Vijayaraghavan Rangachari

发表

Accumulation of Pathological Tau Species and Memory Loss in a Conditional Model of Tauopathy

K. Ashe, M. Hutton, Z. Wszolek, 2007, The Journal of Neuroscience.

Granulins modulate liquid–liquid phase separation and aggregation of the prion-like C-terminal domain of the neurodegeneration-associated protein TDP-43

V. Uversky, Vijayaraghavan Rangachari, Anukool A. Bhopatkar, 2020, The Journal of Biological Chemistry.

Granulins modulate liquid-liquid phase separation and aggregation of TDP-43 C-terminal domain

V. Uversky, Vijayaraghavan Rangachari, Anukool A. Bhopatkar, 2019, bioRxiv.

Aqueous RAFT Synthesis of Low Molecular Weight Anionic Polymers for Determination of Structure/Binding Interactions with Gliadin.

Lisa K. Kemp, S. Karim, Vijayaraghavan Rangachari, 2020, Macromolecular bioscience.

Dopamine‐induced α‐synuclein oligomers show self‐ and cross‐propagation properties

Vijayaraghavan Rangachari, S. Morgan, Matthew S Planchard, 2014, Protein science : a publication of the Protein Society.

Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity

L. Petrucelli, D. Dickson, C. Link, 2009, Proceedings of the National Academy of Sciences.

Disorder and cysteines in proteins: A design for orchestration of conformational see-saw and modulatory functions.

V. Uversky, Vijayaraghavan Rangachari, Anukool A. Bhopatkar, 2020, Progress in molecular biology and translational science.

Prion-like C-terminal domain of TDP-43 and α-Synuclein interact synergistically to generate neurotoxic hybrid fibrils.

Vijayaraghavan Rangachari, S. Morgan, S. Dhakal, 2021, Journal of molecular biology.

Prion-like C-terminal domain of TDP-43 and α-Synuclein interact synergistically to generate neurotoxic hybrid fibrils

Vijayaraghavan Rangachari, S. Morgan, S. Dhakal, 2020, bioRxiv.

Disulfide bonds and disorder in granulin‐3: An unusual handshake between structural stability and plasticity

V. Uversky, Vijayaraghavan Rangachari, T. Kukar, 2017, Protein science : a publication of the Protein Society.

BRI2 (ITM2b) Inhibits Aβ Deposition In Vivo

D. Dickson, S. Younkin, F. Zou, 2008, The Journal of Neuroscience.

Ganglioside enriched phospholipid vesicles induce cooperative Aβ oligomerization and membrane disruption

P. Ghosh, Vijayaraghavan Rangachari, Priyanka Bose, 2022, bioRxiv.

Cytoplasmic Colocalization of Granulins and TDP-43 Prion-like Domain Involves Electrostatically Driven Coacervation Tuned by the Redox State of Cysteines

Vijayaraghavan Rangachari, Anukool A. Bhopatkar, S. Dhakal, 2021, bioRxiv.

Distinct neurotoxic TDP-43 fibril polymorphs are generated by heterotypic interactions with α-Synuclein

R. Kayed, A. Paravastu, Vijayaraghavan Rangachari, 2022, bioRxiv.

Effects of Stereochemistry and Hydrogen Bonding on Glycopolymer - Amyloid-β Interactions.

Lisa K. Kemp, Vijayaraghavan Rangachari, S. Morgan, 2020, Biomacromolecules.

Propagation of an Aβ Dodecamer Strain Involves a Three-Step Mechanism and a Key Intermediate.

P. Ghosh, Ryan P. Campbell, Vijayaraghavan Rangachari, 2018, Biophysical journal.

Biophysical characteristics of lipid‐induced Aβ oligomers correlate to distinctive phenotypes in transgenic mice

Y. Levites, Vijayaraghavan Rangachari, K. Dillon, 2021, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

Strain-specific Fibril Propagation by an Aβ Dodecamer

P. Ghosh, Y. Levites, Vijayaraghavan Rangachari, 2017, Scientific Reports.

Measurement of Critical Micelle Concentration

J. Correia, Amit Kumar, Vijayaraghavan Rangachari, 2012 .

Rationally designed dehydroalanine (ΔAla)‐containing peptides inhibit amyloid‐β (Aβ) peptide aggregation

T. Rosenberry, Vijayaraghavan Rangachari, Ghulam M. Maharvi, 2009, Biopolymers.

Are Granulins Copper Sequestering Proteins?

Vijayaraghavan Rangachari, Anukool A. Bhopatkar, 2020, bioRxiv.

Cysteine-rich granulin-3 rapidly promotes amyloid-β fibrils in both redox states.

Vijayaraghavan Rangachari, Anukool A. Bhopatkar, M. Moss, 2019, The Biochemical journal.

Cloning, expression and purification of the low-complexity region of RanBP9 protein.

