Problems in merging Earth sensing satellite data sets

Satellite remote sensing systems provide a tremendous source of data flow to the Earth science community. These systems provide scientists with data of types and on a scale previously unattainable. Looking forward to the capabilities of Space Station and the Earth Observing System (EOS), the full realization of the potential of satellite remote sensing will be handicapped by inadequate information systems. There is a growing emphasis in Earth science research to ask questions which are multidisciplinary in nature and global in scale. Many of these research projects emphasize the interactions of the land surface, the atmosphere, and the oceans through various physical mechanisms. Conducting this research requires large and complex data sets and teams of multidisciplinary scientists, often working at remote locations. A review of the problems of merging these large volumes of data into spatially referenced and manageable data sets is presented

How do patients with end-stage ankle arthritis decide between two surgical treatments?:A qualitative study

To examine how patients decide between ankle fusion and ankle replacement in end-stage ankle arthritis

Evaluating Unions: Labor Economics and the Law

A Review ofWhat Do Unions Do? by Richard B. Freeman and James L. Medof

Unfair competition governs the interaction of pCPI-17 with myosin phosphatase (PP1-MYPT1).

The small phosphoprotein pCPI-17 inhibits myosin light-chain phosphatase (MLCP). Current models postulate that during muscle relaxation, phosphatases other than MLCP dephosphorylate and inactivate pCPI-17 to restore MLCP activity. We show here that such hypotheses are insufficient to account for the observed rapidity of pCPI-17 inactivation in mammalian smooth muscles. Instead, MLCP itself is the critical enzyme for pCPI-17 dephosphorylation. We call the mutual sequestration mechanism through which pCPI-17 and MLCP interact inhibition by unfair competition: MLCP protects pCPI-17 from other phosphatases, while pCPI-17 blocks other substrates from MLCP\u27s active site. MLCP dephosphorylates pCPI-17 at a slow rate that is, nonetheless, both sufficient and necessary to explain the speed of pCPI-17 dephosphorylation and the consequent MLCP activation during muscle relaxation