Skip to main content
SpringerLink
Log in

Tau Fibrillogenesis

  • Chapter
  • First Online:
Protein Aggregation and Fibrillogenesis in Cerebral and Systemic Amyloid Disease

Part of the book series: Subcellular Biochemistry ((SCBI,volume 65))

Abstract

The protein tau is the most abundant microtubule associated protein in the central and peripheral nervous system. In the brain, tau plays a role in the assembly and stabilization of microtubules. The function of tau, however, appears to overlap with other microtubule binding proteins. The observation that tau is associated with neurodegenerative diseases has renewed interest in this protein. Various aspects of structure and biochemistry of tau, fibril formation and clinical perspectives, including therapeutic strategies are reviewed in this chapter.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Log in via an institution
Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 169.00
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 219.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 219.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Abbreviations

NFTs:

Neurofibrillary tangles

AD:

Alzheimer’s disease

PHFs:

Paired helical filaments

EM:

Electron microscopy

References

  • Alonso A, Zaidi T, Novak M, Grundke-Iqbal I, Iqbal K (2001) Hyperphosphorylation induces self-assembly of tau into tangles of paired helical filaments/straight filaments. Proc Natl Acad Sci U S A 98:6923–6928

    Article  PubMed  CAS  Google Scholar 

  • Alonso AC, Grundke-Iqbal I, Iqbal K (1996) Alzheimer’s disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules. Nat Med 2:783–787

    Article  PubMed  CAS  Google Scholar 

  • Barghorn S, Zheng-Fischhofer Q, Ackmann M, Biernat J, Von Bergen M, Mandelkow EM, Mandelkow E (2000) Structure, microtubule interactions, and paired helical filament aggregation by tau mutants of frontotemporal dementias. Biochemistry 39:11714–11721

    Article  PubMed  CAS  Google Scholar 

  • Billingsley ML, Kincaid RL (1997) Regulated phosphorylation and dephosphorylation of tau protein: effects on microtubule interaction, intracellular trafficking and neurodegeneration. Biochem J 323:577–591

    PubMed  CAS  Google Scholar 

  • Brion JP, Smith C, Couck AM, Gallo JM, Anderton BH (1993) Developmental changes in tau phosphorylation: fetal tau is transiently phosphorylated in a manner similar to paired helical filament-tau characteristic of Alzheimer’s disease. J Neurochem 61:2071–2080

    Article  PubMed  CAS  Google Scholar 

  • Buee L, Bussiere T, Buee-Scherrer V, Delacourte A, Hof PR (2000) Tau protein isoforms, phosphorylation and role in neurodegenerative disorders. Brain Res Brain Res Rev 33:95–130

    Article  PubMed  CAS  Google Scholar 

  • Cohen TJ, Guo JL, Hurtado, DE, Kwong LK, Mills IP, Trojanowski JQ, Lee VM (2011) The acetylation of tau inhibits its function and promotes pathological tau aggregation. Nat Commun 2:252

    Article  PubMed  Google Scholar 

  • Couchie D, Mavilia C, Georgieff IS, Liem RK, Shelanski ML, Nunez J (1992) Primary structure of high molecular weight tau present in the peripheral nervous system. Proc Natl Acad Sci U S A 89:4378–4381

    Article  PubMed  CAS  Google Scholar 

  • Crowther, R.A. (1991) Straight and paired helical filaments in Alzheimer disease have a common structural unit. Proc Natl Acad Sci USA 88:2288–2292

    Article  PubMed  CAS  Google Scholar 

  • Crowther RA, Olesen OF, Jakes R, Goedert M (1992) The microtubule binding repeats of tau protein assemble into filaments like those found in Alzheimer’s disease. FEBS Lett 309:199–202

    Article  PubMed  CAS  Google Scholar 

  • Crowther RA, Olesen OF, Smith MJ, Jakes R, Goedert M (1994) Assembly of Alzheimer-like filaments from full-length tau protein. FEBS Lett 337:135–138

    Article  PubMed  CAS  Google Scholar 

  • Crowther RA, Wischik CM (1985) Image reconstruction of the Alzheimer paired helical filament. EMBO J 4:3661–3665

    PubMed  CAS  Google Scholar 

  • Dickey CA, Kamal A, Lundgren K, Klosak N, Bailey RM, Dunmore J, Ash P, Shoraka S, Zlatkovic J, Eckman CB, Patterson C, Dickson DW, Nahman NS Jr, Hutton M, Burrows F, Petrucelli L (2007) The high-affinity HSP90-CHIP complex recognizes and selectively degrades phosphorylated tau client proteins. J Clin Invest 117:648–658

