TERRE HAUTE ? Lea-Rachel Kosnik, a professor at the University of Missouri-St. Louis, will give two lectures on small-scale hydropower and the regulatory environment in Indiana State University?s Cunningham Memorial Library?s Events Area on March 6.
Kosnik?s first talk at 10 a.m. will focus on small-scale hydroelectric power and river-basin regulation while her noon talk will concern completeness of contracts for small-scale hydropower development. Both talks are free and open to the community.
Debra Israel, Indiana State associate professor of economics, said she was excited to bring Kosnik to speak to students and the community.
?Her work on river basin regulation and small scale hydropower will show students a practical application of the environmental economics concepts that they have been learning in class,? Israel said. ?When we think of hydropower we usually think of large dams which are associated with large environmental impacts ? the surprising aspect of Dr. Kosnik?s area of research is that small scale hydropower has the potential as an alternate energy source without major environmental disruption.?
Kosnik?s research also examines the regulatory environment, using small scale hydropower as an example, but with broader implications for other alternate energy technologies.
?Given the interest on campus in alternative energy, now symbolized in our new wind turbine, and the excitement in Terre Haute about the 2013 Year of the River, this is a perfect time to bring in a speaker who is thinking about river basin regulation in innovative ways,? Israel said.
In Kosnik?s 10 a.m. talk, ?River Basin Regulation and Small Scale Hydropower,? she will discuss the demands such as irrigation, recreation, hydropower and municipal use, made on the United States? limited water resources.
?Looking forward, this situation of water resource scarcity is only projected to worsen as climate change effects and continued population growth are added to the mix,? Kosnik wrote in her presentation?s abstract.
Kosnik conducted an assessment of river-basin water regulation using small scale hydropower permitting in the United States to see if reform was needed. Her research found that reform is essential.
In the noon brownbag session, Kosnik will speak on ?Determinants of Contract Completeness: A Renewable Energy Application.?
?There is a tradeoff that must be addressed any time a contract is written; whether or not to make a contract flexible but incomplete or rigid but comprehensive,? she said in the presentation?s abstract.
She investigated hydroelectric contracts spanning nearly three decades and found that as environmental concerns increase so did contract flexibility. Her presentation will focus on the historical look of U.S. hydroelectric dam license as it ages and responds to growing environmental concerns.
Kosnik joined the economics department at the University of Missouri-St. Louis in 2004, after receiving her Ph.D. from the University of California, Los Angeles. Her main areas of expertise include environmental economics, energy economics, and behavioral economics. She received her B.A. in economics from the University of Michigan, Ann Arbor, and spent a year as a Fulbright Scholar in Ankara, Turkey. She is a member of the American Economic Association, the Midwest Economics Association, the Committee on the Status of Women in the Economics Profession, the Association of Environmental and Resource Economists, the Society for the Advancement of Behavioral Economics, and the Transportation and Public Utilities Group.
The talks are sponsored by Interdisciplinary Programs, the department of economics, the College of Arts and Sciences, the Foundational Studies Program and Cunningham Memorial Library.
Adding to the list of disease-causing proteins in brain disordersPublic release date: 3-Mar-2013 [ | E-mail | Share ]
Contact: Karen Kreeger karen.kreeger@uphs.upenn.edu 215-349-5658 University of Pennsylvania School of Medicine
Proteins with mutations in 'prion-like' segments considered candidates for inherited forms of ALS, multisystem proteinopathy
PHILADELPHIA A multi-institution group of researchers has found new candidate disease proteins for neurodegenerative disorders. James Shorter, Ph.D., assistant professor of Biochemistry and Biophysics at the Perelman School of Medicine, University of Pennsylvania, Paul Taylor, M.D., PhD, St. Jude Children's Research Hospital, and colleagues describe in an advanced online publication of Nature that mutations in prion-like segments of two RNA-binding proteins are associated with a rare inherited degeneration disorder affecting muscle, brain, motor neurons and bone (called multisystem proteinopathy) and one case of the familial form of amyotrophic lateral sclerosis (ALS).
"This study uses a variety of scientific approaches to provide powerful evidence that unregulated polymerization of proteins involved in RNA metabolism may contribute to ALS and related diseases," said Amelie Gubitz, Ph.D., a program director at the National Institute of Neurological Disorders and Stroke (NINDS).
