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DPDW chart... Company seems to be turning a corner... Threat of reverse split over, "uplisted", all it needs to light the fire is for a few insiders to pony up and buy on the open market instead of rewarding themselves with free shares. Lots of DD to be found on the DPDW I hub board.
http://scharts.co/QZMMBD
Good volume, long downtrend line broken, RSI hasnt been this high in a long time.
http://stockcharts.com/h-sc/ui?s=PRAN&p=D&yr=1&mn=0&dy=0&id=p89302780751
$PRAN getting volume today while most biotechs tread lightly.
$PRAN had big volume yesterday and regained the 50sma on yet another failed trial of a competitor's plaque-clearing Alzheimer's drug. $PRAN has the only data for improved cognition in humans and pbt2 has a completely different MOA than those drugs. Pbt2 is unpartnered and JNJ was in talks with them until they bought into the flawed amyloid hypothesis, so the speculation is that big pharma is going to see the light.
http://www.fiercebiotech.com/tags/bapineuzumab
http://scharts.co/MmnpTe
Pran had big volume yesterday and regained the 50sma on yet another failed trial of a competitor's plaque-clearing Alzheimer's drug. Pran has the only data for improved cognition in humans and pbt2 has a completely different MOA than those drugs. Pbt2 is unpartnered and JNJ was in talks with them until they bought into the flawed amyloid hypothesis, so the speculation is that big pharma is going to see the light.
http://www.fiercebiotech.com/tags/bapineuzumab
http://scharts.co/MmnpTe
I agree that bigger money is being attracted.... Retailers aren't going to purchase that $5,000 report.
I'm ready!
Possible substituts for IVIG:
This one is recombinant Fc, if the MOA involves the Fc region: http://f1000.com/1108172
Alternatively, it should be not too hard to make transgenic cows or pigs with fully human antibodies.
I smell financing soon!
For stockchart links to work, click link able version, a new feature is that it also gives an option for a short URL.
http://scharts.co/MjDeee
Can anyone recommend some biotech twitter feeds?
Pretty god volume today...http://scharts.co/MmnpTe
a vaccine provides immunity for a long time and could be added to one of the other standard vaccines:
http://www.cdc.gov/vaccines/schedules/downloads/child/0-18yrs-11x17-fold-pr.pdf
NVAX
NOVAVAX Reports on Progress with RSV Vaccine at New International Conference on Modern Vaccines
Press Release: Novavax, Inc. – 43 minutes ago
ROCKVILLE, Md., July 5, 2012 (GLOBE NEWSWIRE) -- Novavax, Inc. (NVAX) reported this week that Gregory Glenn, M.D., Senior Vice President and Chief Medical Officer of Novavax, reviewed recent preclinical and clinical findings from the company's respiratory syncytial virus (RSV) vaccine development program at the first Modern Vaccines Adjuvants and Delivery Systems conference in Copenhagen, Denmark. He reported that the findings from the recent Phase I trial were consistent with the preclinical results in relevant animal models, which indicated that the Novavax Fusion (F) protein nanoparticle RSV vaccine candidate was generally well-tolerated, highly immunogenic and produced functional antibodies that neutralized RSV. There is currently no vaccine available to prevent RSV, which is the leading cause of bronchiolitis and pneumonia in infants under one year of age and a leading cause of pneumonia in older adults.
Dr. Glenn stated during his presentation: "The past development of an RSV vaccine has been very challenging to the vaccine industry. In reviewing our clinical and preclinical data, we recently uncovered some important insights about natural infection by RSV that should assist us in the development of an effective vaccine. These insights include:
"In both clinical and preclinical studies, we found that while subjects exposed to RSV infections had anti-F antibodies, there are almost no antibodies to a specific antigenic site (site II) on the highly conserved Fusion (F) protein of RSV.
"In clinical studies, a monoclonal antibody that targets the antigenic site II (i.e., palivizumab) has been shown to be highly effective at preventing RSV disease. In fact, palivizumab (trade name Synagis(R)) has been approved in multiple countries for years to prevent RSV disease in pre-mature infants.
