Source: http://feeds.sciencedaily.com/~r/sciencedaily/top_news/~3/cFyV_GmYWjs/130813112301.htm
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Tuesday, August 13, 2013
Decellularized mouse heart beats again after regenerating with human heart precursor cells
[unable to retrieve full-text content]For the first time, a mouse heart beat again after its own cells were stripped and replaced with human heart precursor cells. The findings show the promise that regenerating a functional organ by placing human induced pluripotent stem cells -- which could be personalized for the recipient -- in a three-dimensional scaffold could have for transplantation and understanding heart development.
ActiveNotifications Lets You Bring The Moto X's Best Feature To Other Android Devices
I've been spending a lot of time with the Moto X lately (full review coming shortly), and while the spec sheet isn't to everyone's liking, it packs some smart features that I'd love to wind up on other devices. Motorola's motion-sensitive Active Display notifications are currently sitting at the top of that transplant list, and a developer over on the XDA forums has already cooked up a pretty solid approximation with an app called ActiveNotifications.
Source: http://feedproxy.google.com/~r/Techcrunch/~3/SXLFhs0R4W8/
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New materials for bio-based hydrogen synthesis
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Public release date: 12-Aug-2013[ | E-mail |
Share ] Contact: Dr. Thomas Happe
thomas.happe@rub.de
49-234-322-7026
Ruhr-University Bochum
Synthetic biology enables spontaneous protein activation
Researchers at the Ruhr-Universitt Bochum (RUB) have discovered an efficient process for hydrogen biocatalysis. They developed semi-synthetic hydrogenases, hydrogen-generating enzymes, by adding the protein's biological precursor to a chemically synthesized inactive iron complex. From these two components, the biological catalyst formed spontaneously in a test tube. "Extracting hydrogenases from living cells is highly difficult," says Prof Dr Thomas Happe, head of the work group Photobiotechnology at the RUB. "Therefore, their industrial application has always been a long way off. Now, we have made a decisive step towards the generation of bio-based materials." Together with colleagues from the MPI Mlheim and from Grenoble, the RUB researchers report their findings in the journal "Nature Chemical Biology".
Application of hydrogenases: huge potential, difficult implementation
"Under ideal conditions, one single hydrogenase enzyme can generate 9,000 hydrogen molecules per second," says Thomas Happe. "Nature has created a catalyst that is incredibly active even without any rare noble metals." The researchers from Bochum examine so-called iron-iron [FeFe] hydrogenases whose catalysis is based on an active centre with a complex structure that contains iron, carbon monoxide and cyanide only few living organisms are able to synthesize it. In order to skip the tedious and inefficient process of hydrogenase production, chemists have recreated the enzyme component that is catalytically active. Even though the reproduction was successful, these so-called mimics chemical imitations only generate small volumes of hydrogen (H2). Due to the difficulty of extracting active hydrogenases from living organisms, Thomas Happe's team suggested an optimisation of the method that had been reported by the research team from Bochum and their collaboration partners in "Nature" in June 2013 (German press release: http://aktuell.ruhr-uni-bochum.de/pm2013/pm00194.html.de).
Synthetic component enables the generation of H2 "at the push of a button"
The RUB biologists mixed the inactive hydrogenase precursor and the inactive chemical mimic, which was synthesised by their colleagues from Grenoble, within a test tube. A few minutes later, a strong generation of H2 was observed. The hydrogenase precursor had spontaneously integrated the chemically synthesised iron substance into its protein scaffold. Biophysical analyses at the MPI in Mlheim showed that the enzyme thus generated is indistinguishable from natural hydrogenase. "Until now, it has been assumed that enzymes with a complex structure such as hydrogenases require helper proteins to integrate the metal catalyst unit," explains Happe. "When I proposed the idea for this experiment for the first time, nobody believed that it could work."
Use of established commercial processes possible thanks to new method
"Mimics have made the process of working with hydrogenases much easier," sums up Happe's PhD student Julian Esselborn. "Using the 'biotechnologist's pet' Escherichia coli, we are able to quickly produce several milligram of the hydrogenase's precursor. Subsequently, we add the chemical mimic and thereby create fully activated enzymes within a short period of time." Industrial application is now within reach, because commercial processes for the cultivation of E. coli are already established. "The new method has the potential of becoming a milestone in hydrogenase research," says Happe. It works with the hydrogenases of various organisms. "Moreover, it is suitable for high-throughput analysis of hydrogenase proteins that have been newly discovered or altered on the molecular biological level as well as of various potentially optimised chemical substances," adds Julian Esselborn.
