A study about monk parakeets shows that the places they stand depend on the bird's carefully calibrated perceptions of the rank of their fellow-feathered friends.
Generally, after a week of interactions, which more frequently against those nearby in rank rather than with lower-ranked birds, newly formed groups of monk parakeets quickly perceive rank.
But how do the birds infer rank? It remains to be discovered.
The study published recently in the PLOS Computational Biology indicates how socially complex animal societies evolve and how dominance hierarchies are established.
"Parakeets appear to be able to connect the dots in their groups, remembering chains of aggression, so if A fights B, then watches how B fights C and how C fights D and how D fights E, then A will use this knowledge to adjust how it interacts with E based on all of the fights in between," according to the study's lead author Elizabeth Hobson, a postdoctoral fellow at the National Institute for Mathematical and Biological Synthesis.
In the study, Hobson and co-author Simon DeDeo of Indiana University and the SantaFe Institute analyzed detailed observations of aggression in two independent groups of captive monk parakeets. Each group was observed over the course of 24 days. A total of 1013 wins in one group and 1360 wins in the second group were analyzed.
The complex data shows that as individuals begin to interact and watch the fights of others, they accumulate knowledge of who wins in fights against whom. Once this knowledge is present, the birds use it refine their own behavior, for instance, they focused their aggression by choosing individuals with whom they might be closely matched. You can see that the aggression becomes more strategically directed.
From above we can learn that it's the bird's careful observation of how the other birds interact, which is an act of cognitive complexity, that determines rank amongst these socially precocious birds.
The study allows people to start to understand the interaction between social and cognitive complexity and to begin to compare what we see in the parakeet groups to other socially complex species like primates. That may be of great significance.
Read more:http://about.cusabio.com/m-190.html
2015年9月10日星期四
2015年9月9日星期三
A protein that plays a central role in maintaining genomic structural stability
We all know that the double-helix shape allows genetic information to be packed into a molecule of human DNA. But how the complex information is packed into the cellular nucleus is still unknown to all. The secret of how this crush of genetic code avoids chaos has been revealed recently. An international team has determined that a protein known as lamin A plays a central role in maintaining genomic structural stability after tracking and analyzing the movement of fluorescently-tagged genomic regions within the nuclei of live cells.
The research group was led by Prof. Yuval Garini of Israel's Bar-Ilan University, and with the participation of members of his lab including Dr. Irena Bronshtein-Berger and Dr. Eldad Kepten, then a PhD candidate. They have shown how this protein is involved in the formation of "cross-links" that limit genetic material's freedom of movement within the nucleus. This creates a stable and linked polymeric structure that promotes chromosomal integrity and makes normal cellular replication possible.
In the study, they explain the biophysical underpinnings of chromosome dynamics and organization and provides biophysical underpinnings of chromosome dynamics and organization.
The mechanism discovered by Garini and his colleagues may have significant implications for the understanding and clinical treatment of disease. What's more, it may pave the way to new approaches toward conditions associated with mutations in the lamin A protein.
Their findings were published on August 24th, 2015 in Nature Communications. If you want to know more about the discovery about the protein-based genome-stabilizing mechanism, you can read more online.
Read more:http://www.cusabio.com/catalog-13-1.html
The research group was led by Prof. Yuval Garini of Israel's Bar-Ilan University, and with the participation of members of his lab including Dr. Irena Bronshtein-Berger and Dr. Eldad Kepten, then a PhD candidate. They have shown how this protein is involved in the formation of "cross-links" that limit genetic material's freedom of movement within the nucleus. This creates a stable and linked polymeric structure that promotes chromosomal integrity and makes normal cellular replication possible.
In the study, they explain the biophysical underpinnings of chromosome dynamics and organization and provides biophysical underpinnings of chromosome dynamics and organization.
The mechanism discovered by Garini and his colleagues may have significant implications for the understanding and clinical treatment of disease. What's more, it may pave the way to new approaches toward conditions associated with mutations in the lamin A protein.
Their findings were published on August 24th, 2015 in Nature Communications. If you want to know more about the discovery about the protein-based genome-stabilizing mechanism, you can read more online.