"Together, these data points suggest a survival advantage for the RSV virus based on keeping the RSV F antigenic site II cryptic during natural infections, and that the antigenic site II specific immunity can be exploited for an effective vaccine."
Dr. Glenn went on to add: "Immunization with the Novavax RSV F nanoparticle vaccine antigen, which contains multiple copies of the antigenic site II epitope, induced robust antigenic site II specific antibodies in both our preclinical and clinical studies. In preclinical studies, immunization of cotton rats with RSV F nanoparticles induced anti-RSV IgG that was neutralizing, competitive for the binding of palivizumab to RSV F, and was completely protective against viral challenge.
"Similarly, in a Phase I placebo-controlled trial, the same vaccine given to healthy adults induced both RSV A and B microneutralizing antibodies that were significantly increased in vaccinees versus placebo and in excess of what has been observed to be protective in other epidemiological studies. Antibodies that both bind to and compete with the F protein antigenic site II were readily induced by the vaccine. Quantitative estimation of palivizumab-like activity found the highest dose group had a mean of 335 ug/ml, exceeding by around 10-fold the trough level used as guidance in palivizumab efficacy evaluations.
"The Novavax RSV F nanoparticle vaccine candidate displays the antigenic site II epitope in its native configuration and was found to induce functional immunity as measured both by microneutralization and palivizumab-like antibodies at levels that exceed those associated with decreased risk of hospitalization. Together, the results suggest that our RSV F nanoparticle vaccine holds great promise as a vaccine candidate for infants, children and the elderly who would benefit from protective immunity against RSV."
Dr. Glenn's plenary presentation, entitled "Recombinant nanoparticle vaccine: Preclinical and clinical evaluation of an Sf9 insect cell-derived respiratory syncytial virus fusion protein," is available in the Our Science/Presentations tab of the company's website, www.novavax.com. Dr. Glenn also served as a scientific advisor to the conference, which was organized to address the urgent need for new adjuvants, delivery systems and technologies to support the development of new vaccines. For more information about the conference, please visit www.meetingsmanagement.co.uk.
About Novavax
Novavax, Inc. (NVAX) is a clinical-stage biopharmaceutical company creating novel vaccines to address a broad range of infectious diseases worldwide. Using innovative virus-like particle (VLP) and recombinant nanoparticle technology, as well as new and efficient manufacturing approaches, the company produces vaccine candidates to combat diseases, with the goal of allowing countries to better prepare for and more effectively respond to rapidly spreading infections. Novavax is committed to using its technology platforms to create geographic-specific vaccine solutions and is therefore involved in several international partnerships, including collaborations with Cadila Pharmaceuticals of India and LG Life Sciences of Korea. Together, these companies have worldwide commercialization capacity and the global reach to create real and lasting change in the biopharmaceutical field. Additional information about Novavax is available on the company's website, www.novavax.com.
Forward-Looking Statements
Statements herein relating to the future of Novavax and its ongoing development of its vaccine candidates are forward-looking statements. Novavax cautions that these forward-looking statements are subject to numerous risks and uncertainties, which could cause actual results to differ materially from those expressed or implied by such statements. These risks and uncertainties include those identified under the heading "Risk Factors" in the Novavax Annual Report on Form 10-K for the year ended December 31, 2011, and filed with the Securities and Exchange Commission. We caution investors not to place considerable reliance on the forward-looking statements contained in this press release. You are encouraged to read our filings with the SEC, available at www.sec.gov, for a discussion of these and other risks and uncertainties. The forward-looking statements in this press release speak only as of the date of this document, and we undertake no obligation to update or revise any of the statements. Our business is subject to substantial risks and uncertainties, including those referenced above. Investors, potential investors, and others should give careful consideration to these risks and uncertainties.
Contact:
Frederick W. Driscoll
VP, Chief Financial Officer and Treasurer
Novavax, Inc.
