Thousands of scientists and health professionals from the field of medical physics will meet at the 52nd meeting of the American Association of Physicists in Medicine (AAPM) from July 18 - 22, 2010 in Philadelphia, Pennsylvania. They will present the latest technological advances in medical imaging and radiation therapy and discuss the safety and regulatory issues facing the field today.
AAPM is the premier organization in medical physics, a broadly-based scientific and professional discipline encompassing physics principles and applications in medicine and biology. Its membership includes medical physicists who specialize in research that develops cutting-edge technologies and board-certified clinical medical physicists who apply these technologies in community hospitals, clinics, and academic medical centers.
The presentations at the AAPM meeting will cover topics ranging from new ways of imaging the human body to the latest clinical developments on treating cancer with high energy X-rays and electrons from accelerators, brachytherapy with radioactive sources, and protons. Many of the talks and posters are focused on patient safety -- tailoring therapy to the specific needs of people undergoing treatment, such as shaping emissions to conform to tumors, or finding ways to image children safely at lower radiation exposures while maintaining good image quality.
Source:
Jason Bardi
American Institute of Physics
суббота, 28 мая 2011 г.
Microscale Environments Could Be Probed By Super Small Nanoelectrodes
Investigating the composition and behavior of microscale environments, including those within living cells, could become easier and more precise with nanoelectrodes being developed at the University of Illinois.
"The individual nanotube-based probes can be used for electrochemical and biochemical sensing," said Min-Feng Yu, a U. of I. professor of mechanical science and engineering, and a researcher at the university's Beckman Institute. "The position of the nanoelectrodes can be controlled very accurately."
To fabricate the nanoelectrodes, Yu and graduate students Kyungsuk Yum, Jie Hu and Han Na Cho begin by attaching a strong, rigid, boron-nitride nanotube to a much larger, conductive probe. The nanotube will form the insulating core of the nanoelectrode.
The researchers then coat the nanotube with a thin film of gold about 10-50 nanometers thick (a nanometer is 1 billionth of a meter.) The gold layer is then coated with an insulating polymer coating about 10 nanometers thick. Lastly, the researchers use a focused ion beam to slice off the end of the nanotube, exposing a conducting ring of gold sandwiched between an insulating core and an insulating outer ring.
The process yields nanoelectrodes with a diameter of 100 nanometers, and a length of up to 30 microns.
Because the nanotube is attached to a much larger probe, the researchers can manipulate the nanotube like a needle. They can control precisely where the nanotube penetrates a cell, for example, and even pinpoint smaller cell structures, such as the nucleus or mitochondrion.
"Nanoelectrodes offer new opportunities for electrochemical sensing in intracellular environments," said Yu, who will describe the fabrication process and demonstrate the feasibility of nanoelectrodes at the March meeting of the American Physical Society, to be held in Denver, March 5-9. "By functionalizing the active area of the nanoelectrode with an appropriate chemical, we can target the detection of specific chemical species."
The researchers have demonstrated that their nanoelectrode can sense the chemical environment within a droplet 10 microns in diameter. Their next step is to show that the probe can penetrate the cellular membrane of a living cell, without damaging the cell.
The National Science Foundation and the University of Illinois funded the work.
Contact: James E. Kloeppel
University of Illinois at Urbana-Champaign
"The individual nanotube-based probes can be used for electrochemical and biochemical sensing," said Min-Feng Yu, a U. of I. professor of mechanical science and engineering, and a researcher at the university's Beckman Institute. "The position of the nanoelectrodes can be controlled very accurately."
To fabricate the nanoelectrodes, Yu and graduate students Kyungsuk Yum, Jie Hu and Han Na Cho begin by attaching a strong, rigid, boron-nitride nanotube to a much larger, conductive probe. The nanotube will form the insulating core of the nanoelectrode.
The researchers then coat the nanotube with a thin film of gold about 10-50 nanometers thick (a nanometer is 1 billionth of a meter.) The gold layer is then coated with an insulating polymer coating about 10 nanometers thick. Lastly, the researchers use a focused ion beam to slice off the end of the nanotube, exposing a conducting ring of gold sandwiched between an insulating core and an insulating outer ring.
The process yields nanoelectrodes with a diameter of 100 nanometers, and a length of up to 30 microns.
