Effect of cellular polyanion mimetics on tau peptide aggregation
dc.contributor.author | Ismail, Tania | |
dc.contributor.author | Kanapathipillai, Mathumai | |
dc.date.accessioned | 2018-11-20T15:34:27Z | |
dc.date.available | 2020-01-06T16:40:59Z | en |
dc.date.issued | 2018-11 | |
dc.identifier.citation | Ismail, Tania; Kanapathipillai, Mathumai (2018). "Effect of cellular polyanion mimetics on tau peptide aggregation." Journal of Peptide Science 24(11): n/a-n/a. | |
dc.identifier.issn | 1075-2617 | |
dc.identifier.issn | 1099-1387 | |
dc.identifier.uri | https://hdl.handle.net/2027.42/146415 | |
dc.publisher | Wiley Periodicals, Inc. | |
dc.subject.other | Alzheimer’s | |
dc.subject.other | aggregation | |
dc.subject.other | glycosaminoglycans | |
dc.subject.other | RNA | |
dc.subject.other | tau peptide | |
dc.title | Effect of cellular polyanion mimetics on tau peptide aggregation | |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | |
dc.subject.hlbsecondlevel | Biological Chemistry | |
dc.subject.hlbsecondlevel | Chemical Engineering | |
dc.subject.hlbsecondlevel | Chemistry | |
dc.subject.hlbsecondlevel | Materials Science and Engineering | |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | |
dc.subject.hlbtoplevel | Engineering | |
dc.subject.hlbtoplevel | Health Sciences | |
dc.subject.hlbtoplevel | Science | |
dc.description.peerreviewed | Peer Reviewed | |
dc.description.bitstreamurl | https://deepblue.lib.umich.edu/bitstream/2027.42/146415/1/psc3125.pdf | |
dc.description.bitstreamurl | https://deepblue.lib.umich.edu/bitstream/2027.42/146415/2/psc3125_am.pdf | |
dc.identifier.doi | 10.1002/psc.3125 | |
dc.identifier.source | Journal of Peptide Science | |
dc.identifier.citedreference | Zhao J, Huvent I, Lippens G, et al. Glycan determinants of heparin‐tau interaction. Biophys J. 2017; 112 ( 5 ): 921 ‐ 932. | |
dc.identifier.citedreference | Evans LD, Wassmer T, Fraser G, et al. Extracellular monomeric and aggregated tau efficiently enter human neurons through overlapping but distinct pathways. Cell Rep. 2018; 22 ( 13 ): 3612 ‐ 3624. | |
dc.identifier.citedreference | Avila J. Intracellular and extracellular tau. Front Neurosci. 2010; 4: 49. | |
dc.identifier.citedreference | Eschmann NA, Do TD, LaPointe NE, et al. Tau aggregation propensity engrained in its solution state. J Phys Chem B. 2015; 119 ( 45 ): 14421 ‐ 14432. | |
dc.identifier.citedreference | Nadimidla K, Ismail T, Kanapathipillai M. Tau peptides and tau mutant protein aggregation inhibition by cationic polyethyleneimine and polyarginine. Biopolymers. 2017; 107 ( 9 ). | |
dc.identifier.citedreference | Ariga T, Miyatake T, Yu RK. Role of proteoglycans and glycosaminoglycans in the pathogenesis of Alzheimer’s disease and related disorders: amyloidogenesis and therapeutic strategies—a review. J Neurosci Res. 2010; 88 ( 11 ): 2303 ‐ 2315. | |
dc.identifier.citedreference | McLaurin J, Franklin T, Zhang X, Deng J, Fraser PE. Interactions of Alzheimer amyloid‐beta peptides with glycosaminoglycans effects on fibril nucleation and growth. Eur J Biochem. 1999; 266 ( 3 ): 1101 ‐ 1110. | |
dc.identifier.citedreference | Goedert M, Jakes R, Spillantini MG, Hasegawa M, Smith MJ, Crowther RA. Assembly of microtubule‐associated protein tau into Alzheimer‐like filaments induced by sulphated glycosaminoglycans. Nature. 1996; 383 ( 6600 ): 550 ‐ 553. | |
dc.identifier.citedreference | Paudel HK, Li W. Heparin‐induced conformational change in microtubule‐associated protein tau as detected by chemical cross‐linking and phosphopeptide mapping. J Biol Chem. 1999; 274 ( 12 ): 8029 ‐ 8038. | |
dc.identifier.citedreference | Ramachandran G, Udgaonkar JB. Understanding the kinetic roles of the inducer heparin and of rod‐like protofibrils during amyloid fibril formation by tau protein. J Biol Chem. 2011; 286 ( 45 ): 38948 ‐ 38959. | |
