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Free access to archived research articles: navigating through troubled waters
354
News & Comment
TRENDS in Biochemical Sciences Vol.26 No.6 June 2001
In Brief
The challenge of clarifying complexity A highly sensitive technique that is capable of quantifying the amount of proteins at the single-cell level has recently been developed. This technique, termed ‘immunodetection amplified by T7 RNA polymerase’ (IDAT), is the product of two research teams at the University of Pennsylvania (Philadelphia, PA, USA) [Proc. Natl. Acad. Sci. U. S. A. (2001) 10.1073/pnas.101124598]. For this method, an antibody to the protein of interest is attached to a microplate and allowed to capture the protein from cell lysates. A second antibody to this protein, conjugated to a double-stranded oligonucleotide containing the T7 promoter, is then allowed to bind these antibody–antigen complexes and T7 RNA polymerase is used to amplify RNA from these oligonucleotides. When used for detecting the HER2/neu receptor, a 185-kD surface membrane protein that is overexpressed in ~25% of human breast cancers, IDAT was nine-orders of magnitude more sensitive than conventional methods such as ELISA. IDAT might be useful in aiding the development of proteomics because advances in this area are currently limited by the inability of techniques to detect and reliably quantify individual proteins from complex mixtures of cellular molecules. AR (http://www.med.upenn.edu/news)
Fragmentation of science policy in Europe: the cost of non-Europe A study conducted by the Europolis project (April 2001) has tagged the excessive fragmentation of European research efforts and institutions as a handicap for the European science, technology and innovation policy. The Europolis project, representing a collaboration of eight science policy organizations led by the Observatoire des Sciences et des Techniques (OST) in Paris, France, and funded by the 5th Framework Programme, began in February 2000 with the aim of fostering in-depth debates on the evolution of Europe’s science and technology policy. To solve this fragmentation problem, the study recommended that one or more independent European research councils
should be created, in fields such as life sciences, biotechnology, agriculture and physical sciences. The study suggested that, based on the template of the National Science Foundation (NSF) or the National Institute of Health (NIH) in the USA, such new organizations could originate from the existing European Science Foundation (ESF) and the national research councils. AR (http://www.obs-ost.fr/ost_en/news.htm)
Smart as a frog
Studies in frogs have demonstrated for the first time the in vivo induction of defense peptides in a vertebrate. The soft, scale-less skin of frogs, coupled with the moist, warm environments inhabited by these amphibians, is an ideal breeding ground for microbial pathogens. The skin glands of frogs provide relief from this onslaught by secreting an array of structurally diverse peptides with antibiotic activity. A research group led by Maurizio Simmaco and Donatella Barra at the University of Rome ‘La Sapienza’ (Italy) now shows that the synthesis of antimicrobial peptides in the skin of Rana esculenta is, in fact, stimulated by microorganisms [FASEB J. (2001) 10.1096/fj.00-0695fje]. Frogs kept in a sterile environment did not produce antimicrobial peptides; however, exposure to even a single type of microorganism (one which contributes to the frog’s natural flora) was sufficient to elicit a marked production of these peptides. In support of this observation, the secretions of frogs kept in bacteria-containing water (but not of those kept under sterile conditions) contained NF-κB-binding activity; a characteristic previously associated with the production of antimicrobial peptides. These findings will help researchers learn more about the molecular mechanisms governing the role of peptide antibiotics in the innate immune system. AR
Free access to archived research articles: navigating through troubled waters Hot debate regarding the future availability of online publications is turning into turmoil for the scientific-publishing world. This debate was initiated last autumn, when the advocacy group called the Public Library of Science (http://www.publiclibraryofscience.org) distributed an ‘open letter’ urging publishers to archive original research articles from their journals into a centralized, freely-available public database [see also Trends Biochem. Sci. (2001) 26, 14]. Communication of the results of research impacts on everyone involved in science, including publishers, authors, librarians, editors, database managers and, of course, scientists. With the aim of encouraging discussions about how best to disseminate scientific research, Nature and Science have recently (April 2001) launched freely accessible online debates discussing the impact of the web on the publication of original research and the possibility of constructing a public archive for primary scientific literature. One significant contribution to this debate (hosted on the Nature site) is a position statement by the American Society for Biochemistry and Molecular Biology, publisher of the Journal of Biological Chemistry. Compiled by Robert D. Wells and Herbert Tabor, this statement raises some objections (both practical and a matter of principle) to centralized, government-run archives like PubMed Central, and explains why the free content of their journal will not be transferred to such repositories. In addition, on 23rd April, Science announced that they had made their back research content freely available one year after initial publication. AR (http://www.nature.com/nature/debates/ e-access/index.html; http://www.sciencemag.org/feature/data/ hottopics/plsdebate.shtml)
Please, don’t push me on protein structure data When is protein data produced by public structural genomics programs to be released? According to a document supported by all participants at the First
http://tibs.trends.com 0968-0004/01/$ – see front matter © 2001 Elsevier Science Ltd. All rights reserved.
