Molecular Medicine, Biochemistry, Cancer Research, Biophysics
34
Scopus Publications
2135
Scholar Citations
21
Scholar h-index
30
Scholar i10-index
Scopus Publications
Mechanism-selective inhibition of α-synuclein aggregation by the chaperone-like BRICHOS domain Laurène Adam, Willem Hendrik Molenkamp, Jan Stanislaw Nowak, Azad Farzadfard, Koen Gaarthuis, Rakesh Kumar, Janni Nielsen, Daniel E. Otzen, Jan Johansson, Axel Abelein Journal of Biological Chemistry, 2026 Current therapeutic approaches for Parkinson's disease and other synucleinopathies alleviate symptoms but fail to effectively prevent disease progression. As a result, there is an increasing focus on alternative disease-modifying strategies where molecular chaperones are emerging candidates. Recently, the chaperone-like Bri2 BRICHOS domain has been shown to be a promising therapeutic candidate, inhibiting amyloid formation and associated toxicity of multiple amyloidogenic proteins including human α-synuclein (αSyn). To advance the development of Bri2 BRICHOS as a therapeutic, in vivo tests in mice are necessary, which commonly rely on the injections of preformed fibrils of mouse αSyn. Here, we investigate the inhibitory mechanism of Bri2 BRICHOS on mouse αSyn aggregation and fibril interaction. In contrast to previous results on human αSyn, we found that Bri2 BRICHOS exhibits a very modest inhibitory effect on mouse αSyn aggregation, which is only observed under gentle shaking or quiescent conditions. While Bri2 BRICHOS binds with similar affinities to the respective fibrils, we observed that differences in the underlying nucleation mechanisms of mouse versus human αSyn fibril formation explain the impaired suppression of mouse αSyn fibrillation under strong shaking conditions. The more fragile nature of mouse αSyn fibrils causes stronger contributions of fibril fragmentation processes compared to surface-catalyzed secondary nucleation-the dominant nucleation mechanism for human αSyn. In conclusion, these findings provide molecular insights into the mechanism-of-action of Bri2 BRICHOS-mediated inhibition of αSyn aggregation as a selective chaperone-based inhibitor of surface-catalyzed secondary nucleation pathways, which facilitates informed choices of in vivo model systems for future treatment studies.
Diagnostic Performance of the α-Synuclein Seed Amplification Assay for Dementia With Lewy Bodies Rakesh Kumar, Stephanie Gravett, Vesna Jelic, Johannes Lange, Linn Oftedal, Arianna Ciullini, Merve Begüm Bacınoğlu, Chiara Maria Giulia De Luca, Lola Hamied, Catherine Birck, Frederic Blanc, Patty L. Hoede, Afina W. Lemstra, Maria Camila Gonzalez, Dag Aarsland, Charlotte E. Teunissen, Olivier Bousiges, Fabio Moda, Jodi Maple-Grødem, Axel Abelein, Daniel Ferreira Neurology, 2026 BACKGROUND AND OBJECTIVES: The α-synuclein (α-syn) seed amplification assay (SAA) has shown promising results for diagnosing dementia with Lewy bodies (DLB) using CSF samples. A barrier to implementing α-syn SAA clinically is the use of different protocols for the assay. It is unknown how different protocols perform in comparison with each other. We compared the performance of α-syn SAA across 4 laboratories using CSF samples of patients with DLB. METHODS: This was a retrospective cross-sectional study that included data from 4 different European laboratories. We included probable patients with DLB with a positive dopamine transporter (DaT)-SCAN and known amyloid-β status who had mild-to-moderate dementia, along with age-matched and sex-matched controls. The α-syn SAA was run across 4 laboratories using different protocols varying α-syn concentration and plate reader settings. CSF samples were provided by a fifth independent laboratory, which