Corpus overview


MeSH Disease

Human Phenotype

Pneumonia (1)

Anosmia (1)


There are no transmission terms in the subcorpus


There are no seroprevalence terms in the subcorpus

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    18F-FDG brain PET metabolism in post-SARS-CoV-2 infection MESHD: substrate for persistent/delayed disorders?

    Authors: Eric Guedj; Matthieu Million; Pierre Dudouet; Hervé Tissot-Dupont; Fabienne Bregeon; Serge Cammilleri; Didier Raoult

    doi:10.21203/ Date: 2020-07-03 Source: ResearchSquare

    Purpose: Several brain complications of SARS-CoV-2 infection MESHD have been reported. It has been moreover speculated that this neurotropism could potentially cause a delayed outbreak of neuropsychiatric and neurodegenerative diseases MESHD of neuroinflammatory origin. A propagation mechanism has been proposed across the cribriform plate of the ethmoid bone, from the nose to the olfactory epithelium, and possibly afterwards to other limbic structures, and deeper parts of the brain including the brainstem. Methods: Review of clinical examination, and whole-brain voxel-based analysis of 18F-FDG PET metabolism in comparison to healthy subjects (p-voxel<0.001, p-cluster<0.05), of two patients with confirmed diagnosis of SARS-CoV-2 pneumonia MESHD pneumonia HP explored at the post-viral stage of the disease MESHD.Results: Hypometabolism of the olfactory/rectus gyrus was found on the two patients, especially one with 4 weeks prolonged anosmia HP. Additional hypometabolisms were found within bilateral amygdala, hippocampus, cingulate cortex, thalamus, pons and medulla brainstem in the other patient who complained of delayed onset of an atypical painful syndrome MESHD.Conclusion: These preliminary findings reinforce the hypotheses of SARS-CoV-2 neurotropism through the olfactory bulb, and the possible extension of this impairment to other limbic structures and to the brainstem. 18F-FDG PET hypometabolism could constitute a cerebral quantitative biomarker of this involvement. Post-viral cohort studies are required to specify the exact relationship between limbic/brainstem hypometabolisms and the possible persistent disorders, especially involving cognitive or emotion disturbances, residual respiratory symptoms or painful complaints.

    Engineered unnatural ubiquitin for optimal detection of deubiquitinating enzymes

    Authors: Wioletta Rut; Mikolaj Zmudzinski; Scott J. Snipas; Miklos Bekes; Tony T. Huang; Marcin Drag

    doi:10.1101/2020.01.30.926881 Date: 2020-01-31 Source: bioRxiv

    Deubiquitinating enzymes (DUBs) are responsible for removing ubiquitin (Ub) from its protein conjugates. DUBs have been implicated as attractive therapeutic targets in the treatment of viral diseases, neurodegenerative MESHD disorders and cancer. The lack of selective chemical tools for the exploration of these enzymes significantly impairs the determination of their roles in both normal and pathological states. Commercially available fluorogenic substrates are based on the C-terminal Ub motif or contain Ub coupled to a fluorophore (Z-LRGG-AMC, Ub-AMC); therefore, these substrates suffer from lack of selectivity. By using a hybrid combinatorial substrate library (HyCoSuL) and a defined P2 library containing a wide variety of nonproteinogenic amino acids, we established a full substrate specificity profile for two DUBs--MERS PLpro and human UCH-L3. Based on these results, we designed and synthesized Ub-based substrates and activity-based probes (ABPs) containing selected unnatural amino acids located in the C-terminal Ub motif. Biochemical analysis and cell-based experiments confirmed the activity and selectivity of engineered Ub-based substrates and probes. Using this approach, we propose that for any protease that recognizes Ub and Ub-like substrates, a highly active and selective unnatural substrate or probe can be engineered.

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MeSH Disease
Human Phenotype

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