240-268-2000
@yahoofinance on Twitter, become a fan on Facebook
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Cort is another that I've been in and out of for a long time... Raising $50m cash right now... Should climb nicely once the deal closes.
http://scharts.co/MD8YhW
I've been in pran for a few years... The chart is looking juicy... A few closes above 50sma and 50 starting to curl upwards http://scharts.co/N0CD2K
Awesome
Post-Anesthesia Dementia, Like Alzheimer's, Looks Micro-'Tubular'
ScienceDaily (June 27, 2012) — Modern anesthesia is extremely safe. But as risks to heart, lungs and other organs have waned, another problem has emerged in the elderly: post-operative cognitive dysfunction. Mentally, some patients "just aren't the same" for months or longer after surgery. Other factors play a role, but a small number of patients deteriorate mentally due to anesthesia per se. Those with Alzheimer's disease suffer exacerbations, and those without the diagnosis may have it unmasked by anesthesia, suggesting some relationship.
Alzheimer's disease has two types of brain lesions. Beta-amyloid deposits accumulate outside neurons but don't cause cognitive problems. Neurofibrillary tangles inside neurons, composed of hyper-phosphorylated 'tau', a protein normally attached to microtubules, do correlate with dementia. These same tau tangles are found in post-anesthesia dementia.
Microtubules (MTs) polymerize from 'tubulin' proteins to grow, shape and regulate neurons. Synaptic components are transported by motor proteins which move like railroad trains along MT tracks. In branching dendrites, motors change MTs repeatedly to reach their destination. Tau is a traffic signal, telling motors where to get on and off, the route encoded in MT binding sites for tau.
That MTs process information stems from Charles Sherrington in the 1950s, with recent controversial suggestions of MT computing, and even quantum computing mediating consciousness and memory. But whether MTs play a primary, or mere supportive role, their stability and function are essential to cognition and consciousness.
Excessive phosphorylation had been thought the culprit in detaching tau and causing tangles. But destabilized MTs now appear to be the primary problem in both Alzheimer's and post-anesthesia dementia, releasing tau which then becomes hyperphosphorylated. Anesthetics are known to bind to tubulin, in some cases for days after exposure, and in high doses to cause MT disassembly.
Now, in a study in PLoS ONE, a team from Canada, Portugal and the USA report molecular modeling showing 32 anesthetic binding sites per tubulin, with at least 1 percent (10 million) of the billion tubulins per brain neuron binding an anesthetic molecule at clinical concentration (1 'MAC'). Two particular anesthetic binding regions may destabilize MTs, one inactivating tubulin C-termini tails (which otherwise knit together neighboring tubulins). The other weakens side-to-side tubulin couplings, the critical link in MT lattices, but only at high anesthetic concentrations, or perhaps with other MT destabilizing factors (low temperature, low zinc, high calcium, acidosis).
Travis Craddock PhD, lead author on the study said: "The good news is that therapies aimed at microtubule stabilization may help in both Alzheimer's and post-anesthetic dementias. Clinical trials are underway, or planned, for microtubule stabilizers Epothilone D, NAPVSIPQ, and the zinc ionophore PBT2, as well as brain ultrasound, shown in vitro to excite MT resonances and promote polymerization. However it's done, 'tightening the tubules' may best treat dementia."
http://www.sciencedaily.com/releases/2012/06/120627091617.htm
Post-Anesthesia Dementia, Like Alzheimer's, Looks Micro-'Tubular'
ScienceDaily (June 27, 2012) — Modern anesthesia is extremely safe. But as risks to heart, lungs and other organs have waned, another problem has emerged in the elderly: post-operative cognitive dysfunction. Mentally, some patients "just aren't the same" for months or longer after surgery. Other factors play a role, but a small number of patients deteriorate mentally due to anesthesia per se. Those with Alzheimer's disease suffer exacerbations, and those without the diagnosis may have it unmasked by anesthesia, suggesting some relationship.
Alzheimer's disease has two types of brain lesions. Beta-amyloid deposits accumulate outside neurons but don't cause cognitive problems. Neurofibrillary tangles inside neurons, composed of hyper-phosphorylated 'tau', a protein normally attached to microtubules, do correlate with dementia. These same tau tangles are found in post-anesthesia dementia.
Microtubules (MTs) polymerize from 'tubulin' proteins to grow, shape and regulate neurons. Synaptic components are transported by motor proteins which move like railroad trains along MT tracks. In branching dendrites, motors change MTs repeatedly to reach their destination. Tau is a traffic signal, telling motors where to get on and off, the route encoded in MT binding sites for tau.