Hydrogen clean energy carrier
Hydrogenases play an important role in the energy balance of many single-cell organisms. Their relevance for humans derives from the fact that they can help to generate a clean energy carrier, because hydrogen combusts to form pure water. Consequently, biologists and chemists have for many years been working towards making these enzymes and their chemical blueprints fit for industrial applications as affordable and eco-friendly material for novel fuel cells and even for the direct generation of hydrogen from solar energy by means of photosynthesis.
###
Funding
Thomas Happe's research is funded by the Volkswagen Foundation under the title "LigH2t".
Bibliographic record
J. Esselborn, C. Lambertz, A. Adamska-Venkatesh, T. Simmons, G. Berggren, J. Noth, J. Siebel, A. Hemschemeier, V. Artero, E. Reijerse, M. Fontecave, W. Lubitz, T. Happe, (2013): Spontaneous activation of [FeFe]-hydrogenases by an inorganic [2Fe] active site mimic, Nature Chemical Biology, DOI: 10.1038/nchembio.1311
Further information
Prof Dr Thomas Happe, Work Group Photobiotechnology, Department Plant Biochemistry, Faculty of Biology and Biotechnology at the Ruhr-Universitt, 44780 Bochum, Germany, phone +49/234/32-27026, e-mail: thomas.happe@rub.de
Editor: Dr Julia Weiler
[ | E-mail | Share ] ?
AAAS and EurekAlert! are not responsible for the accuracy of news releases posted to EurekAlert! by contributing institutions or for the use of any information through the EurekAlert! system.
Public release date: 12-Aug-2013[ | E-mail |
Share ] Contact: Dr. Thomas Happe
thomas.happe@rub.de
49-234-322-7026
Ruhr-University Bochum
Synthetic biology enables spontaneous protein activation
Researchers at the Ruhr-Universitt Bochum (RUB) have discovered an efficient process for hydrogen biocatalysis. They developed semi-synthetic hydrogenases, hydrogen-generating enzymes, by adding the protein's biological precursor to a chemically synthesized inactive iron complex. From these two components, the biological catalyst formed spontaneously in a test tube. "Extracting hydrogenases from living cells is highly difficult," says Prof Dr Thomas Happe, head of the work group Photobiotechnology at the RUB. "Therefore, their industrial application has always been a long way off. Now, we have made a decisive step towards the generation of bio-based materials." Together with colleagues from the MPI Mlheim and from Grenoble, the RUB researchers report their findings in the journal "Nature Chemical Biology".
Application of hydrogenases: huge potential, difficult implementation
"Under ideal conditions, one single hydrogenase enzyme can generate 9,000 hydrogen molecules per second," says Thomas Happe. "Nature has created a catalyst that is incredibly active even without any rare noble metals." The researchers from Bochum examine so-called iron-iron [FeFe] hydrogenases whose catalysis is based on an active centre with a complex structure that contains iron, carbon monoxide and cyanide only few living organisms are able to synthesize it. In order to skip the tedious and inefficient process of hydrogenase production, chemists have recreated the enzyme component that is catalytically active. Even though the reproduction was successful, these so-called mimics chemical imitations only generate small volumes of hydrogen (H2). Due to the difficulty of extracting active hydrogenases from living organisms, Thomas Happe's team suggested an optimisation of the method that had been reported by the research team from Bochum and their collaboration partners in "Nature" in June 2013 (German press release: http://aktuell.ruhr-uni-bochum.de/pm2013/pm00194.html.de).
Synthetic component enables the generation of H2 "at the push of a button"
The RUB biologists mixed the inactive hydrogenase precursor and the inactive chemical mimic, which was synthesised by their colleagues from Grenoble, within a test tube. A few minutes later, a strong generation of H2 was observed. The hydrogenase precursor had spontaneously integrated the chemically synthesised iron substance into its protein scaffold. Biophysical analyses at the MPI in Mlheim showed that the enzyme thus generated is indistinguishable from natural hydrogenase. "Until now, it has been assumed that enzymes with a complex structure such as hydrogenases require helper proteins to integrate the metal catalyst unit," explains Happe. "When I proposed the idea for this experiment for the first time, nobody believed that it could work."
