Human steroid 5-alpha reductase, isoform S5A1_HUMAN.

<p>Enzyme human steroid 5-alpha reductase, isoform S5A1_HUMAN (SRD5A1 gene) in the Main cluster. The number after HUMAN indicates the length of the protein.</p

Circadian locomoter output cycles protein kaput and NAD-dependent protein deacetylase sirtuin-1 amino acids relative frequencies.

<p>The graph compare the relative frequencies of the Circadian locomoter output cycles protein kaput (CLOCK gene) and NAD-dependent protein deacetylase sirtuin-1 (SIRT1) highlighting the different level of glutamate and glutamine. CLOCK means high glutamine and bases synthesis and switch on DNA synthesis. SIRT1 means low glutamine and high glutamate and acetylCoA and switch off DNA synthesis.</p

A representative group of Keratin associated proteins.

<p>A representative group of keratin associated proteins in the Cladogram from Main Cluster using TreeGraph2. In the Cladrogram we can find KRTAPs family type 1, 2, 3, 4, 9, 10, 11-1, 12, 16, 29-1. The number after HUMAN indicates the length of the protein.</p

A subset of the Aquaporins.

<p>A subset of the Aquaporins from MIP, Major intrinsic proteins Domain, in the Cladogram from Main Cluster using TreeGraph2. The number after HUMAN indicates the length of the protein.</p

Human steroid 5-alpha reductase, isoform S5A2_HUMAN.

<p>Enzyme human steroid 5-alpha reductase, isoform S5A2_HUMAN (SRD5A2 gene) in the Cladogram from Main Cluster using TreeGraph2. The number after HUMAN indicates the length of the protein.</p

Human steroid 5-alpha reductase, isoform PORED_HUMAN.

<p>Enzyme human steroid 5-alphareductase, isoform PORED_HUMAN (SRD5A3 gene) in the Cladogram from Main Cluster using TreeGraph2. The number after HUMAN indicates the length of the protein.</p

A portion of Cadherins subtree.

<p>A portion of cadherin subtree in the Cladogram from Main Cluster using TreeGraph2. In this portion of the Cladrogram we can find the Cadherin domains (5) proteins. The number after HUMAN indicates the length of the protein.</p

Data_Sheet_1_COVID-19 hospitalizations and patients' age at admission: The neglected importance of data variability for containment policies.docx

IntroductionAn excess in the daily fluctuation of COVID-19 in hospital admissions could cause uncertainty and delays in the implementation of care interventions. This study aims to characterize a possible source of extravariability in the number of hospitalizations for COVID-19 by considering age at admission as a potential explanatory factor. Age at hospitalization provides a clear idea of the epidemiological impact of the disease, as the elderly population is more at risk of severe COVID-19 outcomes. Administrative data for the Veneto region, Northern Italy from February 1, 2020, to November 20, 2021, were considered.MethodsAn inferential approach based on quasi-likelihood estimates through the generalized estimation equation (GEE) Poisson link function was used to quantify the overdispersion. The daily variation in the number of hospitalizations in the Veneto region that lagged at 3, 7, 10, and 15 days was associated with the number of news items retrieved from Global Database of Events, Language, and Tone (GDELT) regarding containment interventions to determine whether the magnitude of the past variation in daily hospitalizations could impact the number of preventive policies.ResultsThis study demonstrated a significant increase in the pattern of hospitalizations for COVID-19 in Veneto beginning in December 2020. Age at admission affected the excess variability in the number of admissions. This effect increased as age increased. Specifically, the dispersion was significantly lower in people under 30 years of age. From an epidemiological point of view, controlling the overdispersion of hospitalizations and the variables characterizing this phenomenon is crucial. In this context, the policies should prevent the spread of the virus in particular in the elderly, as the uncontrolled diffusion in this age group would result in an extra variability in daily hospitalizations.DiscussionThis study demonstrated that the overdispersion, together with the increase in hospitalizations, results in a lagged inflation of the containment policies. However, all these interventions represent strategies designed to contain a mechanism that has already been triggered. Further efforts should be directed toward preventive policies aimed at protecting the most fragile subjects, such as the elderly. Therefore, it is essential to implement containment strategies before the occurrence of potentially out-of-control situations, resulting in congestion in hospitals and health services.</p

The central domain of Tab2 contains the major determinants of Tab2/ERα interaction.

<p>a. Scheme of Tab2 fragments of different length expressed in bacteria as MBP fusion proteins. The functional domains are indicated as follows: the CUE domain, the CC (coiled coil) domain including the nuclear export sequence, the NZF (novel zinc finger) domain and the sequence (II) containing two phosphorylation sites (S419 and S423). <b>b</b>. MBP pull-down assays, using ERα-overexpressing HEK293T cell lysate and MBP-Tab2 fusion proteins described in a). The loading control for all Tab2 fragments is provided in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0168639#pone.0168639.s001" target="_blank">S1 Fig</a>. <b>c</b>. MBP pull-down assays using the MBP fusion proteins Tab2 full-length, ΔsinoSTab2 and Tab2_(406–531) as a control, and ERα-overexpressing HEK293T cell lysates in the presence or not of the <i>in vitro</i> transcribed and translated Tab2_(406–531) fragment. The lower bands represent the total amount of MBP-Tab2 fusions present in the assay.</p

A Tab2 mimic peptide displaces the Tab2/ERα interaction.

<p><b>a</b>. Aminoacid sequences of the three synthetic partially overlapping 17-aa each peptides, corresponding to different portions of the Fragment 4 described in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0168639#pone.0168639.s002" target="_blank">S2 Fig</a>. (here called Tab2-pept1, Tab2-pept2 and Tab2-pept3). <b>b</b>. MBP pull-down assays, using MBP-Tab2_(406–531), recombinant hERα (1 nM) and the three different synthetic Tab2 peptides (at a concentration of 10 μM each). <b>c</b>. Dose-response curve on pull-down assays, using MBP-Tab2_(406–531), recombinant hERα (1 nM) and the Tab2-pept3 at concentrations ranging from 0 to 10 μM.</p