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Virender Singh

As seen in: Nature, Wiley Online Library, PLOS ONE, Frontiers, American Chemical Society, Royal Society of Chemistry, BioRxiv, Lexology, Amar Ujala, Mondaq and
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Articles

Cryo-EM reveals structural variability of apolipoprotein A-I amyloid fibrils across organs, mutations, and clinical presentations

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By Parker T. Bassett, Virender Singh, Preeti Singh Verified, Yasmin Ahmed, Andrew Lemoff, Bret M. Evers, Christian Lopez, Barbara Kluve-Beckerman, Lorena Saelices, Layla Villalon
| Nature Verified
Abstract Hereditary apolipoprotein A-I (AApoA‑I) amyloidosis is a rare systemic disease caused by the deposition of amyloid fibrils formed by apolipoprotein A‑I in multiple organs, leading to severe clinical outcomes. With no available therapies or diagnostic tools, defining the structure of AApoA‑I fibrils is crucial to understanding disease mechanisms and guiding intervention.
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Structural polymorphism of ex-vivo ALECT2 amyloid fibrils revealed by cryo-EM

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By Shumaila Afrin, Virender Singh, Preeti Singh Verified, Parker T. Bassett, Maja Pekala, Bret M. Evers, Christian Lopez, Yasmin Ahmed, Raja Reddy Kallem, Andrew Lemoff, Christos Argyropoulos, Barbara Kluve-Beckerman, Lorena Saelices
| Nature Verified
Abstract ALECT2 amyloidosis is a rare systemic disease characterized by the pathological deposition of leukocyte cell-derived chemotaxin-2 (LECT2) as amyloid fibrils, primarily affecting the kidneys and liver. The molecular mechanisms underlying LECT2 aggregation remain poorly defined, hindering diagnostic and therapeutic development. Here, we present cryo-electron microscopy structures of ex-vivo ALECT2 fibrils extracted from a patient’s kidney.
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Amyloid fibril polymorphism in the heart and liver of a patient with polyneuropathic ATTRv-V122Δ amyloidosis

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By Yasmin Ahmed, Candace Kelly, Shumaila Afrin, Virender Singh, Bret M. Evers, John M. Shelton, Christian Escobar, Preeti Singh Verified, Rose Pedretti, Lanie Wang, Parker T. Bassett, Maja Pekala, Andrew Lemoff, Barbara Kluve-Beckerman, Lorena Saelices
| Nature Verified
Abstract ATTR amyloidosis is a phenotypically heterogeneous disease characterized by the pathological deposition of transthyretin in the form of amyloid fibrils into various organs. ATTR amyloidosis may result from mutations in variant (ATTRv) amyloidosis, or aging in wild-type (ATTRwt) amyloidosis. ATTRwt generally manifests as cardiomyopathy, whereas ATTRv may present as polyneuropathy, cardiomyopathy, or mixed, in combination with many other symptoms deriving from multisystem organ involvement.
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