Because the nanotube is attached to a much larger probe, the researchers can manipulate the nanotube like a needle. They can control precisely where the nanotube penetrates a cell, for example, and even pinpoint smaller cell structures, such as the nucleus or mitochondrion.
"Nanoelectrodes offer new opportunities for electrochemical sensing in intracellular environments," said Yu, who will describe the fabrication process and demonstrate the feasibility of nanoelectrodes at the March meeting of the American Physical Society, to be held in Denver, March 5-9. "By functionalizing the active area of the nanoelectrode with an appropriate chemical, we can target the detection of specific chemical species."
The researchers have demonstrated that their nanoelectrode can sense the chemical environment within a droplet 10 microns in diameter. Their next step is to show that the probe can penetrate the cellular membrane of a living cell, without damaging the cell.
The National Science Foundation and the University of Illinois funded the work.
Contact: James E. Kloeppel
University of Illinois at Urbana-Champaign
News From The Journal Of Clinical Investigation: Aug. 25, 2010
BACTERIOLOGY: Antifreeze molecule enhances survival of bacteria-carrying ticks
Ticks can carry and transmit to humans disease-causing bacteria. For example, the black-legged tick, Ixodes scapularis, can transmit several bacteria that cause disease in humans, including Anaplasma phagocytophilum, which causes human granulocytic anaplasmosis, a disease characterized by fever, severe headache, muscle aches, chills, and shaking. If bacteria can in any way enhance the survival of the ticks that transmit them, this increases their likelihood of infecting a human, thereby impacting human health. A team of researchers, led by Erol Fikrig, at Yale University School of Medicine, New Haven, has now determined that Anaplasma phagocytophilum induces Ixodes scapularis ticks to express an antifreeze molecule that enhances tick survival in the cold. As Ixodes scapularis ticks overwinter in the US in the Northeast and Upper Midwest, this likely increases the number of Anaplasma phagocytophilum available to infect humans. As noted by Stephen Dumler, at The Johns Hopkins University School of Medicine, Baltimore, in an accompanying commentary, these data highlight how important understanding ecology and tick biology can be to unraveling the intricacies of human disease.
Title: Anaplasma phagocytophilum induces Ixodes scapularis ticks to express an antifreeze glycoprotein gene that enhances their survival in the cold
Accompanying Commentary Title: Fitness and freezing: vector biology and human health
BACTERIOLOGY: Immune interference, an explanation for vaccine failure?
Infection with Staphylococcus aureus bacteria is a major cause of bloodstream, lower respiratory tract, and skin and soft tissue infections. Given the dramatic increase in the number of infections caused by methicillin-resistant Staphylococcus aureus (MRSA), a Staphylococcus aureus vaccine is much needed. However, vaccines developed thus far have failed to induce protection in clinical trials, and even prior infection with the bacterium fails to engender protection against subsequent infection. A team of researchers, led by Gerald Pier, at Brigham and Women's Hospital, Harvard Medical School, Boston, has now generated data in mice to explain why vaccines and prior infection do not provide individuals with protection from Staphylococcus aureus.
In the study, immune molecules known as antibodies that target the Staphylococcus aureus components CP and PNAG were each shown to indirectly mediate bacterial killing in vitro and to provide protection in mouse models of Staphylococcus aureus infection. However, when mixed together, in vitro killing and in vivo protection were markedly reduced because the antibodies interfered with each other. Further analysis indicated that interference occurred because the parts of the antibodies that bound CP and PNAG interacted with each other in a process known as idiotype-anti-idiotype binding. Similar binding was observed for antibodies isolated from humans with Staphylococcus aureus bloodstream infections. As noted by the authors, and Liise-anne Pirofski, at Albert Einstein College of Medicine, New York, in an accompanying commentary, this identification of a mechanism to explain the inability of humans to mount good protective antibody responses to Staphylococcus aureus should help in the design of future candidate vaccines.