Use of established commercial processes possible thanks to new method
"Mimics have made the process of working with hydrogenases much easier," sums up Happe's PhD student Julian Esselborn. "Using the 'biotechnologist's pet' Escherichia coli, we are able to quickly produce several milligram of the hydrogenase's precursor. Subsequently, we add the chemical mimic and thereby create fully activated enzymes within a short period of time." Industrial application is now within reach, because commercial processes for the cultivation of E. coli are already established. "The new method has the potential of becoming a milestone in hydrogenase research," says Happe. It works with the hydrogenases of various organisms. "Moreover, it is suitable for high-throughput analysis of hydrogenase proteins that have been newly discovered or altered on the molecular biological level as well as of various potentially optimised chemical substances," adds Julian Esselborn.
Hydrogen clean energy carrier
Hydrogenases play an important role in the energy balance of many single-cell organisms. Their relevance for humans derives from the fact that they can help to generate a clean energy carrier, because hydrogen combusts to form pure water. Consequently, biologists and chemists have for many years been working towards making these enzymes and their chemical blueprints fit for industrial applications as affordable and eco-friendly material for novel fuel cells and even for the direct generation of hydrogen from solar energy by means of photosynthesis.
###
Funding
Thomas Happe's research is funded by the Volkswagen Foundation under the title "LigH2t".
Bibliographic record
J. Esselborn, C. Lambertz, A. Adamska-Venkatesh, T. Simmons, G. Berggren, J. Noth, J. Siebel, A. Hemschemeier, V. Artero, E. Reijerse, M. Fontecave, W. Lubitz, T. Happe, (2013): Spontaneous activation of [FeFe]-hydrogenases by an inorganic [2Fe] active site mimic, Nature Chemical Biology, DOI: 10.1038/nchembio.1311
Further information
Prof Dr Thomas Happe, Work Group Photobiotechnology, Department Plant Biochemistry, Faculty of Biology and Biotechnology at the Ruhr-Universitt, 44780 Bochum, Germany, phone +49/234/32-27026, e-mail: thomas.happe@rub.de
Editor: Dr Julia Weiler
[ | E-mail | Share ] ?
AAAS and EurekAlert! are not responsible for the accuracy of news releases posted to EurekAlert! by contributing institutions or for the use of any information through the EurekAlert! system.
Source: http://www.eurekalert.org/pub_releases/2013-08/rb-nmf081213.php
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Monday, August 12, 2013
Why you should teach your dog to use an iPad
At School For The Dogs, my training partner Kate and I have been doing something kind of silly recently: We've been teaching dogs to use iPads.
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Harrison Ford habla sobre sus cameos en Anchorman 2 y Expendables 3 y dice que no le importan ninguna de las dos
| ?ltimas Noticias | |
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Se filtra online el trailer de la nueva pel?cula sobre boxeo de Sylvester Stallone y Robert De Niro: "Grudge Match" Aug 11th, 2013 |
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?Ser? Orlando Bloom Batman en la secuela de "Man of Steel"? Aug 11th, 2013 |
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Revelado el nuevo argumento de "Captain America: The Winter Soldier" Aug 11th, 2013 |
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Trailer de "The Pirate Fairy" de Disney, con Tom Hiddleston y Christina Hendricks Aug 11th, 2013 |
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Foto: A Mark Wahlberg no le importa que le confundas con Matt Damon Aug 10th, 2013 |
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Nueva foto de Dwayne Johnson en "Hercules" Aug 10th, 2013 |
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Harrison Ford habla sobre sus cameos en "Anchorman 2" y "Expendables 3" y dice que no le importan ninguna de las dos Aug 10th, 2013 |
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Ya hay nuevas im?genes y detalles de argumento para las pel?culas de Pixar "The Good Dinosaur," "Inside Out" y "Finding Dory" Aug 10th, 2013 |
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Se le ofreci? a Christian Bale $50 millones para regresar a "Man of Steel 2"? Aug 10th, 2013 |
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Amber Heard utiliza un dildo para hacerle una broma a Liam Hemsworth durante una escena de sexo de "Paranoia" Aug 10th, 2013 |
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Mel Gibson es el villano en "The Expendables 3" Aug 10th, 2013 |
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"Now You See Me" a obtener una secuela Aug 9th, 2013 |
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Video: La actriz de "Sharknado", Tara Reid, cree que los tiburones ballena son el resultado del sexo entre tiburones y ballenas Aug 9th, 2013 |
