Caspase cleavage of tau: Linking amyloid and neurofibrillary tangles in Alzheimer's disease

By T. C. Gamblin, Feng Chen, A. Zambrano, A. Abraha, Sarita Lagalwar, A. Guillozet, Meiling Lu, Yifan Fu, F. García-Sierra, Nichole E Lapointe and 4 more. Proceedings of the National Academy of Sciences of the United States of America, 2003

873 citations recorded by the source corpus.

Subfields: Biomaterials, Molecular Biology, Physiology

View Paper: https://www.semanticscholar.org/paper/26e29cd1fe343ac31fadd99bbeee6d5280dc65ce

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

1. Fei Liu
2. C. Gong
3. I. Grundke‐Iqbal
4. E. Mandelkow
5. L. Mucke

In Physiology

1. Fei Liu
2. C. Gong
3. I. Grundke‐Iqbal
4. L. Mucke
5. Ludovic Martin
6. X. Latypova
7. F. Terro
8. E. Mandelkow

Citations in the corpus

• Neuronal Cell Death. (2018, neutral): “, caspases (138, 232, 384) or asparagine endopeptidase (797).”
• Amyloid β-based therapy for Alzheimer’s disease: challenges, successes and future (2023, background): “In addition to its stimulatory effect on tau phosphorylation, Aβ also affected tau oligomerization and tangle formation.(134) Aβ triggered caspase-3 (CASP3)-induced cleavage of tau at Asp421 to yield an N-terminal product, which self-aggregated and further assembled into neurotoxic oligomers.”
• Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020, background): “Abbreviations AD: Alzheimer’s disease; APOE: Apolipoprotein E; Aβ: β-Amyloid; APP: Amyloid precursor protein; KCC2: K-Cl cotransporter 2; GABA : γaminobutyric acid; sAPP: Soluble amyloid precursor proteins; CNS: Central nervous system; PS1/2: Presenilins 1/2; CSF: Cerebral spinal fluid; LRP1: Lowden”
• Structural Polymorphism of 441-Residue Tau at Single Residue Resolution (2009, background): “Notably, truncation of the C terminus behind Asp(421) was suggested to be an early molecular event in tau aggregation [51], suggesting that the conformational properties of (428)Leu-Ala(437) can influence proteolytic cleavage.”
• Post-translational modifications of tau protein: implications for Alzheimer's disease. (2011, positive): “contribute to tau aggregation in AD brains (Gamblin et al., 2003; Rissman et al., 2004).”
• The Many Faces of Tau (2011, background): “Ab treatment of cortical neurons causes caspase cleavage of tau at Asp421, and cleavage at this site facilitates the formation of tau aggregates in cell-free conditions (Gamblin et al., 2003).”
• Mechanisms of tau-induced neurodegeneration (2009, neutral): “In addition to abnormal hyperphosphorylation, conformational changes and cleavage of tau have also been implicated in the pathogenesis of AD [43, 82, 126, 137].”
• Biochemistry and cell biology of tau protein in neurofibrillary degeneration. (2012, background): “For example, cleavage of the tails by caspases (behind D421 or behind D13; Gamblin et al. 2003; Horowitz et al. 2004; Rissman et al. 2004) perturbs the paperclip folding of Tau (Jeganathan et al.”
• Tau in Alzheimer Disease and Related Tauopathies (2010, background): “In addition to abnormal hyperphosphorylation, conformational changes and cleavage of tau have also been implicated in the pathogenesis of AD [34, 37, 38, 94].”