My name is Ryan, and I am one of the terrible things.

(It's worth noting that I reblog a decent amount of nsfw stuff. I try to keep it relatively tame...mostly.)

19th October 2014

Photo reblogged from アトモス with 1,119 notes

thedemon-hauntedworld:

The space shuttle Discovery climbs toward Earth orbit following a successful liftoff from KSC’s Pad 39A at 8:41:50 a.m. (EDT), Aug. 30, 1984. Inside the spacecraft are six crewmembers looking forward to a busy week in space. The scene was photographed by astronaut John W. Young in the Shuttle Training Aircraft (STA). 
Photo credit: NASA

thedemon-hauntedworld:

The space shuttle Discovery climbs toward Earth orbit following a successful liftoff from KSC’s Pad 39A at 8:41:50 a.m. (EDT), Aug. 30, 1984. Inside the spacecraft are six crewmembers looking forward to a busy week in space. The scene was photographed by astronaut John W. Young in the Shuttle Training Aircraft (STA).
Photo credit: NASA

Source: thedemon-hauntedworld

19th October 2014

Post reblogged from It's a Writer Thing with 63,557 notes

mikulios:

making HONEST ANTAGONISTS who believe they’re in the right and firmly believe in what they’re doing is SO MUCH MORE INTERESTING than making them “crazy” because of some outside influence. make villains who believe they are the protagonists

Source: mikleos

19th October 2014

Photo reblogged from アトモス with 281 notes

Source: 69marius

19th October 2014

Quote reblogged from Kindle Quotes with 6 notes

So not only is it wrong to refer to ‘the’ human genome, but in a sense we don’t even have ‘a’ human genome. We have 6 billion of them. We are all 99.9 per cent the same, but equally, in the words of the biochemist David Cox, ‘you could say all humans share nothing, and that would be correct, too30.’ But we have still to explain why so little of that DNA has any discernible purpose. It starts to get a little unnerving, but it does really seem that the purpose of life is to perpetuate DNA. The 97 per cent of our DNA commonly called junk is largely made up of clumps of letters that, in Matt Ridley’s words, ‘exist for the pure and simple reason that they are good at getting themselves duplicated31’.fn2 Most of your DNA, in other words, is devoted not to you but to itself: you are a machine …

19th October 2014

Photoset reblogged from Billions and Billions with 678 notes

zubat:

Astronauts selfies (1966, 2003, 2008, 2012, 2014)

Source: zubat

19th October 2014

Photo reblogged from ▲ http://goo.gl/4HTd5 ▲ with 201 notes

neurosciencestuff:

