Mitoribosomes are present in the mitochondria of all eukaryotic cells. Their function is to allow the translation of mitochondrial mRNA that exclusively encodes components of the oxidative phosphorylation complexes (OXPHOS).
Researchers from Tel Aviv Sourasky Medical Center presented data from a study that aimed to investigate the genetic mechanisms underlying yellow nail syndrome (YNS), a rare disorder characterized by three features, namely yellow dystrophic nails, lymphedema and chronic lung disease.
T-cell leukemia homeobox protein 3 (TLX3) is a key regulator of fate specification of excitatory neurons and found expressed in proliferating granule neuron progenitors (GNPs) of the cerebellum, but its main role is not well known.
Multisystem inflammatory syndrome in children (MIS-C) is a rare and severe condition following SARS-CoV-2 infection associated with intestinal manifestations. The most common clinical features include fever, abdominal pain, rash, myocardial dysfunction and elevated inflammatory biomarkers.
Prostatic-specific antigen (PSA) is commonly used as a screening tool for prostate cancer but presents limited sensitivity and specificity. Therefore, research efforts are focused on searching for novel noninvasive diagnostic biomarkers.
Researchers at the University of Rochester have described a neuroimaging-based biomarker that could identify individuals with early psychosis, and improved their identification when it was added to a standard neurocognitive diagnostic test. In a group of roughly 160 participants in the Human Connectome Early Psychosis Project, individuals who were in the early stages of psychosis had stronger connections from the thalamus (a midbrain sensory processing area) to the cortex, but weaker connections between different cortical areas, than controls.
WD repeat domain 83 opposite strand (WDR83OS) encodes the 106-aa (amino acid) protein Asterix, which is a binding partner for CCDC47. More specifically, Asterix heterodimerizes with CCDC47 to form the protein associated with ER translocon (PAT) complex that specifically chaperones large proteins containing transmembrane domains.
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