also performed statistical and result analyses. RESULTS: We included 20 patients with DLB (mean age 67 ± 6 years, 60% male) and 10 controls (mean age 67 ± 2 years, 70% male). Neuropathologic confirmation was available for 2 patients with DLB. On average, the 4 laboratories achieved 78.8% sensitivity (minimum 55%, maximum 100%), 77.5% specificity (minimum 60%, maximum 100%), and 78.5% accuracy (minimum 57%, maximum 100%) for discriminating DLB from controls, but our findings show that diagnostic performance of SAA varied across laboratories: Lab A achieved 100% sensitivity (CI 84%-100%) and 100% specificity (CI 72%-100%); Lab B achieved 85% sensitivity (CI 64%-95%) and 90% specificity (CI 59%-99%); Lab C achieved 55% sensitivity (CI 34%-74%) and 60% specificity (CI 31%-83%); and Lab D achieved 75% sensitivity (CI 53%-89%) and 60% specificity (CI 31%-83%). In general, SAA results showed numerically lower sensitivity in β-amyloid (Aβ)-positive patients with DLB (70%) compared with Aβ-negative patients with DLB (87.5%) (nonstatistically significant). A fair agreement of SAA results was obtained across the 4 laboratories (average κ = 0.246). DISCUSSION: This study highlights challenges for the reproducibility of α-syn SAA results across different protocols applied by different laboratories. This finding, together with the methodological variability reported across laboratories, may challenge the clinical implementation of the α-syn SAA. This study provides relevant support for initiating harmonization and standardization of SAA protocols to move the field toward the clinical implementation of SAAs for the biomarker-based diagnosis of DLB. CLASSIFICATION OF EVIDENCE: This study provides Class III evidence of variations in the accuracy of CSF α-syn SAA across 4 separate laboratories in distinguishing patients with DLB from healthy controls.
Chaperone-Mediated Regulation of Tau Phase Separation, Fibrillation, and Toxicity Cecilia Mörman, Axel Leppert, Giusy Pizzirusso, Zihan Zheng, Xun Sun, Rakesh Kumar, Henrik Biverstål, Michael Landreh, Jan Johansson, Luis Enrique Arroyo-Garcia, Jinghui Luo, Gefei Chen, Axel Abelein Journal of the American Chemical Society, 2025 Biological condensates are involved in several essential processes but may also be tangled into disease progression in protein misfolding diseases such as Alzheimer's disease and tauopathies. One hallmark of these disorders is the appearance of fibrillar aggregates formed by microtubule-stabilizing Tau protein. Notably, Tau can also assemble into biological condensates and droplets via liquid-liquid phase separation (LLPS). The molecular mechanisms of the conversion of functional Tau toward insoluble fibrils, potentially via LLPS processes, remain largely unknown, and efficient treatment approaches to target toxic pathways and species are still missing. Here, we show that the molecular chaperone-like Bri2 BRICHOS domain efficiently inhibits full-length Tau fibril formation and subsequent neurotoxicity by specifically suppressing secondary nucleation processes. Further, at substoichiometric ratios, Bri2 BRICHOS modulates the potency of Tau to form droplets, incorporates into Tau droplets, and alters the dynamic behavior of Tau. In contrast, at superstoichiometric Bri2 BRICHOS ratios, Tau droplet formation is abolished. Finally, Bri2 BRICHOS reduces Tau fibril toxicity in electrophysiological experiments on hippocampal slice preparations. Taken together, Bri2 BRICHOS targets molecular processes related to protein misfolding, where our study provides molecular insights into how the inhibition of secondary nucleation pathways and modulated droplet formation are eventually linked to attenuated neurotoxicity.
