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Granulin loss of function in human mature brain organoids implicates astrocytes in TDP-43 pathology Open
Loss of function (LoF) of TAR-DNA binding protein 43 (TDP-43) and mis-localization, together with TDP-43-positive and hyperphosphorylated inclusions, are found in post-mortem tissue of amyotrophic lateral sclerosis (ALS) and frontotemporal…
Granulin Loss of Function in Human Mature Brain Organoids Implicates Astrocytes in TDP-43 Pathology Open
Summary Loss of function (LoF) of Tar-binding protein 43 (TDP-43) and mislocalization, together with TDP-43-positive and hyperphosphorylated inclusions, are found in postmortem tissue of amyotrophic lateral sclerosis (ALS) and frontotempor…
View article: The amphibian antimicrobial peptide uperin 3.5 is a cross-α/cross-β chameleon functional amyloid
The amphibian antimicrobial peptide uperin 3.5 is a cross-α/cross-β chameleon functional amyloid Open
Significance We determined the crystal structure of the full-length amphibian antimicrobial peptide (AMP) uperin 3.5 and showed fibrillation into helical “cross-α” amyloid fibril, correlated with its antibacterial activity. This provides a…
Emerging Roles of Functional Bacterial Amyloids in Gene Regulation, Toxicity, and Immunomodulation Open
Bacteria often reside in multicellular communities, called biofilms, held together by an extracellular matrix. In many bacteria, the major proteinaceous component of the biofilm are amyloid fibers. Amyloids are highly stable and structured…
View article: The Amphibian Antimicrobial Peptide Uperin 3.5 is a Cross-α/Cross-β Chameleon Functional Amyloid
The Amphibian Antimicrobial Peptide Uperin 3.5 is a Cross-α/Cross-β Chameleon Functional Amyloid Open
Antimicrobial activity is being increasingly linked to amyloid fibril formation, suggesting physiological roles for some human amyloids, which have historically been viewed as strictly pathological agents. This work reports on formation of…
Structural Insights into Curli CsgA Cross-β Fibril Architecture Inspire Repurposing of Anti-amyloid Compounds as Anti-biofilm Agents Open
Curli amyloid fibrils secreted by Enterobacteriaceae mediate host cell adhesion and contribute to biofilm formation, thereby promoting bacterial resistance to environmental stressors. Here, we present crystal structures of amyloid-forming …
Extreme amyloid polymorphism in <i>Staphylococcus aureus</i> virulent PSMα peptides Open
The mechanisms of amyloid protein assembly into fibrous structures have been studied for decades, particularly since amyloids are associated with neurodegenerative and systemic human diseases.In contrast, functional amyloids that participa…
Structural Insights into Curli CsgA Cross-β Fibril Architecture Inspired Repurposing of Anti-amyloid Compounds as Anti-biofilm Agents Open
Curli amyloid fibrils secreted by Enterobacteriaceae mediate host cell adhesion and contribute to biofilm formation, thereby promoting bacterial resistance to environmental stressors. Here, we present crystal structures of amyloid-forming …
<i>Staphylococcus aureus</i> PSMα3 Cross-α Fibril Polymorphism and Determinants of Cytotoxicity Open
Summary The phenol-soluble modulin (PSM) peptide family, secreted by Staphylococcus aureus, performs various virulence activities, some mediated by the formation of amyloid fibrils of diverse architectures. Specifically, PSMα1 and PSMα4 st…
Extreme Amyloid Polymorphism in <i>Staphylococcus aureus</i> Virulent PSMα Peptides Open
Members of the Staphylococcus aureus phenol-soluble modulin (PSM) peptide family are secreted as functional amyloids that serve diverse roles in pathogenicity and may be present as full-length peptides or as naturally occurring truncations…