Explanipedia

Characterization of α-synuclein oligomers formed in the presence of lipid vesicles Open

Anvesh K. R. Dasari, Urmi Sengupta, Elizabeth Viverette, Mario J. Borgnia, Rakez Kayed , et al. · 2024

Aggregation of α-synuclein into oligomers and fibrils is associated with numerous neurodegenerative diseases such as Parkinson's disease (PD). Although the identity of the pathogenic species formed during the aggregation process is still u…

Characterization of Α-Synuclein Oligomers Formed in the Presence of Lipid Vesicles Open

Anvesh K. R. Dasari, Urmi Sengupta, Elizabeth Viverette, Mario J. Borgnia, Rakez Kayed , et al. · 2024

Distinct Effect of the Pathogenic Mutations on Α-Synuclein Aggregation in the Presence of Lipid Vesicles Open

Anvesh K. R. Dasari, Sungsool Wi, Rakez Kayed, Kwang Hun Lim · 2024

CD and Solid-State NMR Studies of Low-Order Oligomers of Transthyretin Open

Anvesh K. R. Dasari, Kwang Hun Lim · 2022

Toxic Misfolded Transthyretin Oligomers with Different Molecular Conformations Formed through Distinct Oligomerization Pathways Open

Anvesh K. R. Dasari, Sujung Yi, Matthew F. Coats, Sungsool Wi, Kwang Hun Lim · 2022

Protein aggregation is initiated by structural changes from native polypeptides to cytotoxic oligomers, which form cross-β structured amyloid. Identification and characterization of oligomeric intermediates are critically important for und…

Untwisted α-Synuclein Filaments Formed in the Presence of Lipid Vesicles Open

Anvesh K. R. Dasari, Lucas Dillard, Sujung Yi, Elizabeth Viverette, Alimohammad Hojjatian , et al. · 2022

Accumulation of filamentous aggregates of α-synuclein is a pathological hallmark of several neurodegenerative diseases, including Parkinson's disease (PD). The interaction between α-synuclein and phospholipids has been shown to play a crit…

Untwisted α-synuclein Filaments formed in the Presence of Lipid Vesicles Open

Anvesh K. R. Dasari, Lucas Dillard, Alimohammad Hojjatian, Urmi Sengupta, Rakez Kayed , et al. · 2021

Accumulation of filamentous aggregates of α-synuclein is a pathological hallmark of several neurodegenerative diseases including Parkinson’s disease (PD). Interaction between α-synuclein and lipids has been shown to play a critical role in…

Tau induces formation of α-synuclein filaments with distinct molecular conformations Open

Alimohammad Hojjatian, Anvesh K. R. Dasari, Urmi Sengupta, Dianne W. Taylor, Nadia Daneshparvar , et al. · 2021

Distinct cryo-EM Structure of α-synuclein Filaments derived by Tau Open

Alimohammad Hojjatian, Anvesh K. R. Dasari, Urmi Sengupta, Dianne W. Taylor, Nadia Daneshparvar , et al. · 2021

Recent structural studies of ex vivo amyloid filaments extracted from human patients demonstrated that the ex vivo filaments associated with different disease phenotypes adopt diverse molecular conformations distinct from those in vitro am…

Alpha-synuclein Fibrils Structure Determination in the Presence of Tau Using CryoEM Open

Alimohammad Hojjatian, Anvesh K. R. Dasari, Dianne W. Taylor, Nadia Daneshparvar, Fatemeh Abbasi Yeganeh , et al. · 2020

With the resolution revolution in cryo-EM structure determination [1], near atomic resolution of 3Dreconstruction became almost routinely possible opening the way for a "future which is not crystallized".Due to the low Signal to Noise Rati…

Disruption of the CD Loop by Enzymatic Cleavage Promotes the Formation of Toxic Transthyretin Oligomers through a Common Transthyretin Misfolding Pathway Open

Anvesh K. R. Dasari, Jenette Arreola, Brian Michael, Robert G. Griffin, Jeffery W. Kelly , et al. · 2020

Amyloid formation of full-length TTR involves dissociation of the native tetramers into misfolded monomers that self-assemble into amyloid. In addition to the full-length TTR, C-terminal fragments including residues 49-127 were also observ…

Structural Characterization of Cardiac Ex Vivo Transthyretin Amyloid: Insight into the Transthyretin Misfolding Pathway In Vivo Open

Anvesh K. R. Dasari, Ivan Hung, Brian Michael, Zhehong Gan, Jeffery W. Kelly , et al. · 2020