Helicobacter pylori CagA protein is a potent and broad-spectrum amyloid inhibitor Zhen Jin, William Pallisgaard Olsen, Cecilia Mörman, Axel Leppert, Rakesh Kumar, Andreas Møllebjerg, Lotte Godthaab Nielsen, Olena V. Moshynets, Mykhaylo S. Frasinyuk, Jokin Yeregui Elosua, Daniel Ferreira, Axel Abelein, Michael Landreh, Stefan D. Knight, Jan Johansson, Daniel E. Otzen, Gefei Chen Science Advances, 2025 Bacteria, the smallest and most abundant life forms on Earth, have been a source of insights that have had a considerable impact on human health. Helicobacter pylori has captured substantial attention due to its role in provoking an array of gastrointestinal ailments and other human diseases. Here, we report that H. pylori releases the protein CagA (cytotoxin-associated gene A) that strongly inhibits formation of both functional (bacterial biofilm) and pathogenic amyloid assemblies by targeting various stages during fibril formation. CagA’s broad substrate specificity reveals a mechanism whereby H. pylori interferes with other bacteria and humans, offering approaches to combat bacterial infections and human protein misfolding diseases.
Identification of potential aggregation hotspots on Aβ42 fibrils blocked by the anti-amyloid chaperone-like BRICHOS domain Rakesh Kumar, Tanguy Le Marchand, Laurène Adam, Raitis Bobrovs, Gefei Chen, Jēkabs Fridmanis, Nina Kronqvist, Henrik Biverstål, Kristaps Jaudzems, Jan Johansson, Guido Pintacuda, Axel Abelein Nature Communications, 2024 Protein misfolding can generate toxic intermediates, which underlies several devastating diseases, such as Alzheimer’s disease (AD). The surface of AD-associated amyloid-β peptide (Aβ) fibrils has been suggested to act as a catalyzer for self-replication and generation of potentially toxic species. Specifically tailored molecular chaperones, such as the BRICHOS protein domain, were shown to bind to amyloid fibrils and break this autocatalytic cycle. Here, we identify a site on the Aβ42 fibril surface, consisting of three C-terminal β-strands and particularly the solvent-exposed β-strand stretching from residues 26–28, which is efficiently sensed by a designed variant of Bri2 BRICHOS. Remarkably, while only a low amount of BRICHOS binds to Aβ42 fibrils, fibril-catalyzed nucleation processes are effectively prevented, suggesting that the identified site acts as a catalytic aggregation hotspot, which can specifically be blocked by BRICHOS. Hence, these findings provide an understanding how toxic nucleation events can be targeted by molecular chaperones.
Specific inhibition of α-synuclein oligomer generation and toxicity by the chaperone domain Bri2 BRICHOS Laurène Adam, Rakesh Kumar, Luis Enrique Arroyo‐Garcia, Willem Hendrik Molenkamp, Jan Stanislaw Nowak, Hannah Klute, Azad Farzadfard, Rami Alkenayeh, Janni Nielsen, Henrik Biverstål, Daniel E. Otzen, Jan Johansson, Axel Abelein Protein Science, 2024 Protein misfolding and aggregation are involved in several neurodegenerative disorders, such as α‐synuclein (αSyn) implicated in Parkinson's disease, where new therapeutic approaches remain essential to combat these devastating diseases. Elucidating the microscopic nucleation mechanisms has opened new opportunities to develop therapeutics against toxic mechanisms and species. Here, we show that naturally occurring molecular chaperones, represented by the anti‐amyloid Bri2 BRICHOS domain, can be used to target αSyn‐associated nucleation processes and structural species related to neurotoxicity. Our findings revealed that BRICHOS predominantly suppresses the formation of new nucleation units on the fibrils surface (secondary nucleation), decreasing the oligomer generation rate. Further, BRICHOS directly binds to oligomeric αSyn species and effectively diminishes αSyn fibril‐related toxicity. Hence, our studies show that molecular chaperones can be utilized as tools to target molecular processes and structural species related to αSyn neurotoxicity and have the potential as protein‐based treatments against neurodegenerative disorders.
