|
Select an Option
About the PRCs
Caprion Proteomics Inc. (Caprion)
Biodefense Proteomics Research Center at Albert Einstein College of Medicine (Einstein)
The Harvard Institute of Proteomics (HIP)
Myriad Genetics, Inc. (Myriad)
Pacific Northwest National Laboratory (PNNL)
The Scripps Research Institute - FSPS (FSPS)
The University of Michigan (U-M) |
About The Scripps Research Institute - FSPS
Dr. Peter Kuhn, PI
The Scripps Research Institute - FSPS' goal is to provide a comprehensive molecular characterization and cataloging of all SARS-CoV related proteins and associated functions at the viral and host levels. FSPS will provide the required knowledge, experimental protocols, and materials to enable the development of therapeutic interventions by achieving the following objectives:
- Discover bioinformatics and analyze comprehensive proteomes for the functional mapping of the SARS-CoV proteome.
- Create and maintain a SARS-CoV expression-ready clone library containing all known and predicted coding regions for all available strains. The expression-ready clone library will be constructed using experimentally validated clones for E. coli, baculovirus and mammalian expression systems.
- Determine the function and biological role of SARS-CoV and related proteins. This includes the characterization of the life cycle and host response, the identification and characterization of protein-protein interactions, and the identification and characterization of ligands.
- Comprehensive three-dimensional structure determination of these proteins by NMR and X-ray crystallography using rapid optimization through variations in clones, expression systems, and crystallization conditions.
- Bioinformatics prediction and correlation will be used to integrate the functional and structural data generated by the FSPS project and other groups.
For more information regarding work taking place at Scripps, see our May 2006 newsletter. See the Biodefense Proteomics Catalog for Scripps' publicly available proteomic data or view an in-depth summary of the SARS-CoV proteome.
[ click on a link above for further information or here to see page in full ]
Goal and Objectives
- Bioinformatics discovery and comprehensive proteome analysis for the functional mapping of the SARS-CoV proteome
- Create and maintain a SARS-CoV expression ready clone library containing all known and predicted coding regions for all available strains
- Determine the function and biological role of SARS-CoV and related proteins
- Comprehensive three-dimensional structure determination of these proteins by NMR and X-ray crystallography using rapid optimization through variations in clones, expression systems, and crystallization conditions
- Bioinformatics prediction and correlation used to integrate the functional and structural data generated
Presentations
- Structural Proteomics of SARS CoV: Update and Progress Toward a Functional and Structural Catalog of the SARS-CoV Proteome
Peter Kuhn, The Kuhn-Stevens Laboratories (6/10/08) (22 slides/5.8MB)
- Antiviral Effects of Antisense Morpholino Oligomers in Murine Coronavirus Infection Models
Renaud Burrer, Benjamin W. Neuman, Joey P.C. Ting, David A. Stein, Hong M. Moulton, Patrick L. Iversen, Peter Kuhn, and Michael J. Buchmeier (The Scripps Research Institute and AVI Biopharma) [5/30/07 - 1 slide/4MB]
- Functional and Structural Proteomics of SARS CoV Related Proteins
Peter Kuhn (FSPS - The Scripps Research Institute) [5/30/07 - 18 pages/794KB]
- Methods for Simultaneous Detection of Changes in the Proteome of Host and Pathogen
E.I. chen, J.H. Prieto, N.H. Bergman, E.C. Anderson, E.E. Swanson, P.C. Hanna, J.R. Yates III (The Scripps Research Institute and University of Michigan) [5/30/07 - 9 slides/569KB]
- Functional and Structural Proteomics of SARS CoV-related Proteins [10/18/04 - 37 slides/10.1MB]
Publications
- Nuclear magnetic resonance structure of the N-terminal domain of the nonstructural protein 3 from the severe acute respiratory syndrome coronavirus (Subscription to The Journal of Virology Online required to view full article) | Abstract
Serrano P, Johnson, MA, Almeida MS, Horst R, Herrmann T, Joseph JS, Neuman BW, Subramanian V, Saikatendu KS, Buchmeier MJ, Stevens RC, Kuhn P, Wüthrich K.
J. Virol. 2007 Nov;81(21):12049-60 - PMID: 17728234
- Crystal structure of a monomeric form of severe acute respiratory syndrome coronavirus endonuclease nsp15 suggests a role for hexamerization as an allosteric switch | Abstract
Joseph JS, Saikatendu KS, Subramanian V, Neuman BW, Buchmeier MJ, Stevens RC, Kuhn P.
J. Virol. 2007 Jun;81(12):6700-8 - PMID: 17409150
- Antiviral effects of antisense morpholino oligomers in murine coronavirus infection models | Abstract
Burrer R, Neuman BW, Ting JP, Stein DA, Moulton HM, Iversen PL, Kuhn P, Buchmeier MJ.
J. Virol. 2007 Jun;81(11):5637-48 - PMID: 17344287
- Ribonucleocapsid formation of severe acute respiratory syndrome coronavirus through molecular action of the N-terminal domain of N protein | Abstract
Saikatendu KS, Joseph JS, Subramanian V, Neuman BW, Buchmeier MJ, Stevens RC, Kuhn P.
J. Virol. 2007 Apr;81(8):3913-21 - PMID: 17229691
- Novel ß-barrel fold in the nuclear magnetic resonance structure of the replicase nonstructural protein 1 from the severe acute respiratory syndrome coronavirus | Abstract
Almeida MS, Johnson MA, Herrmann T, Geralt M, Wüthrich K.
J. Virol. 2007 Apr;81(7):3151-61 - PMID: 17202208
More publications
|