I've been following this for awhile. Looks like I get to update my "hit list" of gene targets to investigate.
And that's what this will ultimately be...a list of interesting genes to look at for further investigation. No cures right away, it will take time to absorb this data into the collective intelligence of the medical research community and years to turn it into new treatments.
Another example: my local Wal-Mart has had a boxed copy of the now defunct "Tabula Rasa" MMO on clearance for $29 since Christmas 2008. It's still sitting there, collecting dust.
As a biomedical researcher, I'm glad to finally see some of the promises of stem cells. However, this must be tempered by knowing that there exists a fine line between stem cells and cancer cells. Both grow outside of the normal controls that keep excess cell division in check. For stem cells, this is developmentally controlled by the neighboring cells. I wonder how these stem cells will respond when moved to a new environment and what the long term effects will be. I guess that FDA sanctioned or not, we're going to find out.
I've got a Ph.D. in Molecular Biology and am currently a post-doctoral research associate in a molecular/cell biology lab. Although I can't speak for the computer / biology interface, here's some things that I've learned from a wet lab. I also have a student starting in a few weeks, so I'll give you the same advice that I gave him. Here goes:
1. It's called research for a reason - you do the same stuff over and over again until you get it to work. And even then, sometimes it doesn't work. And no one can explain it.
2. Keep a good notebook. You never know when the smallest detail may be the cause of a problem (See #1). Someone who comes later may have to try to reproduce your results. Sometimes this person is you.
3. There are as many PI (principal investigator) types as there are flavors of Jelly Belly candies. Some examples would be the demi-god (You, nor any of your lab mates, have ever seen them except on your first day), the helicopter (They hover over your every move and plan everything for you), the slacker (They have a foosball table in their office, and they schedule weekly tournaments), and the workaholic (They spend 100 hours a week in lab, why don't you?). Once you identify your PI's type, there are various ways to handle them. In general, do what your lab mates do and you'll be fine.
4. Have fun. You're getting payed to screw around with things. And no one expects everything that you do to work the first time. How awesome is that? The only better job is TV weatherman.
Hope this helps.
I keep various old expansion cards, motherboards, and processors hanging on the wall in plain sight of my beige box. The threat of disembowelment seems to keep it inline.
After hearing how this is a flyby mission and the top speed of this spacecraft, I wondered about the current speed champ, Voyager I. According to some of my back of the envelope calculations based upon New Horizons' estimated top speed after a Jupiter assist and the current position and speed of Voyager I, in 26 years New Horizons will surpass Voyager I as the most distant human made object.
An interesting idea. Since these galaxies lie approximately 80% distance across the universe, and space is constantly stretching between us and them, the frequencies of light they emit must be higher than what we are observing. IANAC (I Am Not A Cosmologist), but could they be strongly emitting in the visible or UV regions, and spacetime is stretching them to the infrared?
"... an MP-3 player, since such a device would not be seen as an appropriate for a CD."
Thankfully someone cleared that up. I mean, the last time I tried to cram a CD into my mp3 player I ended up with nothing but busted plastic shards cutting up my hands. They really are thinking of the children!
I don't usually reply to my own posts, but if your office doesn't have flies (The fruit fly labs upstairs would keep my lab well stocked), you can use raw hamburger. Or eventually annoying coworkers if the plant gets big enough.:)
my lab workbench has giant windows that get lots of sunlight.
Being a biologist (but not a botanist) I've experimented with various plants. Currently I have 3 pothos (philodendron) vines, and a small palm tree. The vines are great, you can drape them over anything and they bring a nice natural look to an artificial environment. They don't require a lot of light, and only need watered once a week. On the first of the month, I usually spike their drink with a bit of fertilizer (Miracle grow) to replace nitrogen and minerals in the soil. The big one is about 40 feet long now.
The palm tree gives a nice tropical feel to the area, esecially during the D.C. winters. It does, however, require direct sunlight, and for it I follow the same watering regimen as the philodendrons.
One plant that I've wanted to try in the lab are Venus fly-traps. They can be very tricky to grow. IIRC, they need low to moderate sunlight, and the choice of soil is critical. Too much fertilizer (nitrogen) and they die. In the wild they like moist peat, and they get their nitrogen from catching flies. I always thought that carnivorous plants would be great for an office setting. Especially if you're like me and often just want to work in peace.