ALS, or Lou Gehrig's disease, is a universally fatal neurodegenerative disease. Previous studies found that mutations in two related RNA-binding proteins, TDP-43 and FUS, cause some forms of ALS, but more proteins were suspected of causing other forms of the disease. TDP-43 and FUS regulate how the genetic code is translated for the assembly of proteins.
There are over 200 human RNA-binding proteins, including FUS and TDP-43, raising the possibility that additional RNA-binding proteins might contribute to ALS pathology. Computer algorithms, based on protein sequences, designed to identify yeast prions predict that around 250 human proteins, including several RNA-binding proteins associated with neurodegenerative disease, harbor a distinctive prion-like segment. These segments are essential for the assembly of certain protein complexes. But, the interplay between human prion-like segments and disease is not well understood.
Using yeast as a model organism, co-author Aaron Gitler, while at Penn in 2011, surveyed 133 of 200-plus candidate human RNA-binding proteins to predict new ALS disease genes, other than TDP-43 and FUS. They further winnowed the candidates to about 10 proteins with prion-like segments, and selected two candidates, TAF15 and EWSR1, for further study. Both TAF15 and EWSR1 aggregated in the test tube and were toxic in yeast.
Remarkably, they also uncovered TAF15 and EWSR1 mutations in ALS patients that were not found in healthy individuals. Based on these findings, they proposed that RNA-binding proteins with prion-like segments might contribute very broadly to the pathology of ALS and related brain disorders.
Characterizing the Top-Ten
Taylor, Gitler, Shorter, and others continued to characterize the top-ten human RNA-binding proteins with prion-like segments. The Nature study describes that two more of the top-ten candidates, called hnRNPA1 and hnRNPA2B1, are mutated and cause familial cases of brain disease. The mutations in hnRNPA1 and hnRNPA2B1 were present in two families with an extremely rare inherited degeneration affecting muscle, brain, motor neuron, and bone and another from a person with familial ALS.
Mutations in these two proteins fell in the prion-like segments and coincided with "sticky" regions in the proteins, making these regions more prone to assemble into self-organizing fibrils. The normal form of the proteins shows a natural tendency to assemble into fibrils, which is exacerbated by the disease mutations.
"The mutations accelerate the formation of the fibrils that recruit normal protein to form more fibrils," noted co-first author Emily Scarborough, from Penn. This dysregulated assembly likely contributes to disease. Indeed, the disease mutations also promote excess incorporation of the proteins into stress granules within a cell and the formation of clumps in the cells of animal models of human neurodegenerative disease.
"Neurodegenerative disease could ensue from unregulated fibril formation initiated spontaneously by environmental stress or another factor that regulates a protein's assembly," says Scarborough.
"This paper reflects an amazing collaborative effort and provides a great example of how understanding the underlying pure protein biochemistry can help explain how genetic mutations might cause pathology and disease," says Shorter.
"The findings confirm a strong prediction that the disease-causing mutations make the prion-like segment 'stickier' and more prone to clump," added co-first author Zamia Diaz, also from Penn.
Diseases associated with fibrils forming from prion-like domains in proteins frequently show "spreading" pathology, in which cellular degeneration via inclusions starts in one center of the brain and "spreads" to neighboring tissue. Although not directly addressed in the Nature study, the findings suggest that cell-to-cell transmission of a self-templating protein could contribute to the spreading pathology that is characteristic of these diseases.
"Related proteins with prion-like domains must be considered candidates for initiating and perhaps propagating similar pathologies in muscle, brain, motor neurons, and bone," concluded Shorter.
###
The research was funded in part by the by Ellison Medical Foundation, an NIH Innovator Fund award, NINDS (DP2OD002177, NS067354), and The Packard Center for ALS Research at Johns Hopkins.
Penn Medicine is one of the world's leading academic medical centers, dedicated to the related missions of medical education, biomedical research, and excellence in patient care. Penn Medicine consists of the Raymond and Ruth Perelman School of Medicine at the University of Pennsylvania (founded in 1765 as the nation's first medical school) and the University of Pennsylvania Health System, which together form a $4.3 billion enterprise.
The Perelman School of Medicine is currently ranked #2 in U.S. News & World Report's survey of research-oriented medical schools. The School is consistently among the nation's top recipients of funding from the National Institutes of Health, with $479.3 million awarded in the 2011 fiscal year.