    Article  PubMed  CAS  Google Scholar 

  • Drechsel DN, Hyman AA, Cobb MH, Kirschner MW (1992) Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau. Mol Biol Cell 3:1141–1154

    PubMed  CAS  Google Scholar 

  • D’Souza I, Schellenberg GD (2005) Regulation of tau isoform expression and dementia. Biochim Biophys Acta 1739:104–115

    Article  PubMed  Google Scholar 

  • Dymock B, Barril X, Beswick M, Collier A, Davies N, Drysdale M, Fink A, Fromont C, Hubbard RE, Massey A, Surgenor A, Wright L (2004) Adenine derived inhibitors of the molecular chaperone HSP90-SAR explained through multiple X-ray structures. Bioorg Med Chem Lett 14:325–328

    Article  PubMed  CAS  Google Scholar 

  • Eliezer D, Barre P, Kobaslija M, Chan D, Li X, Heend L (2005) Residual structure in the repeat domain of tau: echoes of microtubule binding and paired helical filament formation. Biochemistry 44:1026–1036

    Article  PubMed  CAS  Google Scholar 

  • Feijoo C, Campbell DG, Jakes R, Goedert M, Cuenda A (2005) Evidence that phosphorylation of the microtubule-associated protein Tau by SAPK4/p38delta at Thr50 promotes microtubule assembly. J Cell Sci 118:397–408

    Article  PubMed  CAS  Google Scholar 

  • Fischer D, Mukrasch MD, Biernat J, Bibow S, Blackledge M, Griesinger C, Mandelkow E, Zweckstetter M (2009) Conformational changes specific for pseudophosphorylation at serine 262 selectively impair binding of tau to microtubules. Biochemistry 48:10047–10055

    Article  PubMed  CAS  Google Scholar 

  • Friedhoff P, Schneider A, Mandelkow EM, Mandelkow E (1998) Rapid assembly of Alzheimer-like paired helical filaments from microtubule-associated protein tau monitored by fluorescence in solution. Biochemistry 37:10223–10230

    Article  PubMed  CAS  Google Scholar 

  • Fulga TA, Elson-Schwab I, Khurana V, Steinhilb ML, Spires TL, Hyman BT, Feany MB (2007) Abnormal bundling and accumulation of F-actin mediates tau-induced neuronal degeneration in vivo. Nat Cell Biol 9:139–148

    Article  PubMed  CAS  Google Scholar 

  • Georgieff IS, Liem RK, Mellado W, Nunez J, Shelanski ML (1991) High molecular weight tau: preferential localization in the peripheral nervous system. J Cell Sci 100 (Pt 1):55–60

    Google Scholar 

  • Goedert M, Jakes R (1990) Expression of separate isoforms of human tau protein: correlation with the tau pattern in brain and effects on tubulin polymerization. EMBO J 9:4225–4230

    PubMed  CAS  Google Scholar 

  • Goedert M, Jakes R, Spillantini MG, Hasegawa M, Smith MJ, Crowther RA (1996) Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans. Nature 383:550–553

    Article  PubMed  CAS  Google Scholar 

  • Goedert M, Spillantini MG, Cairns NJ, Crowther RA (1992a) Tau proteins of Alzheimer paired helical filaments: abnormal phosphorylation of all six brain isoforms. Neuron 8:159–168.

    Article  CAS  Google Scholar 

  • Goedert M, Spillantini MG, Crowther RA (1992b) Cloning of a big tau microtubule-associated protein characteristic of the peripheral nervous system. Proc Natl Acad Sci U S A 89:1983–1987

    Article  CAS  Google Scholar 

  • Gomez-Isla T, Hollister R, West H, Mui S, Growdon JH, Petersen RC, Parisi JE, Hyman BT (1997) Neuronal loss correlates with but exceeds neurofibrillary tangles in Alzheimer’s disease. Ann Neurol 41:17–24

    Article  PubMed  CAS  Google Scholar 

  • Goux WJ, Kopplin L, Nguyen AD, Leak K, Rutkofsky M, Shanmuganandam VD, Sharma D, Inouye H, Kirschner DA (2004) The formation of straight and twisted filaments from short tau peptides. J Biol Chem 279:26868–26875