Short answer : No
Long answer: Using the dimensions of the airship (245 x 145 x 87 feet), the altitude (~65,000 ft), and some very basic trig., the airship would be 13 X 7.6 X 4.6 seconds of arc. if you were standing directly underneath it. Since the human eye has a resolution of roughly 2 mintes of arc, and this is far larger than the angular size of the airship, you wouldn't see it.
A few years ago I remember seeing geothermal heating options being advertised in Ohio. (Not a very geologically active state by any means). The system basically worked by burying hundreds of feet of plastic piping deep underground. A small pump would move water from radiators in the home to the underground "absorber." Considereing that the temperature underground remains around 60-65F year-round, this system was designed to supplement current heating options (i.e. if you wanted your house at a temperature >65 F you had to use something else to boost your temp.
Using a similar method, my father and I built a swimming pool heater using ~400 feet of black plastic pipe and low-energy fountain pump. The pipe was exposed to sunlight, heated up, and the pump moved the water from the pool, through the "absorber," and back to the pool. Siphon action further supplemented the pumps work. Granted there were limitations to heat levels, but this set-up greatly reduced the amount of energy we used to keep the pool warm after the peak summer heat had left.
Well, I doubt that it would use stem cells, per se. For example, we may figure out the mechanism of how stem cells prevent telomere shortening. Using this information, we may be able to devise a a treatment to prevent shortening (or reverse it) in regular body tissue. However, it may be possible to simply replace the old and worn out cells with shiny new ones from stem cells.
IAAB (I Am A Biologist) and what you are referring to is the Hayflick Limit. Cultured human cells (And those in our bodies as well) can only divide a limited number of times. (Usually around 60 times). This may be due to transcriptional errors, but often is due to telomere shortening at the ends of chromosomes. Telomeres are pieces of DNA that help to replicate chromosomes, however after each copy they shorten a bit more. Eventually they are no more, and the cells are incapable of dividing. One interesting feature of stem cells is that, in addition to their ability to differentiate into various tissues, they may contain mechanisms to reverse telomere shortening. This is one reason for more research.
Targeted protein degradation has applicaitons beyond anti-cancer therapies. Alzheimer's Disease seems to be caused by the build-up of amyoloid beta protein in neurons, which is due to the failure to degrade this protein. One potential therapy is to use other ubiquitin ligases to target amyoloid beta for degradation as a method to break up protein plaques.
Similarly, antiviral potential exists as well. For example, if we could engineer ubiquitin ligases to target HIV proteases (The target of the protease inhibitor component of anti-HIV "cocktails"), we would have another method to hamper viral replication.
As with all new developments, however, there exist numerous problems that must to be overcome before we see practical and clinical results.
The biggest problem to developing any potential theapies from these groundbreaking discoveries is to figure out how to target particular proteins or classes of proteins. There are numerous E3 ubiquitin ligases in cells that target a varety of proteins for degradation. However, the molecular mechanisms by which this recognition takes place is still rather uncertain. The structure of the molecular interaction must be determined at atomic resolution (A difficult process which commonly uses X-ray crystallography and very, very intensive computing).
I see two methods which would lead to useful therapies:
The first is the simplest and will therefore also most likely be the first viable strategy: harnessing natural ubiquitin ligases to target and downregulate harmful proteins. This means that any therapies will be limited to natural ubiquitination processes. Humankind will find ways to make these reactions better, or ways stimulate them in diseased cells.
The second approach is de novo design. Once the structure of the target is determined, enzymes can be desgined to target it for ubiquitination/degradation. However, this requires an understanding of biochemistry far beyond what currently exists. Not only does the therapeutic enzyme have to recognize the target, but it must also catalyze the ubiquitination reaction. At this time, I do not believe that anyone has designed a functional protein-based enzyme from the ground up. This technique has greater potential, as we could target ANY protein we dislike, but we are not quite able to implement it yet.
West Virginia is 70 mph on Interstates. Pennsylvania is still 65 mph. Don't know about KY, IN, or MI.
I've been following this for awhile. Looks like I get to update my "hit list" of gene targets to investigate. And that's what this will ultimately be...a list of interesting genes to look at for further investigation. No cures right away, it will take time to absorb this data into the collective intelligence of the medical research community and years to turn it into new treatments.
