Huhmer A.F.R.,Thermo Fisher Scientific |
Paulus A.,Life science Group |
Martin L.B.,Waters Corporation |
Millis K.,Cambridge Isotope Laboratories andover |
And 6 more authors.
Journal of Proteome Research | Year: 2013
The grand vision of the human proteome project (HPP) is moving closer to reality with the recent announcement by HUPO of the creation of the HPP consortium in charge of the development of a two-part HPP, one focused on the description of proteomes of biological samples or related to diseases (B/D-HPP) and the other dedicated to a systematic description of proteins as gene products encoded in the human genome (the C-HPP). This new initiative of HUPO seeks to identify and characterize at least one representative protein from every gene, create a protein distribution atlas and a protein pathway or network map. This vision for proteomics can be the roadmap of biological and clinical research for years to come if it delivers on its promises. The Industrial Advisory Board (IAB) to HUPO shares the visions of C-HPP. The IAB will support and critically accompany the overall project goals and the definitions of the critical milestones. The member companies are in a unique position to develop hardware and software, reagents and standards, procedures, and workflows to ensure a reliable source of tools available to the proteomics community worldwide. In collaboration with academia, the IAB member companies can and must develop the tools to reach the ambitious project goals. We offer to partner with and challenge the academic groups leading the CHPP to define both ambitious and obtainable goals and milestones to make the C-HPP a real and trusted resource for future biology. © 2012 American Chemical Society. Source
Merrill A.E.,University of Wisconsin - Madison |
Hebert A.S.,University of Wisconsin - Madison |
MacGilvray M.E.,University of Wisconsin - Madison |
Rose C.M.,University of Wisconsin - Madison |
And 7 more authors.
Molecular and Cellular Proteomics | Year: 2014
We describe a synthesis strategy for the preparation of lysine isotopologues that differ in mass by as little as 6 mDa. We demonstrate that incorporation of these molecules into the proteomes of actively growing cells does not affect cellular proliferation, and we discuss how to use the embedded mass signatures (neutron encoding (NeuCode)) for multiplexed proteome quantification by means of high-resolution mass spectrometry. NeuCode SILAC amalgamates the quantitative accuracy of SILAC with the multiplexing of isobaric tags and, in doing so, offers up new opportunities for biological investigation. We applied NeuCode SILAC to examine the relationship between transcript and protein levels in yeast cells responding to environmental stress. Finally, we monitored the time-resolved responses of five signaling mutants in a single 18-plex experiment. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc. Source