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Primera imagen de "Labor Day" de Jason Reitman, con Josh Brolin y Kate Winslet Aug 9th, 2013 |
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James Wan desvela un poster teaser de "Fast and Furious 7" Aug 9th, 2013 |
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Primeras im?genes de "Big Hero 6", la primera pel?cula de animaci?n de Marvel Aug 9th, 2013 |
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Pixar desvela nuevo arte conceptual de "The Good Dinosaur" Aug 9th, 2013 |
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Fotos: Los actores de "Back to the Future" envejecen 30 a?os utilizando maquillaje vs envejecer por 30 a?os en realidad Aug 9th, 2013 |
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Trailer de el thriller "The Monuments Men", con George Clooney y Matt Damon Aug 9th, 2013 |
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Dos nuevas pel?culas de "Paranormal Activity" vienen en el 2014 Aug 8th, 2013 |
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T?tulo oficial de "Sharknado 2" revelado Aug 8th, 2013 |
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Trailer para el c?mic de "The Star Wars", basado en gui?n original no utilizado de George Lucas Aug 8th, 2013 |
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Bruce Willis abandon? "Expendables 3" porque no le pagaban $1 mill?n al d?a Aug 8th, 2013 |
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20th Century Fox se disculpa ante la audiencia japonesa por el enga?oso t?tulo "Napoleon Dynamite" Aug 8th, 2013 |
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Tom Hanks lucha contra piratas en el nuevo trailer de "Captain Phillips" Aug 8th, 2013 |
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"The Exorcist" se convertir? en una serie de TV Aug 8th, 2013 |
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Mark Wahlberg dice que "The Lone Ranger" fracas? por falta de creatividad y un abultado presupuesto Aug 8th, 2013 |
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Joaquin Phoenix se enamora de un ordenador en el trailer de "Her" Aug 8th, 2013 |
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Marvel tiene sus pel?culas planeada hasta el 2021 Aug 7th, 2013 |
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Trailer completo para el thriller "The Counselor", con Brad Pitt y Michael Fassbender Aug 7th, 2013 |
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Nuevas fotos de "The Hobbit 2" y el thriller "The Monuments Men" de George Clooney Aug 7th, 2013 |
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Nuevo trailer de "Thor: The Dark World" est? aqu?! Aug 7th, 2013 |
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Comienza el rodaje de "Sharktopus Versus Mermantula", parte hombre, parte pira?a y parte tar?ntula Aug 7th, 2013 |
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Foto: Bryan Singer revela la t?cnica de rodaje para las escenas de Quicksilver en "X-Men: Days of Future Past" Aug 7th, 2013 |
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Trailer de la ?ltima pel?cula de James Gandolfini, "Enough Said" Aug 7th, 2013 |
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WWE anuncia la secuela de la pel?cula de terror "See No Evil" Aug 7th, 2013 |
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Sylvester Stallone emocionado de que Bruce Willis no regresar? para "The Expendables 3," Harrison Ford se une al elenco Aug 7th, 2013 |
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Nuevo trailer de "Ender's Game", con Harrison Ford y Ben Kingsley Aug 7th, 2013 |
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Trailer de "Muppets: Most Wanted" llega en l?nea Aug 6th, 2013 |
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Trailer completo del biopic de la princesa Diana "Diana" con Naomi Watts Aug 6th, 2013 |
| August 10th, 2013 - Pilar Ayala |
 Durante la promoci?n de "Paranoia", Harrison Ford apareci? en "Jimmy Kimmel Live", donde se le pregunt? sobre dos de sus nuevas pel?culas: "Anchorman 2" y "The Expendables 3".En cuanto a "Anchorman 2", el actor dijo que rod? su parte en Atlanta en un solo d?a y que lo hizo casi gratis, a pesar de que "no he visto nunca la primera 'Anchorman'". Y a?adi?: "Llegu? all? y no ten?a ni idea de qui?n eran esos tipos. A?n no s? qui?nes son ni qu? creen que est?n haciendo - porque es claramente invendible. He hecho esto mucho tiempo, s? lo que funciona y lo que no". Cuando se habl? de "The Expendables 3", Kimmel le pregunt? a Ford si hab?a visto las dos primeras entregas. "?Por qu? iba a hacerlo?", contest? el actor. Y cuando Kimmel se ofreci? a explicar lo que pasa en las dos pel?culas, Ford rehus? diciendo: "La verdad es que no me importa". Ford es famoso por su extra?o sentido del humor, que es seguramente de lo que va esto. Pero tambi?n es posible que de verdad no le importen ni "Anchorman" ni "The Expendables" y que haya hecho el trabajo como un favor a los cinemat?grafos. |
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