That MTs process information stems from Charles Sherrington in the 1950s, with recent controversial suggestions of MT computing, and even quantum computing mediating consciousness and memory. But whether MTs play a primary, or mere supportive role, their stability and function are essential to cognition and consciousness.
Excessive phosphorylation had been thought the culprit in detaching tau and causing tangles. But destabilized MTs now appear to be the primary problem in both Alzheimer's and post-anesthesia dementia, releasing tau which then becomes hyperphosphorylated. Anesthetics are known to bind to tubulin, in some cases for days after exposure, and in high doses to cause MT disassembly.
Now, in a study in PLoS ONE, a team from Canada, Portugal and the USA report molecular modeling showing 32 anesthetic binding sites per tubulin, with at least 1 percent (10 million) of the billion tubulins per brain neuron binding an anesthetic molecule at clinical concentration (1 'MAC'). Two particular anesthetic binding regions may destabilize MTs, one inactivating tubulin C-termini tails (which otherwise knit together neighboring tubulins). The other weakens side-to-side tubulin couplings, the critical link in MT lattices, but only at high anesthetic concentrations, or perhaps with other MT destabilizing factors (low temperature, low zinc, high calcium, acidosis).
Travis Craddock PhD, lead author on the study said: "The good news is that therapies aimed at microtubule stabilization may help in both Alzheimer's and post-anesthetic dementias. Clinical trials are underway, or planned, for microtubule stabilizers Epothilone D, NAPVSIPQ, and the zinc ionophore PBT2, as well as brain ultrasound, shown in vitro to excite MT resonances and promote polymerization. However it's done, 'tightening the tubules' may best treat dementia."
http://www.sciencedaily.com/releases/2012/06/120627091617.htm
Alzheimer's Spread Through the Brain Mapped: Infects from Neuron to Neuron
(I would like to see them try this experiment in the presence of one of the plaque busting antibodies... to see if if the antibodies do or don't block neuron to neuron spread)
ScienceDaily (June 26, 2012) — The inexorable spread of Alzheimer's disease through the brain leaves dead neurons and forgotten thoughts in its wake. Researchers at Linköping University in Sweden are the first to show how toxic proteins are transferred from neuron to neuron.
Through experiments on stained neurons, the research team -- under the leadership of Martin Hallbeck, associate professor of Pathology -- has been able to depict the process of neurons being invaded by diseased proteins that are then passed on to nearby cells.
"The spread of Alzheimer's, which can be studied in the brains of diseased patients, always follows the same pattern. But until now how and why this happens has not been understood," says Hallbeck, who along with his research group has now published their results in the Journal of Neuroscience.
The illness starts in the entorhinal cortex -- a part of the cerebral cortex, and then spreads to the hippocampus. Both of these areas are important for memory. Gradually, pathological changes take place in more and more areas of the brain, while the patient becomes even sicker.
Two proteins have been identified in connection with Alzheimer's: beta amyloid and tau. Normally tau is found in the axons -- the outgrowths that connect between neurons -- where it has a stabilising function, while beta amyloid seems to have a role in the synapses where the neurons transfer signal substances to each other. But in Alzheimer's patients, something happens with these proteins; autopsies reveal abnormal accumulations of both.
Why they become abnormal is still unknown, but what is known is that it's not the large accumulations, or plaques, that damage the neurons. Instead, smaller groups of beta amyloid -- called oligomeres -- seem to be the toxic form that gradually destroy the neurons and shrink the brain.
"We wanted to investigate whether these oligomeres can spread from neuron to neuron, something many researchers tried earlier but didn't succeed," Hallbeck says.
The study was inaugurated with an experiment on neuron cultures, where researchers injected oligomeres stained with a phosphorescent red substance called TMR using a very thin needle. The next day the neighbouring, connected neurons were also red, which showed that the oligomeres had spread.