Title: Animal and human antibodies to distinct Staphylococcus aureus antigens mutually neutralize opsonic killing and protection in mice
Accompanying Commentary Title: Why antibodies disobey the Hippocratic Oath and end up doing harm: a new clue
PULMONARY: New cystic fibrosis models teach us about disease
Cystic fibrosis (CF) is caused by genetic mutations that disrupt the function of the protein CFTR. Although many organs are affected in cystic fibrosis, the most life-threatening aspect of the disease is lung disease. To understand this more deeply, animal models of cystic fibrosis that more closely mimic the human disease than do mouse models are needed. To this end, three independent research groups - one led by Kevin Foskett, at the University of Pennsylvania, Philadelphia; one led by John Engelhardt, at the University of Iowa, Iowa City; and one led by Jeffrey Wine, at Stanford University, Stanford - have analyzed pig and ferret models of cystic fibrosis and determined that they represent good models of lung disease in individuals with cystic fibrosis. As concluded by each of the authors and noted by Jonathan Widdicombe, at the University of California Davis, Davis, in an accompanying commentary, these animals will prove valuable models to both further understanding of the mechanisms underlying lung disease in individuals with cystic fibrosis and test potential therapies.
Title: cAMP-activated Ca2+ signaling is required for CFTR-mediated serous cell fluid secretion in porcine and human airways
Accompanying Article: Hyposecretion of fluid from tracheal submucosal glands of CFTR-deficient pigs
Accompanying Article Title: Disease phenotype of a ferret CFTR-knockout model of cystic fibrosis
Accompanying Commentary Title: Transgenic animals may resolve a sticky situation in cystic fibrosis
REPRODUCTIVE BIOLOGY: Long standing question in sperm biology answered
Nahum Sonenberg, Bernard Robaire, and colleagues, at McGill University, Montreal, have generated data in mice that provides insight into a long unanswered question in sperm biology. Specifically, how protein expression is regulated in the late stages of sperm development. The importance of these data are outlined in an accompanying commentary by Stephen Liebhaber and colleagues, at the University of Pennsylvania, Philadelphia.
A protein in a cell is made from a template known as an mRNA molecule, which in turn is a copy of the information contained in a gene. About half way through sperm development, mRNA formation ceases so the mRNA templates for proteins needed in the late stages of sperm development must be made early in development and stored. Understanding of the mechanisms that underlie mRNA storage and subsequent activation has been long sought after. In the study, Sonenberg, Robaire, and colleagues find that mice lacking the protein Paip2a and mice lacking Paip2a and Paip2b exhibit male infertility associated with impaired activation of stored mRNAs. Further analysis indicated that aberrant increased expression of the protein Pabp caused the impaired activation of stored mRNAs, leading the authors to conclude that mRNA activation in late sperm development requires an optimal concentration of Pabp, as determined by Paip2a.
Title: The poly(A)-binding protein partner Paip2a controls translation during late spermiogenesis in mice
Accompanying Commentary Title: Too much PABP, too little translation
Source:
Karen Honey
Journal of Clinical Investigation
Ticks can carry and transmit to humans disease-causing bacteria. For example, the black-legged tick, Ixodes scapularis, can transmit several bacteria that cause disease in humans, including Anaplasma phagocytophilum, which causes human granulocytic anaplasmosis, a disease characterized by fever, severe headache, muscle aches, chills, and shaking. If bacteria can in any way enhance the survival of the ticks that transmit them, this increases their likelihood of infecting a human, thereby impacting human health. A team of researchers, led by Erol Fikrig, at Yale University School of Medicine, New Haven, has now determined that Anaplasma phagocytophilum induces Ixodes scapularis ticks to express an antifreeze molecule that enhances tick survival in the cold. As Ixodes scapularis ticks overwinter in the US in the Northeast and Upper Midwest, this likely increases the number of Anaplasma phagocytophilum available to infect humans. As noted by Stephen Dumler, at The Johns Hopkins University School of Medicine, Baltimore, in an accompanying commentary, these data highlight how important understanding ecology and tick biology can be to unraveling the intricacies of human disease.
Title: Anaplasma phagocytophilum induces Ixodes scapularis ticks to express an antifreeze glycoprotein gene that enhances their survival in the cold
Accompanying Commentary Title: Fitness and freezing: vector biology and human health
BACTERIOLOGY: Immune interference, an explanation for vaccine failure?