Read more:http://www.cusabio.com/catalog-13-1.html
2015年9月8日星期二
Avoid relapse of AML
Researchers have made a small molecule that could deliver a one-two punch to proteins that resist chemotherapy in patients with AML. The researchers are from Rice University, Baylor College of Medicine and the University of Texas MD Anderson Cancer Center. It may be the key to helping patients who are fighting acute myeloid leukemia (AML) avoid a relapse.
The work led by Rice chemist Zachary Ball, Baylor pediatrician Michele Redell and MD Anderson oncologist David Tweardy appears this week in the journal Angewandte Chemie.
The protein STAT3, interferes with chemotherapy by halting the death of cancerous cells and allowing them to proliferate. The molecule locates and attacks a previously unknown binding site on STAT3, thus disrupting its disease-promoting effects.
The STAT3 protein stands for "signal transducer and activator of transcription 3". It is a suspected factor in the relapse of nearly 40 percent of children with AML. The new proximity-driven rhodium(II) catalyst known as MM-206 finds and modifies an inhibitor-binding site on the protein's coiled coil -- literally protein coils coiled around each other -- and delivers the inhibitor, naphthalene sulfonamide, to the modified site.
"We know that increased activity of STAT3 in AML and other cancers helps the cancer cells survive chemotherapy, so any new strategy we can develop to stop that process could mean real benefit for our patients," said Redell, who is also part of the leukemia and lymphoma teams at Texas Children's Hospital.
"Our main advance, from a medicinal perspective, is that this compound also works in a mouse model," Ball said. "All the other compounds worked in cells, but in mice, they weren't potent enough or stable enough."
Follow-up studies should lead to improved versions of the complex. The new discovery is of great importance showing the way to future anti-cancer approaches.
Read more:http://about.cusabio.com/m-171.html
The work led by Rice chemist Zachary Ball, Baylor pediatrician Michele Redell and MD Anderson oncologist David Tweardy appears this week in the journal Angewandte Chemie.
The protein STAT3, interferes with chemotherapy by halting the death of cancerous cells and allowing them to proliferate. The molecule locates and attacks a previously unknown binding site on STAT3, thus disrupting its disease-promoting effects.
The STAT3 protein stands for "signal transducer and activator of transcription 3". It is a suspected factor in the relapse of nearly 40 percent of children with AML. The new proximity-driven rhodium(II) catalyst known as MM-206 finds and modifies an inhibitor-binding site on the protein's coiled coil -- literally protein coils coiled around each other -- and delivers the inhibitor, naphthalene sulfonamide, to the modified site.
"We know that increased activity of STAT3 in AML and other cancers helps the cancer cells survive chemotherapy, so any new strategy we can develop to stop that process could mean real benefit for our patients," said Redell, who is also part of the leukemia and lymphoma teams at Texas Children's Hospital.
"Our main advance, from a medicinal perspective, is that this compound also works in a mouse model," Ball said. "All the other compounds worked in cells, but in mice, they weren't potent enough or stable enough."
Follow-up studies should lead to improved versions of the complex. The new discovery is of great importance showing the way to future anti-cancer approaches.
Read more:http://about.cusabio.com/m-171.html
2015年9月7日星期一
It is proteins that do much of the work in a cell
More than a decade ago scientists found the sequencing of the human genome , and it was undoubtedly considered one of the greatest discoveries in biology. However, it was only the beginning of our in-depth understanding of how cells work. Genes are just blueprints and it is the the proteins, genes' products, that do much of the work in a cell.
A multinational team of scientists have sifted through cells of vastly different organisms, from amoebae to worms to mice to humans, to reveal how proteins fit together to build different cells and bodies.
The wonderful finding is a result of a collaboration between seven research groups from three countries, led by Professor Andrew Emili from the University of Toronto's Donnelly Centre and Professor Edward Marcotte from the University of Texas at Austin. The study uncovered tens of thousands of new protein interactions, accounting for about a quarter of all estimated protein contacts in a cell.
If one of these interactions is lost it can lead to disease, and the map can help scientists spot individual proteins that could be at the root of complex human disorders. Through open access databases, the data will be available to researchers across the world.
Proteins work in teams by sticking to each other to carry out their jobs. Many proteins come together to form so called molecular machines that play key roles, such a building new proteins or recycling those no longer needed by literally grinding them into reusable parts. But when it comes to the vast majority of proteins, for example, there are tens of thousands of them in human cells, we still don't know what they do.