    Article  PubMed  CAS  Google Scholar 

  • Grundke-Iqbal I, Iqbal K, Quinlan M, Tung YC, Zaidi MS, Wisniewski HM (1986) Microtubule-associated protein tau. A component of Alzheimer paired helical filaments. J Biol Chem 261:6084–6089

    PubMed  CAS  Google Scholar 

  • Hartman JJ, Vale RD (1999) Microtubule disassembly by ATP-dependent oligomerization of the AAA enzyme katanin. Science 286:782–785

    Article  PubMed  CAS  Google Scholar 

  • He HJ, Wang XS, Pan R, Wang DL, Liu MN, He RQ (2009) The proline-rich domain of tau plays a role in interactions with actin. BMC Cell Biol 10:81

    Article  PubMed  Google Scholar 

  • Hernandez F, Avila J (2007) Tauopathies. Cell Mol Life Sci 64:2219–2233

    Article  PubMed  CAS  Google Scholar 

  • Hutton M, Lendon CL, Rizzu P, Baker M, Froelich S, Houlden H, Pickering-Brown S, Chakraverty S, Isaacs A, Grover A, Hackett J, Adamson J, Lincoln S, Dickson D, Davies P, Petersen RC, Stevens M, De Graaff E, Wauters E, Van Baren J, Hillebrand M, Joosse M, Kwon JM, Nowotny P, Che LK, Norton J, Morris JC, Reed LA, Trojanowski J, Basun H, Lannfelt L, Neystat M, Fahn S, Dark F, Tannenberg T, Dodd PR, Hayward N, Kwok JB, Schofield PR, Andreadis A, Snowden J, Craufurd D, Neary D, Owen F, Oostra BA, Hardy J, Goate A, Van Swieten J, Mann D, Lynch T, Heutink P (1998) Association of missense and 5’-splice-site mutations in tau with the inherited dementia FTDP−17. Nature 393:702–705

    Article  PubMed  CAS  Google Scholar 

  • Hwang SC, Jhon DY, Bae YS, Kim JH, Rhee SG (1996) Activation of phospholipase C-gamma by the concerted action of tau proteins and arachidonic acid. J Biol Chem 271:18342–18349

    Article  PubMed  CAS  Google Scholar 

  • Irwin DJ, Cohen TJ, Grossman M, Arnold SE, Xie SX, Lee VM, Trojanowski JQ (2012) Acetylated tau, a novel pathological signature in Alzheimer’s disease and other tauopathies. Brain 135:807–818

    Article  PubMed  Google Scholar 

  • Jeganathan S, von Bergen M, Mandelkow EM, Mandelkow E (2008) The natively unfolded character of tau and its aggregation to Alzheimer-like paired helical filaments. Biochemistry 47:10526–10539

    Article  PubMed  CAS  Google Scholar 

  • Jenkins SM, Johnson GV (1998) Tau complexes with phospholipase C-gamma in situ. Neuroreport 9:67–71

    Article  PubMed  CAS  Google Scholar 

  • Jho YS, Zhulina EB, Kim MW, Pincus PA (2010) Monte carlo simulations of tau proteins: effect of phosphorylation. Biophys J 99:2387–2397

    Article  PubMed  CAS  Google Scholar 

  • Kampers T, Friedhoff P, Biernat J, Mandelkow EM, Mandelkow E (1996) RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments. FEBS Lett 399:344–349

    Article  PubMed  CAS  Google Scholar 

  • Karakaya T, Fusser F, Prvulovic D, Hampel H (2012) Treatment options for tauopathies. Curr Treat Options Neurol 14:126–136

    Article  PubMed  Google Scholar 

  • Khatoon S, Grundke-Iqbal I, Iqbal K (1992) Brain levels of microtubule-associated protein tau are elevated in Alzheimer’s disease: a radioimmuno-slot-blot assay for nanograms of the protein. J Neurochem 59:750–753

    Article  PubMed  CAS  Google Scholar 

  • Kidd M (1963) Paired helical filaments in electron microscopy of Alzheimer’s disease. Nature 197:192–193

    Article  PubMed  CAS  Google Scholar 

  • King ME, Kan HM, Baas PW, Erisir A, Glabe CG, Bloom GS (2006) Tau-dependent microtubule disassembly initiated by prefibrillar beta-amyloid. J Cell Biol 175:541–546

    Article  PubMed  CAS  Google Scholar 

  • Kopke E, Tung YC, Shaikh S, Alonso AC, Iqbal K, Grundke-Iqbal I (1993) Microtubule-associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease. J Biol Chem 268:24374–24384

