May 27, 2014

Is this a tragedy or a comedy? Either way it’s a masterpiece.

(Source: harveyspector, via aestheticfeast)

May 27, 2014

globalvoices:

“Quand le village se réveille …” (When the Village Awakes) is a project to collect and share the culture and traditions of Mali through new information and communication technologies, sharing texts, videos, audio, and testimonies drawn from elders – the guardians of tradition, culture, and collective memory of African society.

When the Village Awakes: A New Malian Culture Blog

May 17, 2014

oldfilmsflicker:

Female Filmmaker Friday: Bright Star, 2009 (dir. Jane Campion)

May 17, 2014

bbsrc:

BBSRC go to Space 

Technology developed from BBSRC-funded research will be used in experiments on board the International Space Station, in orbit 150 miles above the Earth.

Alvetex® Scaffold technology, produced by Durham University spin-out company Reinnervate, allows cells to be grown in three dimensions (3D). This 3D scaffold structure allows for a more life-like model of how cell populations grow in real tissues, overcoming problems with two-dimensional (2D) culture, where cells flatten and alter their structure and function according to their 2D surroundings.

Now a team from Massachusetts General Hospital investigating bone loss during bed rest, in microgravity or through diseases such as osteoporosis, has received funding from the USA’s National Institutes of Health and NASA to perform an experiment with bone cells using Alvetex® Scaffold on the space station in 2014.

Find out more: http://youtu.be/ahOGjyRJ-JM

All space images are stills from footage from NASA

Images of Alvetex product copyright Reinnervate

(via spaceexp)

May 17, 2014
spaceexp:

Enceladus, the sixth-largest moon of Saturn

spaceexp:

Enceladus, the sixth-largest moon of Saturn

May 17, 2014
A List of the Women-Directed and Women-Centric Films Looking for Deals in Cannes|Women and Hollywood

(Source: oldfilmsflicker)

May 17, 2014

softpyramid:

Douglas Coupland
100 Slogans for the 21st Century
2011-13
ink-jet print on watercolor paper mounted on aluminum
each 22x17”

May 17, 2014
scienceisbeauty:

Today the Google’s Doodle goes to italian mathematician Maria Gaetana Agnesi, a profession really extravagant for a woman of the early eighteenth century… maybe that’s why she ended evolving towards Philosophy and Theology.

scienceisbeauty:

Today the Google’s Doodle goes to italian mathematician Maria Gaetana Agnesi, a profession really extravagant for a woman of the early eighteenth century… maybe that’s why she ended evolving towards Philosophy and Theology.

(via visualizingmath)

May 17, 2014
neurosciencestuff:

