the suppression of active cell death in the prostate: an hypothesis
Guenette, R. S., & Tenniswood, M. (1994) · Biochemistry and Cell Biology · doi:10.1139/o94-074 · Cited by 48 · see citing works
Modulation of Non‐N‐Methyl‐D‐Aspartate Receptors in Cultured Cerebellar Granule Cells
Gallo, V., Giovannini, C., & Levi, G. (1990) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1990.tb01213.x · Cited by 45 · see citing works
Adenosine and ADP prevent apoptosis in cultured rat cerebellar granule cells
Vitolo, O. V., Ciotti, M. T., Galli, C., Borsello, T., & Calissano, P. (1998) · Brain Research · doi:10.1016/s0006-8993(98)00713-6 · Cited by 43 · see citing works
Self-citation
Co-localization of truncated tau and DNA fragmentation in Alzheimerʼs disease neurones
Ugolini, G., Cattaneo, A., & Novák, M. (1997) · Neuroreport · doi:10.1097/00001756-199712010-00010 · Cited by 40 · see citing works
Self-citation
Site-specific regulation of Alzheimer-like tau phosphorylation in living neurons
Burack, M. A., & Halpain, S. (1996) · Neuroscience · doi:10.1016/0306-4522(95)00546-3 · Cited by 34 · see citing works

Flagged first, then by citations

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 2,617 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 645 · see citing works
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 · see citing works
Structure and Pathology of Tau Protein in Alzheimer Disease
Kolarova, M., García‐Sierra, F., Bartoš, A., Říčný, J., & Řı́pová, D. (2012) · International Journal of Alzheimer s Disease · doi:10.1155/2012/731526 · Cited by 473 · see citing works
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 440 · see citing works
Tau, tangles, and Alzheimer's disease.
Binder, L., Guillozet-Bongaarts, A. L., García-Sierra, F., & Berry, R. (2005) · Biochimica et Biophysica Acta · doi:10.1016/j.bbadis.2004.08.014 · Cited by 443 · see citing works
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 349 · see citing works
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 337 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 242 · see citing works
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 · see citing works
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 · see citing works
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 215 · see citing works
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 · see citing works
Apoptotic mechanisms in Alzheimer neurofibrillary degeneration: cause or effect?
Dickson, D. W. (2004) · Journal of Clinical Investigation · doi:10.1172/jci22317 · Cited by 201 · see citing works
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 · see citing works
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 195 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 169 · see citing works
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 · see citing works
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 162 · see citing works
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 153 · see citing works
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 154 · see citing works
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 · see citing works
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 · see citing works
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 149 · see citing works
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 150 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Proteolytic processing of tau
Wang, Y., Garg, S., Mandelkow, E., & Mandelkow�, E. (2010) · Biochemical Society Transactions · doi:10.1042/bst0380955 · Cited by 139 · see citing works
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 · see citing works
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 · see citing works
and Alzheimer's disease
Brioni, J. D., Esbenshade, T. A., Garrison, T. R., Bitner, S. R., & Cowart, M. (2010) · Cited by 125 · see citing works
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 · see citing works
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 124 · see citing works
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 120 · see citing works
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 125 · see citing works
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 117 · see citing works
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 116 · see citing works
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 · see citing works
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 · see citing works
“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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 101 · see citing works
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 · see citing works
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. (2003) · Neurobiology of Disease · doi:10.1016/j.nbd.2003.07.006 · Cited by 102 · see citing works
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 97 · see citing works
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 · see citing works
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 · see citing works
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 94 · see citing works
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 · see citing works
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 89 · see citing works
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 88 · see citing works
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 84 · see citing works
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 · see citing works
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 · see citing works
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 78 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 72 · see citing works
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 71 · see citing works
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 · see citing works
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 · see citing works
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 69 · see citing works
Tau phosphorylation and proteolysis: Insights and perspectives
Johnson, G. (2006) · Journal of Alzheimer's Disease · doi:10.3233/jad-2006-9s326 · Cited by 73 · see citing works
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 · see citing works
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 · see citing works
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 64 · see citing works
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 · see citing works
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 62 · see citing works
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 · see citing works
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 62 · see citing works
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 57 · see citing works
Tau cleavage and tau aggregation in neurodegenerative disease
Hanger, D. P., & Wray, S. (2010) · Biochemical Society Transactions · doi:10.1042/bst0381016 · Cited by 60 · see citing works
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 60 · see citing works
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 · see citing works
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 58 · see citing works

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 · see citing works
In vitro cultured neurons for molecular studies correlating apoptosis with events related to Alzheimer disease
Canu, N., & Calissano, P. (2003) · The Cerebellum · doi:10.1080/14734220310004289 · Cited by 32 · see citing works
Self-citation
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 · see citing works
Self-citation
Modifications of tau protein during neuronal cell death
Lorío, G., Ávila, J., & Díaz‐Nido, J. (2001) · Journal of Alzheimer s Disease · doi:10.3233/jad-2001-3607 · Cited by 12 · see citing works
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 · see citing works

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: Health Sciences › Medicine › Physiology › 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

Integrity signals

Claims the paper makes

Claims other papers make about this one

Self-check

Cites

Cited by

Related

Record

About these checks