Then Emili and Marcotte's map helps. Using a state-of-the-art method developed by the groups, the researchers were able to fish thousands of protein machineries out of cells and count individual proteins they are made of. They then built a network that, similar to social networks, offers clues into protein function based on which other proteins they hang out with. For example, a new and unstudied protein, whose role we don't yet know, is likely to be involved in fixing damage in a cell if it sticks to cell's known "handymen" proteins
The study gathered information on protein machineries from nine species that represent the tree of life: baker's yeast, sea anemones, amoeba, flies, sea urchins, worms, frogs, mice and humans. The map expands the number of known proteins association over ten fold, and it will trace how they evolved as time goes on.
The researchers discovered that tens of thousands of protein associations remained unchanged since the first ancestral cell appeared, one billion years ago (!), preceding all of animal life on Earth.
The researchers believe that, with tens of thousands of other new protein interactions, the map promises to open many more lines of research into links between proteins and disease, which they are keen to explore in depth over the coming years.
The study comes out in Nature on September 7. Protein assemblies in humans were often identical to those in other species, thus the study will provide the ability to study the genetic basis for a wide variety of diseases and how they present in different species. Hope more secrets can be found.
Read more:http://about.cusabio.com/m-187.html
A multinational team of scientists have sifted through cells of vastly different organisms, from amoebae to worms to mice to humans, to reveal how proteins fit together to build different cells and bodies.
The wonderful finding is a result of a collaboration between seven research groups from three countries, led by Professor Andrew Emili from the University of Toronto's Donnelly Centre and Professor Edward Marcotte from the University of Texas at Austin. The study uncovered tens of thousands of new protein interactions, accounting for about a quarter of all estimated protein contacts in a cell.
If one of these interactions is lost it can lead to disease, and the map can help scientists spot individual proteins that could be at the root of complex human disorders. Through open access databases, the data will be available to researchers across the world.
Proteins work in teams by sticking to each other to carry out their jobs. Many proteins come together to form so called molecular machines that play key roles, such a building new proteins or recycling those no longer needed by literally grinding them into reusable parts. But when it comes to the vast majority of proteins, for example, there are tens of thousands of them in human cells, we still don't know what they do.
Then Emili and Marcotte's map helps. Using a state-of-the-art method developed by the groups, the researchers were able to fish thousands of protein machineries out of cells and count individual proteins they are made of. They then built a network that, similar to social networks, offers clues into protein function based on which other proteins they hang out with. For example, a new and unstudied protein, whose role we don't yet know, is likely to be involved in fixing damage in a cell if it sticks to cell's known "handymen" proteins
The study gathered information on protein machineries from nine species that represent the tree of life: baker's yeast, sea anemones, amoeba, flies, sea urchins, worms, frogs, mice and humans. The map expands the number of known proteins association over ten fold, and it will trace how they evolved as time goes on.
The researchers discovered that tens of thousands of protein associations remained unchanged since the first ancestral cell appeared, one billion years ago (!), preceding all of animal life on Earth.
The researchers believe that, with tens of thousands of other new protein interactions, the map promises to open many more lines of research into links between proteins and disease, which they are keen to explore in depth over the coming years.
The study comes out in Nature on September 7. Protein assemblies in humans were often identical to those in other species, thus the study will provide the ability to study the genetic basis for a wide variety of diseases and how they present in different species. Hope more secrets can be found.
Read more:http://about.cusabio.com/m-187.html
2015年9月6日星期日
Cheaper antivenom is coming
Recently, researchers from six institutions including the University of Copenhagen and the National Aquarium of Denmark (Den Blå Planet) have successfully identified the exact composition of sea snake venom, which makes the future development of synthetic antivenoms more realistic.
At present, sea snake anitvenom costs nearly USD 2000, which is obviously too expensive. The new findings referred to above could result in a future production of synthetic antivenoms for as little as USD 10-100.
In many tropical and subtropical countries, Venomous snakebites becomes a major health concern. There are more than 10 million bites each year. In Sub-Saharan Africa alone, an estimated one million snakebites occur annually and about half of them need treatment, many result in amputations and a significant amount result in deaths.
