Late afternoon buying by Big Boys lifted closing price to end almost at the high of the day. More Big Boys purchases needed to ensure that price momentum continues.
The Ibis T5000™ Biosensor System enables rapid identification and characterization of bacterial, viral, fungal and other infectious organisms as well as analysis of human DNA. The Ibis T5000 has the unique ability to rapidly identify a broad range of infectious organisms in a sample without needing to know beforehand which organisms might be present.
This powerful new approach to microorganism characterization and detection is fundamentally different than traditional methods requiring prior knowledge of a suspected organism´s DNA sequence to enable detection and identification.
The Ibis T5000 was developed originally for government customers and markets such as biodefense and forensics. Ibis Biosensor technology is now available for research applications ranging from epidemiology and disease surveillance to hospital-associated infection (HAI) control. In the future it may be applied for in vitro diagnostics.
http://www.ibisbiosciences.com/pages.asp?ID=8
An important area of Isis' basic research is to understand the molecular mechanisms of antisense. There are at least 12 known antisense mechanisms that can be exploited once an antisense drug binds to its target RNA. Isis has created proprietary chemical modifications to trigger many of these mechanisms for drug discovery. As its understanding of these mechanisms further improves, the Company expects to develop antisense drugs with enhanced performance and for broader therapeutic applications.
An antisense mechanism is defined as the process in which an antisense drug works after it binds (hybridizes) to a target RNA to form a duplex. The formation of this duplex, or two-stranded molecule, prevents the RNA from functioning normally and from producing a protein product.
Progress in Isis' mechanism of action research program is illustrated by the Company's accomplishments in understanding RNase H. The majority of late-stage antisense drugs in development bind to their target RNA and activate a cellular enzyme called RNase H. This enzyme destroys the target RNA, inhibiting production of a specific protein. Isis has cloned and characterized human RNase H and has effectively used that information to design its proprietary second-generation drugs. The Company expects to further improve its drugs, using its insights into the RNase H mechanism.
In addition to its RNase H expertise, Isis has made advancements in understanding and exploiting other antisense mechanisms.
http://www.isispharm.com/antisenseMechanisms.html
Carnivorous plants are not the first organisms to come to mind when searching for biomedical compounds. Yet, like something from science fiction, researchers are discovering enzymes in the digestive fluids of carnivorous pitcher plants that could prove useful in controlling infections.
Most plants support their growth by absorbing nutrients such as nitrogen, phosphorus and potassium from the soil. But for those unlucky enough to live in regions where soils lack these nutrients, alternative arrangements have evolved — such as organs that can catch, kill and digest insects.
Some of these organs develop as spiky mouths that close on unsuspecting insects when they land on them; some develop as seemingly normal leaves that are covered with goo, rather like flypaper; others, such as the structures sported by the plant Nepenthes alata, are slippery pitchers that function like pit traps. Nepenthes alata uses a combination of bright colours and sweet scent to attract insects to the pitcher, where slippery side walls and a deep pit filled with acidic fluid trap and kill the victims.
The fluid at the base of the trap had long been thought to contain digestive enzymes. Previous research had confirmed this, but exactly which enzymes were present was anyone’s guess. “Digestion in pitcher plants has been actively studied for more than 150 years and we still don’t know how it works [because] it is such a complex process,” says Chris Frazier at the University of New Mexico in Albuquerque.
Now, Naoya Hatano from the Harima Institute in Riken and Tatsuro Hamada from Ishikawa Prefectural University in Japan have identified seven proteins in the carnivorous plant's fluid. They grew the carnivorous plants in their lab, and collected the fluid from newly opened pitchers to prevent contamination from recently captured insects. Then they used polyacrylamide gel electrophoresis to separate out the proteins, and mass spectrometry to identify what type of enzymes the proteins were likely to be. Because some of the enzymes they found were unfamiliar, they searched protein databases to find enzymes with similar structures and noted that some of them were probably not digestive at all.
http://www.nature.com/news/2008/080131/full/news.2008.546%20.html
