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Articles by Bret M. Evers
Polymorphic IGLV6-57 AL amyloid fibrils and features of a shared folding pathway
Abstract Immunoglobulin light chain (AL) amyloidosis is a systemic disorder caused by the misfolding and aggregation of free immunoglobulin light chains (LCs) secreted by abnormal plasma cells. The resulting amyloid fibrils deposit in multiple organs, leading to progressive dysfunction and increased morbidity and mortality. Despite recent advances, the molecular determinants of LC aggregation and their effect on phenotypic variability are not fully defined.
Sa2215 EVALUATION OF SELF-ASSEMBLING PEPTIDE RADA-16 FOR PROMOTING ESOPHAGEAL MUCOSAL HEALING AFTER BUTTON BATTERY-INDUCED INJURY IN A PIGLET MODEL
Also available on ScienceDirect
Cryo-EM reveals structural variability of apolipoprotein A-I amyloid fibrils across organs, mutations, and clinical presentations
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.
Structural polymorphism of ex-vivo ALECT2 amyloid fibrils revealed by cryo-EM
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.
Amyloid fibril polymorphism in the heart and liver of a patient with polyneuropathic ATTRv-V122Δ amyloidosis
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.
‘Tripod-like’ lung-targeting (LuT) lipids for highly efficient and selective LNPs for gene delivery and editing
Abstract Developing lung-targeting delivery systems is essential for treating pulmonary conditions such as genetic respiratory diseases, infections, fibrosis and cancer. We synthesized and evaluated 444 lung-targeting lipids (LuT lipids) that form lipid nanoparticles (LNPs) to efficiently deliver messenger RNA and CRISPR–Cas9 genome editors to lungs with minimal side effects.
Cancer cachexia in STK11/LKB1-mutated non-small cell lung cancer is dependent on tumor-secreted GDF15 - Nature Communications
Abstract Cachexia is a wasting syndrome involving adipose, muscle, and body weight loss in cancer patients. Tumor loss-of-function mutations in STK11/LKB1, a regulator of AMP-activated protein kinase, induce cancer cachexia (CC) in preclinical models and are linked to weight loss in non-small cell lung cancer (NSCLC) patients.
Deciphering distinct genetic risk factors for FTLD-TDP pathological subtypes via whole-genome sequencing - Nature Communications
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Abstract Frontotemporal lobar degeneration with neuronal inclusions of the TAR DNA-binding protein 43 (FTLD-TDP) is a fatal neurodegenerative disorder with only a limited number of risk loci identified.
By Cyril Pottier, Fahri Küçükali, Matt Baker Verified, Gregory Jenkins, Cristina T. Vicente, Wouter De Coster, Owen A Ross, Melissa Murray, Stephen J. Haggarty, Merel O. Mol, Ging-Yuek R. Hsiung, Shannon McDonnell, Saurabh Baheti, Keith A. Josephs, Kevin F. Bieniek, Leah Forsberg, Jennifer S. Yokoyama, Kimiko Domoto-Reilly, Matthis Synofzik, Bradford C. Dickerson, Bret M. Evers, Brittany N. Dugger, Ekaterina Rogaeva, Sandra Weintraub, Martin R Farlow, Dieter Edbauer, Richard J. Caselli, Eric M Reiman, Simon Mead, Alissa L. Nana, Nilüfer Ertekin-Taner, David S. Knopman, Ronald Petersen, Zbigniew K. Wszolek, Lea T. Grinberg, Salvatore Spina, Olivier Piguet, John Q. Trojanowski, C. Dirk Keene, Daniel H Geschwind, Carlos Cruchaga, Bernardino Ghetti, Glenda M Halliday, Jochen Herms, Adam L Boxer, Lawrence S. Honig, Oscar Lopez Verified, Jonathan Glass, David J. Irwin, Edward Lee, Vivianna Van Deerlin, Claire Troakes, Clifton L. Dalgard, Harro Seelaar, Bradley F. Boeve, Ian MacKenzie, William W. Seeley, Kristel Sleegers, Dennis W. Dickson, Joanna M. Biernacka, Maria C. Tartaglia
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Nature
Verified
Cancer mutations rewire the RNA methylation specificity of METTL3-METTL14
Published In Science Advances Volume 10 | Issue 51 December 2024 Article versions Submission history Received: 14 August 2024 Accepted: 14 November 2024 Permissions Request permissions for this article. Acknowledgments We thank O. Koczy, J. Parker, and R. Setlem for contributing to preliminary studies. We are grateful for the helpful discussions with B. Xhemalce on genomic data analysis. The Structural Biology Laboratory at UT Southwestern for help with synchrotron data collection.
Alternating Magnetic Fields AMF) and Linezolid Reduce Staphylococcus aureus Biofilm in a Large Animal Implant Model
Abbreviations PJI (Prosthetic joint infections) AMF (Alternating Magnetic Fields) S.
Multi-organ structural homogeneity of amyloid fibrils in ATTRv-T60A amyloidosis patients, revealed by Cryo-EM
Abstract ATTR amyloidosis is a degenerative disorder characterized by the systemic deposition of the protein transthyretin. These amyloid aggregates of transthyretin (ATTR) can deposit in different parts of the body causing diverse clinical manifestations. Our laboratory aims to investigate a potential relationship between the different genotypes, organ of deposition, clinical phenotypes, and the structure of ATTR fibrils.
Amyloid fibril polymorphism in the heart of an ATTR amyloidosis patient with polyneuropathy attributed to the V122Δ variant
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 stem from mutations in variant (ATTRv) amyloidosis, or aging in wild-type (ATTRwt) amyloidosis.
LY6E is a pan-coronavirus restriction factor in the respiratory tract - Nature Microbiology
Abstract LY6E is an antiviral restriction factor that inhibits coronavirus spike-mediated fusion, but the cell types in vivo that require LY6E for protection from respiratory coronavirus infection are unknown. Here we used a panel of seven conditional Ly6e knockout mice to define which Ly6e-expressing cells confer control of airway infection by murine coronavirus and severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2).
eIF5B drives integrated stress response-dependent translation of PD-L1 in lung cancer
Abstract Cancer cells express high levels of programmed death ligand 1 (PD-L1), a ligand of the programmed cell death protein 1 (PD-1) receptor on T cells, allowing tumors to suppress T cell activity. Clinical trials utilizing antibodies that disrupt the PD-1/PD-L1 checkpoint have yielded remarkable results, with anti-PD-1 immunotherapy approved as a first-line therapy for patients with lung cancer.
Lipidomic and Transcriptomic Basis of Lysosomal Dysfunction in Progranulin Deficiency
Extraction and Analysis of Lipids Samples by Infusion-Based MS/MSALL PGRN deficiency manifests itself clinically as two phenotypically distinct diseases, depending on whether the loss of one functional GRN allele induces a state of haploinsufficiency or complete loss of function when both alleles are defective. In the first case, PGRN haploinsufficiency results in a dominant form of FTLD-TDP, in the latter a recessive form of NCL.
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