Another example: my local Wal-Mart has had a boxed copy of the now defunct "Tabula Rasa" MMO on clearance for $29 since Christmas 2008. It's still sitting there, collecting dust.
As a biomedical researcher, I'm glad to finally see some of the promises of stem cells. However, this must be tempered by knowing that there exists a fine line between stem cells and cancer cells. Both grow outside of the normal controls that keep excess cell division in check. For stem cells, this is developmentally controlled by the neighboring cells. I wonder how these stem cells will respond when moved to a new environment and what the long term effects will be. I guess that FDA sanctioned or not, we're going to find out.
I've got a Ph.D. in Molecular Biology and am currently a post-doctoral research associate in a molecular/cell biology lab. Although I can't speak for the computer / biology interface, here's some things that I've learned from a wet lab. I also have a student starting in a few weeks, so I'll give you the same advice that I gave him. Here goes: 1. It's called research for a reason - you do the same stuff over and over again until you get it to work. And even then, sometimes it doesn't work. And no one can explain it. 2. Keep a good notebook. You never know when the smallest detail may be the cause of a problem (See #1). Someone who comes later may have to try to reproduce your results. Sometimes this person is you. 3. There are as many PI (principal investigator) types as there are flavors of Jelly Belly candies. Some examples would be the demi-god (You, nor any of your lab mates, have ever seen them except on your first day), the helicopter (They hover over your every move and plan everything for you), the slacker (They have a foosball table in their office, and they schedule weekly tournaments), and the workaholic (They spend 100 hours a week in lab, why don't you?). Once you identify your PI's type, there are various ways to handle them. In general, do what your lab mates do and you'll be fine. 4. Have fun. You're getting payed to screw around with things. And no one expects everything that you do to work the first time. How awesome is that? The only better job is TV weatherman. Hope this helps.
I concur. They took out an element that defined UT--the dodge jump. Just isn't the same without it.
I keep various old expansion cards, motherboards, and processors hanging on the wall in plain sight of my beige box. The threat of disembowelment seems to keep it inline.
For some reason my mind reads that with a Swedish accent...
After hearing how this is a flyby mission and the top speed of this spacecraft, I wondered about the current speed champ, Voyager I. According to some of my back of the envelope calculations based upon New Horizons' estimated top speed after a Jupiter assist and the current position and speed of Voyager I, in 26 years New Horizons will surpass Voyager I as the most distant human made object.
Oh great, now I've got a big greasy thumbprint on my screen.
It's from the book "2010" by Arthur C. Clarke.
An interesting idea. Since these galaxies lie approximately 80% distance across the universe, and space is constantly stretching between us and them, the frequencies of light they emit must be higher than what we are observing. IANAC (I Am Not A Cosmologist), but could they be strongly emitting in the visible or UV regions, and spacetime is stretching them to the infrared?
As a Slasdot geek, I do NOT want to skip the cleavages.
"... an MP-3 player, since such a device would not be seen as an appropriate for a CD."
Thankfully someone cleared that up. I mean, the last time I tried to cram a CD into my mp3 player I ended up with nothing but busted plastic shards cutting up my hands. They really are thinking of the children!
I don't usually reply to my own posts, but if your office doesn't have flies (The fruit fly labs upstairs would keep my lab well stocked), you can use raw hamburger. Or eventually annoying coworkers if the plant gets big enough. :)
my lab workbench has giant windows that get lots of sunlight.
Being a biologist (but not a botanist) I've experimented with various plants. Currently I have 3 pothos (philodendron) vines, and a small palm tree. The vines are great, you can drape them over anything and they bring a nice natural look to an artificial environment. They don't require a lot of light, and only need watered once a week. On the first of the month, I usually spike their drink with a bit of fertilizer (Miracle grow) to replace nitrogen and minerals in the soil. The big one is about 40 feet long now.
The palm tree gives a nice tropical feel to the area, esecially during the D.C. winters. It does, however, require direct sunlight, and for it I follow the same watering regimen as the philodendrons.
One plant that I've wanted to try in the lab are Venus fly-traps. They can be very tricky to grow. IIRC, they need low to moderate sunlight, and the choice of soil is critical. Too much fertilizer (nitrogen) and they die. In the wild they like moist peat, and they get their nitrogen from catching flies. I always thought that carnivorous plants would be great for an office setting. Especially if you're like me and often just want to work in peace.