New headway in battle against neurodegenerative diseases
Conditions which may accelerate the spread of Parkinson’s disease, and a potential means of enhancing naturally-occurring defences against neurodegenerative disorders, have been identified in two new studies.
Two significant breakthroughs which could inform future treatments for neurodegenerative diseases such as Alzheimer’s and Parkinson’s, have been announced by scientists.
The research, published in two separate studies this week, advances understanding of the early development of such disorders and how they might be prevented – in particular by identifying the biological areas and processes that could be pinpointed by future drugs.
Both sets of results have emerged from collaborations between the research groups led by Chris Dobson, Tuomas Knowles and Michele Vendruscolo at the University of Cambridge, who focus on understanding protein “misfolding” diseases. These include Alzheimer’s and Parkinson’s diseases, as well as numerous others.
The first study provides evidence that the early spread of the protein aggregates associated with Parkinson’s appears to happen at an accelerated rate in mildly acidic conditions. This suggests that particular compartments within brain cells, which are slightly more acidic than others, may turn out to be appropriate targets for future treatments fighting the disease.
Meanwhile, researchers behind the second study appear to have identified a way in which the effectiveness of so-called molecular “chaperones”, responsible for limiting the damage caused by misfolded proteins, can be significantly enhanced.
The papers appear in the latest issue of Proceedings of the National Academy of Sciences of the USA.
As the term suggests, protein misfolding diseases stem from the fact that proteins, which need to fold into a particular shape to carry out their assigned function in the body, can sometimes misfold. In certain cases these misfolded proteins then clump together into fibre-like threads, called amyloid fibrils, potentially becoming toxic to other cells.
How this formation begins at a molecular level is still not completely understood, but comprehending the process will be fundamental to the development of future therapies and is the subject of extensive current research.
The first of the new studies builds on research published in 2013, which showed that in Alzheimer’s sufferers, the initial “nucleation” between proteins, which leads to amyloid formation, is followed by an amplification process called secondary nucleation. In these secondary events, the existing amyloid structures facilitate the formation of new aggregates, leading to their exponential increase. This process is likely to be at the heart of the development and spread of the disease in affected brains.
Using the same techniques, the researchers behind the latest study identified a similar process that is relevant in the early stage development of Parkinson’s Disease. Their work focused on a protein called α-synuclein, which is associated with the disorder, and simulated different conditions in which this protein might misfold and form clumps.
As with the previous study on Alzheimer’s, the research identified that Parkinson’s could spread through a series of secondary nucleation events. In addition, however, it showed that in the case of α-synuclein, this happens at a highly accelerated rate only in solutions which are mildly acidic, with a pH below 5.8. The finding is important because certain sub-compartments within cells are more acidic than others, meaning that these may be particularly productive areas for future treatments to target.
Dr Tuomas Knowles, from the Department of Chemistry and a Fellow of St John’s College, Cambridge, said: “This tells us much more about the molecular mechanisms underlying protein aggregation in Parkinson’s and suggests that mildly acidic microenvironments within cells may enhance that process by several orders of magnitude. Not every sub-cellular compartment offers these conditions, so it takes us much closer to understanding how the disease might spread.”
The second study meanwhile suggests a potential route to improving the effectiveness of a particular molecular “chaperone” – a loose classification for proteins which assist in the folding of others, thereby preventing them from causing damage when they misfold.
The researchers focused on a chaperone called α2-macroglobulin (α2M), which is found outside cells themselves. This is important because neurodegenerative diseases often stem from a process which begins with extracellular misfolding. The α2M was tested on a substrate of the amyloid-beta peptide associated with Alzheimer’s Disease.
Typically, the potency of α2M is limited. The new study, however, found that when it comes into contact with the oxidant hypochlorite – the same chemical found in household bleach, which also naturally occurs in our immune systems – its structure is modified in a manner that makes it into a much more dynamic defence.
In their report, the researchers suggest that this increased effectiveness stems from the fact that α2M, which is usually found in a four-part, “tetrameric” form, breaks down into “dimeric”, two-part forms when it comes into contact with hypochlorite.
The chaperone usually plays its role by preventing a misfolded protein from interacting with the membranes that surround and protect cells. Once in its dimeric form, however, receptor binding sites within the α2M are exposed, leading to specific interactions with receptors on the cell itself. If the α2M has already interacted with misfolded proteins, this connection triggers the cell to break the potentially harmful protein down.
“It’s almost like a warning flag for the cell, telling it that something is wrong,” Dr Janet Kumita, from the Department of Chemistry, explained. “It triggers the cell to react in a way that subjects the cargo of misfolded protein to a degradation pathway.”
“Increasing its potency in this way is an exciting prospect. If we could find a way of developing a drug that introduces the same structural alterations, we would have a therapeutic intervention capable of increasing this protective activity in patients with Alzheimer’s Disease.”
Professor Christopher Dobson, from the University’s Department of Chemistry and Master of St John’s College, said: “These studies add very substantially to our detailed understanding of the molecular origins of neurodegenerative diseases, which are now becoming one of the greatest threats to healthcare in the modern world.”
“We are beginning to understand exactly how a single, aberrant event can lead to the proliferation and spreading of toxic species throughout the brain, and the manner in which our sophisticated defence mechanisms do their best to suppress such phenomena. It will undoubtedly provide vital clues to the development in due course of new and effective drugs to combat these debilitating and increasingly common disorders.”

neurosciencestuff:

New headway in battle against neurodegenerative diseases

Conditions which may accelerate the spread of Parkinson’s disease, and a potential means of enhancing naturally-occurring defences against neurodegenerative disorders, have been identified in two new studies.

Two significant breakthroughs which could inform future treatments for neurodegenerative diseases such as Alzheimer’s and Parkinson’s, have been announced by scientists.