F. Huang, Vijayaraghavan Rangachari, Krishna Sapkota, 2020, Protein expression and purification.

Substrate-targeting γ-secretase modulators

M. Wolfe, D. Walsh, T. Golde, 2008, Nature.

Fully reduced granulin-B is intrinsically disordered and displays concentration-dependent dynamics.

Vijayaraghavan Rangachari, C. Mundoma, R. Reed, 2016, Protein engineering, design & selection : PEDS.

Hiding in Plain Sight-Could a Common Molecular Mechanism Define Neurodegenerative Diseases ?

Vijayaraghavan Rangachari, 2014 .

Specific Soluble Oligomers of Amyloid-β Peptide Undergo Replication and Form Non-fibrillar Aggregates in Interfacial Environments*

J. Correia, Amit Kumar, Vijayaraghavan Rangachari, 2012, The Journal of Biological Chemistry.

αS Oligomers Generated from Interactions with a Polyunsaturated Fatty Acid and a Dopamine Metabolite Differentially Interact with Aβ to Enhance Neurotoxicity.

Vijayaraghavan Rangachari, S. Dhakal, Courtney E. Wyant, 2021, ACS chemical neuroscience.

αS oligomers generated from polyunsaturated fatty acid and dopamine metabolite differentially interact with Aβ to enhance neurotoxicity

Vijayaraghavan Rangachari, S. Dhakal, Courtney E. Wyant, 2021, bioRxiv.

Biophysical analyses of synthetic amyloid-beta(1-42) aggregates before and after covalent cross-linking. Implications for deducing the structure of endogenous amyloid-beta oligomers.

T. Rosenberry, N. Milkovic, Vijayaraghavan Rangachari, 2009, Biochemistry.

Inhibition of Aβ42 peptide aggregation by a binuclear ruthenium(II)-platinum(II) complex: Potential for multi-metal organometallics as anti-amyloid agents.

Amit Kumar, Vijayaraghavan Rangachari, Yong Zhang, 2010, ACS chemical neuroscience.

Cause and consequence of Aβ - Lipid interactions in Alzheimer disease pathogenesis.

P. Ghosh, A. Vaidya, Vijayaraghavan Rangachari, 2018, Biochimica et biophysica acta. Biomembranes.

Secondary Structure and Interfacial Aggregation of Amyloid- â(1 40) on Sodium Dodecyl Sulfate Micelles

T. Rosenberry, Vijayaraghavan Rangachari, B. Moore, 2022 .

A Modified Stokes-Einstein Equation for A Beta Aggregation

Preetam Ghosh, Ashwin Vaidya, Srisairam Achuthan, 2016 .

A modified Stokes-Einstein equation for Aβ aggregation

Preetam Ghosh, Ashwin Vaidya, Srisairam Achuthan, 2011, BMC Bioinformatics.

Aqueous RAFT Synthesis of Glycopolymers for Determination of Saccharide Structure and Concentration Effects on Amyloid β Aggregation.

Fei Liu, C. McCormick, E. Kharlampieva, 2017, Biomacromolecules.

Non-Esterified Fatty Acids Generate Distinct Low-Molecular Weight Amyloid-beta ( A beta 42 ) Oligomers along Pathway Different from Fibril Formation

Vijayaraghavan Rangachari, Dipti Singh, Dipti Singh, 2018 .

Non-Esterified Fatty Acids Generate Distinct Low-Molecular Weight Amyloid-β (Aβ42) Oligomers along Pathway Different from Fibril Formation

Dipti Singh, Amit Kumar, Vijayaraghavan Rangachari, 2011, PloS one.

Amyloid-beta(1-42) rapidly forms protofibrils and oligomers by distinct pathways in low concentrations of sodium dodecylsulfate.

T. Rosenberry, Vijayaraghavan Rangachari, D. Hartigan, 2007, Biochemistry.

Sugar distributions on gangliosides guide the formation and stability of amyloid-β oligomers

Vijayaraghavan Rangachari, Jhinuk Saha, Brea J. Ford, 2023, bioRxiv.

BRI2 (ITM2b) Inhibits Aβ Deposition In Vivo

D. Dickson, S. Younkin, F. Zou, 2008, Journal of Neuroscience.

Sequence of ligand binding and structure change in the diphtheria toxin repressor upon activation by divalent transition metals.

T. Logan, Vijayaraghavan Rangachari, E. Bienkiewicz, 2005, Biochemistry.

Prolylpeptide binding by the prokaryotic SH3-like domain of the diphtheria toxin repressor: a regulatory switch.

T. Logan, N. Bhattacharya, Vijayaraghavan Rangachari, 2005, Biochemistry.

Conformational Dynamics of Specific Aβ Oligomers Govern Their Ability To Replicate and Induce Neuronal Apoptosis.

Vijayaraghavan Rangachari, Kayla M. Pate, M. Moss, 2016, Biochemistry.

Biomolecular condensates – extant relics or evolving microcompartments?

Vijayaraghavan Rangachari, 2023, Communications biology.

