Post-Traumatic Stress Disorder and Alcohol Use Disorder During the COVID-19 Outbreak: Do Dissociation and Emotional Metacognitive Beliefs Mediate the Role of Emotion Dysregulation?

Objective: Despite the well-documented relationship between emotion dysregulation and both post-traumatic stress disorder (PTSD) and alcohol use disorder symptoms, no studies investigated this issue in the context of the outbreak. Moreover, additional research investigating the role of mediators intervening in these pathways is required. Dissociation and emotional beliefs are two factors that may explain such relationships.

Syntaxin-1A modulates vesicle fusion in mammalian neurons via juxtamembrane domain dependent palmitoylation of its transmembrane domain.

SNAREs are undoubtedly one of the core elements of synaptic transmission. Contrary to the well characterized function of their SNARE domains bringing the plasma and vesicular membranes together, the level of contribution of their juxtamembrane domain (JMD) and the transmembrane domain (TMD) to the vesicle fusion is still under debate. To elucidate this issue, we analyzed three groups of STX1A mutations in cultured mouse hippocampal neurons: (1) elongation of STX1A's JMD by three amino acid insertions in the junction of SNARE-JMD or JMD-TMD; (2) charge reversal mutations in STX1A's JMD; and (3) palmitoylation deficiency mutations in STX1A's TMD.

Densification of cancellous bone with autologous particles can enhance the primary stability of uncemented implants by increasing the interface friction coefficient.

Sufficient primary stability is one of the most important prerequisites for successful osseointegration of cementless implants. Bone grafts, densification and compaction methods have proven clinically successful, but the related effects and causes have not been systematically investigated. Postoperatively, the frictional properties of the bone-implant interface determine the amount of tolerable shear stress.

Deconstructing Synaptotagmin-1's Distinct Roles in Synaptic Vesicle Priming and Neurotransmitter Release.

Synaptotagmin-1 (SYT1) is a synaptic vesicle resident protein that interacts via its C2 domain with anionic lipids from the plasma membrane in a calcium-dependent manner to efficiently trigger rapid neurotransmitter (NT) release. In addition, SYT1 acts as a negative regulator of spontaneous NT release and regulates synaptic vesicle (SV) priming. How these functions relate to each other mechanistically and what role other synaptotagmin (SYT) isoforms play in supporting and complementing the role of SYT1 is still under intensive investigation.