| Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity YJ Zhang, YF Xu, C Cook, TF Gendron, P Roettges, CD Link, WL Lin, ... Proceedings of the National Academy of Sciences 106 (18), 7607-7612, 2009 | 697 | 2009 |
| Accumulation of pathological tau species and memory loss in a conditional model of tauopathy Z Berger, H Roder, A Hanna, A Carlson, V Rangachari, M Yue, Z Wszolek, ... Journal of Neuroscience 27 (14), 3650-3662, 2007 | 580 | 2007 |
| Substrate-targeting γ-secretase modulators TL Kukar, TB Ladd, MA Bann, PC Fraering, R Narlawar, GM Maharvi, ... Nature 453 (7197), 925-929, 2008 | 381 | 2008 |
| Amyloid-β (1− 42) rapidly forms protofibrils and oligomers by distinct pathways in low concentrations of sodium dodecylsulfate V Rangachari, BD Moore, DK Reed, LK Sonoda, AW Bridges, E Conboy, ... Biochemistry 46 (43), 12451-12462, 2007 | 221 | 2007 |
| BRI2 (ITM2b) inhibits Aβ deposition in vivo J Kim, VM Miller, Y Levites, KJ West, CW Zwizinski, BD Moore, ... Journal of Neuroscience 28 (23), 6030-6036, 2008 | 147 | 2008 |
| Secondary structure and interfacial aggregation of amyloid-β (1− 40) on sodium dodecyl sulfate micelles V Rangachari, DK Reed, BD Moore, TL Rosenberry Biochemistry 45 (28), 8639-8648, 2006 | 116 | 2006 |
| Inhibition of Aβ42 peptide aggregation by a binuclear ruthenium (II)− platinum (II) complex: potential for multimetal organometallics as anti-amyloid agents A Kumar, LM Moody, JF Olaivar, NA Lewis, RL Khade, AA Holder, ... ACS chemical neuroscience 1 (10), 691-701, 2010 | 70 | 2010 |
| Biophysical analyses of synthetic Amyloid-β (1− 42) aggregates before and after covalent cross-linking. Implications for deducing the structure of endogenous Amyloid-β oligomers BD Moore, V Rangachari, WM Tay, NM Milkovic, TL Rosenberry Biochemistry 48 (49), 11796-11806, 2009 | 66 | 2009 |
| Prion-like C-Terminal Domain of TDP-43 and α-Synuclein Interact Synergistically to Generate Neurotoxic Hybrid Fibrils. S Dhakal, CE Wyant, HE George, SE Morgan, V Rangachari Journal of Molecular Biology 433 (10), 166953, 2021 | 62 | 2021 |
| Specific soluble oligomers of amyloid-β peptide undergo replication and form non-fibrillar aggregates in interfacial environments A Kumar, LC Paslay, D Lyons, SE Morgan, JJ Correia, V Rangachari Journal of Biological Chemistry 287 (25), 21253-21264, 2012 | 55 | 2012 |
| Cause and consequence of Aβ–Lipid interactions in Alzheimer disease pathogenesis V Rangachari, DN Dean, P Rana, A Vaidya, P Ghosh Biochimica et Biophysica Acta (BBA)-Biomembranes 1860 (9), 1652-1662, 2018 | 53 | 2018 |
| Prolylpeptide Binding by the Prokaryotic SH3-like Domain of the Diphtheria Toxin Repressor: A Regulatory Switch, GP Wylie, V Rangachari, EA Bienkiewicz, V Marin, N Bhattacharya, ... Biochemistry 44 (1), 40-51, 2005 | 52 | 2005 |
| Dynamics of protofibril elongation and association involved in Aβ42 peptide aggregation in Alzheimer’s disease P Ghosh, A Kumar, B Datta, V Rangachari BMC bioinformatics 11, 1-19, 2010 | 50 | 2010 |
| Non-esterified fatty acids generate distinct low-molecular weight amyloid-β (Aβ42) oligomers along pathway different from fibril formation A Kumar, RL Bullard, P Patel, LC Paslay, D Singh, EA Bienkiewicz, ... PloS one 6 (4), e18759, 2011 | 49 | 2011 |
| Dopamine‐induced α‐synuclein oligomers show self‐and cross‐propagation properties MS Planchard, SE Exley, SE Morgan, V Rangachari Protein Science 23 (10), 1369-1379, 2014 | 47 | 2014 |
| Disorder and cysteines in proteins: A design for orchestration of conformational see-saw and modulatory functions AA Bhopatkar, VN Uversky, V Rangachari Progress in molecular biology and translational science 174, 331-373, 2020 | 45 | 2020 |
| Determination of critical nucleation number for a single nucleation amyloid-β aggregation model P Ghosh, A Vaidya, A Kumar, V Rangachari Mathematical biosciences 273, 70-79, 2016 | 43 | 2016 |
| Strain-specific Fibril Propagation by an Aβ Dodecamer. RV Dean DN, Das PK, Rana P, Burg F, Levites Y, Morgan SE, Ghosh P Scientific Reports 7, 40787. doi: 10.1038/srep40787, 2017 | 42 | 2017 |
| The natural product betulinic acid rapidly promotes amyloid-β fibril formation at the expense of soluble oligomers MS Planchard, MA Samel, A Kumar, V Rangachari ACS chemical neuroscience 3 (11), 900-908, 2012 | 41 | 2012 |
| Rationally designed dehydroalanine (ΔAla)‐containing peptides inhibit amyloid‐β (Aβ) peptide aggregation V Rangachari, ZS Davey, B Healy, BD Moore, LK Sonoda, B Cusack, ... Biopolymers: Original Research on Biomolecules 91 (6), 456-465, 2009 | 40 | 2009 |
Preetam GhoshProfessor of Computer Science, Virginia Commonwealth UniversityPotvrđena adresa e-pošte na vcu.edu