Secondary structure and interfacial aggregation of amyloid-beta(1-40) on sodium dodecyl sulfate micelles.

T. Rosenberry, Vijayaraghavan Rangachari, B. Moore, 2006, Biochemistry.

Determination of critical nucleation number for a single nucleation amyloid-β aggregation model.

P. Ghosh, Amit Kumar, A. Vaidya, 2016, Mathematical biosciences.

The natural product betulinic acid rapidly promotes amyloid-β fibril formation at the expense of soluble oligomers.

Amit Kumar, Vijayaraghavan Rangachari, Matthew S. Planchard, 2012, ACS chemical neuroscience.

Self-Propagative Replication of Aβ Oligomers Suggests Potential Transmissibility in Alzheimer Disease

Amit Kumar, Vijayaraghavan Rangachari, Kayla M. Pate, 2014, PloS one.

A network thermodynamic analysis of amyloid aggregation along competing pathways

Vijayaraghavan Rangachari, Preetam Ghosh, J. Pateras, 2021, Appl. Math. Comput..

Sugar distributions on gangliosides guide the formation and stability of amyloid-β oligomers.

Vijayaraghavan Rangachari, S. Morgan, Jhinuk Saha, 2023, Biophysical chemistry.

Fatty Acid Concentration and Phase Transitions Modulate Aβ Aggregation Pathways

P. Ghosh, A. Vaidya, Vijayaraghavan Rangachari, 2017, Scientific Reports.

Stability analysis of 4-species Aβ aggregation model: A novel approach to obtaining physically meaningful rate constants

Preetam Ghosh, Ashwin Vaidya, Vijayaraghavan Rangachari, 2013, Appl. Math. Comput..

Dynamics of protofibril elongation and association involved in Aβ42 peptide aggregation in Alzheimer’s disease

Preetam Ghosh, Amit Kumar, Bhaswati Datta, 2010, BMC Bioinformatics.

Estimating the dynamics of protofibril elongation involved in Aβ42 peptide aggregation in Alzheimer's disease

Preetam Ghosh, Amit Kumar, Bhaswati Datta, 2010, BCB '10.

De novo amyloid peptides with subtle sequence variations differ in their self-assembly and nanomechanical properties

Lisa K. Kemp, Vijayaraghavan Rangachari, P. Wadhwani, 2023, bioRxiv.

Global fitting and parameter identifiability for amyloid-β aggregation with competing pathways

Ashwin Vaidya, Preetam Ghosh, Pratip Rana, 2020, 2020 IEEE 20th International Conference on Bioinformatics and Bioengineering (BIBE).

A game-theoretic approach to deciphering the dynamics of amyloid-β aggregation along competing pathways

P. Ghosh, A. Vaidya, Vijayaraghavan Rangachari, 2019, bioRxiv.

Large Fatty Acid-derived Aβ42 oligomers Form Ring-like Assemblies

U. Hansmann, Wenhui Xi, Vijayaraghavan Rangachari, 2018, bioRxiv.

Large Fatty Acid-derived Aβ42 oligomers Form Ring-like Assemblies

U. Hansmann, Wenhui Xi, Vijayaraghavan Rangachari, 2018, bioRxiv.

Hiding in Plain Sight-Could a Common Molecular Mechanism Define Neurodegenerative

Vijayaraghavan Rangachari, 2013 .

Charge and Redox States Modulate Granulin-TDP-43 Coacervation Toward Phase Separation or Aggregation.

Vijayaraghavan Rangachari, S. Morgan, Anukool A. Bhopatkar, 2022, Biophysical Journal.

α-Synuclein emulsifies TDP-43 prion-like domain – RNA liquid droplets to promote heterotypic amyloid fibrils

Azin Mirzazadeh, Vijayaraghavan Rangachari, Ayanjeet Ghosh, 2023, bioRxiv.

Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity

L. Petrucelli, D. Dickson, C. Link, 2009, Proceedings of the National Academy of Sciences.

Design of peptides with α,β-dehydro residues: a dipeptide with a branched β-carbon dehydro residue at the (i+1) position, methyl N-(benzyloxycarbonyl)-α,β-didehydrovalyl-l-tryptophanate

Vijayaraghavan Rangachari, 2001 .

α-Synuclein emulsifies TDP-43 prion-like domain-RNA liquid droplets to promote heterotypic amyloid fibrils.

Azin Mirzazadeh, Vijayaraghavan Rangachari, Ayanjeet Ghosh, 2023, Communications biology.

The Aquila Digital Community The Aquila Digital Community

Vijayaraghavan Rangachari, Anukool A. Bhopatkar, 2022 .

The Aquila Digital Community The Aquila Digital Community

Vijayaraghavan Rangachari, S. Dhakal, Courtney E. Wyant, 2022 .

The Aquila Digital Community The Aquila Digital Community

Vijayaraghavan Rangachari, E. Bienkiewicz, Lea C. Paslay, 2022 .