Proteolysis of tau by calpain

Microtubule-associated protein tau. A component of Alzheimer paired helical filaments.

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Phosphorylation affects the ability of tau protein to promote microtubule assembly.

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Accumulation of abnormally phosphorylated τ precedes the formation of neurofibrillary tangles in Alzheimer's disease

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Microtubule-Associated Proteins: Their Potential Role In Determining Neuronal Morphology

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Microtubule-Associated Proteins

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Phosphorylation determines two distinct species of tau in the central nervous system

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Structure of the Bovine Tau Gene: Alternatively Spliced Transcripts Generate a Protein Family

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Calcium‐activated neutral protease and its endogenous inhibitor Activation at the cell membrane and biological function

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Dephosphorylation of neurofilament proteins enhances their susceptibility to degradation by calpain

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Separation and characterization of microtubule proteins from calf brain

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Poliovirus infection results in structural alteration of a microtubule-associated protein

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Tau and HMW tau phosphorylation and compartmentalization in apoptotic neuronal PC12 cells

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Tau-related protein present in paired helical filaments has a decreased tubulin binding capacity as compared with microtubule-associated protein tau

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Caspase-3-mediated cleavage of PHF-1 tau during apoptosis irrespective of excitotoxicity and oxidative stress: an implication to Alzheimer's disease

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Oxidation of thiol-proteases in the hippocampus of Alzheimer’s disease

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Immunological characterization of the region of tau protein that is bound to Alzheimer paired helical filaments

Caputo, C. B., Wischik, C. M., Novak, M. A., Scott, C. W., Brunner, W. F., Garcini, E. M. D., Lo, M. M. S., Norris, T. E., & Salama, A. I. (1992) · Neurobiology of Aging · doi:10.1016/0197-4580(92)90039-z · Cited by 26

Calpastatin Overexpression Protects Axonal Transport in an In Vivo Model of Traumatic Axonal Injury

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Concentration-dependent effects of proteasomal inhibition on tau processing in a cellular model of tauopathy.

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Characterization of microtubule-associated protein phosphoisoforms present in isolated growth cones

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Where do Alzheimer s plaques and tangles come from aging-induced protein degradation inefficiency

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Involvement of calpain in AMPA-induced toxicity to rat cerebellar Purkinje neurons

Mansouri, B., Henne, W. M., Oomman, S. K., Bliss, R., Attridge, J., Finckbone, V., Zeitouni, T., Hoffman, T., Bahr, B. A., Strahlendorf, H. K., et al. (2006) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2006.11.032 · Cited by 21

Tau Is Truncated in Five Regions of the Normal Adult Human Brain

Friedrich, M. G., Skora, A. S., Hancock, S. E., Mitchell, T. W., Else, P. L., & Truscott, R. J. W. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22073521 · Cited by 21

Compromised mitochondrial function results in dephosphorylation of tau through a calcium-dependent process in rat brain cerebral cortical slices

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Phosphorylation events mediated by protein kinase Cα and ε participate in regulation of tau steady‐state levels and generation of certain “Alzheimer‐like” phospho‐epitopes

Boyce, J. J., & Shea, T. B. (1997) · International Journal of Developmental Neuroscience · doi:10.1016/s0736-5748(97)00010-5 · Cited by 18

Analysis of Human Tau in Cerebrospinal Fluid

Hanisch, K., Soininen, H., Alafuzoff, I., & Hoffmann, R. (2010) · Journal of Proteome Research · doi:10.1021/pr901002t · Cited by 17

Endogenous overproduction of β-amyloid induces tau hyperphosphorylation and decreases the solubility of tau in N2a cells

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Profiling of calpain activity with a series of FRET-based substrates

Kelly, J. C., Cuerrier, D., Graham, L. A., Campbell, R. L., & Davies, P. L. (2009) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.06.013 · Cited by 16

The effect of postmortem delay on the distribution of microtubule-associated proteins τ, MAP2, and MAP5 in the rat

Irving, E. A., McCulloch, J., & Dewar, D. (1997) · Molecular and Chemical Neuropathology · doi:10.1007/bf02815102 · Cited by 15

Protein Truncation as a Common Denominator of Human Neurodegenerative Foldopathies

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Rapid, single-step procedure for the identification of transglutaminase-mediated isopeptide crosslinks in amino acid digests

Miller, M. L., & Johnson, G. V. W. (1999) · Journal of Chromatography B Biomedical Sciences and Applications · doi:10.1016/s0378-4347(99)00267-4 · Cited by 15

Early but not late conformational changes of tau in association with ubiquitination of neurofibrillary pathology in Alzheimer’s disease brains

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Ischemic preconditioning attenuates of ischemia-induced degradation of spectrin and tau: implications for ischemic tolerance

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Dicyclomine, an M1 Muscarinic Antagonist, Reduces Biomarker Levels, But Not Neuronal Degeneration, in Fluid Percussion Brain Injury

Cox, C. D., West, E. J., Liu, M. C., Wang, K., Hayes, R. L., & Lyeth, B. G. (2008) · Journal of Neurotrauma · doi:10.1089/neu.2008.0671 · Cited by 14

Down-Regulation of Brain-Pancreas Relative Protein in Diabetic Rats and by High Glucose in PC12 Cells: Prevention by Calpain Inhibitors