Infection with Staphylococcus aureus bacteria is a major cause of bloodstream, lower respiratory tract, and skin and soft tissue infections. Given the dramatic increase in the number of infections caused by methicillin-resistant Staphylococcus aureus (MRSA), a Staphylococcus aureus vaccine is much needed. However, vaccines developed thus far have failed to induce protection in clinical trials, and even prior infection with the bacterium fails to engender protection against subsequent infection. A team of researchers, led by Gerald Pier, at Brigham and Women's Hospital, Harvard Medical School, Boston, has now generated data in mice to explain why vaccines and prior infection do not provide individuals with protection from Staphylococcus aureus.
In the study, immune molecules known as antibodies that target the Staphylococcus aureus components CP and PNAG were each shown to indirectly mediate bacterial killing in vitro and to provide protection in mouse models of Staphylococcus aureus infection. However, when mixed together, in vitro killing and in vivo protection were markedly reduced because the antibodies interfered with each other. Further analysis indicated that interference occurred because the parts of the antibodies that bound CP and PNAG interacted with each other in a process known as idiotype-anti-idiotype binding. Similar binding was observed for antibodies isolated from humans with Staphylococcus aureus bloodstream infections. As noted by the authors, and Liise-anne Pirofski, at Albert Einstein College of Medicine, New York, in an accompanying commentary, this identification of a mechanism to explain the inability of humans to mount good protective antibody responses to Staphylococcus aureus should help in the design of future candidate vaccines.
Title: Animal and human antibodies to distinct Staphylococcus aureus antigens mutually neutralize opsonic killing and protection in mice
Accompanying Commentary Title: Why antibodies disobey the Hippocratic Oath and end up doing harm: a new clue
PULMONARY: New cystic fibrosis models teach us about disease
Cystic fibrosis (CF) is caused by genetic mutations that disrupt the function of the protein CFTR. Although many organs are affected in cystic fibrosis, the most life-threatening aspect of the disease is lung disease. To understand this more deeply, animal models of cystic fibrosis that more closely mimic the human disease than do mouse models are needed. To this end, three independent research groups - one led by Kevin Foskett, at the University of Pennsylvania, Philadelphia; one led by John Engelhardt, at the University of Iowa, Iowa City; and one led by Jeffrey Wine, at Stanford University, Stanford - have analyzed pig and ferret models of cystic fibrosis and determined that they represent good models of lung disease in individuals with cystic fibrosis. As concluded by each of the authors and noted by Jonathan Widdicombe, at the University of California Davis, Davis, in an accompanying commentary, these animals will prove valuable models to both further understanding of the mechanisms underlying lung disease in individuals with cystic fibrosis and test potential therapies.
Title: cAMP-activated Ca2+ signaling is required for CFTR-mediated serous cell fluid secretion in porcine and human airways
Accompanying Article: Hyposecretion of fluid from tracheal submucosal glands of CFTR-deficient pigs
Accompanying Article Title: Disease phenotype of a ferret CFTR-knockout model of cystic fibrosis
Accompanying Commentary Title: Transgenic animals may resolve a sticky situation in cystic fibrosis
REPRODUCTIVE BIOLOGY: Long standing question in sperm biology answered
Nahum Sonenberg, Bernard Robaire, and colleagues, at McGill University, Montreal, have generated data in mice that provides insight into a long unanswered question in sperm biology. Specifically, how protein expression is regulated in the late stages of sperm development. The importance of these data are outlined in an accompanying commentary by Stephen Liebhaber and colleagues, at the University of Pennsylvania, Philadelphia.
A protein in a cell is made from a template known as an mRNA molecule, which in turn is a copy of the information contained in a gene. About half way through sperm development, mRNA formation ceases so the mRNA templates for proteins needed in the late stages of sperm development must be made early in development and stored. Understanding of the mechanisms that underlie mRNA storage and subsequent activation has been long sought after. In the study, Sonenberg, Robaire, and colleagues find that mice lacking the protein Paip2a and mice lacking Paip2a and Paip2b exhibit male infertility associated with impaired activation of stored mRNAs. Further analysis indicated that aberrant increased expression of the protein Pabp caused the impaired activation of stored mRNAs, leading the authors to conclude that mRNA activation in late sperm development requires an optimal concentration of Pabp, as determined by Paip2a.
Title: The poly(A)-binding protein partner Paip2a controls translation during late spermiogenesis in mice
Accompanying Commentary Title: Too much PABP, too little translation
Source:
Karen Honey
Journal of Clinical Investigation
Discovery Of Access Code For Tick-Borne Encephalitis Virus
Fritz et al. have identified an amino acid switch that flaviviruses flip to gain access to cells.
