Search Results - "Vigers, Michael"

The proline-rich domain promotes Tau liquid-liquid phase separation in cells by Zhang, Xuemei, Vigers, Michael, McCarty, James, Rauch, Jennifer N, Fredrickson, Glenn H, Wilson, Maxwell Z, Shea, Joan-Emma, Han, Songi, Kosik, Kenneth S

“…Tau protein in vitro can undergo liquid-liquid phase separation (LLPS); however, observations of this phase transition in living cells are limited. To…”
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Cofactors are essential constituents of stable and seeding-active tau fibrils by Fichou, Yann, Lin, Yanxian, Rauch, Jennifer N., Vigers, Michael, Zeng, Zhikai, Srivastava, Madhur, Keller, Timothy J., Freed, Jack H., Kosik, Kenneth S., Han, Songi

“…Amyloid fibrils are cross-β–rich aggregates that are exceptionally stable forms of protein assembly. Accumulation of tau amyloid fibrils is involved in many…”
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Proteolytic Fragments of tau Produce Seeding-Competent Fibrils by Vigers, Michael, Han, Songi

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Illuminating the Structural Basis of Tau Aggregation by Intramolecular Distance Tracking: A Perspective on Methods by Zeng, Zhikai, Fichou, Yann, Vigers, Michael, Tsay, Karen, Han, Songi

“…The aggregation of the tau protein is central to several neurodegenerative diseases, collectively known as tauopathies. High-resolution views of tau tangles…”
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Heparin-induced tau filaments are structurally heterogeneous and differ from Alzheimer's disease filaments by Fichou, Yann, Vigers, Michael, Goring, Andrew K, Eschmann, Neil A, Han, Songi

“…Alzheimer's disease (AD) is characterized by the presence of tau filaments in the brain whose structure was recently solved. The formation of AD filaments is…”
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Characterizing Biofilm Extracellular Matrices with Mechanical Measurement Techniques by Vigers, Michael P., Wilking, James N.

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Oligomerization of the Human Adenosine A2AReceptor is Driven by the Intrinsically Disordered C-Terminus by Nguyen, Khanh D., Vigers, Michael, Sefah, Eric, Seppala, Susanna, Hoover, Jennifer, Mertz, Blake, O’Malley, Michelle A., Han, Songi

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Dimerization of Human Adenosine A2AReceptor - Impact of the C-Terminus by Nguyen, Khanh D., Seppala, Susanna, Vigers, Michael, Schonenbach, Nicole S., Han, Songi, O'Malley, Michelle A.

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Human Adenosine A2AR Dimerization is Driven by a C-terminal Motif by Nguyen, Khanh D.Q., Seppala, Susanna, Vigers, Michael, Schonenbach, Nicole S., Hoover, Jennifer, O'Malley, Michelle A., Han, Songi

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Precision proteoform design for 4R tau isoform selective templated aggregation by Longhini, Andrew P, DuBose, Austin, Lobo, Samuel, Vijayan, Vishnu, Bai, Yeran, Rivera, Erica Keane, Sala-Jarque, Julia, Nikitina, Arina, Carrettiero, Daniel C, Unger, Matthew T, Sclafani, Olivia R, Fu, Valerie, Beckett, Emily R, Vigers, Michael, Buée, Luc, Landrieu, Isabelle, Shell, Scott, Shea, Joan E, Han, Songi, Kosik, Kenneth S

“…Prion-like spread of disease-specific tau conformers is a hallmark of all tauopathies. A 19-residue probe peptide containing a P301L mutation and spanning the…”
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Probing the Aggregation Transition of the Disordered Protein Tau by Vigers, Michael P

“…In the Tauopathy subfamily of neurodegenerative diseases, the intrinsically disordered protein (IDP), Tau, undergoes a transition from its native disordered…”
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Homo-oligomerization of the human adenosine A2A receptor is driven by the intrinsically disordered C-terminus by Nguyen, Khanh Dinh Quoc, Vigers, Michael, Sefah, Eric, Seppälä, Susanna, Hoover, Jennifer Paige, Schonenbach, Nicole Star, Mertz, Blake, O'Malley, Michelle Ann, Han, Songi

“…G protein-coupled receptors (GPCRs) have long been shown to exist as oligomers with functional properties distinct from those of the monomeric counterparts,…”
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Homo-oligomerization of the human adenosine A 2A receptor is driven by the intrinsically disordered C-terminus by Nguyen, Khanh Dinh Quoc, Vigers, Michael, Sefah, Eric, Seppälä, Susanna, Hoover, Jennifer Paige, Schonenbach, Nicole Star, Mertz, Blake, O'Malley, Michelle Ann, Han, Songi

“…G protein-coupled receptors (GPCRs) have long been shown to exist as oligomers with functional properties distinct from those of the monomeric counterparts,…”
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