Evaluation of Papain-Urea for Enzymatic Debridement of Coagulation Zones Following Ablative Fractional Laser Treatment.

Background: Ablative fractional CO laser (10,600 nm) treatment creates an array of microscopic treatment zones composed of an ablation zone (AZ) surrounded by a denatured coagulation zone (CZ). The CZ is believed to play a functional role in skin tightening, posttreatment inflammation, and laser-assisted drug delivery. This study investigates the viability of enzymatic post-processing to remove the CZ without affecting the surrounding tissue.

Crystal structures of cables formed by the acetylated and unacetylated forms of the Schizosaccharomyces pombe tropomyosin ortholog Tpm.

Cables formed by head-to-tail polymerization of tropomyosin, localized along the length of sarcomeric and cytoskeletal actin filaments, play a key role in regulating a wide range of motile and contractile processes. The stability of tropomyosin cables, their interaction with actin filaments and the functional properties of the resulting co-filaments are thought to be affected by N-terminal acetylation of tropomyosin. Here, we present high-resolution structures of cables formed by acetylated and unacetylated Schizosaccharomyces pombe tropomyosin ortholog Tpm.

Focal point technology: Controlling treatment depth and pattern of skin injury by a novel highly focused laser.

Background: Selective photothermolysis has limitations in efficacy and safety for dermal targets. We describe a novel concept using scanned focused laser microbeams for precise control of dermal depth and pattern of injury, using a 1550 nm laser that generates an array of conical thermal zones while minimizing injury to the epidermis.

Objective: To characterize the conical thermal zones in vivo and determine safe starting parameters to transition to a second phase to explore potential clinical indications.

Motor properties of Myosin 5c are modulated by tropomyosin isoforms and inhibited by pentabromopseudilin.

Myosin 5c (Myo5c) is a motor protein that is produced in epithelial and glandular tissues, where it plays an important role in secretory processes. Myo5c is composed of two heavy chains, each containing a generic motor domain, an elongated neck domain consisting of a single α-helix with six IQ motifs, each of which binds to a calmodulin (CaM) or a myosin light chain from the EF-hand protein family, a coiled-coil dimer-forming region and a carboxyl-terminal globular tail domain. Although Myo5c is a low duty cycle motor, when two or more Myo5c-heavy meromyosin (HMM) molecules are linked together, they move processively along actin filaments.