User:Sarah A Boswell: Difference between revisions
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We have developed a novel mass spectrometry method that promises to be sufficiently cheap, straightforward and reliable to provide high-throughput measurements of the absolute level of proteins in cells and tissues, and at the same time both identify peptides that are post-translationally modified and quantite the level of modification. Our primary goal in this proposal is to comprehensively characterize 1,000 proteins and thereby to demonstrate that it is possible to scale the technology to make such measurements at a quasi-genomic level across multiple cell types (6 cell lines). | We have developed a novel mass spectrometry method that promises to be sufficiently cheap, straightforward and reliable to provide high-throughput measurements of the absolute level of proteins in cells and tissues, and at the same time both identify peptides that are post-translationally modified and quantite the level of modification. Our primary goal in this proposal is to comprehensively characterize 1,000 proteins and thereby to demonstrate that it is possible to scale the technology to make such measurements at a quasi-genomic level across multiple cell types (6 cell lines). | ||
==Research interests== | ==Other Research interests== | ||
<!-- Feel free to add brief descriptions to your research interests as well --> | <!-- Feel free to add brief descriptions to your research interests as well --> | ||
# | # Protein folding and misfolding | ||
# | # The cellular response to reactive oxygen stress (ROS) | ||
# | # The unfolded protein response (UPR) | ||
==Publications== | ==Publications== | ||
Revision as of 07:18, 9 June 2011
I am a new member of OpenWetWare!
Contact Info
Sarah A Boswell
Harvard Medical School
200 Longwood Ave.
Boston, MA 02115
I work in the Springer_Lab at Harvard Medical School. I learned about OpenWetWare from a grad student in lab.
Education
- 2003, PhD, Rensselaer Polytechnic Institute
Dissertation: The folding of the dimeric protein factor for inversion stimulation
- 1999, BS, Rensselaer Polytechnic Institute
Research Project in the Springer Lab - FLEXIQuant
We have developed a novel mass spectrometry method that promises to be sufficiently cheap, straightforward and reliable to provide high-throughput measurements of the absolute level of proteins in cells and tissues, and at the same time both identify peptides that are post-translationally modified and quantite the level of modification. Our primary goal in this proposal is to comprehensively characterize 1,000 proteins and thereby to demonstrate that it is possible to scale the technology to make such measurements at a quasi-genomic level across multiple cell types (6 cell lines).
Other Research interests
- Protein folding and misfolding
- The cellular response to reactive oxygen stress (ROS)
- The unfolded protein response (UPR)
Publications
- Goldbeter A and Koshland DE Jr. An amplified sensitivity arising from covalent modification in biological systems. Proc Natl Acad Sci U S A. 1981 Nov;78(11):6840-4. DOI:10.1073/pnas.78.11.6840 |
- JACOB F and MONOD J. Genetic regulatory mechanisms in the synthesis of proteins. J Mol Biol. 1961 Jun;3:318-56. DOI:10.1016/s0022-2836(61)80072-7 |
leave a comment about a paper here
- ISBN:0879697164