Short answer : No Long answer: Using the dimensions of the airship (245 x 145 x 87 feet), the altitude (~65,000 ft), and some very basic trig., the airship would be 13 X 7.6 X 4.6 seconds of arc. if you were standing directly underneath it. Since the human eye has a resolution of roughly 2 mintes of arc, and this is far larger than the angular size of the airship, you wouldn't see it.
A few years ago I remember seeing geothermal heating options being advertised in Ohio. (Not a very geologically active state by any means). The system basically worked by burying hundreds of feet of plastic piping deep underground. A small pump would move water from radiators in the home to the underground "absorber." Considereing that the temperature underground remains around 60-65F year-round, this system was designed to supplement current heating options (i.e. if you wanted your house at a temperature >65 F you had to use something else to boost your temp. Using a similar method, my father and I built a swimming pool heater using ~400 feet of black plastic pipe and low-energy fountain pump. The pipe was exposed to sunlight, heated up, and the pump moved the water from the pool, through the "absorber," and back to the pool. Siphon action further supplemented the pumps work. Granted there were limitations to heat levels, but this set-up greatly reduced the amount of energy we used to keep the pool warm after the peak summer heat had left.
That's not the solution to this image. However, it is the solution to the APOD from September 13th which can be seen at: http://antwrp.gsfc.nasa.gov/apod/ap040913.html
Well, I doubt that it would use stem cells, per se. For example, we may figure out the mechanism of how stem cells prevent telomere shortening. Using this information, we may be able to devise a a treatment to prevent shortening (or reverse it) in regular body tissue. However, it may be possible to simply replace the old and worn out cells with shiny new ones from stem cells.
IAAB (I Am A Biologist) and what you are referring to is the Hayflick Limit. Cultured human cells (And those in our bodies as well) can only divide a limited number of times. (Usually around 60 times). This may be due to transcriptional errors, but often is due to telomere shortening at the ends of chromosomes. Telomeres are pieces of DNA that help to replicate chromosomes, however after each copy they shorten a bit more. Eventually they are no more, and the cells are incapable of dividing. One interesting feature of stem cells is that, in addition to their ability to differentiate into various tissues, they may contain mechanisms to reverse telomere shortening. This is one reason for more research.
Well, with the flu vaccine shortage in the US right now, your cover story (and ultimately my own) becomes all the more believable ;)
Targeted protein degradation has applicaitons beyond anti-cancer therapies. Alzheimer's Disease seems to be caused by the build-up of amyoloid beta protein in neurons, which is due to the failure to degrade this protein. One potential therapy is to use other ubiquitin ligases to target amyoloid beta for degradation as a method to break up protein plaques.
Similarly, antiviral potential exists as well. For example, if we could engineer ubiquitin ligases to target HIV proteases (The target of the protease inhibitor component of anti-HIV "cocktails"), we would have another method to hamper viral replication.
As with all new developments, however, there exist numerous problems that must to be overcome before we see practical and clinical results.
The biggest problem to developing any potential theapies from these groundbreaking discoveries is to figure out how to target particular proteins or classes of proteins. There are numerous E3 ubiquitin ligases in cells that target a varety of proteins for degradation. However, the molecular mechanisms by which this recognition takes place is still rather uncertain. The structure of the molecular interaction must be determined at atomic resolution (A difficult process which commonly uses X-ray crystallography and very, very intensive computing).
I see two methods which would lead to useful therapies:
The first is the simplest and will therefore also most likely be the first viable strategy: harnessing natural ubiquitin ligases to target and downregulate harmful proteins. This means that any therapies will be limited to natural ubiquitination processes. Humankind will find ways to make these reactions better, or ways stimulate them in diseased cells.
The second approach is de novo design. Once the structure of the target is determined, enzymes can be desgined to target it for ubiquitination/degradation. However, this requires an understanding of biochemistry far beyond what currently exists. Not only does the therapeutic enzyme have to recognize the target, but it must also catalyze the ubiquitination reaction. At this time, I do not believe that anyone has designed a functional protein-based enzyme from the ground up. This technique has greater potential, as we could target ANY protein we dislike, but we are not quite able to implement it yet.
...is another man's successful honeypot.