Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Edwin E. Escobar"'
Autor:
Molly S. Blevins, Kyle J. Juetten, Virginia K. James, Jamie P. Butalewicz, Edwin E. Escobar, Michael B. Lanzillotti, James D. Sanders, Kyle L. Fort, Jennifer S. Brodbelt
Publikováno v:
Journal of Proteome Research. 21:2493-2503
The direct correlation between proteoforms and biological phenotype necessitates the exploration of mass spectrometry (MS)-based methods more suitable for proteoform detection and characterization. Here, we couple nano-hydrophobic interaction chromat
Autor:
Joshua E Mayfield, Seema Irani, Edwin E Escobar, Zhao Zhang, Nathaniel T Burkholder, Michelle R Robinson, M Rachel Mehaffey, Sarah N Sipe, Wanjie Yang, Nicholas A Prescott, Karan R Kathuria, Zhijie Liu, Jennifer S Brodbelt, Yan Zhang
Publikováno v:
eLife, Vol 8 (2019)
The Positive Transcription Elongation Factor b (P-TEFb) phosphorylates Ser2 residues of the C-terminal domain (CTD) of the largest subunit (RPB1) of RNA polymerase II and is essential for the transition from transcription initiation to elongation in
Externí odkaz:
https://doaj.org/article/53e0122eb0c34ddbb874f06e2b7e518b
Autor:
Gregory K. Potts, Edwin E. Escobar, Janice Lee, Damien B. Ready, Jennifer S. Brodbelt, Eleanor Watts, Alayna M. George Thompson, Melanie J. Patterson
Publikováno v:
Analytical Chemistry. 93:13134-13142
Identifying major histocompatibility complex (MHC) class I immunopeptide antigens represents a key step in the development of immune-based targeted therapeutics and vaccines. However, the complete characterization of these antigens by tandem mass spe
Publikováno v:
J Am Chem Soc
The critical role of site-specific phosphorylation in eukaryotic transcription has motivated efforts to decipher the complex phosphorylation patterns exhibited by the carboxyl-terminal domain (CTD) of RNA polymerase II. Phosphorylation remains a chal
Autor:
Edwin E. Escobar, Jennifer S. Brodbelt, Yan Zhang, R Yvette Moreno, Mukesh Kumar Venkat Ramani, Blase M LeBlanc
Publikováno v:
RSC Chemical Biology
RNA polymerase II (RNAP II) is one of the primary enzymes responsible for expressing protein-encoding genes and some small nuclear RNAs. The enigmatic carboxy-terminal domain (CTD) of RNAP II and its phosphorylation state are critically important in
Autor:
Edwin E. Escobar, Shuaishuai Wang, Rupanjan Goswami, Michael B. Lanzillotti, Lei Li, Jason S. McLellan, Jennifer S. Brodbelt
Publikováno v:
Anal Chem
Characterization of protein glycosylation by tandem mass spectrometry remains challenging owing to the vast diversity of oligosaccharides bound to proteins, the variation in monosaccharide linkage patterns, and the lability of the linkage between the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de79f2ba9b191347a5cdd87f9e4d697f
https://europepmc.org/articles/PMC9272412/
https://europepmc.org/articles/PMC9272412/
Autor:
James D. Sanders, Samuel W. Shields, Edwin E. Escobar, Michael B. Lanzillotti, Jamie P. Butalewicz, Virginia K. James, Molly S. Blevins, Sarah N. Sipe, Jennifer S. Brodbelt
Publikováno v:
Analytical chemistry. 94(10)
The structural diversity of phospholipids plays a critical role in cellular membrane dynamics, energy storage, and cellular signaling. Despite its importance, the extent of this diversity has only recently come into focus, largely owing to advances i
Autor:
Edwin E. Escobar, Erin H. Seeley, Jesús E. Serrano-Negrón, David J. Vocadlo, Jennifer S. Brodbelt
Publikováno v:
Cancers
Volume 15
Issue 4
Pages: 1224
Volume 15
Issue 4
Pages: 1224
Post-translational O-glycosylation of proteins via the addition of N-acetylglucosamine (O-GlcNAc) is a regulator of many aspects of cellular physiology. Processes driven by perturbed dynamics of O-GlcNAcylation modification have been implicated in ca
Publikováno v:
The FASEB Journal. 35
Autor:
Jennifer S. Brodbelt, Keith R. Morgenstern, Michael B. Lanzillotti, George Georgiou, M. Rachel Mehaffey, Edwin E. Escobar, Jiwon Lee, Jiwon Jung
Publikováno v:
Anal Chem
As the importance of effective vaccines and the role of protein therapeutics in the drug industry continue to expand, alternative strategies to characterize protein complexes are needed. Mass spectrometry (MS) in conjunction with enzymatic digestion