Bret M. Evers on Muck Rack

Bret M. Evers

As seen in: Nature, Science Magazine, Cell Press, Cell Reports, The Journal of Clinical Investigation, Journal of Infection, Gastrointestinal Endoscopy
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Articles

Sa2215 EVALUATION OF SELF-ASSEMBLING PEPTIDE RADA-16 FOR PROMOTING ESOPHAGEAL MUCOSAL HEALING AFTER BUTTON BATTERY-INDUCED INJURY IN A PIGLET MODEL

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By Carrie Moore, Geoffrey Daves, Ashley Polachek, Carrie Moore, Christian Lopez, Bret M. Evers, David M. Troendle, Geoffrey Daves, Ashley Polachek
| Gastrointestinal Endoscopy
Also available on ScienceDirect
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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 , Yasmin Ahmed, Andrew Lemoff, Bret M. Evers, Christian Lopez, Barbara Kluve-Beckerman, Lorena Saelices, Layla Villalon
| Nature
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 , 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
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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