Structural characterization of misfolded protein aggregates is essential to understanding the molecular mechanism of protein aggregation associated with various protein misfolding disorders. Here, we report structural analyses of ex vivo t…

Single Particle Cryo-EM Structure of Alpha-Synuclein Fibrils Interacting with Tau Open

Alimohammad Hojjatian, Anvesh K. R. Dasari, Dianne W. Taylor, Nadia Daneshparvar, Fatemeh Abbasi Yeganeh , et al. · 2020

Covalent and Non-Covalent Strategies for the Immobilization of Tobacco Etch Virus (TEV) Protease on Superparamagnetic Nanoparticles Open

Jessica L. Norris, Tulsi Patel, Anvesh K. R. Dasari, T. A. Cope, Kwang Hun Lim , et al. · 2019

TEV protease fusion proteins were prepared and immobilized on superparamagnetic nanoparticles (SPIONs). Non-covalent (avidin-biotin) and covalent (HALOtag-chloroalkane) strategies were explored for TEV immobilization. HALOtag immobilized T…

Covalent and Non-Covalent Strategies for the Immobilization of Tobacco Etch Virus (TEV) Protease on Superparamagnetic Nanoparticles Open

Jessica L. Norris, Tulsi Patel, Anvesh K. R. Dasari, Thomas A. Cope, Kwang Hun Lim , et al. · 2019

TEV protease fusion proteins were prepared and immobilized on superparamagnetic nanoparticles (SPIONs). Non-covalent (avidin-biotin) and covalent (HALOtag-chloroalkane) strategies were explored for TEV immobilization. HALOtag immobilized T…

Transthyretin Aggregation Pathway toward the Formation of Distinct Cytotoxic Oligomers Open

Anvesh K. R. Dasari, Robert M. Hughes, Sungsool Wi, Ivan Hung, Zhehong Gan , et al. · 2019

Pathogenic Mutations Induce Partial Structural Changes in the Native β-Sheet Structure of Transthyretin and Accelerate Aggregation Open

Kwang Hun Lim, Anvesh K. R. Dasari, Renze Ma, Ivan Hung, Zhehong Gan , et al. · 2017

Amyloid formation of natively folded proteins involves global and/or local unfolding of the native state to form aggregation-prone intermediates. Here we report solid-state nuclear magnetic resonance (NMR) structural studies of amyloid der…

A Comparative Analysis of Translesion DNA Synthesis Catalyzed by a High-Fidelity DNA Polymerase Open

Anvesh K. R. Dasari, Tejal Deodhar, Anthony J. Berdis · 2017

Using Nucleotide Analogs as Biochemical Probes to Evaluate the Mechanisms Involved in Translesion Replication by a High Fidelity DNA Polymerase Open

Anvesh K. R. Dasari · 2017

Translesion DNA synthesis (TLS) allows DNA polymerases to incorporate nucleotides opposite and beyond damaged DNA. This activity is an important risk factor for the initiation and progression of genetic diseases including cancer. My study …

Solid-State NMR Studies Reveal Native-like β-Sheet Structures in Transthyretin Amyloid Open

Kwang Hun Lim, Anvesh K. R. Dasari, Ivan Hung, Zhehong Gan, Jeffery W. Kelly , et al. · 2016

Structural characterization of amyloid rich in cross-β structures is crucial for unraveling the molecular basis of protein misfolding and amyloid formation associated with a wide range of human disorders. Elucidation of the β-sheet structu…

Structural Changes Associated with Transthyretin Misfolding and Amyloid Formation Revealed by Solution and Solid-State NMR Open

Kwang Hun Lim, Anvesh K. R. Dasari, Ivan Hung, Zhehong Gan, Jeffery W. Kelly , et al. · 2016

Elucidation of structural changes involved in protein misfolding and amyloid formation is crucial for unraveling the molecular basis of amyloid formation. Here we report structural analyses of the amyloidogenic intermediate and amyloid agg…

The use of modified and non-natural nucleotides provide unique insights into pro-mutagenic replication catalyzed by polymerase eta Open

Jung-Suk Choi, Anvesh K. R. Dasari, Zhenxin Hu, Stephen J. Benkovic, Anthony J. Berdis · 2015

This report evaluates the pro-mutagenic behavior of 8-oxo-guanine (8-oxo-G) by quantifying the ability of high-fidelity and specialized DNA polymerases to incorporate natural and modified nucleotides opposite this lesion. Although high-fid…

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