Misfolded alpha-synuclein detection by RT-QuIC in dementia with lewy bodies: a systematic review and meta-analysis Carmen Peña-Bautista, Rakesh Kumar, Miguel Baquero, Jan Johansson, Consuelo Cháfer-Pericás, Axel Abelein, Daniel Ferreira Frontiers in Molecular Biosciences, 2023 Introduction: Dementia with Lewy Bodies (DLB) is the second most common cause of neurodegenerative dementia after Alzheimer’s disease (AD), but the field is still lacking a specific biomarker for its core pathology: alpha synuclein (α-syn). Realtime quaking induced conversion (RT-QuIC) has recently emerged as a strong biomarker candidate to detect misfolded α-syn in DLB. However, the variability in the parameters of the technique and the heterogeneity of DLB patients make the reproducibility of the results difficult. Here, we provide an overview of the state-of-the-art research of α-syn RT-QuIC in DLB focused on: (1) the capacity of α-syn RT-QuIC to discriminate DLB from controls, Parkinson’s disease (PD) and AD; (2) the capacity of α-syn RT-QuIC to identify prodromal stages of DLB; and (3) the influence of co-pathologies on α-syn RT-QuIC’s performance. We also assessed the influence of different factors, such as technical conditions (e.g., temperature, pH, shaking-rest cycles), sample type, and clinical diagnosis versus autopsy confirmation.Methods: We conducted a systematic review following the PRISMA guidelines in August 2022, without any limits in publication dates. Search terms were combinations of “RT-QuIC” and “Lewy Bodies,” “DLB” or “LBD”.Results: Our meta-analysis shows that α-syn RT-QuIC reaches very high diagnostic performance in discriminating DLB from both controls (pooled sensitivity and specificity of 0.94 and 0.96, respectively) and AD (pooled sensitivity and specificity of 0.95 and 0.88) and is promising for prodromal phases of DLB. However, the performance of α-syn RT-QuIC to discriminate DLB from PD is currently low due to low specificity (pooled sensitivity and specificity of 0.94 and 0.11). Our analysis showed that α-syn RT-QuIC’s performance is not substantially influenced by sample type or clinical diagnosis versus autopsy confirmation. Co-pathologies did not influence the performance of α-syn RT-QuIC, but the number of such studies is currently limited. We observed technical variability across published articles. However, we could not find a clear effect of technical variability on the reported results.Conclusion: There is currently enough evidence to test misfolded α-syn by RT-QuIC for clinical use. We anticipate that harmonization of protocols across centres and advances in standardization will facilitate the clinical establishment of misfolded α-syn detection by RT-QuIC.
Molecular Mechanisms of Amyloid-β Self-Assembly Seeded by In Vivo-Derived Fibrils and Inhibitory Effects of the BRICHOS Chaperone Rakesh Kumar, Luis Enrique Arroyo-García, Shaffi Manchanda, Laurène Adam, Giusy Pizzirusso, Henrik Biverstål, Per Nilsson, André Fisahn, Jan Johansson, Axel Abelein ACS Chemical Neuroscience, 2023 Self-replication of amyloid-β-peptide (Aβ) fibril formation is a hallmark in Alzheimer’s disease (AD). Detailed insights have been obtained in Aβ self-assembly in vitro, yet whether similar mechanisms are relevant in vivo has remained elusive. Here, we investigated the ability of in vivo-derived Aβ fibrils from two different amyloid precursor protein knock-in AD mouse models to seed Aβ42 aggregation, where we quantified the microscopic rate constants. We found that the nucleation mechanism of in vivo-derived fibril-seeded Aβ42 aggregation can be described with the same kinetic model as that in vitro. Further, we identified the inhibitory mechanism of the anti-amyloid BRICHOS chaperone on seeded Aβ42 fibrillization, revealing a suppression of secondary nucleation and fibril elongation, which is strikingly similar as observed in vitro. These findings hence provide a molecular understanding of the Aβ42 nucleation process triggered by in vivo-derived Aβ42 propagons, providing a framework for the search for new AD therapeutics.