The University of Pennsylvania Health System's patient care facilities include: The Hospital of the University of Pennsylvania -- recognized as one of the nation's top "Honor Roll" hospitals by U.S. News & World Report; Penn Presbyterian Medical Center; and Pennsylvania Hospital the nation's first hospital, founded in 1751. Penn Medicine also includes additional patient care facilities and services throughout the Philadelphia region.
Penn Medicine is committed to improving lives and health through a variety of community-based programs and activities. In fiscal year 2011, Penn Medicine provided $854 million to benefit our community.
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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.
Adding to the list of disease-causing proteins in brain disordersPublic release date: 3-Mar-2013 [ | E-mail | Share ]
Contact: Karen Kreeger karen.kreeger@uphs.upenn.edu 215-349-5658 University of Pennsylvania School of Medicine
Proteins with mutations in 'prion-like' segments considered candidates for inherited forms of ALS, multisystem proteinopathy
PHILADELPHIA A multi-institution group of researchers has found new candidate disease proteins for neurodegenerative disorders. James Shorter, Ph.D., assistant professor of Biochemistry and Biophysics at the Perelman School of Medicine, University of Pennsylvania, Paul Taylor, M.D., PhD, St. Jude Children's Research Hospital, and colleagues describe in an advanced online publication of Nature that mutations in prion-like segments of two RNA-binding proteins are associated with a rare inherited degeneration disorder affecting muscle, brain, motor neurons and bone (called multisystem proteinopathy) and one case of the familial form of amyotrophic lateral sclerosis (ALS).
"This study uses a variety of scientific approaches to provide powerful evidence that unregulated polymerization of proteins involved in RNA metabolism may contribute to ALS and related diseases," said Amelie Gubitz, Ph.D., a program director at the National Institute of Neurological Disorders and Stroke (NINDS).
ALS, or Lou Gehrig's disease, is a universally fatal neurodegenerative disease. Previous studies found that mutations in two related RNA-binding proteins, TDP-43 and FUS, cause some forms of ALS, but more proteins were suspected of causing other forms of the disease. TDP-43 and FUS regulate how the genetic code is translated for the assembly of proteins.
There are over 200 human RNA-binding proteins, including FUS and TDP-43, raising the possibility that additional RNA-binding proteins might contribute to ALS pathology. Computer algorithms, based on protein sequences, designed to identify yeast prions predict that around 250 human proteins, including several RNA-binding proteins associated with neurodegenerative disease, harbor a distinctive prion-like segment. These segments are essential for the assembly of certain protein complexes. But, the interplay between human prion-like segments and disease is not well understood.
Using yeast as a model organism, co-author Aaron Gitler, while at Penn in 2011, surveyed 133 of 200-plus candidate human RNA-binding proteins to predict new ALS disease genes, other than TDP-43 and FUS. They further winnowed the candidates to about 10 proteins with prion-like segments, and selected two candidates, TAF15 and EWSR1, for further study. Both TAF15 and EWSR1 aggregated in the test tube and were toxic in yeast.
Remarkably, they also uncovered TAF15 and EWSR1 mutations in ALS patients that were not found in healthy individuals. Based on these findings, they proposed that RNA-binding proteins with prion-like segments might contribute very broadly to the pathology of ALS and related brain disorders.
Characterizing the Top-Ten
Taylor, Gitler, Shorter, and others continued to characterize the top-ten human RNA-binding proteins with prion-like segments. The Nature study describes that two more of the top-ten candidates, called hnRNPA1 and hnRNPA2B1, are mutated and cause familial cases of brain disease. The mutations in hnRNPA1 and hnRNPA2B1 were present in two families with an extremely rare inherited degeneration affecting muscle, brain, motor neuron, and bone and another from a person with familial ALS.
Mutations in these two proteins fell in the prion-like segments and coincided with "sticky" regions in the proteins, making these regions more prone to assemble into self-organizing fibrils. The normal form of the proteins shows a natural tendency to assemble into fibrils, which is exacerbated by the disease mutations.
"The mutations accelerate the formation of the fibrils that recruit normal protein to form more fibrils," noted co-first author Emily Scarborough, from Penn. This dysregulated assembly likely contributes to disease. Indeed, the disease mutations also promote excess incorporation of the proteins into stress granules within a cell and the formation of clumps in the cells of animal models of human neurodegenerative disease.