Tie, L., Xu, Y., Lin, Y.-H., Yao, X., Wu, H.-L., Li, Y.-H., Shen, Z.-F., Yu, H.-M., & Li, X.-J. (2008) · Journal of Pharmacological Sciences · doi:10.1254/jphs.fp0071092 · Cited by 14

Effect of Ca2+ on the microtubule‐severing enzyme p60‐katanin. Insight into the substrate‐dependent activation mechanism

Iwaya, N., Akiyama, K., Goda, N., Tenno, T., Fujiwara, Y., Hamada, D., Ikura, T., Shirakawa, M., & Hiroaki, H. (2012) · FEBS Journal · doi:10.1111/j.1742-4658.2012.08528.x · Cited by 14

Platelet-derived growth factor delays oligodendrocyte differentiation and axonal myelination in vivo in the anterior medullary velum of the developing rat

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Calpain inhibitors reduce depolarization induced loss of tau protein in primary septo-hippocampal cultures

Kampfl, A., Whitson, J. S., Zhao, X., Posmantur, R. M., Clifton, G. L., & Hayes, R. L. (1995) · Neuroscience Letters · doi:10.1016/0304-3940(95)11745-i · Cited by 14

Characterization of Phosphorylation Dependent Antibodies To Study the Phosphorylation Status of the Tau Protein

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Oxidative stress inhibits ionomycin‐mediated cell death in cortical neurons

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Comparison of Ca2+-activated proteinase enzyme and endogeneous inhibitor activity in brain tissue from normal and Alzheimer's disease cases

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Cisteína proteasas y neurodegeneración

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The C-Terminus of Tau Protein Plays an Important Role in Its Stability and Toxicity

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Measurement of Calpain Activity In Vitro and In Situ Using a Fluorescent Compound and Tau as Substrates

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Alzheimers Disease: Review of Emerging Treatment Role for Intravenous Immunoglobulins

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Calpain in Traumatic Brain Injury: From Cinderella to Central Player

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Thiol-protease oxidation in age-related neuropathology

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Regulation of tau proteolysis by phosphatases

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Alterations of choline acetyltransferase, phosphoinositide hydrolysis, and cytoskeletal proteins in rat brain in response to colchicine administration

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hiPSC-neurons recapitulate the subtype-specific cell intrinsic nature of susceptibility to neurodegenerative disease-relevant aggregation

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Mapping of phosphorylation-dependent anti-tau monoclonal antibodies in immunoblots using human tau-constructs synthesized by native chemical ligation

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Purification of bovine Tau versions by affinity chromatography

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Inhibition of proteolysis enhances aluminum-induced perikaryal neurofilament accumulation but does not enhance tau accumulation

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Influence of Phospholipids and Sequential Kinase Activities on Tau in Vitro

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The microtubule cytoskeleton in neuronal development and degeneration

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Metal (Fe3+) affinity chromatography: differential adsorption of tau phosphoproteins

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Usefulness of Cerebrospinal Fluid Biomarkers in Diagnosis of Early Alzheimer's Disease

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Tau Oligomers as Potential Drug Target for Alzheimer Disease (AD) Treatment

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Brain casein kinase 2: Affinity purification procedure using immobilized polyethylenimine

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Regulation of neuronal differentiation by the α and ϵ isoforms of protein kinase C

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Potential Role of Hyperactivation of Signal Transduction Pathways in Alzheimer’s Disease: Protein Kinase C Regulates PHF-like Phosphorylation of Tau within Neuronal Cells

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A Quantitative Analysis of Insulin Signaling in Neurodegeneration

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Análisis de imagen in vivo, a partir de Resonancia Magnética, de los Procesos Neurodegenerativos que acontecen en ratones knock out para la proteína sustrato del receptor insulínico IRS-2

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The Contribution of Ammonia to Methamphetamine Neurotoxicity

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The Effect of Acute LPS-Induced Immune Activation and Brain Insulin Signaling Disruption in a Diabetic Model of Alzheimer's Disease

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CALPAIN: TRANSITIONING FROM THE USE OF THE PROTEASE CORE TO THE FULL-LENGTH ENZYME FOR THE DEVELOPMENT OF SPECIFIC SUBSTRATES AND INHIBITORS

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Investigating the mechanisms underlying Alzheimer's disease using a novel organotypic brain slice culture model

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Insight into the substrate-dependent activation mechanism

Iwaya, N., Akiyama, K., Goda, N., Tenno, T., Fujiwara, Y., Hamada, D., Ikura, T., Shirakawa, M., & Hiroaki, H. (2012)

Author Index

(2005) · FEBS Letters · doi:10.1016/s0014-5793(05)01501-2

Étude de la toxicité neuronale induite par la protéine Tau dans la maladie d’Alzheimer, sur un modèle Invertébré : Drosophila melanogaster

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Untitled work

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Effect of Calpain on The Degradation of Tau in Rat Brain Co rtex Extracts

Fang, Z. (2003) · PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS

Degradation of Microtubule‐Associated Protein 2 and Brain Spectrin by Calpain: A Comparative Study

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Proteolysis of tubulin and microtubule-associated proteins 1 and 2 by calpain I and II. Difference in sensitivity of assembled and disassembled microtubules

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Calpain processing of brain microtubules from the Atlantic Cod, Gadus morhua

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Proteolytic degradation of tau via calpain may be involved in tau-induced neurodegeneration

Reinecke, J. B., & Steinhilb, M. L. (2007)