Zobrazeno 1 - 10
of 50
pro vyhledávání: '"Brian L. Frey"'
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-9 (2021)
Protein turnover underpins biology but is challenging to measure in vivo across the entire proteome. Here, the authors provide a comprehensive resource of protein turnover in mouse tissues and develop a visualization platform to analyze these data.
Externí odkaz:
https://doaj.org/article/359b0c6145de48979dd2971a3e56b364
Autor:
Anthony J. Cesnik, Bing Yang, Andrew Truong, Tyler Etheridge, Michele Spiniello, Maisie I. Steinbrink, Michael R. Shortreed, Brian L. Frey, David F. Jarrard, Lloyd M. Smith
Publikováno v:
Translational Oncology, Vol 11, Iss 3, Pp 808-814 (2018)
INTRODUCTION: The molecular mechanisms underlying aggressive versus indolent disease are not fully understood. Recent research has implicated a class of molecules known as long noncoding RNAs (lncRNAs) in tumorigenesis and progression of cancer. Our
Externí odkaz:
https://doaj.org/article/946ec19bd6de47cfb548eee57a882295
Autor:
Rachel M. Miller, Rachel A. Knoener, Bayleigh E. Benner, Brian L. Frey, Mark Scalf, Michael R. Shortreed, Nathan M. Sherer, Lloyd M. Smith
Publikováno v:
J Proteome Res
Human immunodeficiency virus type 1 (HIV-1) remains a deadly infectious disease despite existing antiretroviral therapies. A comprehensive understanding of the specific mechanisms of viral infectivity remains elusive and currently limits the developm
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1455a18ed0c3f83ed19bcae11ee6cb1d
https://doi.org/10.1021/acs.jproteome.1c00867
https://doi.org/10.1021/acs.jproteome.1c00867
Autor:
Austin V. Carr, Brian L. Frey, Mark Scalf, Anthony J. Cesnik, Zach Rolfs, Kyndal A. Pike, Bing Yang, Mark P. Keller, David F. Jarrard, Michael R. Shortreed, Lloyd M. Smith
Publikováno v:
J Proteome Res
Interpreting proteomics data remains challenging due to the large number of proteins that are quantified by modern mass spectrometry methods. Weighted gene correlation network analysis (WGCNA) can identify groups of biologically related proteins usin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ac5e64e8362d6e726bf3ef10f2422dd4
https://doi.org/10.1021/acs.jproteome.1c00756
https://doi.org/10.1021/acs.jproteome.1c00756
Autor:
Lei Liu, Lloyd M. Smith, Brian L. Frey, Rachel M. Miller, Leah V. Schaffer, Zach Rolfs, Robert J. Millikin, Michael R. Shortreed
Publikováno v:
J Proteome Res
Journal of proteome research, vol 20, iss 4
Journal of proteome research, vol 20, iss 4
MetaMorpheus is a free, open-source software program for the identification of peptides and proteoforms from data-dependent acquisition tandem MS experiments. There is inherent uncertainty in these assignments for several reasons, including the limit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ceb28ee3b657779a2350e4b2885a0247
https://doi.org/10.1021/acs.jproteome.0c00838
https://doi.org/10.1021/acs.jproteome.0c00838
Autor:
Lei Lu, Brian L. Frey, Robert J. Millikin, Khairina Ibrahim, Lloyd M. Smith, Rachel M. Miller, Michael R. Shortreed, Anthony J. Cesnik
Publikováno v:
J Proteome Res
Proteoforms are the workhorses of the cell, and subtle differences between their amino acid sequence or post-translational modifications (PTMs) can change their biological function. To most effectively identify and quantify proteoforms in genetically
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f58931c1c9cd6935c724adf18490632a
https://doi.org/10.1101/2020.06.08.140681
https://doi.org/10.1101/2020.06.08.140681
Autor:
Leah V. Schaffer, Mark Scalf, Lloyd M. Smith, Brian L. Frey, Yunxiang Dai, Stefan K. Solntsev, Michael R. Shortreed, Anthony J. Cesnik
Publikováno v:
Journal of Proteome Research. 16:4156-4165
A proteoform family is a group of related molecular forms of a protein (proteoforms) derived from the same gene. We have previously described a strategy to identify proteoforms and elucidate proteoform families in complex mixtures of intact proteins.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::06bebe6ff8b41036674c85a340a8b89e
https://doi.org/10.1021/acs.jproteome.7b00516
https://doi.org/10.1021/acs.jproteome.7b00516
Autor:
Mark Scalf, Craig D. Wenger, Michael R. Shortreed, Brian L. Frey, Leah V. Schaffer, Lloyd M. Smith, Qiyao Li
Publikováno v:
Journal of Proteome Research
A new global post-translational modification (PTM) discovery strategy, G-PTM-D, is described. A proteomics database containing UniProt-curated PTM information is supplemented with potential new modification types and sites discovered from a first-rou
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7fa66be2579786baf7193794ecae4ddf
https://doi.org/10.1021/acs.jproteome.6b00034
https://doi.org/10.1021/acs.jproteome.6b00034
Autor:
Katherine E. Buxton, Michael R. Shortreed, Yunxiang Dai, Brian L. Frey, Mark Scalf, Robert J. Millikin, Lloyd M. Smith, Rachel M. Miller, Leah V. Schaffer
Publikováno v:
J Proteome Res
Complex human biomolecular processes are made possible by the diversity of human proteoforms. Constructing proteoform families, groups of proteoforms derived from the same gene, is one way to represent this diversity. Comprehensive, high-confidence i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5ce1a3da74326215efd784c378c04d67
https://pubmed.ncbi.nlm.nih.gov/31479276
https://pubmed.ncbi.nlm.nih.gov/31479276
Autor:
Brian L. Frey, Rachel A. Knoener, Mark Scalf, Anthony J. Cesnik, Lloyd M. Smith, Michael R. Shortreed
Publikováno v:
Journal of Proteome Research
Proteomics is presently dominated by the "bottom-up" strategy, in which proteins are enzymatically digested into peptides for mass spectrometric identification. Although this approach is highly effective at identifying large numbers of proteins prese
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e8a27f60806f124633e554e56e35688c
https://doi.org/10.1021/acs.jproteome.5b01090
https://doi.org/10.1021/acs.jproteome.5b01090