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Items: 34


Driving tau into phase-separated liquid droplets.

Margittai M.

J Biol Chem. 2019 Jul 19;294(29):11060-11061. doi: 10.1074/jbc.H119.009703.


Time-resolved multirotational dynamics of single solution-phase tau proteins reveals details of conformational variation.

Foote AK, Manger LH, Holden MR, Margittai M, Goldsmith RH.

Phys Chem Chem Phys. 2019 Jan 23;21(4):1863-1871. doi: 10.1039/c8cp06971a.


Structural disorder in four-repeat Tau fibrils reveals a new mechanism for barriers to cross-seeding of Tau isoforms.

Weismiller HA, Murphy R, Wei G, Ma B, Nussinov R, Margittai M.

J Biol Chem. 2018 Nov 9;293(45):17336-17348. doi: 10.1074/jbc.RA118.005316. Epub 2018 Sep 21.


The distinct structural preferences of tau protein repeat domains.

Li X, Dong X, Wei G, Margittai M, Nussinov R, Ma B.

Chem Commun (Camb). 2018 May 31;54(45):5700-5703. doi: 10.1039/c8cc01263f.


Revealing Conformational Variants of Solution-Phase Intrinsically Disordered Tau Protein at the Single-Molecule Level.

Manger LH, Foote AK, Wood SL, Holden MR, Heylman KD, Margittai M, Goldsmith RH.

Angew Chem Int Ed Engl. 2017 Dec 4;56(49):15584-15588. doi: 10.1002/anie.201708242. Epub 2017 Nov 14.


Fracture and Growth Are Competing Forces Determining the Fate of Conformers in Tau Fibril Populations.

Meyer V, Holden MR, Weismiller HA, Eaton GR, Eaton SS, Margittai M.

J Biol Chem. 2016 Jun 3;291(23):12271-81. doi: 10.1074/jbc.M116.715557. Epub 2016 Apr 14.


How Does Hyperphopsphorylation Promote Tau Aggregation and Modulate Filament Structure and Stability?

Xu L, Zheng J, Margittai M, Nussinov R, Ma B.

ACS Chem Neurosci. 2016 May 18;7(5):565-75. doi: 10.1021/acschemneuro.5b00294. Epub 2016 Feb 24.


Spin Labeling and Characterization of Tau Fibrils Using Electron Paramagnetic Resonance (EPR).

Meyer V, Margittai M.

Methods Mol Biol. 2016;1345:185-99. doi: 10.1007/978-1-4939-2978-8_12.


RNA Binds to Tau Fibrils and Sustains Template-Assisted Growth.

Dinkel PD, Holden MR, Matin N, Margittai M.

Biochemistry. 2015 Aug 4;54(30):4731-40. doi: 10.1021/acs.biochem.5b00453. Epub 2015 Jul 27.


Amplification of Tau fibrils from minute quantities of seeds.

Meyer V, Dinkel PD, Rickman Hager E, Margittai M.

Biochemistry. 2014 Sep 16;53(36):5804-9. doi: 10.1021/bi501050g. Epub 2014 Aug 29.


Single mutations in tau modulate the populations of fibril conformers through seed selection.

Meyer V, Dinkel PD, Luo Y, Yu X, Wei G, Zheng J, Eaton GR, Ma B, Nussinov R, Eaton SS, Margittai M.

Angew Chem Int Ed Engl. 2014 Feb 3;53(6):1590-3. doi: 10.1002/anie.201308473. Epub 2014 Jan 22.


Molecular insights into the reversible formation of tau protein fibrils.

Luo Y, Dinkel P, Yu X, Margittai M, Zheng J, Nussinov R, Wei G, Ma B.

Chem Commun (Camb). 2013 May 4;49(34):3582-4. doi: 10.1039/c3cc00241a.


Small misfolded Tau species are internalized via bulk endocytosis and anterogradely and retrogradely transported in neurons.

Wu JW, Herman M, Liu L, Simoes S, Acker CM, Figueroa H, Steinberg JI, Margittai M, Kayed R, Zurzolo C, Di Paolo G, Duff KE.

J Biol Chem. 2013 Jan 18;288(3):1856-70. doi: 10.1074/jbc.M112.394528. Epub 2012 Nov 27.


Conformational basis for asymmetric seeding barrier in filaments of three- and four-repeat tau.

Siddiqua A, Luo Y, Meyer V, Swanson MA, Yu X, Wei G, Zheng J, Eaton GR, Ma B, Nussinov R, Eaton SS, Margittai M.

J Am Chem Soc. 2012 Jun 20;134(24):10271-8. doi: 10.1021/ja303498q. Epub 2012 Jun 12.


Cross-seeding and conformational selection between three- and four-repeat human Tau proteins.

Yu X, Luo Y, Dinkel P, Zheng J, Wei G, Margittai M, Nussinov R, Ma B.

