Emory University School of Medicine Department of Human Genetics
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Junmin Peng, Ph.D.
Assistant Professor
jpeng@genetics.emory.edu
404.712.8510
Office: 505 P
Lab: 525
Whitehead Biomedical Research Building
615 Michael St.
Atlanta, GA 30322

Publication search for Dr. Junmin Peng

Education:
2000-2002 Postdoctoral Fellow in Proteomics, Harvard Medical School, Boston, MA
1999-2000 Postdoctoral Fellow in Neuroscience, Harvard Medical School, Boston, MA
1994-1999 Ph.D. in Biochemistry, University of Iowa, Iowa City, IA

Research Description:

Introduction
An ultimate goal in biology is to discover the molecular mechanism of life. During decades, the main approaches are reductionism methods such as studying one or a few genes. Although those methods have contributed to our understanding of many basic principles, a comprehensive picture of biology will not be captured until more integrative approaches are utilized. Recently, efforts in genomics have made many genome sequences available. The next step is research in proteomics (more information in www.bio-itworld.com/bio/proteomics).

Proteomics Technologies: Mass Spectrometry
Mass spectrometry is a powerful technology for identifying proteins and their modifications such as phosphorylation and ubiquitination. Moreover, the technology can be used to quantify the relative and absolute amount of proteins in a mixture. Using a technique termed multidimensional liquid chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS), we can determine the identity of hundreds to thousands of protein components in a complex sample at a sensitivity in the femtomole range (10-15 mole). Technologies will be further developed to increase throughput and sensitivity. In addition, we are developing bioinformatics tools for proteomic analysis.

Medical Challenges: Neurodegenerative Diseases
Neurodegenerative diseases such as Alzheimer's, Parkinson's, and Huntington's share some common features: an age-related onset and deposition of protein aggregates. Protein modifications have been found to be common in the aggregates, but their roles in pathogenesis are poorly understood. We are interested in mapping and profiling proteins and their modifications in the aggregates from patients and animal models. Combining with tools in molecular biology, cell biology and genetics, we will explore the function of these proteins and their modifications in the development of these devastating diseases. These studies may provide proteins for drug targeting and strategies for therapeutic intervention.

Visit the Peng Laboratory

Selected Publications (of 33 papers):
Peng J and Gygi SP (2001) Proteomics: the move to mixtures. J. Mass Spectrom. 36:1083

Peng J, Elias JE, Thoreen CC, Licklider LJ, and Gygi SP (2003) Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: the yeast proteome J. Proteome Res. 2:43

Peng J, Elias JE, Schwartz D, Thoreen CC, Cheng D, Marshiscky G, Roelofs J, Finely D, and Gygi SP (2003) A proteomics approach to protein ubiquitination. Nature Biotechnol. 21:921

Peng J, Kim MJ, Cheng D, Duong DM, Gygi SP, and Sheng M (2004) Semi-quantitative proteomic analysis of rat forebrain postsynaptic density fractions by mass spectrometry. J. Biol. Chem. 279:21003

Liao L, Cheng D, Wang J, Duong DM, Losik TG, Gearing M, Rees HD, Lah JJ, Levey AI, and Peng J (2004) Proteomic characterization of postmortem amyloid plaques isolated by laser capture microdissection. J. Biol. Chem. 279:37061

Peng J and Cheng D (2005) Proteomic analysis of ubiquitin conjugates in yeast, Methods Enzymol., In press

 

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