    PubMed  CAS  Google Scholar 

  • Kosik KS, Joachim CL, Selkoe DJ (1986) Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease. Proc Natl Acad Sci U S A 83:4044–4048

    Article  PubMed  CAS  Google Scholar 

  • Kosik KS, Orecchio LD, Bakalis S, Neve RL (1989) Developmentally regulated expression of specific tau sequences. Neuron 2:1389–1397

    Article  PubMed  CAS  Google Scholar 

  • Kotani S, Nishida E, Kumagai H, Sakai H (1985) Calmodulin inhibits interaction of actin with MAP2 and Tau, two major microtubule-associated proteins. J Biol Chem 260:10779–10783

    PubMed  CAS  Google Scholar 

  • Lasagna-Reeves CA, Castillo-Carranza DL, Guerrero-Muoz MJ, Jackson GR, Kayed R (2010) Preparation and characterization of neurotoxic tau oligomers. Biochemistry 49:10039–10041

    Article  PubMed  CAS  Google Scholar 

  • Lee G, Newman ST, Gard DL, Band H, Panchamoorthy G (1998) Tau interacts with src-family non-receptor tyrosine kinases. J Cell Sci 111 (Pt 21):3167–3177

    Google Scholar 

  • Lee VM, Goedert M, Trojanowski JQ (2001) Neurodegenerative tauopathies. Annu Rev Neurosci 24:1121–1159

    Article  PubMed  CAS  Google Scholar 

  • Li W, Lee VM (2006) Characterization of two VQIXXK motifs for tau fibrillization in vitro. Biochemistry 45:15692–15701

    Article  PubMed  CAS  Google Scholar 

  • Maeda S, Sahara N, Saito Y, Murayama M, Yoshiike Y, Kim H, Miyasaka T, Murayama S, Ikai A, Takashima A (2007) Granular tau oligomers as intermediates of tau filaments. Biochemistry 46:3856–3861

    Article  PubMed  CAS  Google Scholar 

  • Maeda S, Sahara N, Saito Y, Murayama S, Ikai A, Takashima A (2006) Increased levels of granular tau oligomers: an early sign of brain aging and Alzheimer’s disease. Neurosci Res 54:197–201

    Article  PubMed  CAS  Google Scholar 

  • Matsuo ES, Shin RW, Billingsley ML, Van deVoorde A, O’Connor M, Trojanowski JQ, Lee VM (1994) Biopsy-derived adult human brain tau is phosphorylated at many of the same sites as Alzheimer’s disease paired helical filament tau. Neuron 13:989–1002

    Google Scholar 

  • Mazanetz MP, Fischer PM (2007) Untangling tau hyperphosphorylation in drug design for neurodegenerative diseases. Nat Rev Drug Discov 6:464–479

    Article  PubMed  CAS  Google Scholar 

  • McNally FJ, Vale RD (1993) Identification of katanin, an ATPase that severs and disassembles stable microtubules. Cell 75:419–429

    Article  PubMed  CAS  Google Scholar 

  • Min SW, Cho SH, Zhou Y, Schroeder S, Haroutunian V, Seeley WW, Huang EJ, Shen Y, Masliah E, Mukherjee C, Meyers D, Cole PA, Ott M, Gan L (2010) Acetylation of tau inhibits its degradation and contributes to tauopathy. Neuron 67:953–966

    Article  PubMed  CAS  Google Scholar 

  • Moreno-Herrero F, Perez M, Baro AM, Avila J (2004) Characterization by atomic force microscopy of Alzheimer paired helical filaments under physiological conditions. Biophys J 86:517–525

    Article  PubMed  CAS  Google Scholar 

  • Mukrasch MD, Biernat J, von Bergen M, Griesinger C, Mandelkow E, Zweckstetter M (2005) Sites of tau important for aggregation populate {beta}-structure and bind to microtubules and polyanions. J Biol Chem 280:24978–24986

    Article  PubMed  CAS  Google Scholar 

  • Perez M, Valpuesta JM, Medina M, Montejo de Garcini E, Avila J (1996) Polymerization of tau into filaments in the presence of heparin: the minimal sequence required for tau-tau interaction. J Neurochem 67:1183–1190

    Article  PubMed  CAS  Google Scholar 

  • Peterson DW, Zhou H, Dahlquist FW, Lew J (2008) A soluble oligomer of tau associated with fiber formation analyzed by NMR. Biochemistry 47:7393–7404

