Year |
Citation |
Score |
2023 |
Holden MR, Krzesinski BJ, Weismiller HA, Shady JR, Margittai M. MAP2 caps tau fibrils and inhibits aggregation. The Journal of Biological Chemistry. 104891. PMID 37286038 DOI: 10.1016/j.jbc.2023.104891 |
0.586 |
|
2021 |
Ledreux A, Thomas S, Hamlett ED, Trautman C, Gilmore A, Rickman Hager E, Paredes DA, Margittai M, Fortea J, Granholm AC. Small Neuron-Derived Extracellular Vesicles from Individuals with Down Syndrome Propagate Tau Pathology in the Wildtype Mouse Brain. Journal of Clinical Medicine. 10. PMID 34501378 DOI: 10.3390/jcm10173931 |
0.42 |
|
2021 |
Devitt G, Crisford A, Rice W, Weismiller HA, Fan Z, Commins C, Hyman BT, Margittai M, Mahajan S, Mudher A. Conformational fingerprinting of tau variants and strains by Raman spectroscopy. Rsc Advances. 11: 8899-8915. PMID 34381596 DOI: 10.1039/d1ra00870f |
0.542 |
|
2021 |
Weismiller HA, Holub TJ, Krzesinski BJ, Margittai M. A thiol-based intramolecular redox switch in four-repeat tau controls fibril assembly and disassembly. The Journal of Biological Chemistry. 101021. PMID 34339733 DOI: 10.1016/j.jbc.2021.101021 |
0.563 |
|
2019 |
Margittai M. Driving tau into phase-separated liquid droplets. The Journal of Biological Chemistry. 294: 11060-11061. PMID 31324714 DOI: 10.1074/Jbc.H119.009703 |
0.409 |
|
2019 |
Foote AK, Manger LH, Holden MR, Margittai M, Goldsmith RH. Time-resolved multirotational dynamics of single solution-phase tau proteins reveals details of conformational variation. Physical Chemistry Chemical Physics : Pccp. PMID 30632561 DOI: 10.1039/C8Cp06971A |
0.433 |
|
2018 |
Weismiller HA, Murphy R, Wei G, Ma B, Nussinov R, Margittai M. Structural disorder in four-repeat Tau fibrils reveals a new mechanism for barriers to cross-seeding of Tau isoforms. The Journal of Biological Chemistry. PMID 30242125 DOI: 10.1074/Jbc.Ra118.005316 |
0.71 |
|
2018 |
Li X, Dong X, Wei G, Margittai M, Nussinov R, Ma B. The distinct structural preferences of tau protein repeat domains. Chemical Communications (Cambridge, England). PMID 29774342 DOI: 10.1039/C8Cc01263F |
0.479 |
|
2017 |
Manger L, Foote A, Wood S, Holden M, Heylman K, Margittai M, Goldsmith RH. Revealing Conformational Variants of Solution-Phase Intrinsically Disordered Tau Protein at the Single-Molecule Level. Angewandte Chemie (International Ed. in English). PMID 29063723 DOI: 10.1002/Anie.201708242 |
0.398 |
|
2016 |
Meyer V, Holden MR, Weismiller HA, Eaton GR, Eaton SS, Margittai M. Fracture and Growth Are Competing Forces Determining the Fate of Conformers in Tau Fibril Populations. The Journal of Biological Chemistry. PMID 27080260 DOI: 10.1074/Jbc.M116.715557 |
0.58 |
|
2016 |
Xu L, Zheng J, Margittai M, Nussinov R, Ma B. Hyperphopsphorylation Promotes Tau Aggregation by Modulating Filament Structure and Stability. Acs Chemical Neuroscience. PMID 26854860 DOI: 10.1021/Acschemneuro.5B00294 |
0.617 |
|
2016 |
Meyer V, Margittai M. Spin Labeling and Characterization of Tau Fibrils Using Electron Paramagnetic Resonance (EPR). Methods in Molecular Biology (Clifton, N.J.). 1345: 185-99. PMID 26453213 DOI: 10.1007/978-1-4939-2978-8_12 |
0.542 |
|
2015 |
Dinkel PD, Holden MR, Matin N, Margittai M. RNA Binds to Tau Fibrils and Sustains Template-Assisted Growth. Biochemistry. 54: 4731-40. PMID 26177386 DOI: 10.1021/Acs.Biochem.5B00453 |
0.766 |
|
2015 |
Wood SL, Manger L, Holden M, Margittai M, Goldsmith R. Single Molecule Studies of Tau Protein in the Abel Trap Biophysical Journal. 108: 165a. DOI: 10.1016/J.Bpj.2014.11.908 |
0.547 |
|
2015 |
Xu L, Margittai M, Nussinov R, Ma B. Simulation of the Distribution of Disordered Tau Proteins Around Its Amyloid Fibrils Core Biophysical Journal. 108: 62a. DOI: 10.1016/J.Bpj.2014.11.371 |