News & Comment
TRENDS in Biochemical Sciences Vol.26 No.6 June 2001
In Brief
The challenge of clarifying complexity A highly sensitive technique that is capable of quantifying the amount of proteins at the single-cell level has recently been developed. This technique, termed ‘immunodetection amplified by T7 RNA polymerase’ (IDAT), is the product of two research teams at the University of Pennsylvania (Philadelphia, PA, USA) [Proc. Natl. Acad. Sci. U. S. A. (2001) 10.1073/pnas.101124598]. For this method, an antibody to the protein of interest is attached to a microplate and allowed to capture the protein from cell lysates. A second antibody to this protein, conjugated to a double-stranded oligonucleotide containing the T7 promoter, is then allowed to bind these antibody–antigen complexes and T7 RNA polymerase is used to amplify RNA from these oligonucleotides. When used for detecting the HER2/neu receptor, a 185-kD surface membrane protein that is overexpressed in ~25% of human breast cancers, IDAT was nine-orders of magnitude more sensitive than conventional methods such as ELISA. IDAT might be useful in aiding the development of proteomics because advances in this area are currently limited by the inability of techniques to detect and reliably quantify individual proteins from complex mixtures of cellular molecules. AR (http://www.med.upenn.edu/news)
Fragmentation of science policy in Europe: the cost of non-Europe A study conducted by the Europolis project (April 2001) has tagged the excessive fragmentation of European research efforts and institutions as a handicap for the European science, technology and innovation policy. The Europolis project, representing a collaboration of eight science policy organizations led by the Observatoire des Sciences et des Techniques (OST) in Paris, France, and funded by the 5th Framework Programme, began in February 2000 with the aim of fostering in-depth debates on the evolution of Europe’s science and technology policy. To solve this fragmentation problem, the study recommended that one or more independent European research councils
should be created, in fields such as life sciences, biotechnology, agriculture and physical sciences. The study suggested that, based on the template of the National Science Foundation (NSF) or the National Institute of Health (NIH) in the USA, such new organizations could originate from the existing European Science Foundation (ESF) and the national research councils. AR (http://www.obs-ost.fr/ost_en/news.htm)
Smart as a frog
Studies in frogs have demonstrated for the first time the in vivo induction of defense peptides in a vertebrate. The soft, scale-less skin of frogs, coupled with the moist, warm environments inhabited by these amphibians, is an ideal breeding ground for microbial pathogens. The skin glands of frogs provide relief from this onslaught by secreting an array of structurally diverse peptides with antibiotic activity. A research group led by Maurizio Simmaco and Donatella Barra at the University of Rome ‘La Sapienza’ (Italy) now shows that the synthesis of antimicrobial peptides in the skin of Rana esculenta is, in fact, stimulated by microorganisms [FASEB J. (2001) 10.1096/fj.00-0695fje]. Frogs kept in a sterile environment did not produce antimicrobial peptides; however, exposure to even a single type of microorganism (one which contributes to the frog’s natural flora) was sufficient to elicit a marked production of these peptides. In support of this observation, the secretions of frogs kept in bacteria-containing water (but not of those kept under sterile conditions) contained NF-κB-binding activity; a characteristic previously associated with the production of antimicrobial peptides. These findings will help researchers learn more about the molecular mechanisms governing the role of peptide antibiotics in the innate immune system. AR
Free access to archived research articles: navigating through troubled waters Hot debate regarding the future availability of online publications is turning into turmoil for the scientific-publishing world. This debate was initiated last autumn, when the advocacy group called the Public Library of Science (http://www.publiclibraryofscience.org) distributed an ‘open letter’ urging publishers to archive original research articles from their journals into a centralized, freely-available public database [see also Trends Biochem. Sci. (2001) 26, 14]. Communication of the results of research impacts on everyone involved in science, including publishers, authors, librarians, editors, database managers and, of course, scientists. With the aim of encouraging discussions about how best to disseminate scientific research, Nature and Science have recently (April 2001) launched freely accessible online debates discussing the impact of the web on the publication of original research and the possibility of constructing a public archive for primary scientific literature. One significant contribution to this debate (hosted on the Nature site) is a position statement by the American Society for Biochemistry and Molecular Biology, publisher of the Journal of Biological Chemistry. Compiled by Robert D. Wells and Herbert Tabor, this statement raises some objections (both practical and a matter of principle) to centralized, government-run archives like PubMed Central, and explains why the free content of their journal will not be transferred to such repositories. In addition, on 23rd April, Science announced that they had made their back research content freely available one year after initial publication. AR (http://www.nature.com/nature/debates/ e-access/index.html; http://www.sciencemag.org/feature/data/ hottopics/plsdebate.shtml)
Please, don’t push me on protein structure data When is protein data produced by public structural genomics programs to be released? According to a document supported by all participants at the First
http://tibs.trends.com 0968-0004/01/$ – see front matter © 2001 Elsevier Science Ltd. All rights reserved.