    Article  PubMed  CAS  Google Scholar 

  • Petrucelli L, Dickson D, Kehoe K, Taylor J, Snyder H, Grover A, De Lucia M, McGowan E, Lewis J, Prihar G, Kim J, Dillmann WH, Browne SE, Hall A, Voellmy R, Tsuboi Y, Dawson TM, Wolozin B, Hardy J, Hutton M (2004) CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation. Hum Mol Genet 13:703–714

    Article  PubMed  CAS  Google Scholar 

  • Pollanen MS, Markiewicz P, Bergeron C, Goh MC (1994) Twisted ribbon structure of paired helical filaments revealed by atomic force microscopy. Am J Pathol 144:869–873

    PubMed  CAS  Google Scholar 

  • Qiang L, Yu W, Andreadis A, Luo M, Baas PW (2006) Tau protects microtubules in the axon from severing by katanin. J Neurosci 26:3120–3129

    Article  PubMed  CAS  Google Scholar 

  • Reynolds CH, Garwood CJ, Wray S, Price C, Kellie S, Perera T, Zvelebil M, Yang A, Sheppard PW, Varndell IM, Hanger DP, Anderton BH (2008) Phosphorylation regulates tau interactions with Src homology 3 domains of phosphatidylinositol 3-kinase, phospholipase Cgamma1, Grb2, and Src family kinases. J Biol Chem 283:18177–18186

    Article  PubMed  CAS  Google Scholar 

  • Rizzu P, Van Swieten JC, Joosse M, Hasegawa M, Stevens M, Tibben A, Niermeijer MF, Hillebrand M, Ravid R, Oostra BA, Goedert M, van Duijn CM, Heutink P (1999) High prevalence of mutations in the microtubule-associated protein tau in a population study of frontotemporal dementia in the Netherlands. Am J Hum Genet 64:414–421

    Article  PubMed  CAS  Google Scholar 

  • Ruben GC, Iqbal K, Grundke-Iqbal I, Johnson JE Jr (1993) The organization of the microtubule associated protein tau in Alzheimer paired helical filaments. Brain Res 602:1–13

    Article  PubMed  CAS  Google Scholar 

  • Schweers O, Schonbrunn-Hanebeck E, Marx A, Mandelkow E (1994) Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for beta-structure. J Biol Chem 269:24290–24297

    PubMed  CAS  Google Scholar 

  • Sergeant N, David JP, Lefranc D, Vermersch P, Wattez A, Delacourte A (1997) Different distribution of phosphorylated tau protein isoforms in Alzheimer’s and Pick’s diseases. FEBS Lett 412:578–582

    Article  PubMed  CAS  Google Scholar 

  • Spillantini MG, Murrell JR, Goedert M, Farlow MR, Klug A, Ghetti B (1998) Mutation in the tau gene in familial multiple system tauopathy with presenile dementia. Proc Natl Acad Sci U S A 95:7737–7741

    Article  PubMed  CAS  Google Scholar 

  • Takahashi M, Tsujioka Y, Yamada T, Tsuboi Y, Okada H, Yamamoto T, Liposits Z (1999) Glycosylation of microtubule-associated protein tau in Alzheimer’s disease brain. Acta Neuropathol 97:635–641

    Article  PubMed  CAS  Google Scholar 

  • Takei Y, Teng J, Harada A, Hirokawa N (2000) Defects in axonal elongation and neuronal migration in mice with disrupted tau and map1b genes. J Cell Biol 150:989–1000

    Article  PubMed  CAS  Google Scholar 

  • Tanimukai H, Kudo T, Tanaka T, Grundke-Iqbal I, Iqbal K, Takeda M (2009) Novel therapeutic strategies for neurodegenerative disease. Psychogeriatrics 9:103–109

    Article  PubMed  Google Scholar 

  • Trojanowski JQ, Lee VM (2002) The role of tau in Alzheimer’s disease. Med Clin North Am 86:615–627

    Article  PubMed  CAS  Google Scholar 

  • von Bergen M, Barghorn S, Li L, Marx A, Biernat J, Mandelkow EM, Mandelkow E (2001) Mutations of tau protein in frontotemporal dementia promote aggregation of paired helical filaments by enhancing local beta-structure. J Biol Chem 276:48165–48174

    PubMed  CAS  Google Scholar 

  • von Bergen M, Friedhoff P, Biernat J, Heberle J, Mandelkow EM, Mandelkow E (2000) Assembly of tau protein into Alzheimer paired helical filaments depends on a local sequence motif ((306)VQIVYK(311)) forming beta structure. Proc Natl Acad Sci U S A 97:5129–5134

