Effect of Unna's boot on venous ulcer healing: a systematic review and meta-analysis.

Objective: To analyze the effect of Unna's Boot on the healing of venous ulcers compared to other therapies.

Methods: Systematic Review carried out in the databases Scopus, Embase, Cochrane Library, Web of Science, PubMed, Cumulative Index of Nursing and Allied Health Literature, Latin American and Caribbean Literature in Health Sciences, and grey literature. Population - adult patients with venous ulcers; Intervention- Unna's Boot (UB); Control - other compression therapies (CT); Outcome- healing; Designs- randomized clinical trial, cohort study, and case control, published from 2001 to 2024.

Transferring knowledge towards understanding the pore stabilizing variations in K(+) channels: pore stability in K(+) channels.

Recent advances in structural biology underlying mechanisms of channel gating have strengthened our knowledge about how K(+) channels can be inter-convertible between conductive and non-conductive states. We have reviewed and combined mutagenesis with biochemical, biophysical and structural information in order to understand the critical roles of the pore residues in stabilizing the pore structure and channel open state. We also discuss how the latest knowledge on the K(+) channel KcsA may provide a step towards better understanding of distinct pore stabilizing differences among diversified K(+) channels.

Improved technique for reconstituting incredibly high and soluble amounts of tetrameric K⁺ channel in natural membranes.

The reconstitution of large amounts of integral proteins into lipid vesicles is largely prompted by the complexity of most biological membranes and protein stability. We optimized a particular system which maximized the incorporation efficiency of large soluble amounts of KcsA potassium channel in Escherichia coli membranes. The effects of two detergents, octylglucoside and 3-[(cholamidopropyl)-dimethyl-ammonio]-1-propanesulfonate (CHAPS), on KcsA reconstitution were compared.

The "flipped" state in E71A-K+-channel KcsA exclusively alters the channel gating properties by tetraethylammonium and phosphatidylglycerol.

Mutation E71A in the bacterial K(+)-channel KcsA has been shown to abolish the activation-coupled inactivation of KcsA via significant alterations of the peptide backbone in the vicinity of the selectivity filter. In the present study, we examined channel-blocking behavior of KcsA-E71A by tetraethylammonium (TEA) from both the extra- and the intracellular sides. First, we found that E71A is inserted either in cis or trans orientation in a planar lipid bilayer; however, it exhibits only one orientation in proteoliposomes as determined by extravesicular partial chymotrypsin digestion.

Mutations in the K(+)-channel KcsA toward Kir channels alter salt-induced clusterization and blockade by quaternary alkylammonium ions.

Protein aggregation is a result of malfunction in protein folding, assembly, and transport, caused by protein mutation and/or changes in the cell environment, thus triggering many human diseases. We have shown that bacterial K(+)-channel KcsA, which acts as a representative model for ion channels, forms salt-induced large conductive complexes in a particular environment. In the present study, we investigated the effects of point mutations in the selectivity filter of KcsA on intrinsic stability, aggregation, and channel blocking behavior.