Flaviviruses such as tick-borne encephalitis virus (TBEV), yellow fever, and dengue are dangerous human pathogens. These membrane-encircled viruses enter cells by being gobbled up into endosomes and fusing their membrane with that of the endosome.
Fusion is triggered by the endosome's acidic environment. Low pH prompts the aptly named fusion protein, on the virus's outer membrane, to change shape and grab hold of the endosome membrane, bringing the two membranes together. In their search for possible pH sensors, researchers have focused on five highly conserved histidine residues in the flavivirus fusion protein. The chemical properties of histidines make them prime candidates - they switch from uncharged to having a double positive charge upon acidification of their environment, such as that in endosomes.
Fritz et al. replaced each of the five histidines of the TBEV fusion protein with alternative residues and observed the virus's fusion ability. Given the conservation of the five histidines, the team was surprised, that mutation of one of the histidines, His323, was sufficient to completely abolish fusion. Individual mutation of three of the others had no effect on fusion whatsoever, and mutation of the fourth led to an untestable ill-formed fusion protein.
The team went on to show that mutation of the crucial His323 interfered with the pH-induced shape change of the fusion protein.
Fritz, R., et al. 2008. J. Cell Biol. doi:10.1083/jcb.200806081.
Source: Sati Motieram
Rockefeller University Press
Flaviviruses such as tick-borne encephalitis virus (TBEV), yellow fever, and dengue are dangerous human pathogens. These membrane-encircled viruses enter cells by being gobbled up into endosomes and fusing their membrane with that of the endosome.
Fusion is triggered by the endosome's acidic environment. Low pH prompts the aptly named fusion protein, on the virus's outer membrane, to change shape and grab hold of the endosome membrane, bringing the two membranes together. In their search for possible pH sensors, researchers have focused on five highly conserved histidine residues in the flavivirus fusion protein. The chemical properties of histidines make them prime candidates - they switch from uncharged to having a double positive charge upon acidification of their environment, such as that in endosomes.
Fritz et al. replaced each of the five histidines of the TBEV fusion protein with alternative residues and observed the virus's fusion ability. Given the conservation of the five histidines, the team was surprised, that mutation of one of the histidines, His323, was sufficient to completely abolish fusion. Individual mutation of three of the others had no effect on fusion whatsoever, and mutation of the fourth led to an untestable ill-formed fusion protein.
The team went on to show that mutation of the crucial His323 interfered with the pH-induced shape change of the fusion protein.
Fritz, R., et al. 2008. J. Cell Biol. doi:10.1083/jcb.200806081.
Source: Sati Motieram
Rockefeller University Press
What Does Testosterone Do For Red Deer Males?
The study shows that testosterone levels during the reproductive season have important effects in the life of male red deer.
Stags with high testosterone had larger testes and high quality sperm, translating into higher reproductive success. They also present stronger antlers, expectedly allowing them to win more male to male combats for females.
These males also have more red blood cells supplying oxygen to the muscles, giving them more stamina and endurance to defeat more males in combat and copulate with more females.
However, testosterone also presents costs, as stags with higher levels have more parasites.
Proceedings of the Royal Society B: Biological Sciences
Proceedings B is the Royal Society's flagship biological research journal, dedicated to the rapid publication and broad dissemination of high-quality research papers, reviews and comment and reply papers. The scope of journal is diverse and is especially strong in organismal biology.
Proceedings of the Royal Society B: Biological Sciences
Stags with high testosterone had larger testes and high quality sperm, translating into higher reproductive success. They also present stronger antlers, expectedly allowing them to win more male to male combats for females.
These males also have more red blood cells supplying oxygen to the muscles, giving them more stamina and endurance to defeat more males in combat and copulate with more females.
However, testosterone also presents costs, as stags with higher levels have more parasites.
Proceedings of the Royal Society B: Biological Sciences
Proceedings B is the Royal Society's flagship biological research journal, dedicated to the rapid publication and broad dissemination of high-quality research papers, reviews and comment and reply papers. The scope of journal is diverse and is especially strong in organismal biology.