Spidroin N-terminal domain forms amyloid-like fibril based hydrogels and provides a protein immobilization platform Tina Arndt, Kristaps Jaudzems, Olga Shilkova, Juanita Francis, Mathias Johansson, Peter R. Laity, Cagla Sahin, Urmimala Chatterjee, Nina Kronqvist, Edgar Barajas-Ledesma, Rakesh Kumar, Gefei Chen, Roger Strömberg, Axel Abelein, Maud Langton, Michael Landreh, Andreas Barth, Chris Holland, Jan Johansson, Anna Rising Nature Communications, 2022 Recombinant spider silk proteins (spidroins) have multiple potential applications in development of novel biomaterials, but their multimodal and aggregation-prone nature have complicated production and straightforward applications. Here, we report that recombinant miniature spidroins, and importantly also the N-terminal domain (NT) on its own, rapidly form self-supporting and transparent hydrogels at 37 °C. The gelation is caused by NT α-helix to β-sheet conversion and formation of amyloid-like fibrils, and fusion proteins composed of NT and green fluorescent protein or purine nucleoside phosphorylase form hydrogels with intact functions of the fusion moieties. Our findings demonstrate that recombinant NT and fusion proteins give high expression yields and bestow attractive properties to hydrogels, e.g., transparency, cross-linker free gelation and straightforward immobilization of active proteins at high density.
Molecular Structure of Cu(II)-Bound Amyloid-β Monomer Implicated in Inhibition of Peptide Self-Assembly in Alzheimer's Disease Axel Abelein, Simone Ciofi-Baffoni, Cecilia Mörman, Rakesh Kumar, Andrea Giachetti, Mario Piccioli, Henrik Biverstål Jacs Au, 2022 Metal ions, such as copper and zinc ions, have been shown to strongly modulate the self-assembly of the amyloid-β (Aβ) peptide into insoluble fibrils, and elevated concentrations of metal ions have been found in amyloid plaques of Alzheimer’s patients. Among the physiological transition metal ions, Cu(II) ions play an outstanding role since they can trigger production of neurotoxic reactive oxygen species. In contrast, structural insights into Cu(II) coordination of Aβ have been challenging due to the paramagnetic nature of Cu(II). Here, we employed specifically tailored paramagnetic NMR experiments to determine NMR structures of Cu(II) bound to monomeric Aβ. We found that monomeric Aβ binds Cu(II) in the N-terminus and combined with molecular dynamics simulations, we could identify two prevalent coordination modes of Cu(II). For these, we report here the NMR structures of the Cu(II)–bound Aβ complex, exhibiting heavy backbone RMSD values of 1.9 and 2.1 Å, respectively. Further, applying aggregation kinetics assays, we identified the specific effect of Cu(II) binding on the Aβ nucleation process. Our results show that Cu(II) efficiently retards Aβ fibrillization by predominately reducing the rate of fibril-end elongation at substoichiometric ratios. A detailed kinetic analysis suggests that this specific effect results in enhanced Aβ oligomer generation promoted by Cu(II). These results can quantitatively be understood by Cu(II) interaction with the Aβ monomer, forming an aggregation inert complex. In fact, this mechanism is strikingly similar to other transition metal ions, suggesting a common mechanism of action of retarding Aβ self-assembly, where the metal ion binding to monomeric Aβ is a key determinant.