The research, published in two separate studies this week, advances understanding of the early development of such disorders and how they might be prevented – in particular by identifying the biological areas and processes that could be pinpointed by future drugs.

Both sets of results have emerged from collaborations between the research groups led by Chris Dobson, Tuomas Knowles and Michele Vendruscolo at the University of Cambridge, who focus on understanding protein “misfolding” diseases. These include Alzheimer’s and Parkinson’s diseases, as well as numerous others.

The first study provides evidence that the early spread of the protein aggregates associated with Parkinson’s appears to happen at an accelerated rate in mildly acidic conditions. This suggests that particular compartments within brain cells, which are slightly more acidic than others, may turn out to be appropriate targets for future treatments fighting the disease.

Meanwhile, researchers behind the second study appear to have identified a way in which the effectiveness of so-called molecular “chaperones”, responsible for limiting the damage caused by misfolded proteins, can be significantly enhanced.

The papers appear in the latest issue of Proceedings of the National Academy of Sciences of the USA.

As the term suggests, protein misfolding diseases stem from the fact that proteins, which need to fold into a particular shape to carry out their assigned function in the body, can sometimes misfold. In certain cases these misfolded proteins then clump together into fibre-like threads, called amyloid fibrils, potentially becoming toxic to other cells.

How this formation begins at a molecular level is still not completely understood, but comprehending the process will be fundamental to the development of future therapies and is the subject of extensive current research.

The first of the new studies builds on research published in 2013, which showed that in Alzheimer’s sufferers, the initial “nucleation” between proteins, which leads to amyloid formation, is followed by an amplification process called secondary nucleation. In these secondary events, the existing amyloid structures facilitate the formation of new aggregates, leading to their exponential increase. This process is likely to be at the heart of the development and spread of the disease in affected brains.

Using the same techniques, the researchers behind the latest study identified a similar process that is relevant in the early stage development of Parkinson’s Disease. Their work focused on a protein called α-synuclein, which is associated with the disorder, and simulated different conditions in which this protein might misfold and form clumps.

As with the previous study on Alzheimer’s, the research identified that Parkinson’s could spread through a series of secondary nucleation events. In addition, however, it showed that in the case of α-synuclein, this happens at a highly accelerated rate only in solutions which are mildly acidic, with a pH below 5.8. The finding is important because certain sub-compartments within cells are more acidic than others, meaning that these may be particularly productive areas for future treatments to target.

Dr Tuomas Knowles, from the Department of Chemistry and a Fellow of St John’s College, Cambridge, said: “This tells us much more about the molecular mechanisms underlying protein aggregation in Parkinson’s and suggests that mildly acidic microenvironments within cells may enhance that process by several orders of magnitude. Not every sub-cellular compartment offers these conditions, so it takes us much closer to understanding how the disease might spread.”

The second study meanwhile suggests a potential route to improving the effectiveness of a particular molecular “chaperone” – a loose classification for proteins which assist in the folding of others, thereby preventing them from causing damage when they misfold.

The researchers focused on a chaperone called α2-macroglobulin (α2M), which is found outside cells themselves. This is important because neurodegenerative diseases often stem from a process which begins with extracellular misfolding. The α2M was tested on a substrate of the amyloid-beta peptide associated with Alzheimer’s Disease.

Typically, the potency of α2M is limited. The new study, however, found that when it comes into contact with the oxidant hypochlorite – the same chemical found in household bleach, which also naturally occurs in our immune systems – its structure is modified in a manner that makes it into a much more dynamic defence.

In their report, the researchers suggest that this increased effectiveness stems from the fact that α2M, which is usually found in a four-part, “tetrameric” form, breaks down into “dimeric”, two-part forms when it comes into contact with hypochlorite.

The chaperone usually plays its role by preventing a misfolded protein from interacting with the membranes that surround and protect cells. Once in its dimeric form, however, receptor binding sites within the α2M are exposed, leading to specific interactions with receptors on the cell itself. If the α2M has already interacted with misfolded proteins, this connection triggers the cell to break the potentially harmful protein down.

“It’s almost like a warning flag for the cell, telling it that something is wrong,” Dr Janet Kumita, from the Department of Chemistry, explained. “It triggers the cell to react in a way that subjects the cargo of misfolded protein to a degradation pathway.”