Proceedings of the Royal Society B: Biological Sciences
Dopamine's Opposing Effects Separated By A Few Millimeters In The Brain
The chemical dopamine induces both desire and dread, according to new animal research in the July 9 issue of The Journal of Neuroscience. Although dopamine is well known to motivate animals and people to seek positive rewards, the study indicates that it also can promote negative feelings like fear. The finding may help explain why dopamine dysfunction is implicated not only in drug addiction, which involves excessive desire, but in schizophrenia and some phobias, which involve excessive fear.
"This study changes our thinking about what dopamine does," said Howard Fields, MD, PhD, of the University of California, San Francisco, an expert unaffiliated with the study. "There is a huge body of evidence out there to support the idea that dopamine mediates positive effects, like reward, happiness, and pleasure. This study says, it does do that, but it can also promote negative behaviors through actions in an adjacent brain area," Fields said.
Kent Berridge, PhD, and his colleagues at the University of Michigan, identified dopamine's dual effect on the nucleus accumbens, a brain region that motivates people and animals to seek out pleasurable rewards like food, sex, or drugs, but is also involved in fear. They found that inhibiting dopamine's normal function prevented the nucleus accumbens neurons from inducing both rewarding and fearful behaviors, suggesting that dopamine is important in both.
In previous research, Berridge and colleagues showed that a distance of only a few millimeters separated desire and dread functions in the nucleus accumbens (which is only about 5 millimeters long in humans). Because dopamine is an important neurotransmitter in this brain structure, the researchers investigated its role in generating these functions in the current study.
When dopamine was allowed to act normally, injection of a chemical to model normal signaling in the front of the nucleus accumbens caused rats to eat nearly three times as much as they normally do. In contrast, injection of the chemical in the back of the nucleus accumbens caused rats to display fearful behavior normally shown in response to a predator.
"It has always been assumed that discrete neurotransmitters might separate fear from desire, but this report shows that transmitters such as dopamine play a constant role and that the anatomy is providing for emotional discretion," said Peter Kalivas, PhD, at the Medical University of South Carolina, who was unaffiliated with the study.
Berridge speculates that disruption of dopamine neurotransmission in one region of the nucleus accumbens may be a mechanism for pathological excesses of fear in disorders such as schizophrenia, whereas disruptions in dopamine neurotransmission in an adjacent region may be a mechanism for excessive reward-seeking in conditions like addiction.
The research was supported by the National Institute of Mental Health and the National Institute on Drug Abuse.
The Journal of Neuroscience is published by the Society for Neuroscience, an organization of more than 38,000 basic scientists and clinicians who study the brain and nervous system.
Source: DeeDee Clendenning
Society for Neuroscience
"This study changes our thinking about what dopamine does," said Howard Fields, MD, PhD, of the University of California, San Francisco, an expert unaffiliated with the study. "There is a huge body of evidence out there to support the idea that dopamine mediates positive effects, like reward, happiness, and pleasure. This study says, it does do that, but it can also promote negative behaviors through actions in an adjacent brain area," Fields said.
Kent Berridge, PhD, and his colleagues at the University of Michigan, identified dopamine's dual effect on the nucleus accumbens, a brain region that motivates people and animals to seek out pleasurable rewards like food, sex, or drugs, but is also involved in fear. They found that inhibiting dopamine's normal function prevented the nucleus accumbens neurons from inducing both rewarding and fearful behaviors, suggesting that dopamine is important in both.
In previous research, Berridge and colleagues showed that a distance of only a few millimeters separated desire and dread functions in the nucleus accumbens (which is only about 5 millimeters long in humans). Because dopamine is an important neurotransmitter in this brain structure, the researchers investigated its role in generating these functions in the current study.
When dopamine was allowed to act normally, injection of a chemical to model normal signaling in the front of the nucleus accumbens caused rats to eat nearly three times as much as they normally do. In contrast, injection of the chemical in the back of the nucleus accumbens caused rats to display fearful behavior normally shown in response to a predator.
"It has always been assumed that discrete neurotransmitters might separate fear from desire, but this report shows that transmitters such as dopamine play a constant role and that the anatomy is providing for emotional discretion," said Peter Kalivas, PhD, at the Medical University of South Carolina, who was unaffiliated with the study.
Berridge speculates that disruption of dopamine neurotransmission in one region of the nucleus accumbens may be a mechanism for pathological excesses of fear in disorders such as schizophrenia, whereas disruptions in dopamine neurotransmission in an adjacent region may be a mechanism for excessive reward-seeking in conditions like addiction.
