Reconfiguration of Intrinsic Depletion-Mode Characteristics of MoS Field-Effect Transistors to High-Performance Enhancement-Mode Operation Using an Argon Plasma-Induced p-Type Doping Technique.

The intrinsic n-type behavior and unavailability of the appropriate p-type doping method for MoS allows only n-type conduction with depletion mode (D-mode) characteristics and forbids the implementation of p-type field-effect transistors (FETs). The D-mode characteristic results in a high off-current (I) at zero gate bias, which limits the usage of MoS FETs for industry-scale (n-channel metal-oxide semiconductor) NMOS/(complementary metal-oxide semiconductor) CMOS-logic-based applications due to significant power dissipation. Both these issues, i.

extracellular vesicles up-regulate and directly transfer adherence factors promoting host cell colonization.

, a common sexually transmitted parasite that colonizes the human urogenital tract, secretes extracellular vesicles (TvEVs) that are taken up by human cells and are speculated to be taken up by parasites as well. While the crosstalk between TvEVs and human cells has led to insight into host:parasite interactions, roles for TvEVs in infection have largely been one-sided, with little known about the effect of TvEV uptake by . Approximately 11% of infections are found to be coinfections of multiple strains.

MoS Field-Effect Transistor Performance Enhancement by Contact Doping and Defect Passivation via Fluorine Ions and Its Cyclic Field-Assisted Activation.

MoS-based field-effect transistors (FETs) and, in general, transition metal dichalcogenide channels are fundamentally limited by high contact resistance () and intrinsic defects, which results in low drive current and lower carrier mobilities, respectively. This work addresses these issues using a technique based on CF plasma treatment in the contacts and further cyclic field-assisted drift and activation of the fluorine ions (F), which get introduced into the contact region during the CF plasma treatment. The F ions are activated using cyclic pulses applied across the source-drain (S/D) contacts, which leads to their migration to the contact edges via the channel.

A Novel Trichomonas vaginalis Surface Protein Modulates Parasite Attachment via Protein:Host Cell Proteoglycan Interaction.

is a highly prevalent, sexually transmitted parasite which adheres to mucosal epithelial cells to colonize the human urogenital tract. Despite adherence being crucial for this extracellular parasite to thrive within the host, relatively little is known about the mechanisms or key molecules involved in this process. Here, we have identified and characterized a hypothetical protein, TVAG_157210 (TvAD1), as a surface protein that plays an integral role in parasite adherence to the host.

Extracellular vesicles produced by the protozoan parasite Trichomonas vaginalis contain a preferential cargo of tRNA-derived small RNAs.

Trichomonas vaginalis is a protozoan parasite that causes trichomoniasis, the most prevalent non-viral sexually transmitted infection worldwide. Trichomonas vaginalis releases extracellular vesicles that play a role in parasite:parasite and parasite:host interactions. The aim of this study was to characterise the RNA cargo of these vesicles.

extracellular vesicles are internalized by host cells using proteoglycans and caveolin-dependent endocytosis.

, a human-infective parasite, causes the most prevalent nonviral sexually transmitted infection worldwide. This pathogen secretes extracellular vesicles (EVs) that mediate its interaction with host cells. Here, we have developed assays to study the interface between parasite EVs and mammalian host cells and to quantify EV internalization by mammalian cells.

A Novel Cadherin-like Protein Mediates Adherence to and Killing of Host Cells by the Parasite Trichomonas vaginalis.

, a prevalent sexually transmitted parasite, adheres to and induces cytolysis of human mucosal epithelial cells. We have characterized a hypothetical protein, TVAG_393390, with predicted tertiary structure similar to that of mammalian cadherin proteins involved in cell-cell adherence. TVAG_393390, renamed cadherin-like protein (CLP), contains a calcium-binding site at a position conserved in cadherins.

Electrocardiographic Associations Seen with Obstructive Sleep Apnea.

Background: Obstructive sleep apnea (OSA) is a chronic respiratory disorder associated with repeated nocturnal partial or complete collapse that is often underdiagnosed and associated with multiple comorbidities. The association between specific features on an electrocardiogram and OSA has not been well studied. This retrospective study attempts to bridge this gap in knowledge.

Revisiting the oligomerization mechanism of Vibrio cholerae cytolysin, a beta-barrel pore-forming toxin.

Vibrio cholerae cytolysin (VCC) is a membrane-damaging beta-barrel pore-forming toxin (beta-PFT). VCC causes permeabilization of the target membranes by forming transmembrane oligomeric beta-barrel pores. Oligomerization is a key step in the mode of action of any beta-PFT, including that of VCC.

Physicochemical constraints of elevated pH affect efficient membrane interaction and arrest an abortive membrane-bound oligomeric intermediate of the beta-barrel pore-forming toxin Vibrio cholerae cytolysin.

Vibrio cholerae cytolysin (VCC) is a potent membrane-damaging cytotoxic protein. VCC causes permeabilization of the target cell membranes by forming transmembrane oligomeric beta-barrel pores. Membrane pore formation by VCC involves following key steps: (i) membrane binding, (ii) formation of a pre-pore oligomeric intermediate, (iii) membrane insertion of the pore-forming motifs, and (iv) formation of the functional transmembrane pore.

Revisiting the membrane interaction mechanism of a membrane-damaging β-barrel pore-forming toxin Vibrio cholerae cytolysin.

Vibrio cholerae cytolysin (VCC) permeabilizes target cell membranes by forming transmembrane oligomeric β-barrel pores. VCC has been shown to associate with the target membranes via amphipathicity-driven spontaneous partitioning into the membrane environment. More specific interaction(s) of VCC with the membrane components have also been documented.

Trapping of Vibrio cholerae cytolysin in the membrane-bound monomeric state blocks membrane insertion and functional pore formation by the toxin.

Vibrio cholerae cytolysin (VCC) is a potent membrane-damaging cytolytic toxin that belongs to the family of β barrel pore-forming protein toxins. VCC induces lysis of its target eukaryotic cells by forming transmembrane oligomeric β barrel pores. The mechanism of membrane pore formation by VCC follows the overall scheme of the archetypical β barrel pore-forming protein toxin mode of action, in which the water-soluble monomeric form of the toxin first binds to the target cell membrane, then assembles into a prepore oligomeric intermediate, and finally converts into the functional transmembrane oligomeric β barrel pore.

Immeasurable glycosylated haemoglobin: a marker for severe haemolysis.

Glycosylated haemoglobin (HbA1c) is a measurement commonly performed in patients with diabetes. Factors causing a change in the life span of the red blood cell (RBC) can affect the measurement of HbA1c. Thus haemolysis is an important factor that may affect the HbA1c level determination.

Functional mapping of the lectin activity site on the β-prism domain of vibrio cholerae cytolysin: implications for the membrane pore-formation mechanism of the toxin.

Vibrio cholerae cytolysin (VCC) is a prominent member in the family of β-barrel pore-forming toxins. It induces lysis of target eukaryotic cells by forming transmembrane oligomeric β-barrel channels. VCC also exhibits prominent lectin-like activity in interacting with β1-galactosyl-terminated glycoconjugates.