To test whether a sick neuron can "infect" others, they conducted a round of experiments with mature human neurons stained green and mixed with others that were red after having taken up stained oligomeres. After a day, approximately half of the green cells had been in contact with a few of the red ones. After two more days, the axons had lost their shape and organelles in the cell nucleus had started to leak.
"Gradually more and more of the green cells became sick. Those that hadn't taken up the oligomeres, on the other hand, weren't affected," Hallbeck says.
The study is a breakthrough in understanding Alzheimer's and its progress. If a way of stopping the transfer can be found, it could lead to a more effective inhibitor against the disease.
http://www.sciencedaily.com/releases/2012/06/120626172728.htm
Nice freakin' HOD close! Chart looking strong... 50sma curling upwards now.
Plenty of follow through
http://scharts.co/Oyx7GT
They should test PBT2 from Prana. This review below is authored by Dennis Selkoe, whom masterlongevity highlighted in his post...
"oligomers are neurotoxic, plaques are neuroprotective" is a theme that is being tossed about nowadays.
Below the masters and selkoe review is an article reviewing the "target the oligomer" strategy...bold and italics are my influence or comments.
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3367542/?tool=pubmed
excerpts from full text:
DIFFUSIBLE OLIGOMERS OF Aß.If one considers the trajectory of biochemical studies of Aß, it is clear that the field has moved over the last dozen years from an initial emphasis on the fibrillar state found in amyloid plaques and meningocerebral vessels to a range of smaller, oligomeric Aß assemblies that are relatively soluble and diffusible and thus more able to exert a toxic effect on the neuronal plasma membrane, including synapses. (but big pharma has spent too much money already on plaque dissolution and is hoping their antibodies will soak up oligomers) A rich and confusing vocabulary has developed to describe the oligomers of Aß as they assemble along pathways which may or may not lead to the classical 8 nm amyloid fibrils found in plaques and blood vessels (Table 1). The methods of analysis often determine nomenclature: biochemical characterization of synthetic or natural (cellular and brain) Aß peptides using SDS-PAGE or size exclusion chromatography has led to descriptions of assemblies containing a few (e.g., 2–20) monomers, usually designated soluble oligomers; other methods, particularly those using morphological or biophysical approaches on synthetic Aß such as electron microscopy or atomic force microscopy, may describe linear protofilaments (often ~4 nm in diameter) or spherical/globular particles, each of which has been interpreted as a precursor of amyloid fibrils. It is important to emphasize here that many of the synthetic Aß assembly forms reported in the literature have been made in vitro using supraphysiological concentrations of a single-length peptide (e.g., Aß1–40), and the occurrence of closely similar or identical species in AD brain tissue may not have been explicitly confirmed structurally (immunochemical cross-reaction would not be sufficient confirmation). One caveat in this regard is that natural Aß oligomers isolated from AD brain tissue or APP-expressing cell cultures are far more potent in electrophysiological or cytotoxicity assays than are synthetic assembly mixtures such as ADDLs (“Aß-derived diffusible ligands”) (Lambert et al. 1998) or protofibrils (Harper et al. 1997; Walsh et al. 1997), which require high nanomolar concentrations to induce biological effects, suggesting that they contain many “off-pathway” (unnatural) assembly forms that do not interact with neuronal membranes the way natural oligomers do. Indeed, some such synthetic “oligomers” have not been proven to be truly soluble in aqueous buffers (i.e., not pelletable at 100,000 g in an ultracentrifuge), which is the case for natural oligomers (see, for further reviews of the complexity of Aß assembly forms, Haass and Selkoe 2007; Walsh and Selkoe 2007; Di Carlo 2010; Sakono and Zako 2010)......
