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Reduced PI3K(p110α) induces atrial myopathy, and PI3K-related lipids are dysregulated in athletes with atrial fibrillation.

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January 2025

Baker Heart and Diabetes Institute, Melbourne, VIC 3004, Australia; Department of Physiology, Anatomy and Microbiology, La Trobe University, Bundoora, VIC 3086, Australia; Department of Diabetes, Central Clinical School, Monash University, Clayton, VIC 3800, Australia; Department of Cardiometabolic Health, University of Melbourne, Melbourne, VIC 3010, Australia; Department of Cardiovascular Research, Translation and Implementation, La Trobe University, Bundoora, VIC 3086, Australia; Department of Physiology and Department of Medicine Alfred Hospital, Monash University, Clayton, VIC 3800, Australia; Heart Research Institute, Newtown, NSW 2042, Australia. Electronic address:

Background: Elucidating mechanisms underlying atrial myopathy, which predisposes individuals to atrial fibrillation (AF), will be critical for preventing/treating AF. In a serendipitous discovery, we identified atrial enlargement, fibrosis, and thrombi in mice with reduced phosphoinositide 3-kinase (PI3K) in cardiomyocytes. PI3K(p110α) is elevated in the heart with exercise and is critical for exercise-induced ventricular enlargement and protection, but the role in the atria was unknown.

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S-layers: from a serendipitous discovery to a toolkit for nanobiotechnology.

Q Rev Biophys

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Institute of Synthetic Bioarchitectures, Department of Bionanosciences, University of Natural Resources and Life Sciences, Vienna, Austria.

Prokaryotic microorganisms, comprising and , exhibit a fascinating diversity of cell envelope structures reflecting their adaptations that contribute to their resilience and survival in diverse environments. Among these adaptations, surface layers (S-layers) composed of monomolecular protein or glycoprotein lattices are one of the most observed envelope components. They are the most abundant cellular proteins and represent the simplest biological membranes that have developed during evolution.

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Serendipitous high-resolution structure of Escherichia coli carbonic anhydrase 2.

Acta Crystallogr F Struct Biol Commun

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Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, USA.

X-ray crystallography remains the dominant method of determining the three-dimensional structure of proteins. Nevertheless, this resource-intensive process may be hindered by the unintended crystallization of contaminant proteins from the expression source. Here, the serendipitous discovery of two novel crystal forms and one new, high-resolution structure of carbonic anhydrase 2 (CA2) from Escherichia coli that arose during a crystallization campaign for an unrelated target is reported.

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Serendipitous Discovery of Dearomatized Dimers in Anthracene Derivative Oxidation.

Org Lett

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Department of Chemistry, University at Albany, State University of New York, Albany, New York 12222, United States.

We present the serendipitous discovery of an unusual dimer formed from anthracene-derived polyarenes. Unlike the typical oxidative coupling of substituted aromatic scaffolds, the reaction yielded a dearomatized enone dimer as the sole product. This dearomatized motif, notably, does not undergo the commonly observed rearomatization, and no biaryl products were detected.

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Differences and Interplay between serendipitous and theory-driven discoveries in treating disorders of consciousness.

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January 2025

Department of Neuro-Rehabilitation, Hospices Civils de Lyon, Université Claude Bernard Lyon 1, Lyon, France; Université de Lyon, Université Lyon 1, INSERM U1028, CNRS UMR5292, Lyon Neuroscience Research Center, Trajectoires Team, Lyon, France. Electronic address:

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