α-Synuclein Aggregation Intermediates form Fibril Polymorphs with Distinct Prion-like Properties Surabhi Mehra, Sahil Ahlawat, Harish Kumar, Debalina Datta, Ambuja Navalkar, Nitu Singh, Komal Patel, Laxmikant Gadhe, Pradeep Kadu, Rakesh Kumar, Narendra N. Jha, Arunima Sakunthala, Ajay S. Sawner, Ranjith Padinhateeri, Jayant B. Udgaonkar, Vipin Agarwal, Samir K. Maji Journal of Molecular Biology, 2022
P53 amyloid formation leading to its loss of function: Implications in cancer pathogenesis Saikat Ghosh, Shimul Salot, Shinjinee Sengupta, Ambuja Navalkar, Dhiman Ghosh, Reeba Jacob, Subhadeep Das, Rakesh Kumar, Narendra Nath Jha, Shruti Sahay, Surabhi Mehra, Ganesh M Mohite, Santanu K Ghosh, Mamata Kombrabail, Guruswamy Krishnamoorthy, Pradip Chaudhari, Samir K Maji Cell Death and Differentiation, 2017
Mechanism-selective inhibition of α-synuclein aggregation by the chaperone-like BRICHOS domain L Adam, WH Molenkamp, JS Nowak, A Farzadfard, K Gaarthuis, R Kumar, ... Journal of Biological Chemistry, 113117 , 2026 2026
Diagnostic performance of the α-synuclein seed amplification assay for dementia with lewy bodies: a comparison across 4 laboratories R Kumar, S Gravett, V Jelic, J Lange, L Oftedal, A Ciullini, MB Bacınoğlu, ... Neurology 106 (4), e214614 , 2026 2026 Citations: 3
BPS2026–Regulation and inhibition of tau protein phase separation, aggregation, and toxicity by a molecular chaperone C Mörman, A Leppert, G Pizzirusso, Z Zheng, X Sun, R Kumar, H Biverstal, ... Biophysical Journal 125 (4), 363a , 2026 2026
Chaperone-mediated regulation of tau phase separation, fibrillation, and toxicity C Morman, A Leppert, G Pizzirusso, Z Zheng, X Sun, R Kumar, ... Journal of the American Chemical Society 147 (27), 23504-23518 , 2025 2025 Citations: 13
Helicobacter pylori CagA protein is a potent and broad-spectrum amyloid inhibitor Z Jin, WP Olsen, C Mörman, A Leppert, R Kumar, A Møllebjerg, ... Science Advances 11 (24), eads7525 , 2025 2025 Citations: 5
Specific inhibition of α‐synuclein oligomer generation and toxicity by the chaperone domain Bri2 BRICHOS L Adam, R Kumar, LE Arroyo‐Garcia, WH Molenkamp, JS Nowak, H Klute, ... Protein Science 33 (8), e5091 , 2024 2024 Citations: 12
Identification of potential aggregation hotspots on Aβ42 fibrils blocked by the anti-amyloid chaperone-like BRICHOS domain R Kumar, T Le Marchand, L Adam, R Bobrovs, G Chen, J Fridmanis, ... Nature Communications 15 (1), 965 , 2024 2024 Citations: 28
Inhibitory mechanism of the BRICHOS protein on asynuclein aggregation related to familial Parkinson's disease H Klute, L Adam, W Molenkamp, R Kumar, J Johansson, A Abelein EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS 52 (SUPPL 1), S189-S189 , 2023 2023
Predictable Morphology of Metal Nanocrystals Templated by Amyloidogenic Proteins/Peptides and Photonic Polymerase Chain Reaction using Triangular Nanoparticles P Kadu, S Pandey, L Gadhe, S Neekhra, A Navalkar, K Patel, R Kumar, ... EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS 52 (SUPPL 1), S187-S187 , 2023 2023
Targeting a-synuclein amyloid aggregates with the BRICHOS domain-basis for treatment of Parkinson's disease L Adam, R Kumar, W Molenkamp, R Alkenayeh, H Biverstal, J Johansson, ... EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS 52 (SUPPL 1), S168-S168 , 2023 2023
Structural insights into aggregation hotspots on Alzheimer's associated amyloid-beta fibrils blocked by the BRICHOS chaperone A Abelein, R Kumar, T Le Marchand, L Adam, G Chen, J Fridmanis, ... EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS 52 (SUPPL 1), S54-S54 , 2023 2023