New front in war on Alzheimer’s, other protein-folding diseases
A surprise discovery that overturns decades of thinking about how the body fixes proteins that come unraveled greatly expands opportunities for therapies to prevent diseases such as Alzheimer’s and Parkinson’s, which have been linked to the accumulation of improperly folded proteins in the brain.
“This finding provides a whole other outlook on protein-folding diseases; a new way to go after them,” said Andrew Dillin, the Thomas and Stacey Siebel Distinguished Chair of Stem Cell Research in the Department of Molecular and Cell Biology and Howard Hughes Medical Institute investigator at the University of California, Berkeley.
Dillin, UC Berkeley postdoctoral fellows Nathan A. Baird and Peter M. Douglas and their colleagues at the University of Michigan, The Scripps Research Institute and Genentech Inc., will publish their results in the Oct. 17 issue of the journal Science.
Cells put a lot of effort into preventing proteins – which are like a string of beads arranged in a precise three-dimensional shape – from unraveling, since a protein’s activity as an enzyme or structural component depends on being properly shaped and folded. There are at least 350 separate molecular chaperones constantly patrolling the cell to refold misfolded proteins. Heat is one of the major threats to proteins, as can be demonstrated when frying an egg – the clear white albumen turns opaque as the proteins unfold and then tangle like spaghetti.
Heat shock
For 35 years, researchers have worked under the assumption that when cells undergo heat shock, as with a fever, they produce a protein that triggers a cascade of events that field even more chaperones to refold unraveling proteins that could kill the cell. The protein, HSF-1 (heat shock factor-1), does this by binding to promoters upstream of the 350-plus chaperone genes, upping the genes’ activity and launching the army of chaperones, which originally were called “heat shock proteins.”
Injecting animals with HSF-1 has been shown not only to increase their tolerance of heat stress, but to increase lifespan.
Because an accumulation of misfolded proteins has been implicated in aging and in neurodegenerative diseases such as Alzheimer’s, Parkinson’s and Huntington’s diseases, scientists have sought ways to artificially boost HSF-1 in order to reduce the protein plaques and tangles that eventually kill brain cells. To date, such boosters have extended lifespan in lab animals, including mice, but greatly increased the incidence of cancer.
Dillin’s team found in experiments on the nematode worm C. elegans that HSF-1 does a whole lot more than trigger release of chaperones. An equal if not more important function is to stabilize the cell’s cytoskeleton, which is the highway that transports essential supplies – healing chaperones included – around the cell.
“We are suggesting that, rather than making more of HSF-1 to prevent diseases like Huntington’s, we should be looking for ways to make the actin cytoskeleton better,” Dillin said. Such tactics might avoid the carcinogenic side effects of upping HSF-1.
Dillin is codirector of the Paul F. Glenn Center for Aging Research, a new collaboration between UC Berkeley and UC San Francisco supported by the Glenn Foundation for Medical Research. Center investigators will study the many ways that proteins malfunction within cells, ideally paving the way for novel treatments for neurodegenerative diseases.
A cell at war
Dillin compares a cell experiencing heat shock to a country under attack. In a war, an aggressor first cuts off all communications, such as roads, train and bridges, which prevents the doctors from treating the wounded. Similarly, heat shock disrupts the cytoskeletal highway, preventing the chaperone “doctors” from reaching the patients, the misfolded proteins.
“We think HSF-1 not only makes more chaperones, more doctors, but also insures that the roadways stay intact to keep everything functional and make sure the chaperones can get to the sick and wounded warriors,” he said.
The researchers found specifically that HSF-1 up-regulates another gene, pat-10, that produces a protein that stabilizes actin, the building blocks of the cytoskeleton.
By boosting pat-10 activity, they were able to cure worms that had been altered to express the Huntington’s disease gene, and also extend the lifespan of normal worms.
Dillin suspects that HSF-1’s main function is, in fact, to protect the actin cytoskeleton. He and his team mutated HSF-1 so that it no longer boosted chaperones, demonstrating, he said, that “you can survive heat shock with the normal level of heat shock proteins, as long as you make your cytoskeleton work better.”
He noted that the team’s results – that boosting chaperones is not essential to surviving heat stress – were so contradictory to current thinking that “I made my post-docs’ lives hell for three years” insisting on more experiments to rule out errors. Yet, when Dillin presented the results recently to members of the protein-folding community, he said the first reaction of many was, “That makes perfect sense.”

neurosciencestuff:

New front in war on Alzheimer’s, other protein-folding diseases

A surprise discovery that overturns decades of thinking about how the body fixes proteins that come unraveled greatly expands opportunities for therapies to prevent diseases such as Alzheimer’s and Parkinson’s, which have been linked to the accumulation of improperly folded proteins in the brain.

“This finding provides a whole other outlook on protein-folding diseases; a new way to go after them,” said Andrew Dillin, the Thomas and Stacey Siebel Distinguished Chair of Stem Cell Research in the Department of Molecular and Cell Biology and Howard Hughes Medical Institute investigator at the University of California, Berkeley.

Dillin, UC Berkeley postdoctoral fellows Nathan A. Baird and Peter M. Douglas and their colleagues at the University of Michigan, The Scripps Research Institute and Genentech Inc., will publish their results in the Oct. 17 issue of the journal Science.

Cells put a lot of effort into preventing proteins – which are like a string of beads arranged in a precise three-dimensional shape – from unraveling, since a protein’s activity as an enzyme or structural component depends on being properly shaped and folded. There are at least 350 separate molecular chaperones constantly patrolling the cell to refold misfolded proteins. Heat is one of the major threats to proteins, as can be demonstrated when frying an egg – the clear white albumen turns opaque as the proteins unfold and then tangle like spaghetti.

Heat shock

For 35 years, researchers have worked under the assumption that when cells undergo heat shock, as with a fever, they produce a protein that triggers a cascade of events that field even more chaperones to refold unraveling proteins that could kill the cell. The protein, HSF-1 (heat shock factor-1), does this by binding to promoters upstream of the 350-plus chaperone genes, upping the genes’ activity and launching the army of chaperones, which originally were called “heat shock proteins.”

Injecting animals with HSF-1 has been shown not only to increase their tolerance of heat stress, but to increase lifespan.

Because an accumulation of misfolded proteins has been implicated in aging and in neurodegenerative diseases such as Alzheimer’s, Parkinson’s and Huntington’s diseases, scientists have sought ways to artificially boost HSF-1 in order to reduce the protein plaques and tangles that eventually kill brain cells. To date, such boosters have extended lifespan in lab animals, including mice, but greatly increased the incidence of cancer.

Dillin’s team found in experiments on the nematode worm C. elegans that HSF-1 does a whole lot more than trigger release of chaperones. An equal if not more important function is to stabilize the cell’s cytoskeleton, which is the highway that transports essential supplies – healing chaperones included – around the cell.