When people in poor countries are bitten, including working fishermen and children playing in the ocean, they are more likely to be left to die because it is extremely expensive to save them, not because they cannot be saved. More lives can be saved if there are more inexpensive antivenoms produced.
Antivenoms are still produced by traditional animal immunization procedures, which has a number of drawbacks, such as allergic reactions, which in the worst instances end in death. Yet technological advances within biopharmaceuticals and medicinal chemistry could pave the way for rational drug design approaches to snake toxins. This could eliminate the use of animals and bring forward more effective therapies for snakebite envenoming.
Hope more people can benefit from the new findings.
Read more:http://www.cusabio.com/catalog-13-1.html
At present, sea snake anitvenom costs nearly USD 2000, which is obviously too expensive. The new findings referred to above could result in a future production of synthetic antivenoms for as little as USD 10-100.
In many tropical and subtropical countries, Venomous snakebites becomes a major health concern. There are more than 10 million bites each year. In Sub-Saharan Africa alone, an estimated one million snakebites occur annually and about half of them need treatment, many result in amputations and a significant amount result in deaths.
When people in poor countries are bitten, including working fishermen and children playing in the ocean, they are more likely to be left to die because it is extremely expensive to save them, not because they cannot be saved. More lives can be saved if there are more inexpensive antivenoms produced.
Antivenoms are still produced by traditional animal immunization procedures, which has a number of drawbacks, such as allergic reactions, which in the worst instances end in death. Yet technological advances within biopharmaceuticals and medicinal chemistry could pave the way for rational drug design approaches to snake toxins. This could eliminate the use of animals and bring forward more effective therapies for snakebite envenoming.
Hope more people can benefit from the new findings.
Read more:http://www.cusabio.com/catalog-13-1.html
2015年9月5日星期六
New proteins have been found to save plants facing with high salt problem
Studies before show that high salt in soil dramatically stresses plant biology and reduces the growth and yield of crops. A study led by professor Staffan Persson, from University of Melbourne, Australia, formerly at the Max Planck Institute of Molecular Plant Physiology, found specific proteins that allow plants to grow better under salt stress, and may help breed future generations of more salt-tolerant crop plants.
Humans can move away from the salty snacks or drink more water, but if a plant is stuck in high salt (or saline) soils, it must use other tactics to cope. More and more of the world' crops are facing salt stress with high salt in soils (also known as salinity) affecting 20% of the total, and 33% of irrigated, agricultural lands worldwide. We need to increase production of food by 70% to feed an additional 2.3 billion people by 2050. Salinity is a major limiting factor for this goal as more than 50% of the arable land may be salt afflicted by the year 2050. Thus finding genes and mechanisms that can improve plant growth under such conditions is of utmost urgency.
"Plants need to make bigger cells and more of them if they want to grow and develop, " said Prof Persson.
"Unlike animal cells, plant cells are surrounded by a cellular exoskeleton, called cell walls which direct plant growth and protect the plant against diseases. Importantly, most of the plants biomass is made up of the cell wall with cellulose being the major component.
"Hence, plant growth largely depend on the ability of plants to produce cell walls and cellulose, also under stress conditions, and it is therefore no surprise that research on cell wall biosynthesis is of high priority."
The present study shows that an previously unknown family of proteins supports the cellulose synthase machinery under salt stress conditions, and was named "Companions of Cellulose synthase (CC). These CC proteins are part of the cellulose synthase complex during cellulose synthesis. The researchers found that the CC gene activity was increased when plants were exposed to high salt concentrations.
"In an additional step, we made fluorescent versions of the CC proteins and observed, with the help of a special microscope, where and how they function. It was quite a surprise to see that they were able to maintain the organization of microtubules under salt stress. This function helped the plants to maintain cellulose synthesis during the stress", said Dr. Anne Endler, co-first author of this study.
The research group proved that the plants lacking the CC activity were unable to maintain their microtubules intact. The loss in microtubule function led to a failure in maintaining cellulose synthesis, which explained the reduction in plant growth on salt.
The results of the study provide a mechanism for how the CC proteins aid plant biomass production under salt stress and help plants to grow on salt. The team has identified a protein family that helps plants to grow on salt, and outlined a mechanism for how these proteins aid the plants to produce their biomass under salt stress conditions. The study was published the day before yesterday in the journal Cell.