    Article  PubMed  CAS  Google Scholar 

  • Wang JZ, Grundke-Iqbal I, Iqbal K (1996) Glycosylation of microtubule-associated protein tau: an abnormal posttranslational modification in Alzheimer’s disease. Nat Med 2:871–875

    Article  PubMed  CAS  Google Scholar 

  • Wei ML, Andreadis A (1998) Splicing of a regulated exon reveals additional complexity in the axonal microtubule-associated protein tau. J Neurochem 70:1346–1356

    Article  PubMed  CAS  Google Scholar 

  • Weingarten MD, Lockwood AH, Hwo SY, Kirschner MW (1975) A protein factor essential for microtubule assembly. Proc Natl Acad Sci U S A 72:1858–1862

    Article  PubMed  CAS  Google Scholar 

  • Wille H, Drewes G, Biernat J, Mandelkow EM, Mandelkow E (1992) Alzheimer-like paired helical filaments and antiparallel dimers formed from microtubule-associated protein tau in vitro. J Cell Biol 118:573–584

    Article  PubMed  CAS  Google Scholar 

  • Wilson DM, Binder LI (1997) Free fatty acids stimulate the polymerization of tau and amyloid beta peptides. In vitro evidence for a common effector of pathogenesis in Alzheimer’s disease. Am J Pathol 150:2181–2195

    PubMed  CAS  Google Scholar 

  • Wischik CM, Crowther RA, Stewart M, Roth M (1985) Subunit structure of paired helical filaments in Alzheimer’s disease. J Cell Biol 100:1905–1912

    Article  PubMed  CAS  Google Scholar 

  • Wischik CM, Novak M, Thogersen HC, Edwards PC, Runswick MJ, Jakes R, Walker JE, Milstein C, Roth M, Klug A (1988) Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease. Proc Natl Acad Sci U S A 85:4506–4510

    Article  PubMed  CAS  Google Scholar 

  • Wisniewski HM, Merz PA, Iqbal K (1984) Ultrastructure of paired helical filaments of Alzheimer’s neurofibrillary tangle. J Neuropathol Exp Neurol 43:643–656

    Article  PubMed  CAS  Google Scholar 

  • Wisniewski HM, Narang HK, Terry RD (1976) Neurofibrillary tangles of paired helical filaments. J Neurol Sci 27:173–181

    Article  PubMed  CAS  Google Scholar 

  • Wisniewski HM, Wen GY (1985) Substructures of paired helical filaments from Alzheimer’s disease neurofibrillary tangles. Acta Neuropathol 66:173–176

    Article  PubMed  CAS  Google Scholar 

  • Wittmann CW, Wszolek MF, Shulman JM, Salvaterra PM, Lewis J, Hutton M, Feany MB (2001) Tauopathy in Drosophila: neurodegeneration without neurofibrillary tangles. Science 293:711–714

    Article  PubMed  CAS  Google Scholar 

  • Zhang B, Maiti A, Shively S, Lakhani F, McDonald-Jones G, Bruce J, Lee EB, Xie SX, Joyce S, Li C, Toleikis PM, Lee VM, Trojanowski JQ (2005) Microtubule-binding drugs offset tau sequestration by stabilizing microtubules and reversing fast axonal transport deficits in a tauopathy model. Proc Natl Acad Sci U S A 102:227–231

    Article  PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Biotechnology, Indian Institute of Technology Guwahati, Guwahati, 781 039, Assam, India

    Nitin Chaudhary

  2. CSIR-Centre for Cellular and Molecular Biology, Uppal Road, Hyderabad, 500 007, Andhra Pradesh, India

    Ramakrishnan Nagaraj

Authors
  1. Nitin Chaudhary
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Ramakrishnan Nagaraj
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Nitin Chaudhary .

Editor information

Editors and Affiliations

  1. Inst. of Zoology, University of Mainz, Becherweg 6, Mainz, 55099, Germany

    J. Robin Harris

Rights and permissions

Reprints and permissions

Copyright information

© 2012 Springer Science+Business Media Dordrecht

About this chapter

Cite this chapter

Chaudhary, N., Nagaraj, R. (2012). Tau Fibrillogenesis. In: Harris, J. (eds) Protein Aggregation and Fibrillogenesis in Cerebral and Systemic Amyloid Disease. Subcellular Biochemistry, vol 65. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-5416-4_4

Download citation

Publish with us

Policies and ethics

Search

Navigation