Metal Ions
Because of their ubiquitous presence in human tissues, the bioavailable metal ions, Cu, Zn, and Fe, have been obvious choices for investigation of amyloid association. For decades, uncertainty has reigned over the quantitative elemental analysis of whole brain homogenates—and of isolated plaques or tangles—in AD compared to normal aged controls and other neurodegenerative diseases. At the level of grey matter homogenates, there is no agreement that any particular metal ion is specifically elevated or lowered in AD brain. Most techniques have detected elevations in Cu, Zn, or Fe in AD amyloid plaques, either in situ or after their purification (see, for example, Rajendran et al. 2009), but such analytical approaches have never been entirely convincing. The observations that both APP and Aß have sequences consistent with metal-binding motifs and metallo-complexing activities add a new dimension to this line of enquiry (Faller 2009; Duce et al. 2010). Measuring the affinities of metal–protein interactions is challenging (Xiao and Wedd 2010) but, as technologies have improved, the general rule has emerged that the metal affinities increase as the proteins move toward their sites of final subcellular compartmentalization and utilization. Thus, certain other proteins act as chaperones to take the metal ions into compartments where their higher affinity end-user proteins reside. The synapse has proven to be a subcellular site where ions such as Zn2+ and Cu2+ are used to modulate the activities of key excitatory NMDA/AMPA receptors. It is in the vicinity of this cellular compartment that Aß may interact with these divalent cations in a fashion that can alter the peptide’s conformation. This metal-based mechanism, as well as the overall level of local excitatory neurotransmission (Cirrito et al. 2005), could help provide an explanation for the topographic selectivity of Aß aggregation and extracellular deposition in the AD brain, as there is an intriguing overlap between those areas of the brain rich in glutamatergic terminals, free vesicular zinc, and Aß amyloid plaques in certain APP transgenic mice (Stoltenberg et al. 2007).
With an emerging understanding of the pathways leading to soluble oligomer or insoluble fibril production, therapeutic strategies loosely termed as “anti-Aß aggregation” need to be refocused on the specific steps being targeted (Rodriguez-Rodriguez et al. 2009; Yadav and Sonker 2009; Dickens and Franz 2010), particularly with regard to the concept of “therapeutic chelation” of metal ions. The concept of therapeutic chelation needs to be qualified by the relative affinities each metal ion has for its target protein. Thus, metal “chaperone” is a preferred concept when discussing the reversible interactions divalent cations can have with Aß, regardless of which oligomeric or fibrillar assembly is being considered.
Aß and Copper
The average KD of Cu2+ for Aß is about 10-10 m (i.e., low nanomolar) for both soluble and fibrillar forms of the synthetic peptide in vitro (R?zga et al. 2010; Xiao and Wedd 2010). This means that other metallo-chaperone proteins with higher (i.e., high picomolar or greater) affinities will prevent Cu2+ binding to Aß. This criterion would include human serum albumin (Perrone et al. 2009), suggesting that Aß in locations (e.g., CSF or blood) remote from parenchymal brain compartments such as neurites and synapses should be unmetallated. Furthermore, therapeutic compounds designed to act as metal-ion chaperones with low picomolar affinities would be expected to compete with Aß for Cu2+ binding only within the brain parenchyma.
Aß may have more than one Cu2+-binding site (Behbehani and Mirzaie 2009; Jun et al. 2009; Sarell et al. 2009). Depending on the stoichiometry, Cu2+–Aß interactions can cause synthetic Aß to aggregate in vitro principally via an oligomer-forming pathway or a fibrillogenic pathway (Brzyska et al. 2009; Moore et al. 2009; Olofsson et al. 2009a; Tõugu et al. 2009; Haeffner et al. 2010). That is, at sub-equimolar Cu2+:Aß ratios, amyloid fibrils form; at supra-equimolar ratios, stable oligomers form first, then dityrosine cross-linkages occur (Smith et al. 2007). The principal Cu2+-binding site is coordinated within the first 16 residues and involves His6, His13, and His14, together with the first two residues (Asp1, Ala2) (Dorlet et al. 2009; Drew et al. 2009a,b; Hureau et al. 2009a,b). This coordination environment is pleiotropic (Drew et al. 2009b), adding to the complexity of the analysis (Drochioiu et al. 2009; Hureau et al. 2009a). As was predicted when the Aß sequence became known, the protonation of the histidine residues, dependent on pH, should have a major effect in the Aß folding pathway: metallation and folding of Aß in the endosome/lysosome pathway will probably be quite different from that in the extracellular or peri-synaptic compartments.