J Biol Chem. 2012 Apr 27;287(18):14950-9. doi: 10.1074/jbc.M112.340794. Epub 2012 Mar 5.


Variations in filament conformation dictate seeding barrier between three- and four-repeat tau.

Dinkel PD, Siddiqua A, Huynh H, Shah M, Margittai M.

Biochemistry. 2011 May 24;50(20):4330-6. doi: 10.1021/bi2004685. Epub 2011 May 2.


Three- and four-repeat Tau coassemble into heterogeneous filaments: an implication for Alzheimer disease.

Siddiqua A, Margittai M.

J Biol Chem. 2010 Nov 26;285(48):37920-6. doi: 10.1074/jbc.M110.185728. Epub 2010 Oct 4.


Fibrils with parallel in-register structure constitute a major class of amyloid fibrils: molecular insights from electron paramagnetic resonance spectroscopy.

Margittai M, Langen R.

Q Rev Biophys. 2008 Aug-Nov;41(3-4):265-97. doi: 10.1017/S0033583508004733. Review.


Investigation of alpha-synuclein fibril structure by site-directed spin labeling.

Chen M, Margittai M, Chen J, Langen R.

J Biol Chem. 2007 Aug 24;282(34):24970-9. Epub 2007 Jun 15.


Spin labeling analysis of amyloids and other protein aggregates.

Margittai M, Langen R.

Methods Enzymol. 2006;413:122-39.


Side chain-dependent stacking modulates tau filament structure.

Margittai M, Langen R.

J Biol Chem. 2006 Dec 8;281(49):37820-7. Epub 2006 Oct 5.


Template-assisted filament growth by parallel stacking of tau.

Margittai M, Langen R.

Proc Natl Acad Sci U S A. 2004 Jul 13;101(28):10278-83. Epub 2004 Jul 6.


Determinants of liposome fusion mediated by synaptic SNARE proteins.

Schuette CG, Hatsuzawa K, Margittai M, Stein A, Riedel D, Küster P, König M, Seidel C, Jahn R.

Proc Natl Acad Sci U S A. 2004 Mar 2;101(9):2858-63. Epub 2004 Feb 23.


Single-molecule fluorescence resonance energy transfer reveals a dynamic equilibrium between closed and open conformations of syntaxin 1.

Margittai M, Widengren J, Schweinberger E, Schröder GF, Felekyan S, Haustein E, König M, Fasshauer D, Grubmüller H, Jahn R, Seidel CA.

Proc Natl Acad Sci U S A. 2003 Dec 23;100(26):15516-21. Epub 2003 Dec 10.


A transient N-terminal interaction of SNAP-25 and syntaxin nucleates SNARE assembly.

Fasshauer D, Margittai M.

J Biol Chem. 2004 Feb 27;279(9):7613-21. Epub 2003 Dec 9.


The Habc domain and the SNARE core complex are connected by a highly flexible linker.

Margittai M, Fasshauer D, Jahn R, Langen R.

Biochemistry. 2003 Apr 15;42(14):4009-14.


SNAREs in native plasma membranes are active and readily form core complexes with endogenous and exogenous SNAREs.

Lang T, Margittai M, Hölzler H, Jahn R.

J Cell Biol. 2002 Aug 19;158(4):751-60. Epub 2002 Aug 12.


Rapid and selective binding to the synaptic SNARE complex suggests a modulatory role of complexins in neuroexocytosis.

Pabst S, Margittai M, Vainius D, Langen R, Jahn R, Fasshauer D.

J Biol Chem. 2002 Mar 8;277(10):7838-48. Epub 2001 Dec 20.


Homo- and heterooligomeric SNARE complexes studied by site-directed spin labeling.

Margittai M, Fasshauer D, Pabst S, Jahn R, Langen R.

J Biol Chem. 2001 Apr 20;276(16):13169-77. Epub 2001 Jan 19.


Inhibition of SNARE complex assembly differentially affects kinetic components of exocytosis.

Xu T, Rammner B, Margittai M, Artalejo AR, Neher E, Jahn R.

Cell. 1999 Dec 23;99(7):713-22.


Mixed and non-cognate SNARE complexes. Characterization of assembly and biophysical properties.

Fasshauer D, Antonin W, Margittai M, Pabst S, Jahn R.

J Biol Chem. 1999 May 28;274(22):15440-6.


The synaptophysin-synaptobrevin complex: a hallmark of synaptic vesicle maturation.

Becher A, Drenckhahn A, Pahner I, Margittai M, Jahn R, Ahnert-Hilger G.

J Neurosci. 1999 Mar 15;19(6):1922-31.


Immunoglobulin light chain class multiplicity and alternative organizational forms in early vertebrate phylogeny.

Rast JP, Anderson MK, Ota T, Litman RT, Margittai M, Shamblott MJ, Litman GW.

Immunogenetics. 1994;40(2):83-99.


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