“Increasing its potency in this way is an exciting prospect. If we could find a way of developing a drug that introduces the same structural alterations, we would have a therapeutic intervention capable of increasing this protective activity in patients with Alzheimer’s Disease.”

Professor Christopher Dobson, from the University’s Department of Chemistry and Master of St John’s College, said: “These studies add very substantially to our detailed understanding of the molecular origins of neurodegenerative diseases, which are now becoming one of the greatest threats to healthcare in the modern world.”

“We are beginning to understand exactly how a single, aberrant event can lead to the proliferation and spreading of toxic species throughout the brain, and the manner in which our sophisticated defence mechanisms do their best to suppress such phenomena. It will undoubtedly provide vital clues to the development in due course of new and effective drugs to combat these debilitating and increasingly common disorders.”

May 17, 2014
empyrean-princess:

This is literally so fucking important

empyrean-princess:

This is literally so fucking important

(Source: xoxstarlight, via shintophie)

May 17, 2014
wherethenightingalesings:

Katharina Mischer & Thomas Traxler, Vienna

wherethenightingalesings:

Katharina Mischer & Thomas Traxler, Vienna

(via literatureismyutopia)

May 17, 2014
neurosciencestuff:

Herpes-loaded stem cells used to kill brain tumors 
Harvard Stem Cell Institute (HSCI) scientists at Massachusetts General Hospital have a potential solution for how to more effectively kill tumor cells using cancer-killing viruses. The investigators report that trapping virus-loaded stem cells in a gel and applying them to tumors significantly improved survival in mice with glioblastoma multiforme, the most common brain tumor in human adults and also the most difficult to treat.
The work, led by Khalid Shah, MS, PhD, an HSCI Principal Faculty member, is published in the Journal of the National Cancer Institute. Shah heads the Molecular Neurotherapy and Imaging Laboratory at Massachusetts General Hospital.
Cancer-killing or oncolytic viruses have been used in numerous phase 1 and 2 clinical trials for brain tumors but with limited success. In preclinical studies, oncolytic herpes simplex viruses seemed especially promising, as they naturally infect dividing brain cells. However, the therapy hasn’t translated as well for human patients. The problem previous researchers couldn’t overcome was how to keep the herpes viruses at the tumor site long enough to work.
Shah and his team turned to mesenchymal stem cells (MSCs)—a type of stem cell that gives rise to bone marrow tissue—which have been very attractive drug delivery vehicles because they trigger a minimal immune response and can be utilized to carry oncolytic viruses. Shah and his team loaded the herpes virus into human MSCs and injected the cells into glioblastoma tumors developed in mice. Using multiple imaging markers, it was possible to watch the virus as it passed from the stem cells to the first layer of brain tumor cells and subsequently into all of the tumor cells.
“So, how do you translate this into the clinic?” asked Shah, who also is an Associate Professor at Harvard Medical School.
“We know that 70-75 percent of glioblastoma patients undergo surgery for tumor debulking, and we have previously shown that MSCs encapsulated in biocompatible gels can be used as therapeutic agents in a mouse model that mimics this debulking,” he continued. “So, we loaded MSCs with oncolytic herpes virus and encapsulated these cells in biocompatible gels and applied the gels directly onto the adjacent tissue after debulking. We then compared the efficacy of virus-loaded, encapsulated MSCs versus direct injection of the virus into the cavity of the debulked tumors.”
Using imaging proteins to watch in real time how the virus combated the cancer, Shah’s team noticed that the gel kept the stem cells alive longer, which allowed the virus to replicate and kill any residual cancer cells that were not cut out during the debulking surgery. This translated into a higher survival rate for mice that received the gel-encapsulated stem cells.
“They survived because the virus doesn’t get washed out by the cerebrospinal fluid that fills the cavity,” Shah said. “Previous studies that have injected the virus directly into the resection cavity did not follow the fate of the virus in the cavity. However, our imaging and side-by-side comparison studies showed that the naked virus rarely infects the residual tumor cells. This could give us insight into why the results from clinical trials with oncolytic viruses alone were modest.”
The study also addressed another weakness of cancer-killing viruses, which is that not all brain tumors are susceptible to the therapy. The researchers’ solution was to engineer oncolytic herpes viruses to express an additional tumor-killing agent, called TRAIL. Again, using mouse models of glioblastoma—this time created from brain tumor cells that were resistant to the herpes virus—the therapy led to increased animal survival.
“Our approach can overcome problems associated with current clinical procedures,” Shah said. “The work will have direct implications for designing clinical trials using oncolytic viruses, not only for brain tumors, but for other solid tumors.”
Further preclinical work will be needed to use the herpes-loaded stem cells for breast, lung and skin cancer tumors that metastasize to the brain. Shah predicts the approach will enter clinical trials within the next two to three years.