"Neurodegenerative disease could ensue from unregulated fibril formation initiated spontaneously by environmental stress or another factor that regulates a protein's assembly," says Scarborough.
"This paper reflects an amazing collaborative effort and provides a great example of how understanding the underlying pure protein biochemistry can help explain how genetic mutations might cause pathology and disease," says Shorter.
"The findings confirm a strong prediction that the disease-causing mutations make the prion-like segment 'stickier' and more prone to clump," added co-first author Zamia Diaz, also from Penn.
Diseases associated with fibrils forming from prion-like domains in proteins frequently show "spreading" pathology, in which cellular degeneration via inclusions starts in one center of the brain and "spreads" to neighboring tissue. Although not directly addressed in the Nature study, the findings suggest that cell-to-cell transmission of a self-templating protein could contribute to the spreading pathology that is characteristic of these diseases.
"Related proteins with prion-like domains must be considered candidates for initiating and perhaps propagating similar pathologies in muscle, brain, motor neurons, and bone," concluded Shorter.
###
The research was funded in part by the by Ellison Medical Foundation, an NIH Innovator Fund award, NINDS (DP2OD002177, NS067354), and The Packard Center for ALS Research at Johns Hopkins.
Penn Medicine is one of the world's leading academic medical centers, dedicated to the related missions of medical education, biomedical research, and excellence in patient care. Penn Medicine consists of the Raymond and Ruth Perelman School of Medicine at the University of Pennsylvania (founded in 1765 as the nation's first medical school) and the University of Pennsylvania Health System, which together form a $4.3 billion enterprise.
The Perelman School of Medicine is currently ranked #2 in U.S. News & World Report's survey of research-oriented medical schools. The School is consistently among the nation's top recipients of funding from the National Institutes of Health, with $479.3 million awarded in the 2011 fiscal year.
The University of Pennsylvania Health System's patient care facilities include: The Hospital of the University of Pennsylvania -- recognized as one of the nation's top "Honor Roll" hospitals by U.S. News & World Report; Penn Presbyterian Medical Center; and Pennsylvania Hospital the nation's first hospital, founded in 1751. Penn Medicine also includes additional patient care facilities and services throughout the Philadelphia region.
Penn Medicine is committed to improving lives and health through a variety of community-based programs and activities. In fiscal year 2011, Penn Medicine provided $854 million to benefit our community.
[ | 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.
Your smartphone and / or tablet is just begging for an update. From time to time, these mobile devices are blessed with maintenance refreshes, bug fixes, custom ROMs and anything in between, and so many of them are floating around that it's easy for a sizable chunk to get lost in the mix. To make sure they don't escape without notice, we've gathered every possible update, hack, and other miscellaneous tomfoolery we could find during the last week and crammed them into one convenient roundup. If you find something available for your device, please give us a shout at tips at engadget dawt com and let us know. Enjoy!
Private jet owners are? hoping to lease part of Syracuse Hancock International Airport as a lure to other fly-through business people.
The Syracuse Jet Association plans to build a new hangar and office space for visiting businesspeople who arrive by private jet.? ?It is going to attract owners, both individuals and corporations, to reposition their aircrafts to Syracuse from other airports and spend their money here,? said Stacey Fruschello, general manager for the Syracuse Jet Association.
The new facility will have 40,00 square feet of hangar space, and 10,000 square feet of office and meeting space for the use of the association?s members and others who come in by private jets.? The Syracuse Jet Association has five members. They are investing in the property themselves, making it the first privately owned aircraft facility in New York.
In order to build the facility, the jet association needs the Syracuse City Council to approve on a 40-year lease for the five-acre site.? The proposed lease calls for? the association to pay $65,000 a year to the city, with annual increases of 2 percent per year. The Common Council is to vote on the lease in March. The Syracuse Jet Association hopes to recruit five more members and complete construction by the fall.
The Syracuse Jet Association describes the facility as a good investment because of the services it will be able to provide and the business it will be able to bring into the area. It demonstrates members? desire to invest back into their city, say some members.
The new facility will be designed to cater primarily to the business traveler, said? Christina Callahan, commissioner of aviation in Syracuse. Members and other private-jet visitors will have access to aircraft storage, ground support, and cheaper fuel services. ?It will give them space to have meetings with clients, to conduct business interviews, employment interviews,? Callahan said.