Development of a sensitive blood-based amyloid amplification assay for diagnosis of Parkinson's disease L Gadhe, R Kumar, A Sakunthala, S Rawat, SK Maji EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS 52 (SUPPL 1), S81-S81 , 2023 2023
Molecular mechanisms of amyloid-beta self-assembly and chaperone-mediated inhibition can be translated to in vivo-derived fibril seeds R Kumar, LEA Garcia, S Manchanda, L Adam, G Pizzirusso, H Biverstal, ... EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS 52 (SUPPL 1), S89-S89 , 2023 2023
Misfolded alpha-synuclein detection by RT-QuIC in dementia with lewy bodies: a systematic review and meta-analysis C Peña-Bautista, R Kumar, M Baquero, J Johansson, C Cháfer-Pericás, ... Frontiers in molecular biosciences 10, 1193458 , 2023 2023 Citations: 47
Molecular mechanisms of amyloid-β self-assembly seeded by in vivo-derived fibrils and inhibitory effects of the BRICHOS chaperone R Kumar, LE Arroyo-Garcia, S Manchanda, L Adam, G Pizzirusso, ... ACS Chemical Neuroscience 14 (8), 1503-1511 , 2023 2023 Citations: 9
Alpha synuclein by RT-QuIC in dementia with Lewy Bodies: a systematic review and meta-analysis C PEÑA-BAUTISTA, R KUMAR, M BAQUERO, C CHÁFER-PERICÁS, ... 2023
Molecular structure of Cu (II)-bound amyloid-β monomer implicated in inhibition of peptide self-assembly in Alzheimer’s disease A Abelein, S Ciofi-Baffoni, C Mörman, R Kumar, A Giachetti, M Piccioli, ... Jacs Au 2 (11), 2571-2584 , 2022 2022 Citations: 62
Alpha-Synuclein mutants and uses thereof SK Maji, GL GANESHRAO, R Kumar, S RAY US Patent App. 17/724,168 , 2022 2022
α-Synuclein aggregation intermediates form fibril polymorphs with distinct prion-like properties S Mehra, S Ahlawat, H Kumar, D Datta, A Navalkar, N Singh, K Patel, ... Journal of molecular biology 434 (19), 167761 , 2022 2022 Citations: 29
Spidroin N-terminal domain forms amyloid-like fibril based hydrogels and provides a protein immobilization platform T Arndt, K Jaudzems, O Shilkova, J Francis, M Johansson, PR Laity, ... Nature Communications 13 (1), 4695 , 2022 2022 Citations: 35
MOST CITED SCHOLAR PUBLICATIONS
α-Synuclein aggregation nucleates through liquid–liquid phase separation S Ray, N Singh, R Kumar, K Patel, S Pandey, D Datta, J Mahato, ... Nature chemistry 12 (8), 705-716 , 2020 2020 Citations: 913
p53 amyloid formation leading to its loss of function: implications in cancer pathogenesis S Ghosh, S Salot, S Sengupta, A Navalkar, D Ghosh, R Jacob, S Das, ... Cell Death & Differentiation 24 (10), 1784-1798 , 2017 2017 Citations: 164
Lipopolysaccharide from gut microbiota modulates α-synuclein aggregation and alters its biological function D Bhattacharyya, GM Mohite, J Krishnamoorthy, N Gayen, S Mehra, ... ACS chemical neuroscience 10 (5), 2229-2236 , 2019 2019 Citations: 131
Comparison of α-synuclein fibril inhibition by four different amyloid inhibitors NN Jha, R Kumar, R Panigrahi, A Navalkar, D Ghosh, S Sahay, M Mondal, ... ACS chemical neuroscience 8 (12), 2722-2733 , 2017 2017 Citations: 79
Glycosaminoglycans have variable effects on α-synuclein aggregation and differentially affect the activities of the resulting amyloid fibrils S Mehra, D Ghosh, R Kumar, M Mondal, LG Gadhe, S Das, A Anoop, ... Journal of Biological Chemistry 293 (34), 12975-12991 , 2018 2018 Citations: 72
Comparison of kinetics, toxicity, oligomer formation, and membrane binding capacity of α-synuclein familial mutations at the A53 site, including the newly discovered A53V mutation GM Mohite, R Kumar, R Panigrahi, A Navalkar, N Singh, D Datta, S Mehra, ... Biochemistry 57 (35), 5183-5187 , 2018 2018 Citations: 71