neurosciencestuff:

Herpes-loaded stem cells used to kill brain tumors

Harvard Stem Cell Institute (HSCI) scientists at Massachusetts General Hospital have a potential solution for how to more effectively kill tumor cells using cancer-killing viruses. The investigators report that trapping virus-loaded stem cells in a gel and applying them to tumors significantly improved survival in mice with glioblastoma multiforme, the most common brain tumor in human adults and also the most difficult to treat.

The work, led by Khalid Shah, MS, PhD, an HSCI Principal Faculty member, is published in the Journal of the National Cancer Institute. Shah heads the Molecular Neurotherapy and Imaging Laboratory at Massachusetts General Hospital.

Cancer-killing or oncolytic viruses have been used in numerous phase 1 and 2 clinical trials for brain tumors but with limited success. In preclinical studies, oncolytic herpes simplex viruses seemed especially promising, as they naturally infect dividing brain cells. However, the therapy hasn’t translated as well for human patients. The problem previous researchers couldn’t overcome was how to keep the herpes viruses at the tumor site long enough to work.

Shah and his team turned to mesenchymal stem cells (MSCs)—a type of stem cell that gives rise to bone marrow tissue—which have been very attractive drug delivery vehicles because they trigger a minimal immune response and can be utilized to carry oncolytic viruses. Shah and his team loaded the herpes virus into human MSCs and injected the cells into glioblastoma tumors developed in mice. Using multiple imaging markers, it was possible to watch the virus as it passed from the stem cells to the first layer of brain tumor cells and subsequently into all of the tumor cells.

“So, how do you translate this into the clinic?” asked Shah, who also is an Associate Professor at Harvard Medical School.

“We know that 70-75 percent of glioblastoma patients undergo surgery for tumor debulking, and we have previously shown that MSCs encapsulated in biocompatible gels can be used as therapeutic agents in a mouse model that mimics this debulking,” he continued. “So, we loaded MSCs with oncolytic herpes virus and encapsulated these cells in biocompatible gels and applied the gels directly onto the adjacent tissue after debulking. We then compared the efficacy of virus-loaded, encapsulated MSCs versus direct injection of the virus into the cavity of the debulked tumors.”

Using imaging proteins to watch in real time how the virus combated the cancer, Shah’s team noticed that the gel kept the stem cells alive longer, which allowed the virus to replicate and kill any residual cancer cells that were not cut out during the debulking surgery. This translated into a higher survival rate for mice that received the gel-encapsulated stem cells.

“They survived because the virus doesn’t get washed out by the cerebrospinal fluid that fills the cavity,” Shah said. “Previous studies that have injected the virus directly into the resection cavity did not follow the fate of the virus in the cavity. However, our imaging and side-by-side comparison studies showed that the naked virus rarely infects the residual tumor cells. This could give us insight into why the results from clinical trials with oncolytic viruses alone were modest.”

The study also addressed another weakness of cancer-killing viruses, which is that not all brain tumors are susceptible to the therapy. The researchers’ solution was to engineer oncolytic herpes viruses to express an additional tumor-killing agent, called TRAIL. Again, using mouse models of glioblastoma—this time created from brain tumor cells that were resistant to the herpes virus—the therapy led to increased animal survival.

“Our approach can overcome problems associated with current clinical procedures,” Shah said. “The work will have direct implications for designing clinical trials using oncolytic viruses, not only for brain tumors, but for other solid tumors.”

Further preclinical work will be needed to use the herpes-loaded stem cells for breast, lung and skin cancer tumors that metastasize to the brain. Shah predicts the approach will enter clinical trials within the next two to three years.