The research was supported by the National Institute of Mental Health and the National Institute on Drug Abuse.
The Journal of Neuroscience is published by the Society for Neuroscience, an organization of more than 38,000 basic scientists and clinicians who study the brain and nervous system.
Source: DeeDee Clendenning
Society for Neuroscience
P[acman]-Generated Fruit Fly Gene 'Library': A New Research Tool
Using a specially adapted tool called P[acman], a collaboration of researchers led by Baylor College of Medicine has established a library of clones that cover most of the genome of Drosophila melanogaster (fruit fly) and should speed the pace of genetic research.
In a report in the current online issue of the journal Nature Methods, Dr. Hugo Bellen, a professor of molecular and human genetics at BCM and a Howard Hughes Medical Institute investigator, and his colleagues describe the new libraries.
P[acman] - developed by Dr. Koen Venken in Bellen's laboratory - allows scientists to study large chunks of DNA in living flies. The vector - officially P/phiC31 artificial chromosome for manipulation - combines different technologies: a specially designed bacterial artificial chromosome (BAC) that allows maintenance of large pieces of DNA in bacteria, recombineering that allows the manipulation of large pieces of DNA in bacteria, and the ability to insert the genomic DNA into the genome of the fly at a specific site using phiC31-mediated transgenesis.
Venken adapted the P[acman] vector to create genomic libraries, so that a researcher can choose a gene and find the corresponding clones in the library that cover that gene. Their collaborators at Lawrence Berkeley National Laboratory, Drs. Roger Hoskins and Joseph Carlson, played a key role in the design, construction, and annotation of the libraries.
"You can insert a single copy of a gene and rescue a mutation, or do a structure/function analysis of the gene," Bellen said. "If you don't know where the gene is expressed, you can tag it, put it back and locate where it is expressed."
The library is available at pacmanfly/.
The report is available at nature/nmeth/index.html
Others who took part in this work include Karen L. Schulze, Hongling Pan and Yuchun He of BCM, Ken Wan (LBNL), Rebecca Spokony and Kevin P. White of the University of Chicago, and Maxim Koriabine and Pieter J. de Jong of Children's Hospital Oakland Research Institute in California.
Funding for this work came from the Howard Hughes Medical Institute, the National Institutes of Health and the BCM Intellectual and Developmental Disabilities Research Center.
Source:
Glenna Picton
Baylor College of Medicine
In a report in the current online issue of the journal Nature Methods, Dr. Hugo Bellen, a professor of molecular and human genetics at BCM and a Howard Hughes Medical Institute investigator, and his colleagues describe the new libraries.
P[acman] - developed by Dr. Koen Venken in Bellen's laboratory - allows scientists to study large chunks of DNA in living flies. The vector - officially P/phiC31 artificial chromosome for manipulation - combines different technologies: a specially designed bacterial artificial chromosome (BAC) that allows maintenance of large pieces of DNA in bacteria, recombineering that allows the manipulation of large pieces of DNA in bacteria, and the ability to insert the genomic DNA into the genome of the fly at a specific site using phiC31-mediated transgenesis.
Venken adapted the P[acman] vector to create genomic libraries, so that a researcher can choose a gene and find the corresponding clones in the library that cover that gene. Their collaborators at Lawrence Berkeley National Laboratory, Drs. Roger Hoskins and Joseph Carlson, played a key role in the design, construction, and annotation of the libraries.
"You can insert a single copy of a gene and rescue a mutation, or do a structure/function analysis of the gene," Bellen said. "If you don't know where the gene is expressed, you can tag it, put it back and locate where it is expressed."
The library is available at pacmanfly/.
The report is available at nature/nmeth/index.html
Others who took part in this work include Karen L. Schulze, Hongling Pan and Yuchun He of BCM, Ken Wan (LBNL), Rebecca Spokony and Kevin P. White of the University of Chicago, and Maxim Koriabine and Pieter J. de Jong of Children's Hospital Oakland Research Institute in California.
Funding for this work came from the Howard Hughes Medical Institute, the National Institutes of Health and the BCM Intellectual and Developmental Disabilities Research Center.
Source:
Glenna Picton
Baylor College of Medicine
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