Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Jason J. Cournoyer"'
Autor:
Susan Elliott, Norman Buroker, Jason J. Cournoyer, Anna M. Potier, Joseph D. Trometer, Carole Elbin, Mack J. Schermer, Jaana Kantola, Aaron Boyce, Frantisek Turecek, Michael H. Gelb, C. Ronald Scott
Publikováno v:
Data in Brief, Vol 8, Iss , Pp 915-924 (2016)
In this data article we provide a detailed standard operating procedure for performing a tandem mass spectrometry, multiplex assay of 6 lysosomal enzymes for newborn screening of the lysosomal storage diseases Mucopolysaccharidosis-I, Pompe, Fabry, N
Externí odkaz:
https://doaj.org/article/c73301248a7d40c9a109b27c9bec71a8
Autor:
Jason J. Cournoyer, Subhakar Dey
Publikováno v:
Rapid Communications in Mass Spectrometry. 34
Mass spectrometry (MS) generally delivers more accurate results than immunoassay (IA) for certain clinically relevant analytes, but IA is still the more prevalent methodology used by clinical laboratories because of barriers to MS adoption, such as l
Publikováno v:
Journal of the American Society for Mass Spectrometry. 18:48-56
Relative quantitation of aspartyl and isoaspartyl residue mixtures from asparagine deamidation is demonstrated using electron capture dissociation without prior HPLC separation. The method utilizes the linear relationship found between the relative a
Publikováno v:
Journal of the American Society for Mass Spectrometry. 17:1605-1615
The relative abundances of fragment ions in electron capture dissociation (ECD) are often greatly affected by the secondary and tertiary structures of the precursor ion, and have been used to derive the gas-phase conformations of the protein ions. In
Publikováno v:
Journal of the American Society for Mass Spectrometry. 17:1429-1436
To further test the hypothesis that electron capture dissociation (ECD) involves long-lived radical intermediates and radical migration occurs within these intermediates before fragmentation, radical trap moieties were attached to peptides with the a
Publikováno v:
Analytical Chemistry. 78:1264-1271
A nonenzymatic posttranslational modification of proteins and peptides is the spontaneous deamidation of asparaginyl residues via a succinimide intermediate to form a varying mixture of aspartyl and isoaspartyl residues. The isoaspartyl residue is ge
Autor:
Eric Fallows, Lucy Waskell, Jason L. Pittman, Catherine E. Costello, Jason J. Cournoyer, Peter B. O’Connor, Vera B. Ivleva
Publikováno v:
Protein Science. 14:452-463
Deamidation of asparaginyl and isomerization of aspartyl residues in proteins proceed through a succinimide intermediate producing a mixture of aspartyl and isoaspartyl residues. Isoaspartic acid is an isomer of aspartic acid with the C(beta) incorpo
Autor:
Gianine M. Figliozzi, and Taline Makdessian, Pascal P. Fantauzzi, Jason J. Cournoyer, Tushar Kshirsagar, Bing Yan
Publikováno v:
Journal of Combinatorial Chemistry. 4:120-124
We report the development of a sensitive and specific color test for the detection of the presence of resin-bound aldehyde groups using 4-amino-3-hydrazino-5-mercapto-1,2,4-triazole (Purpald). Aldehyde resin turns dark-brown to purple after a 5 min r
The effect of infrared (IR) irradiation on the electron capture dissociation (ECD) fragmentation pattern of peptide ions was investigated. IR heating increases the internal energy of the precursor ion, which often amplifies secondary fragmentation, r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f53c1932c67ee9c32025fd4b6cd28c5a
https://europepmc.org/articles/PMC3117249/
https://europepmc.org/articles/PMC3117249/
Autor:
Jason J. Cournoyer, Peter B. O’Connor
Publisher Summary Deamidation of asparagine (Asn) and glutamine (Gln) residues to their acidic counterparts is a common posttranslational modification (PTM) on proteins. Deamidation occurs nonenzymatically in solution and with the exception of –NP
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0063240a02235f113ea977640473ab41
https://doi.org/10.1016/s0166-526x(08)00216-x
https://doi.org/10.1016/s0166-526x(08)00216-x