Read more:http://www.cusabio.com/catalog-13-1.html
Humans can move away from the salty snacks or drink more water, but if a plant is stuck in high salt (or saline) soils, it must use other tactics to cope. More and more of the world' crops are facing salt stress with high salt in soils (also known as salinity) affecting 20% of the total, and 33% of irrigated, agricultural lands worldwide. We need to increase production of food by 70% to feed an additional 2.3 billion people by 2050. Salinity is a major limiting factor for this goal as more than 50% of the arable land may be salt afflicted by the year 2050. Thus finding genes and mechanisms that can improve plant growth under such conditions is of utmost urgency.
"Plants need to make bigger cells and more of them if they want to grow and develop, " said Prof Persson.
"Unlike animal cells, plant cells are surrounded by a cellular exoskeleton, called cell walls which direct plant growth and protect the plant against diseases. Importantly, most of the plants biomass is made up of the cell wall with cellulose being the major component.
"Hence, plant growth largely depend on the ability of plants to produce cell walls and cellulose, also under stress conditions, and it is therefore no surprise that research on cell wall biosynthesis is of high priority."
The present study shows that an previously unknown family of proteins supports the cellulose synthase machinery under salt stress conditions, and was named "Companions of Cellulose synthase (CC). These CC proteins are part of the cellulose synthase complex during cellulose synthesis. The researchers found that the CC gene activity was increased when plants were exposed to high salt concentrations.
"In an additional step, we made fluorescent versions of the CC proteins and observed, with the help of a special microscope, where and how they function. It was quite a surprise to see that they were able to maintain the organization of microtubules under salt stress. This function helped the plants to maintain cellulose synthesis during the stress", said Dr. Anne Endler, co-first author of this study.
The research group proved that the plants lacking the CC activity were unable to maintain their microtubules intact. The loss in microtubule function led to a failure in maintaining cellulose synthesis, which explained the reduction in plant growth on salt.
The results of the study provide a mechanism for how the CC proteins aid plant biomass production under salt stress and help plants to grow on salt. The team has identified a protein family that helps plants to grow on salt, and outlined a mechanism for how these proteins aid the plants to produce their biomass under salt stress conditions. The study was published the day before yesterday in the journal Cell.
Read more:http://www.cusabio.com/catalog-13-1.html
2015年9月2日星期三
DNA origami contributing to building nanodevices
Recent years scientists have been studying ways to use synthetic DNA as a building block to create smaller and faster devices, and they have made great progress in this field. Each DNA strand is formed of one of four "codes" which can link to only one complementary code each, thus binding two DNA strands together. Scientists are using this inherent coding to manipulate and "fold" DNA to form "origami nanostructures": extremely small two- and three-dimensional shapes that can then be used as construction material to build nanodevices such as nanomotors for use in targeted drug delivery inside the body. But assembling DNA origami units into larger structures remains challenging.
A team of scientists at Kyoto University's Institute for Integrated Cell-Material Sciences (iCeMS) has developed an approach that could bring us one step closer to the nanomachines of the future.
They used a double layer of lipids (fats) containing both a positive and a negative charge. DNA origami structures were weakly absorbed onto the lipid layer through an electrostatic interaction. The weak bond between the origami structures and the lipid layer allowed them to move more freely than in other approaches, facilitating their interaction with one another to assemble and form larger structures.
The scientists anticipate that this approach will further expand the potential applications of DNA origami structures and their assemblies in the fields of nanotechnology, biophysics and synthetic biology.
Read more:http://about.cusabio.com/m-179.html
A team of scientists at Kyoto University's Institute for Integrated Cell-Material Sciences (iCeMS) has developed an approach that could bring us one step closer to the nanomachines of the future.
They used a double layer of lipids (fats) containing both a positive and a negative charge. DNA origami structures were weakly absorbed onto the lipid layer through an electrostatic interaction. The weak bond between the origami structures and the lipid layer allowed them to move more freely than in other approaches, facilitating their interaction with one another to assemble and form larger structures.
The scientists anticipate that this approach will further expand the potential applications of DNA origami structures and their assemblies in the fields of nanotechnology, biophysics and synthetic biology.
Read more:http://about.cusabio.com/m-179.html
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