“We are suggesting that, rather than making more of HSF-1 to prevent diseases like Huntington’s, we should be looking for ways to make the actin cytoskeleton better,” Dillin said. Such tactics might avoid the carcinogenic side effects of upping HSF-1.

Dillin is codirector of the Paul F. Glenn Center for Aging Research, a new collaboration between UC Berkeley and UC San Francisco supported by the Glenn Foundation for Medical Research. Center investigators will study the many ways that proteins malfunction within cells, ideally paving the way for novel treatments for neurodegenerative diseases.

A cell at war

Dillin compares a cell experiencing heat shock to a country under attack. In a war, an aggressor first cuts off all communications, such as roads, train and bridges, which prevents the doctors from treating the wounded. Similarly, heat shock disrupts the cytoskeletal highway, preventing the chaperone “doctors” from reaching the patients, the misfolded proteins.

“We think HSF-1 not only makes more chaperones, more doctors, but also insures that the roadways stay intact to keep everything functional and make sure the chaperones can get to the sick and wounded warriors,” he said.

The researchers found specifically that HSF-1 up-regulates another gene, pat-10, that produces a protein that stabilizes actin, the building blocks of the cytoskeleton.

By boosting pat-10 activity, they were able to cure worms that had been altered to express the Huntington’s disease gene, and also extend the lifespan of normal worms.

Dillin suspects that HSF-1’s main function is, in fact, to protect the actin cytoskeleton. He and his team mutated HSF-1 so that it no longer boosted chaperones, demonstrating, he said, that “you can survive heat shock with the normal level of heat shock proteins, as long as you make your cytoskeleton work better.”

He noted that the team’s results – that boosting chaperones is not essential to surviving heat stress – were so contradictory to current thinking that “I made my post-docs’ lives hell for three years” insisting on more experiments to rule out errors. Yet, when Dillin presented the results recently to members of the protein-folding community, he said the first reaction of many was, “That makes perfect sense.”

Source: neurosciencestuff

19th October 2014

Post reblogged from Sarcasm Self Test Complete. with 159 notes

blowjobreceiver:

*makes literally no progress on homework* ah yes time for a break

Source: blowjobreceiver

19th October 2014

Post reblogged from life with 1,330 notes

asvprock:

*Time to wake up*

*Presses snooze 15 more times*

Source: asvprock

19th October 2014

Photoset reblogged from not shaking the grass with 3,276 notes

likeafieldmouse:

'Bionic Eye' Helps This Man See For The First Time In 30 Years

A video posted Oct. 7 captured the moment when Hester’s eye surgeon, Dr. Paul Hahn, turned on the device’s electronic stimulator for the first time since he implanted the sensor last month.

Watch the full video and learn the science behind this miraculous new procedure.

Source: huffingtonpost

19th October 2014

Photo reblogged from Gravitational Beauty with 71 notes

gravitationalbeauty:

The old pine at the Prow by Chuck Claude

gravitationalbeauty:

The old pine at the Prow by Chuck Claude

19th October 2014

Photoset reblogged from stars, hide your fires with 3,021 notes

makos-lightningrod:

oh damn.

Source: makos-lightningrod

19th October 2014

Photo reblogged from ▲ http://goo.gl/4HTd5 ▲ with 601,183 notes

i-am-superjohnlocked:

allthingshyper:

the-cunning-fire:

This is just so pleasing to watch. 

THE WITCHCRAFT i COULD DO WITH THIS CANDLE

two types of people

i-am-superjohnlocked:

allthingshyper:

the-cunning-fire:

This is just so pleasing to watch. 

THE WITCHCRAFT i COULD DO WITH THIS CANDLE

two types of people

Source: ForGIFs.com

19th October 2014

Post reblogged from ▲ http://goo.gl/4HTd5 ▲ with 183,863 notes

the-unstoppable-juggernaut:

rnusicality:

fun statistics for adults!
“when I was a kid, I had no help with college tuition, I was hardworking and paid it all myself”
-Annual tuition for Yale, 1970: $2,550
-Annual tuition for Yale, 2014: $45,800
-Minimum Wage, 1970: $1.45
-Minimum Wage, 2014: $7.25
-Daily hours at minimum wage needed to pay for tuition in 1970: 4.8
-Daily hours at minimum wage needed to pay for tuition in 2014: 17.3

image

Source: rnusicality

17th October 2014

Post reblogged from Fire Cannot Kill A Dragon with 542,806 notes

rocketpowers:

there are teenagers who have unprotected sex but have a case for their iphone

just let that sink in

Source: sluttyteenwolf

17th October 2014

Photo reblogged from Space Pics with 177 notes

space-pics:

The Wizard Nebulahttp://space-pics.tumblr.com/

space-pics:

The Wizard Nebula
http://space-pics.tumblr.com/