The amenities and services will provide more conveniences for the business traveler and corporations in the area, say its supporters. The location of the facility would provide easy access from the main airport entrance road, as well as for planes coming in and out of the main runway.
Jet association members predict the new facility will help to bring more clients and businesses into the Central New York area because of the conveniences.? Ted Perry, CEO of Metro Air and an association member,? says this is a great investment in the city of Syracuse.
?We want to make an investment in our own hometown and we believe that we can provide that the city needs for general aviation on a private side a little better than that which is currently provided,? said Perry. After the 40- year lease, he said, the land and all of the improvements made on it will be given back to the city.
Kevin Schwab is vice president of air service development at CenterState CEO, a business- promotion organization for Central New York. Even the appearance of the airport, he said, can make a difference in developing a business.
?The Hancock airport really is the gateway for many visitors to the region and certainly you have many businesses or clients or prospective clients that do come into the area on charter or commercial aircraft,? Schwab said. ?A new facility would make a wonderful first impression for many of those visitors.?
(Samantha Sonner is a junior majoring in broadcast and digital journalism.)
Evernote, a Web-based note-sharing service, said it was resetting the passwords of its 50 million users because hackers managed to breach its computer network and access some user names, email addresses and encrypted passwords.
Evernote spokeswoman Ronda Scott said via email on Saturday that the attack "follows a similar pattern" to other cyber attacks on Internet-based companies in recent weeks, but she did not elaborate.
"In our security investigation, we have found no evidence that any of the content you store in Evernote was accessed, changed or lost," the company said on its website. "We also have no evidence that any payment information for Evernote Premium or Evernote Business customers was accessed."
Scott declined to say how many accounts had been exposed or whether it might be possible for the hackers to unscramble encrypted passwords.
A series of technology companies including Facebook, Apple, Microsoft and Twitter have recently disclosed cyber attacks. In the majority of those cases, the companies said that the unknown hackers exploited a bug in Java software and that no user information was compromised.
Twitter is the only major Internet company that has recently reported its user information was exposed to hackers. On Feb. 1, Twitter reset passwords for 250,000 accounts whose encrypted passwords may have been accessed.
Scott said Evernote believed that the hackers did not exploit a bug in Java when they broke into the company's system.
Evernote is a privately held company whose major investors include Meritech Capital, CBC Capital, Sequoia Capital, Morgenthaler Ventures and DOCOMO Capital.
Two educational workshops will be held at Girls Preparatory School next week. GPS is located at 205 Island Ave. in North Chattanooga.
The events, sponsored by the Tennessee Association of Independent Schools, are open to both member and nonmember schools with the association.
* Tuesday: "Flipping the Classroom: Getting Off the Stage" will be held in the GPS Caldwell Commons from noon to 3 p.m.
The forum discusses an environment that personalizes learning, increases student-teacher and student-student interaction, with a goal of greater student understanding of key concepts.
This workshop is free to TAIS member schools, $25 for all others. Reservations are required, since lunch is included. Email Kristi Bryson at kbryson@gps.edu
* Friday: "Engagement 2.0" will be held from 11 a.m. to 3:30 p.m.
The forum shares how schools approach online engagement with alumni and others. Comprised of small group activities and discussion time, it is particularly suited for people in admissions, advancement/development, alumni relations and communications/marketing.
Preregistration is required by Wednesday with TAIS at www.taistn.com/page.cfm?p=562. Cost of the workshop is $70 for representatives of TAIS member schools, $90 for nonmember schools.
Registration links for both workshops can be found on the GPS website, www.gps.edu.
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With the threat of suspension of work looming, the World Intellectual Property Organization Standing Committee of the Law of Patents (SCP) agreed to a minimal programme of work, which includes exceptions and limitations to patent rights, quality of patents, and patents and health. Delegates made significant concessions on all sides, but the Africa Group expressed particular disappointment in the limited commitment to work on the patents and health topic.
The 19th session of the WIPO patent law committee met this week from 25-28 February, adjourning near midnight on the last day. Although member states remained divided on key issues, most were relieved to have come to an agreement.
Meeting documents are available here.
According the chair?s summary [pdf], future work includes exceptions and limitations to patent rights, quality of patents, including opposition systems, patents and health, confidentiality of communications between clients and their patent advisors, and transfer of technology.