Molecular structure of Cu (II)-bound amyloid-β monomer implicated in inhibition of peptide self-assembly in Alzheimer’s disease A Abelein, S Ciofi-Baffoni, C Mörman, R Kumar, A Giachetti, M Piccioli, ... Jacs Au 2 (11), 2571-2584 , 2022 2022 Citations: 62
Cytotoxic oligomers and fibrils trapped in a gel‐like state of α‐synuclein assemblies R Kumar, S Das, GM Mohite, SK Rout, S Halder, NN Jha, S Ray, S Mehra, ... Angewandte Chemie International Edition 57 (19), 5262-5266 , 2018 2018 Citations: 51
Controlled exposure of bioactive growth factor in 3D amyloid hydrogel for stem cells differentiation S Das, R Kumar, NN Jha, SK Maji Advanced healthcare materials 6 (18), 1700368 , 2017 2017 Citations: 48
Misfolded alpha-synuclein detection by RT-QuIC in dementia with lewy bodies: a systematic review and meta-analysis C Peña-Bautista, R Kumar, M Baquero, J Johansson, C Cháfer-Pericás, ... Frontiers in molecular biosciences 10, 1193458 , 2023 2023 Citations: 47
Parkinson’s Disease Associated α-Synuclein Familial Mutants Promote Dopaminergic Neuronal Death in Drosophila melanogaster GM Mohite, S Dwivedi, S Das, R Kumar, S Paluri, S Mehra, N Ruhela, A S, ... ACS chemical neuroscience 9 (11), 2628-2638 , 2018 2018 Citations: 46
Spidroin N-terminal domain forms amyloid-like fibril based hydrogels and provides a protein immobilization platform T Arndt, K Jaudzems, O Shilkova, J Francis, M Johansson, PR Laity, ... Nature Communications 13 (1), 4695 , 2022 2022 Citations: 35
Fabrication of an amyloid fibril-palladium nanocomposite: a sustainable catalyst for C–H activation and the electrooxidation of ethanol R Jayarajan, R Kumar, J Gupta, G Dev, P Kadu, D Chatterjee, D Bahadur, ... Journal of Materials Chemistry A 7 (9), 4486-4493 , 2019 2019 Citations: 33
The familial α-synuclein A53E mutation enhances cell death in response to environmental toxins due to a larger population of oligomers GM Mohite, A Navalkar, R Kumar, S Mehra, S Das, LG Gadhe, D Ghosh, ... Biochemistry 57 (33), 5014-5028 , 2018 2018 Citations: 31
α-Synuclein aggregation intermediates form fibril polymorphs with distinct prion-like properties S Mehra, S Ahlawat, H Kumar, D Datta, A Navalkar, N Singh, K Patel, ... Journal of molecular biology 434 (19), 167761 , 2022 2022 Citations: 29
α-Synuclein aggregation nucleates through liquid–liquid phase separation. Nat Chem 12: 705–716 S Ray, N Singh, R Kumar, K Patel, S Pandey, D Datta, J Mahato, ... 2020 Citations: 29
Identification of potential aggregation hotspots on Aβ42 fibrils blocked by the anti-amyloid chaperone-like BRICHOS domain R Kumar, T Le Marchand, L Adam, R Bobrovs, G Chen, J Fridmanis, ... Nature Communications 15 (1), 965 , 2024 2024 Citations: 28
Functionalization of amyloid fibrils via the Bri2 BRICHOS domain H Biverstål, R Kumar, AK Schellhaus, M Sarr, NP Dantuma, A Abelein, ... Scientific Reports 10 (1), 21765 , 2020 2020 Citations: 26
Liquid-liquid phase separation and liquid-to-solid transition mediate α-synuclein amyloid fibril containing hydrogel formation S Ray, N Singh, S Pandey, R Kumar, L Gadhe, D Datta, K Patel, J Mahato, ... bioRxiv, 619858 , 2019 2019 Citations: 26
Amyloid fibril formation of Arctic amyloid-β 1–42 peptide is efficiently inhibited by the BRICHOS domain X Zhong, R Kumar, Y Wang, H Biverstål, C Ingeborg Jegerschöld, ... ACS Chemical Biology 17 (8), 2201-2211 , 2022 2022 Citations: 24
