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Items: 1 to 20 of 117

1.

Structure of core domain of fibril-forming PHF/Tau fragments.

Inouye H, Sharma D, Goux WJ, Kirschner DA.

Biophys J. 2006 Mar 1;90(5):1774-89. Epub 2005 Dec 9.

2.

The formation of straight and twisted filaments from short tau peptides.

Goux WJ, Kopplin L, Nguyen AD, Leak K, Rutkofsky M, Shanmuganandam VD, Sharma D, Inouye H, Kirschner DA.

J Biol Chem. 2004 Jun 25;279(26):26868-75. Epub 2004 Apr 20.

4.

Secondary nucleating sequences affect kinetics and thermodynamics of tau aggregation.

Moore CL, Huang MH, Robbennolt SA, Voss KR, Combs B, Gamblin TC, Goux WJ.

Biochemistry. 2011 Dec 20;50(50):10876-86. doi: 10.1021/bi2014745. Epub 2011 Nov 29.

5.

Positional effects of phosphorylation on the stability and morphology of tau-related amyloid fibrils.

Inoue M, Konno T, Tainaka K, Nakata E, Yoshida HO, Morii T.

Biochemistry. 2012 Feb 21;51(7):1396-406. doi: 10.1021/bi201451z. Epub 2012 Feb 7.

PMID:
22304362
7.

Prediction of nucleating sequences from amyloidogenic propensities of tau-related peptides.

Rojas Quijano FA, Morrow D, Wise BM, Brancia FL, Goux WJ.

Biochemistry. 2006 Apr 11;45(14):4638-52.

PMID:
16584199
8.

Mutations of tau protein in frontotemporal dementia promote aggregation of paired helical filaments by enhancing local beta-structure.

von Bergen M, Barghorn S, Li L, Marx A, Biernat J, Mandelkow EM, Mandelkow E.

J Biol Chem. 2001 Dec 21;276(51):48165-74. Epub 2001 Oct 17.

9.
10.

Assembly of tau protein into Alzheimer paired helical filaments depends on a local sequence motif ((306)VQIVYK(311)) forming beta structure.

von Bergen M, Friedhoff P, Biernat J, Heberle J, Mandelkow EM, Mandelkow E.

Proc Natl Acad Sci U S A. 2000 May 9;97(10):5129-34.

11.

Resonance Raman spectroscopic measurements delineate the structural changes that occur during tau fibril formation.

Ramachandran G, Milán-Garcés EA, Udgaonkar JB, Puranik M.

Biochemistry. 2014 Oct 21;53(41):6550-65. doi: 10.1021/bi500528x. Epub 2014 Oct 6.

PMID:
25284680
12.

Interplay between I308 and Y310 residues in the third repeat of microtubule-binding domain is essential for tau filament formation.

Naruto K, Minoura K, Okuda R, Taniguchi T, In Y, Ishida T, Tomoo K.

FEBS Lett. 2010 Oct 8;584(19):4233-6. doi: 10.1016/j.febslet.2010.09.012. Epub 2010 Sep 17.

13.

Characterization of two VQIXXK motifs for tau fibrillization in vitro.

Li W, Lee VM.

Biochemistry. 2006 Dec 26;45(51):15692-701. Epub 2006 Dec 19.

PMID:
17176091
14.

β-Sheet core of tau paired helical filaments revealed by solid-state NMR.

Daebel V, Chinnathambi S, Biernat J, Schwalbe M, Habenstein B, Loquet A, Akoury E, Tepper K, Müller H, Baldus M, Griesinger C, Zweckstetter M, Mandelkow E, Vijayan V, Lange A.

J Am Chem Soc. 2012 Aug 29;134(34):13982-9. doi: 10.1021/ja305470p. Epub 2012 Aug 15.

PMID:
22862303
15.

A nucleated assembly mechanism of Alzheimer paired helical filaments.

Friedhoff P, von Bergen M, Mandelkow EM, Davies P, Mandelkow E.

Proc Natl Acad Sci U S A. 1998 Dec 22;95(26):15712-7.

16.

Fibers of tau fragments, but not full length tau, exhibit a cross beta-structure: implications for the formation of paired helical filaments.

Giannetti AM, Lindwall G, Chau MF, Radeke MJ, Feinstein SC, Kohlstaedt LA.

Protein Sci. 2000 Dec;9(12):2427-35.

17.

Formation and growth of oligomers: a Monte Carlo study of an amyloid tau fragment.

Li DW, Mohanty S, Irbäck A, Huo S.

PLoS Comput Biol. 2008 Dec;4(12):e1000238. doi: 10.1371/journal.pcbi.1000238. Epub 2008 Dec 5.

19.

Assemblies of Alzheimer's peptides A beta 25-35 and A beta 31-35: reverse-turn conformation and side-chain interactions revealed by X-ray diffraction.

Bond JP, Deverin SP, Inouye H, el-Agnaf OM, Teeter MM, Kirschner DA.

J Struct Biol. 2003 Feb;141(2):156-70.

PMID:
12615542
20.

beta-Helix is a likely core structure of yeast prion Sup35 amyloid fibers.

Kishimoto A, Hasegawa K, Suzuki H, Taguchi H, Namba K, Yoshida M.

Biochem Biophys Res Commun. 2004 Mar 12;315(3):739-45.

PMID:
14975763

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