Meeting Chair Vittorio Ragonesi, legal adviser for the Italian Ministry of Foreign Affairs, told Intellectual Property Watch, ?The work programme is very minimal, but at least, we?ll keep working. It?s very important that we continue because this is the only multilateral forum to work on the international patent system.?
Toward the end of informal negotiations on 28 February, debate narrowed in on patents and health and quality of patents. The Africa Group pushed hard for more ambitious work on patents and health, included exploration of obstacles countries face using health-related patent flexibilities. Group B, representing developed countries, meanwhile wanted to move forward on a questionnaire to identify definitions and criteria used by member states in defining quality of patents. These priorities are reflected in the ?Draft informal proposal by the Chair on future work in the SCP,? [pdf] which circulated earlier in the day.
Low Ambition on Patents and Health?
Following the meeting close, a delegate from a developed country said, ?Our biggest win this week was not running this committee into the sand.? But for others, the pressure to keep the committee alive resulted in too many concessions.
During the closing remarks, Algeria, on behalf of the Africa Group, said, ?The SCP must make more consequential and useful progress on patents and health. Our countries suffer on a daily basis of a status quo imposed by a patent system that only considers the demands of rights holders.?
?At the end of this session, the African Group found itself alone with the responsibility to continue or to block the work of this committee. Faced with this choice, the group decided it favoured the committee, and the work of this organisation,? the delegate from Algeria said. ?We hope that the Group will not have to save this committee every session.?
According to the chair?s summary, on patents and health, members agreed to ?Organize during SCP/20 a sharing session on countries? use of health-related patent flexibilities.?
As expressed in their opening statement [doc], for the Africa Group, exploring challenges countries face in making use of health-related patent flexibilities was a top priority, as outlined in the proposal submitted by South Africa on behalf of the Africa Group and the Development Agenda Group (SCP/16/17). This proposal was also supported by the Asia Group.
This proposition was strongly opposed by Group B, representing developed countries, which favoured the US delegation?s proposal (SCP/17/11) on studying how the patent system promotes public health.
Nonetheless, several representatives of developing countries expressed relief outside of the meeting that the patents and health topic remained part of the SCP?s future work.
?And Low Ambition on Quality of Patents
If patents and health was the near-redline for the Africa Group, and other developing countries, quality of patents was the equivalent for the US and other developed countries.
The United States? opening statement [pdf] focussed on progress the country has made in aligning the patent system to its international partners with the implementation of America Invents Act (AIA) and the ?first inventor to file? provision. The US delegate also pointed to ?initiatives aimed at improving the quality and efficiency of the patent examination process? through work sharing programs with partner patent office.
In the area of patent quality, the US and other developed countries hope to make progress by moving forward with a questionnaire on quality of patents as proposed in the past by the United Kingdom and Canada (SCP/18/9).
Reticent to any move toward international harmonisation of patent systems, the Africa Group, and other developing countries, asked for more time to allow national patent offices to review the questions before moving forward with the questionnaire.
Work on quality of patents is much less ambitious than the options presented in the chair?s earlier draft. The SCP agreed to the ?compilation, based on information received from Member States, of work-sharing programs among patent offices and use of external information for search and examination.?
Exceptions and Limitations to Patent Rights
Playing a key role in moving the SCP toward an agreement, the delegate from Brazil noted in his closing remarks, ?It?s clear that no delegation is fully satisfied with the result so far. But, we have managed to come together on a common result, and that is important.?
Brazil came to this session with a new proposal on how the committee could address exceptions and limitations to patent rights (SCP/19/6) involving analysis of exceptions and limitations most commonly used by countries and a seminar exploring these areas during the next SCP.
While the seminar on exceptions and limitations was not in the chair?s first draft, a half-day session made it into the final work plan. On this issue, the WIPO secretariat will prepare a document on how member states have implemented five exceptions and limitations including private and/or non-commercial use; prior use; use of articles on foreign vessels, aircraft and land vehicles.
On the remaining exceptions and limitations, including compulsory licensing and/or government use, the secretariat will prepare a document on how they are implemented. A follow-up half-day session will be held during the 21st SCP session.
For the next SCP session, three dates have been proposed and most delegates were partial to holding the 20th SCP starting 9 December.
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Public release date: 3-Mar-2013
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