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This profile was last updated on 4/8/13  and contains information from public web pages and contributions from the ZoomInfo community.

Dr. Yuan-Ping Pang Ph.D.

Wrong Dr. Yuan-Ping Pang Ph.D.?

Cons-Researcher

Mayo Foundation
200 1St St Sw
Rochester, Minnesota 55905
United States

 
Background

Employment History

Education

  • Ph.D.
32 Total References
Web References
Mayo Clinic - Moonlighting Enzyme Linked to Neurodegenerative Disease
www.mayoclinic.org, 24 April 2007 [cached]
Other authors of this study include: Ngolela Esther Babady, a Ph.D. student at Mayo Graduate School; Yuan-Ping Pang, Ph.D., director of Mayo Clinic's Computer-Aided Molecular Design Laboratory; and Orly Elpeleg of Hadassah Hebrew University Medical Center in Jerusalem.
The study was funded with grants from the Muscular Dystrophy Association, American Heart Association, U.S. Department of Defense and the National Science Foundation.
Mayo Clinic - Gates, Others Tap Mayo Computer Modeler to Research Malaria
www.mayoclinic.org, 31 Dec 2004 [cached]
Yuan-Ping Pang, Ph.D., a chemist and head of Mayo's Computer-Aided Molecular Design Laboratory, will lead computational work on the three-year project to be funded by a $2.7 million Grand Challenges in Global Health award.
The award is one of 43 projects funded by the Foundation for the National Institutes of Health, in collaboration with the Bill & Melinda Gates Foundation.It reflects an ongoing effort by the Gates Foundation to focus innovative medical research on diseases that impact major international populations.
"It's significant that the foundations recognized Dr. Pang's expertise, but also saw Mayo as a center for innovative biomedical technology," says Robert Rizza, M.D., Mayo Clinic's director for research.
...
Dr. Pang, who built his own supercomputer at Mayo Clinic, will begin the project by determining the protein structures in mosquitoes that carry malaria and how they differ from the structures in human proteins.Using terascale supercomputing at Mayo, the goal is to understand the structural differences so researchers can develop an insecticide that won't hurt humans.
"This is a great opportunity to work with the foundations and a stellar team of scientists at Virginia Tech and Kenya, Africa, to provide a solution that may have worldwide impact on health," says Dr. Pang.
Scientists from Virginia Tech will use Dr. Pang's computer-generated mosquito protein structure as scaffolding on which they will build new molecules.The prototype will be tested in Virginia and then at the International Center for Insect Physiology and Ecology in Kenya.
Despite years of research and eradication efforts by the United Nations and others, malaria is still a widespread health problem.The World Health Organization says upwards of 500 million people suffered malaria in 2003 and the death toll from all mosquito-borne illnesses exceeds 1 million annually; most were children under 5.Children who survive malaria often suffer learning impairments or brain damage.
Dr. Pang previously received national attention when he built his own supercomputer by assembling processing units from hundreds of personal computers.He then used his supercomputer to create the first 3-D model of the viral enzyme that led to the discovery of a small-molecule inhibitor of the Severe Acute Respiratory Syndrome (SARS) virus.For more on Dr. Pang's research, visit his laboratory Web site.
Editorial Board of Journal of Advances and Applications in Bioinformatics and Chemistry
www.dovepress.com, 24 Feb 2010 [cached]
Professor Pang
...
Yuan-Ping Pang, Professor of Biophysics and Pharmacology, Computer-Aided Molecular Design Laboratory, Mayo Clinic, Rochester, MN, USA
Professor Perez
Professor Perez
Mayo Foundation for Medical Education and Research Press Release (October 12, 2006) -- Mayo Clinic Study Could Lead to Safer Pesticides
www.pestlaw.com, 12 Oct 2006 [cached]
The key, according to the study's author, Yuan-Ping Pang, Ph.D., director of Mayo Clinic's Computer-Aided Molecular Design Laboratory, was in identifying an insect-specific enzyme that could be used as a direct target for a new insecticide that would not affect humans and animals.The research was done with the support of a powerful terascale supercomputer Dr. Pang designed to develop a three-dimensional model of an enzyme taken from the two insects. (Terascale refers to a computer so powerful it can perform one trillion operations per second.)
"We now have a blueprint that will enable the development of a new generation of pesticides that will not be toxic to humans.Ultimately, the idea would be that we would be able to eat apples without washing them -- even though it may be covered with pesticides," says Dr. Pang.
Greenbugs are found in North, Central and South America, Europe, Africa, the Middle East and Asia.Aphids have been present since 1912 in southern Europe, central Asia, the Middle East and Africa.Greenbugs are the most damaging of aphids because they suck plant juices and inject a toxin into the plant during the process, Dr. Pang says.
...
The use of potentially dangerous pesticides developed decades ago is based on the hypothesis that these pesticides are used in low doses that humans can tolerate, but pests cannot," Dr. Pang says.
But according to a report by the Environmental Protection Agency's Office of Inspector General, some anticholinesterase pesticides can enter the brain of fetuses and young children and can destroy cells in the developing nervous system.
To date, safer and equally effective insecticides have not been designed to replace insecticides currently used by farmers, Dr. Pang says.
Anticholinesterase-based pesticides target an amino acid within the acetylcholinesterase enzyme, called serine.Serine is not unique to insects, which is why serine-based insecticides affect both humans and animals.Dr. Pang developed a computer-based three-dimensional model that identified a different amino acid called cysteine, which is unique to insects.It is located at the opening of the active site of acetylcholinesterase.
"My goal was to find an enzyme residue that is unique to insects.Doing so would allow us to design a molecule that would selectively inhibit the insect enzyme.Therefore we could conceivably create a pesticide that is only toxic to insects, not humans," Dr. Pang says.
Dr. Pang analyzed the anticholinesterase protein sequences of 72 species ranging from humans to chickens and other mammals and pests.He found a cysteine amino acid present in the acetylcholinesterase protein sequences of the greenbug and English grain aphid, but absent in comparable human and animal sequences.