May 17, 2014
bpod-mrc:

17 May 2014
Good Vibrations
Listening to a piano, guitar or a clarinet it’s not instantly clear what they have in common. Yet all musical instruments produce vibrations, the nature of which gives them each a unique sound. Our body’s building blocks – carbohydrates, fats and proteins, for example – are no different, giving off tiny vibrations that are as individual as a trumpet fanfare. Identifying them is just a case of knowing how to listen. Scientists have done just this, developing a scanner that can recognise these minute vibrational calling cards. These cancer cells’ components are coloured in relation to their ‘sound’ – right down to the tiny fat droplets (dots coloured pink) floating inside. This improves on common imaging techniques, which rely on labelling targets with chemicals, which can be toxic and also disrupt natural processes. The chance to study the body without these invasive techniques will be music to researchers’ ears.
Written by Jan Piotrowski
—
Image by Klaus GerwertRuhr-University Bochum, GermanyCopyright Elsevier 2014Research published in Biophysical Journal, May 2014
—
You can also follow BPoD on Twitter and Facebook

bpod-mrc:

17 May 2014

Good Vibrations

Listening to a piano, guitar or a clarinet it’s not instantly clear what they have in common. Yet all musical instruments produce vibrations, the nature of which gives them each a unique sound. Our body’s building blocks – carbohydrates, fats and proteins, for example – are no different, giving off tiny vibrations that are as individual as a trumpet fanfare. Identifying them is just a case of knowing how to listen. Scientists have done just this, developing a scanner that can recognise these minute vibrational calling cards. These cancer cells’ components are coloured in relation to their ‘sound’ – right down to the tiny fat droplets (dots coloured pink) floating inside. This improves on common imaging techniques, which rely on labelling targets with chemicals, which can be toxic and also disrupt natural processes. The chance to study the body without these invasive techniques will be music to researchers’ ears.

Written by Jan Piotrowski

Image by Klaus Gerwert
Ruhr-University Bochum, Germany
Copyright Elsevier 2014
Research published in Biophysical Journal, May 2014

You can also follow BPoD on Twitter and Facebook

May 10, 2014
lesbeehive:

Les Beehive – Ellen Page by Nino Munez for FLARE June 2014
When I remark that she seemed nervous that night, Page smiles her trademark half-smile and acquiesces with a laugh, a sigh and some rat-a-tat repetition. “I was very nervous. I was very nervous, yes. Yes. Very, very nervous. Yes. I was emotional, deeply, deeply emotional.” Though she told her parents she liked-liked girls when she was 19, she was still coming out to herself eight years on. “You think you’re in a place where you’re all I’m thrilled to be gay, I have no issues about being gay anymore, I don’t feel shame about being gay, but you actually do. You’re just not fully aware of it. I think I still felt scared about people knowing. I felt awkward around gay people; I felt guilty for not being myself.”

lesbeehive:

Les Beehive – Ellen Page by Nino Munez for FLARE June 2014

When I remark that she seemed nervous that night, Page smiles her trademark half-smile and acquiesces with a laugh, a sigh and some rat-a-tat repetition. “I was very nervous. I was very nervous, yes. Yes. Very, very nervous. Yes. I was emotional, deeply, deeply emotional.” Though she told her parents she liked-liked girls when she was 19, she was still coming out to herself eight years on. “You think you’re in a place where you’re all I’m thrilled to be gay, I have no issues about being gay anymore, I don’t feel shame about being gay, but you actually do. You’re just not fully aware of it. I think I still felt scared about people knowing. I felt awkward around gay people; I felt guilty for not being myself.”

(via suicideblonde)

May 9, 2014
"…A white graduate of a public Michigan university who wishes to pass his historical privilege on to his children may freely lobby the board of that university in favor of an expanded legacy admissions policy, whereas a black Michigander who was denied the opportunity to attend that very university cannot lobby the board in favor of a policy that might give his children a chance that he never had and that they might never have absent that policy."

Supreme Court Justice, Sonia Sotomayor, in her dissent following the Supreme Court decision to uphold the Michigan Ban on Affirmative Action in public universities (via sociolab)

(Source: justjachele, via humanrightswatch)

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