dc.identifier.citedreference | Larini L, Gessel MM, LaPointe NE, et al. Initiation of assembly of tau(273‐284) and its DeltaK280 mutant: an experimental and computational study. Phys Chem Chem Phys. 2013; 15 ( 23 ): 8916 ‐ 8928. | |
dc.identifier.citedreference | Aguilera JJ, Zhang F, Beaudet JM, Linhardt RJ, Colon W. Divergent effect of glycosaminoglycans on the in vitro aggregation of serum amyloid a. Biochimie. 2014; 104: 70 ‐ 80. | |
dc.identifier.citedreference | Kizuka Y, Kitazume S, Taniguchi N. N‐glycan and Alzheimer’s disease. Biochim Biophys Acta. 2017; 1861 ( 10 ): 2447 ‐ 2454. | |
dc.identifier.citedreference | Arora A, Ha C, Park CB. Inhibition of insulin amyloid formation by small stress molecules. FEBS Lett. 2004; 564 ( 1‐2 ): 121 ‐ 125. | |
dc.identifier.citedreference | Schlachetzki JC, Saliba SW, Oliveira AC. Studying neurodegenerative diseases in culture models. Rev Bras Psiquiatr. 2013; 35 ( Suppl 2 ): S92 ‐ S100. | |
dc.identifier.citedreference | Giacobini E, Gold G. Alzheimer disease therapy—moving from amyloid‐beta to tau. Nat Rev Neurol. 2013; 9 ( 12 ): 677 ‐ 686. | |
dc.identifier.citedreference | Wischik CM, Harrington CR, Storey JM. Tau‐aggregation inhibitor therapy for Alzheimer’s disease. Biochem Pharmacol. 2014; 88 ( 4 ): 529 ‐ 539. | |
dc.identifier.citedreference | Avila J, Jimenez JS, Sayas CL, et al. Tau structures. Front Aging Neurosci. 2016; 8: 262. | |
dc.identifier.citedreference | Iqbal K, Liu F, Gong CX, Grundke‐Iqbal I. Tau in Alzheimer disease and related tauopathies. Curr Alzheimer Res. 2010; 7 ( 8 ): 656 ‐ 664. | |
dc.identifier.citedreference | von Bergen M, Barghorn S, Biernat J, Mandelkow EM, Mandelkow E. Tau aggregation is driven by a transition from random coil to beta sheet structure. Biochim Biophys Acta. 2005; 1739 ( 2‐3 ): 158 ‐ 166. | |
dc.identifier.citedreference | Mandelkow E, von Bergen M, Biernat J, Mandelkow EM. Structural principles of tau and the paired helical filaments of Alzheimer’s disease. Brain Pathol. 2007; 17 ( 1 ): 83 ‐ 90. | |
dc.identifier.citedreference | Li W, Lee VM. Characterization of two VQIXXK motifs for tau fibrillization in vitro. Biochemistry. 2006; 45 ( 51 ): 15692 ‐ 15701. | |
dc.identifier.citedreference | Goux WJ, Kopplin L, Nguyen AD, et al. The formation of straight and twisted filaments from short tau peptides. J Biol Chem. 2004; 279 ( 26 ): 26868 ‐ 26875. | |
dc.identifier.citedreference | Ganguly P, Do TD, Larini L, et al. Tau assembly: the dominant role of PHF6 (VQIVYK) in microtubule binding region repeat R3. J Phys Chem B. 2015; 119 ( 13 ): 4582 ‐ 4593. | |
dc.identifier.citedreference | Boutajangout A, Wisniewski T. Tau‐based therapeutic approaches for Alzheimer’s disease—a mini‐review. Gerontology. 2014; 60 ( 5 ): 381 ‐ 385. | |
dc.identifier.citedreference | Brunden KR, Ballatore C, Crowe A, Smith AB 3rd, Lee VM, Trojanowski JQ. Tau‐directed drug discovery for Alzheimer’s disease and related tauopathies: a focus on tau assembly inhibitors. Exp Neurol. 2010; 223 ( 2 ): 304 ‐ 310. | |
dc.identifier.citedreference | Mukrasch MD, Biernat J, von Bergen M, Griesinger C, Mandelkow E, Zweckstetter M. Sites of tau important for aggregation populate {beta}‐structure and bind to microtubules and polyanions. J Biol Chem. 2005; 280 ( 26 ): 24978 ‐ 24986. | |
dc.identifier.citedreference | Papy‐Garcia D, Christophe M, Huynh MB, et al. Glycosaminoglycans, protein aggregation and neurodegeneration. Curr Protein Pept Sci. 2011; 12 ( 3 ): 258 ‐ 268. | |
dc.identifier.citedreference | Kampers T, Friedhoff P, Biernat J, Mandelkow EM, Mandelkow E. RNA stimulates aggregation of microtubule‐associated protein tau into Alzheimer‐like paired helical filaments. FEBS Lett. 1996; 399 ( 3 ): 344 ‐ 349. | |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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