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We suggest that the vertebrate myosin-I field adopt a common nomenclature system based on the names adopted by the Human Genome Organization (HUGO). At present, the myosin-I nomenclature is very confusing; not only are several systems in use, but several different genes have been given the same name. Despite their faults, we believe that the names adopted by the HUGO nomenclature group for genome annotation are the best compromise, and we recommend universal adoption.

Focuses on the Florida Legislature's revision of the standing afforded citizens to challenge environmental permitting decisions under F.S. 403.412(5) of the Administrative Procedure Act. Implications for home builders, developers and other business interests; Confusion and controversy on the effectiveness of the bill.

Presents a study on an epidemic of erythema multiforme and erythema nodosum caused by histoplasmosis during the fall of 1962 to 1963 in Greenwood, South Carolina. Clinical and epidemiological features of the epidemic; Description of the town; Diagnosis; Treatment and monitoring.

Organisms with limited motility may use animal transport as a mechanism for dispersal. Migratory birds can provide a vehicle to move small organisms great distances, which may allow them access to areas that are otherwise inaccessible. During normal mist netting operations at a spring migration banding station along the northern Gulf of Mexico coast in Louisiana, USA, we encountered an Indigo Bunting (Passerina cyanea) with numerous snails, possibly Galba cubensis, underneath its breast feathers. While encounters of songbirds carrying snails appear rare, long-distance migrating songbirds represent a possible mechanism to transport small snails great distances to expand ranges, colonize new areas, or maintain genetic continuity. [ABSTRACT FROM AUTHOR]

Reports on the accomplishments of the Florida Bar Association's Environmental & Land Use Law Section in 1999. Continuing legal education programs; Legal publications; Mission of the section.

Cells mechanically interface with their surroundings through cytoskeleton-linked adhesions, allowing them to sense physical cues that instruct development and drive diseases such as cancer. Contractile forces generated by myosin motor proteins mediate these mechanical signal transduction processes through unclear protein structural mechanisms. Here, we show that myosin forces elicit structural changes in actin filaments (F-actin) that modulate binding by the mechanosensitive adhesion protein α-catenin. Using correlative cryo-fluorescence microscopy and cryo-electron tomography, we identify F-actin featuring domains of nanoscale oscillating curvature at cytoskeleton-adhesion interfaces enriched in zyxin, a marker of actin-myosin generated traction forces. We next introduce a reconstitution system for visualizing F-actin in the presence of myosin forces with cryo-electron microscopy, which reveals morphologically similar superhelical F-actin spirals. In simulations, transient forces mimicking tugging and release of filaments by motors produce spirals, supporting a mechanistic link to myosin's ATPase mechanochemical cycle. Three-dimensional reconstruction of spirals uncovers extensive asymmetric remodeling of F-actin's helical lattice. This is recognized by α-catenin, which cooperatively binds along individual strands, preferentially engaging interfaces featuring extended inter-subunit distances while simultaneously suppressing rotational deviations to regularize the lattice. Collectively, we find that myosin forces can deform F-actin, generating a conformational landscape that is detected and reciprocally modulated by a mechanosensitive protein, providing a direct structural glimpse at active force transduction through the cytoskeleton., Competing Interests: Competing Interests The authors have no competing interests to declare.