0.563 |
|
2015 |
Goldsmith RH, Wood S, Manger L, Holden M, Margittai M. Exploring Tau Conformations at the Single-Molecule Level in a Microfluidic Trap Biophysical Journal. 108: 336a. DOI: 10.1016/J.Bpj.2014.11.1835 |
0.371 |
|
2014 |
Meyer V, Dinkel PD, Rickman Hager E, Margittai M. Amplification of Tau fibrils from minute quantities of seeds. Biochemistry. 53: 5804-9. PMID 25153692 DOI: 10.1021/Bi501050G |
0.776 |
|
2014 |
Meyer V, Dinkel PD, Luo Y, Yu X, Wei G, Zheng J, Eaton GR, Ma B, Nussinov R, Eaton SS, Margittai M. Single mutations in tau modulate the populations of fibril conformers through seed selection. Angewandte Chemie (International Ed. in English). 53: 1590-3. PMID 24453187 DOI: 10.1002/Anie.201308473 |
0.774 |
|
2013 |
Luo Y, Dinkel P, Yu X, Margittai M, Zheng J, Nussinov R, Wei G, Ma B. Molecular insights into the reversible formation of tau protein fibrils. Chemical Communications (Cambridge, England). 49: 3582-4. PMID 23527380 DOI: 10.1039/C3Cc00241A |
0.765 |
|
2013 |
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. Small misfolded Tau species are internalized via bulk endocytosis and anterogradely and retrogradely transported in neurons. The Journal of Biological Chemistry. 288: 1856-70. PMID 23188818 DOI: 10.1074/Jbc.M112.394528 |
0.589 |
|
2012 |
Siddiqua A, Luo Y, Meyer V, Swanson MA, Yu X, Wei G, Zheng J, Eaton GR, Ma B, Nussinov R, Eaton SS, Margittai M. Conformational basis for asymmetric seeding barrier in filaments of three- and four-repeat tau. Journal of the American Chemical Society. 134: 10271-8. PMID 22656332 DOI: 10.1021/Ja303498Q |
0.818 |
|
2012 |
Yu X, Luo Y, Dinkel P, Zheng J, Wei G, Margittai M, Nussinov R, Ma B. Cross-seeding and conformational selection between three- and four-repeat human Tau proteins. The Journal of Biological Chemistry. 287: 14950-9. PMID 22393063 DOI: 10.1074/Jbc.M112.340794 |
0.713 |
|
2011 |
Dinkel PD, Siddiqua A, Huynh H, Shah M, Margittai M. Variations in filament conformation dictate seeding barrier between three- and four-repeat tau. Biochemistry. 50: 4330-6. PMID 21510682 DOI: 10.1021/Bi2004685 |
0.731 |
|
2010 |
Siddiqua A, Margittai M. Three- and four-repeat Tau coassemble into heterogeneous filaments: an implication for Alzheimer disease. The Journal of Biological Chemistry. 285: 37920-6. PMID 20921227 DOI: 10.1074/Jbc.M110.185728 |
0.801 |
|
2008 |
Margittai M, Langen R. Fibrils with parallel in-register structure constitute a major class of amyloid fibrils: molecular insights from electron paramagnetic resonance spectroscopy. Quarterly Reviews of Biophysics. 41: 265-97. PMID 19079806 DOI: 10.1017/S0033583508004733 |
0.495 |
|
2007 |
Chen M, Margittai M, Chen J, Langen R. Investigation of alpha-synuclein fibril structure by site-directed spin labeling. The Journal of Biological Chemistry. 282: 24970-9. PMID 17573347 DOI: 10.1074/Jbc.M700368200 |
0.365 |
|
2006 |
Margittai M, Langen R. Spin labeling analysis of amyloids and other protein aggregates. Methods in Enzymology. 413: 122-39. PMID 17046394 DOI: 10.1016/S0076-6879(06)13007-4 |
0.37 |
|
2006 |
Margittai M, Langen R. Side chain-dependent stacking modulates tau filament structure. The Journal of Biological Chemistry. 281: 37820-7. PMID 17023423 DOI: 10.1074/Jbc.M605336200 |
0.445 |
|
2004 |
Margittai M, Langen R. Template-assisted filament growth by parallel stacking of tau. Proceedings of the National Academy of Sciences of the United States of America. 101: 10278-83. PMID 15240881 DOI: 10.1073/Pnas.0401911101 |
0.455 |
|
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