Cleft lip and palate surgery simulator: Open source simulation model.

Objective: Cleft lip and palate is the most common craniofacial birth anomaly and requires surgery in the first year of life. However, craniofacial surgery training opportunities are limited. The aim of this study was to present and evaluate an open-source cleft lip and palate hybrid (casting and three-dimensional (3D) printing) simulation model which can be replicated at low cost to facilitate the teaching and training of cleft surgery anatomy and techniques.

Comparative study on cleft palate morphology after passive presurgical plate therapy in unilateral cleft lip and palate.

Background: Presurgical plate therapy has been widely accepted as a treatment prior to palatal cleft closure. The effects of passive presurgical plate therapy on cleft morphology prior to single-stage unilateral cleft lip and palate (UCLP) repair were quantified.

Patients And Methods: We compared the dimensions of cleft width and cleft area (true cleft and palatal cleft) measured preoperatively at 2 European cleft centers.

Automated and data-driven plate computation for presurgical cleft lip and palate treatment.

Purpose: Presurgical orthopedic plates are widely used for the treatment of cleft lip and palate, which is the most common craniofacial birth defect. For the traditional plate fabrication, an impression is taken under airway-endangering conditions, which recent digital alternatives overcome via intraoral scanners. However, these alternatives demand proficiency in 3D modeling software in addition to the generally required clinical knowledge of plate design.

Digital impressions from newborns to preschoolers with cleft lip and palate: A two-centers experience.

Background: Documenting cleft lip and palate morphology prior to surgery is standard care. Presurgical orthopedic treatment also requires a 3D cleft model. Endangering the airway, conventional impressions require additional safety measures and resources.

Confined Mobility of TonB and FepA in Escherichia coli Membranes.

The important process of nutrient uptake in Escherichia coli, in many cases, involves transit of the nutrient through a class of beta-barrel proteins in the outer membrane known as TonB-dependent transporters (TBDTs) and requires interaction with the inner membrane protein TonB. Here we have imaged the mobility of the ferric enterobactin transporter FepA and TonB by tracking them in the membranes of live E. coli with single-molecule resolution at time-scales ranging from milliseconds to seconds.

Energy-dependent motion of TonB in the Gram-negative bacterial inner membrane.

Gram-negative bacteria acquire iron with TonB-dependent uptake systems. The TonB-ExbBD inner membrane complex is hypothesized to transfer energy to outer membrane (OM) iron transporters. Fluorescence microscopic characterization of green fluorescent protein (GFP)-TonB hybrid proteins revealed an unexpected, restricted localization of TonB in the cell envelope.

Single-molecule imaging in live bacteria cells.

Bacteria, such as Escherichia coli and Caulobacter crescentus, are the most studied and perhaps best-understood organisms in biology. The advances in understanding of living systems gained from these organisms are immense. Application of single-molecule techniques in bacteria have presented unique difficulties owing to their small size and highly curved form.

Single-molecule study of molecular mobility in the cytoplasm of Escherichia coli.

The cytoplasm of bacterial cells is filled with individual molecules and molecular complexes that rely on diffusion to bring them together for interaction. The mobility of molecules in the cytoplasm has been characterized by several techniques mainly using fluorescent probes and ensemble methods. In order to probe the microenvrionment inside the cytoplasm as viewed by an individual molecule, we have studied single green fluorescent proteins (GFPs) diffusing in the cytoplasm of Escherichia coli cells at observation at rates ranging from 60 to 1000 Hz.

Mobility of BtuB and OmpF in the Escherichia coli outer membrane: implications for dynamic formation of a translocon complex.

Diffusion of two Escherichia coli outer membrane proteins-the cobalamin (vitamin B12) receptor (BtuB) and the OmpF porin, which are implicated in the cellular import pathways of colicins and phages-was measured in vivo. The lateral mobility of these proteins is relevant to the mechanism of formation of the translocon for cellular import of colicins such as the rRNase colicin E3. The diffusion coefficient (D) of BtuB, the primary colicin receptor, complexed to fluorescent antibody or colicin, is 0.

MacMARCKS interacts with the metabotropic glutamate receptor type 7 and modulates G protein-mediated constitutive inhibition of calcium channels.

We have previously shown that the interaction of Ca2+/calmodulin with the metabotropic glutamate receptor type 7 (mGluR7) promotes the G-protein-mediated inhibition of voltage-sensitive Ca2+ channels (VSCCs) seen upon agonist activation. Here, we performed a yeast two-hybrid screen of a new-born rat brain cDNA library using the cytoplasmic C-terminal tail of mGluR7 as bait and identified macrophage myristoylated alanine-rich c-kinase substrate (MacMARCKS) as a binding protein. The interaction was confirmed in vitro and in vivo by pull-down assays, immunoprecipitation, and colocalization of mGluR7 and MacMARCKS in transfected HEK293 cells and cultured cerebellar granule cells.

Single hepatitis-B virus core capsid binding to individual nuclear pore complexes in Hela cells.

We investigate the interaction of hepatitis B virus capsids lacking a nuclear localization signal with nuclear pore complexes (NPCs) in permeabilized HeLa cells. Confocal and wide-field optical images of the nuclear envelope show well-spaced individual NPCs. Specific interactions of capsids with single NPCs are characterized by extended residence times of capsids in the focal volume which are characterized by fluorescence correlation spectroscopy.

Kinetics of the initial steps of G protein-coupled receptor-mediated cellular signaling revealed by single-molecule imaging.

We report on an in vivo single-molecule study of the signaling kinetics of G protein-coupled receptors (GPCR) performed using the neurokinin 1 receptor (NK1R) as a representative member. The NK1R signaling cascade is triggered by the specific binding of a fluorescently labeled agonist, substance P (SP). The diffusion of single receptor-ligand complexes in plasma membrane of living HEK 293 cells is imaged using fast single-molecule wide-field fluorescence microscopy at 100 ms time resolution.