Examining the three-dimensional models of both the greenbug and aphid acetylcholinesterase enzymes with the terascale supercomputer he designed was Dr. Pang's crucial next step.He discovered the pest-specific cysteine residue located at the edge of the active site of the insect acetylcholinesterase.
Acetylcholinesterase enzymes have a deep and narrow active site.A cysteine residue is located at the opening of the active site of insect acetylcholinesterases and can react with a small-molecule pesticide.In other words, the cysteine residue serves as a hook that can tether a small molecule in the active site and damage the enzyme.
However, the cysteine is not present in acetylcholinesterase in humans or animals.So the cysteine residue is essentially a species marker for developing new pesticides that would not harm humans because cysteine is not an enzyme active in humans or mammals, Dr. Pang says.
"We inspected the entire active site of the human enzyme and we couldn't find one cysteine residue," he says.
"It is conceivable that a chemically stable molecule could react with insect-specific cysteine residue and irreversibly inhibit the insect acetylcholinesterases upon binding to the active site.This leads me to believe that the cysteine residue can be used as a species marker for developing a new generation of safer pesticides that can inhibit greenbug and aphid acetylcholinesterase, but not human or animal acetylcholinesterases," Dr. Pang says.
"Protein sequences as one-dimensional information can tell us whether an amino acid we are focusing on is unique, but not whether that amino acid is located in the active site of the enzyme.We cannot target the residue if we do not know where it lies.Now, we can examine the location of the residue in three-dimensional space using terascale computers.
"This work offers a structural basis for the possible design of pesticides that are toxic to insects, but not to humans.It demonstrates the benefits in the power of molecular biology that led to the discovery of the functionally important and pest-specific cysteine residue that was hidden in a sea of protein sequences originally reported in 2002," Dr. Pang says.
This study was funded by the Mayo Foundation for Medical Education and Research.
Study could lead to safer pesticides
www.scienceinafrica.co.za, 1 Oct 2006 [cached]
The key, according to the study's author, Yuan-Ping Pang, Ph.D., director of Mayo Clinic's Computer-Aided Molecular Design Laboratory, was in identifying an insect-specific enzyme that could be used as a direct target for a new insecticide that would not affect humans and animals.The research was done with the support of a powerful terascale supercomputer Dr. Pang designed to develop a three-dimensional model of an enzyme taken from the two insects. (Terascale refers to a computer so powerful it can perform one trillion operations per second.)
"We now have a blueprint that will enable the development of a new generation of pesticides that will not be toxic to humans.Ultimately, the idea would be that we would be able to eat apples without washing them -- even though it may be covered with pesticides," says Dr. Pang.
Greenbugs are found in North, Central and South America, Europe, Africa, the Middle East and Asia.Aphids have been present since 1912 in southern Europe, central Asia, the Middle East and Africa.Greenbugs are the most damaging of aphids because they suck plant juices and inject a toxin into the plant during the process, Dr. Pang says.
...
The use of potentially dangerous pesticides developed decades ago is based on the hypothesis that these pesticides are used in low doses that humans can tolerate, but pests cannot," Dr. Pang says.
But according to a report by the Environmental Protection Agency's Office of Inspector General, some anticholinesterase pesticides can enter the brain of fetuses and young children and can destroy cells in the developing nervous system.
To date, safer and equally effective insecticides have not been designed to replace insecticides currently used by farmers, Dr. Pang says.
Anticholinesterase-based pesticides target an amino acid within the acetylcholinesterase enzyme, called serine.Serine is not unique to insects, which is why serine-based insecticides affect both humans and animals.Dr. Pang developed a computer-based three-dimensional model that identified a different amino acid called cysteine, which is unique to insects.It is located at the opening of the active site of acetylcholinesterase.
"My goal was to find an enzyme residue that is unique to insects.Doing so would allow us to design a molecule that would selectively inhibit the insect enzyme.Therefore we could conceivably create a pesticide that is only toxic to insects, not humans," Dr. Pang says.
Dr. Pang analyzed the anticholinesterase protein sequences of 72 species ranging from humans to chickens and other mammals and pests.He found a cysteine amino acid present in the acetylcholinesterase protein sequences of the greenbug and English grain aphid, but absent in comparable human and animal sequences.
Examining the three-dimensional models of both the greenbug and aphid acetylcholinesterase enzymes with the terascale supercomputer he designed was Dr. Pang's crucial next step.He discovered the pest-specific cysteine residue located at the edge of the active site of the insect acetylcholinesterase.
Acetylcholinesterase enzymes have a deep and narrow active site.A cysteine residue is located at the opening of the active site of insect acetylcholinesterases and can react with a small-molecule pesticide.In other words, the cysteine residue serves as a hook that can tether a small molecule in the active site and damage the enzyme.
However, the cysteine is not present in acetylcholinesterase in humans or animals.So the cysteine residue is essentially a species marker for developing new pesticides that would not harm humans because cysteine is not an enzyme active in humans or mammals, Dr. Pang says.
"We inspected the entire active site of the human enzyme and we couldn't find one cysteine residue," he says.
"It is conceivable that a chemically stable molecule could react with insect-specific cysteine residue and irreversibly inhibit the insect acetylcholinesterases upon binding to the active site.This leads me to believe that the cysteine residue can be used as a species marker for developing a new generation of safer pesticides that can inhibit greenbug and aphid acetylcholinesterase, but not human or animal acetylcholinesterases," Dr. Pang says.
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