Cu2+ as a redox-active entity can also induce oxidative modification to Aß, particularly at Tyr10 with consequent dityrosine covalent cross-links (Drew et al. 2009a,b; Moore et al. 2009; Jiang et al. 2010). Other residues, such as Met35, may participate (Barman et al. 2009; Butterfield et al. 2010), but this is not proven (da Silva et al. 2009). Whether the metal-modified Aß is capable of pro- or anti-oxidant activity is also uncertain (Baruch-Suchodolsky and Fischer 2009), but it is an important question that needs to be resolved in terms of understanding the toxicity of Aß oligomers. Reducing intracellular Cu2+ bioavailability has an inhibitory effect on Aß oligomer formation (Crouch et al. 2009a). (Oligomers are neurotoxic)
Aß and Zinc
In contrast to Cu2+, Zn2+ is redox inactive and therefore cannot be directly involved in any oxidative processes involving Aß. In common with Cu2+, Zn2+ has pleotropic binding sites on Aß (Damante et al. 2009; Talmard et al. 2009; Miller et al. 2010) which can serve to drive synthetic Aß aggregation in vitro. The Zn2+-induced formation of cytotoxic Aß oligomers in proximity to excitatory glutamatergic synapses is believed to be a mechanism contributing to synaptic degeneration in AD (Deshpande et al. 2009). Zn–Aß complexes also become more resistant to proteolytic degradation in in vitro experiments (Crouch et al. 2009b), potentially allowing metal-bound Aß fibrils to accumulate in the extracellular space.
Aß and Iron
Studies of Fe3+/Fe2+ complexes with Aß indicate a potential pro-aggregating role for this abundant metal (Jiang et al. 2009a; Uranga et al. 2010), especially if evidence that Aß has significantly higher affinity for Fe2+ than does transferrin (Jiang et al. 2009a) is confirmed.
Target the oligomer:
http://www.aarp.org/health/conditions-treatments/info-05-2010/alzheimers_disease.1.html
“These clumps ... seem to be more toxic to the brain,” Gandy says. He now thinks the oligomers, not plaques, cause the loss of memory and reason that characterize Alzheimer’s. Gandy and colleagues published their work in the Annals of Neurology in April 2010. Dillin, of the Salk Institute of California, started pursuing the same oligomer theory several years ago. Then the idea was so controversial, Dillin says, that some scientists would walk out of the room when he made his presentation at conferences. Now, he says, many of the top researchers in the field are convinced.
Have fun at the AGM... I will be busy vacationing.
FDA: Amylin Pharma Concealed Heart Safety Risks of Key Diabetes Drug
By Adam Feuerstein
SAN DIEGO (TheStreet) -- Amylin Pharmaceuticals(AMLN_) concealed a study from the U.S. Food and Drug Administration that raised heart safety concerns about its diabetes drug Byetta and then hindered FDA access to the data when the agency discovered its existence, newly released FDA records show.
Later, Amylin executives lied to investors by failing to disclose that this hidden Byetta heart-safety study played a key role in FDA rejecting the company's follow-on diabetes drug Bydureon, according to these same FDA records...
http://www.thestreet.com/story/11595037/1/fda-amylin-pharma-concealed-heart-safety-risks-of-key-diabetes-drug.html?puc=yahoo&cm_ven=YAHOO
was the sound of pounding on the table audible on the webcast?
Very nice move happening today!
http://scharts.co/MCkO8k
I have been long PRAN for more than 2 years.
June 1 gap fill on GLD:
http://scharts.co/LINJLJ
perfect set up for new highs... broke out on friday from ascending triangle/bull flag from $14 to $17 and now has new pona data plus monster volume fund reballancing end of june action to push it higher... $20 soon.
perfect set up towards new highs... watching for a strong run starting next week... all that fund rebalancing and window dressing that happens approaching June 29th.
Because there's always somebody that didn't expect it, and there's always an algo waiting for an opportunity... Curse of the crimson hexagon... Plus, the profit taking from asco should provide momentum.
I looked at the weekly an I see a flag from about $14 to $17... That when it breaks out should give another $3 to $20... If it breaks soon... And we do have this nice asco catalyst.
After that I'd expect a few violently negative days surrounding the rida date.
Market toast!
sell in may...