Zobrazeno 1 - 10
of 27
pro vyhledávání: '"John P. McGee"'
Autor:
John P. McGee, Pei Su, Kenneth R. Durbin, Michael A. R. Hollas, Nicholas W. Bateman, G. Larry Maxwell, Thomas P. Conrads, Ryan T. Fellers, Rafael D. Melani, Jeannie M. Camarillo, Jared O. Kafader, Neil L. Kelleher
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-11 (2023)
Abstract The molecular identification of tissue proteoforms by top-down mass spectrometry (TDMS) is significantly limited by throughput and dynamic range. We introduce AutoPiMS, a single-ion MS based multiplexed workflow for top-down tandem MS (MS2)
Externí odkaz:
https://doaj.org/article/7587327dde1148caba435a60d10f292c
Autor:
John P. McGee, Pei Su, Kenneth R. Durbin, Michael A. R. Hollas, Nicholas W. Bateman, G. Larry Maxwell, Thomas P. Conrads, Ryan T. Fellers, Rafael D. Melani, Jeannie M. Camarillo, Jared O. Kafader, Neil L. Kelleher
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-2 (2023)
Externí odkaz:
https://doaj.org/article/d5ee2a0ebd7d47d29c4b70b42651e6af
Publikováno v:
Accounts of chemical research. 55(14)
Biology is driven by a vast set of molecular interactions that evolved over billions of years. Just as covalent modifications like acetylations and phosphorylations can change a protein's function, so too can noncovalent interactions with metals, sma
Autor:
John P. McGee, Michael W. Senko, Kevin Jooß, Benjamin J. Des Soye, Philip D. Compton, Neil L. Kelleher, Jared O. Kafader
Publikováno v:
Analytical chemistry. 94(48)
Charge detection mass spectrometry (CDMS) provides mass domain spectra of large and highly heterogeneous analytes. Over the past few years, we have multiplexed CDMS on Orbitrap instruments, an approach termed Individual Ion Mass Spectrometry (I
Autor:
Pei Su, John P. McGee, Kenneth R. Durbin, Michael A. R. Hollas, Manxi Yang, Elizabeth K. Neumann, Jamie L. Allen, Bryon S. Drown, Fatma Ayaloglu Butun, Joseph B. Greer, Bryan P. Early, Ryan T. Fellers, Jeffrey M. Spraggins, Julia Laskin, Jeannie M. Camarillo, Jared O. Kafader, Neil L. Kelleher
Publikováno v:
Science advances. 8(32)
Imaging of proteoforms in human tissues is hindered by low molecular specificity and limited proteome coverage. Here, we introduce proteoform imaging mass spectrometry (PiMS), which increases the size limit for proteoform detection and identification
Autor:
Michael W. Senko, Ping Yip, Neil L. Kelleher, Rafael D. Melani, Philip D. Compton, John P. McGee, Jared O. Kafader
Publikováno v:
Anal Chem
Native mass spectrometry involves transferring large biomolecular complexes into the gas phase, enabling the characterization of their composition and stoichiometry. However, the overlap in distributions created by residual solvation, ionic adducts,
Autor:
John P. McGee, Rafael D. Melani, Neil L. Kelleher, Philip D. Compton, Romain Huguet, Michael P. Goodwin, Graeme C. McAlister, Michael W. Senko
Publikováno v:
J Am Soc Mass Spectrom
Intact protein mass spectrometry (MS) via electrospray-based methods is often degraded by low-mass contaminants, which can suppress the spectral quality of the analyte of interest via space-charge effects. Consequently, selective removal of contamina
Publikováno v:
American Journal of Biomedical Science & Research. 6:416-425
Autor:
Pei Su, John P. McGee, Kenneth R. Durbin, Michael A. R. Hollas, Manxi Yang, Elizabeth K. Neumann, Jamie L. Allen, Bryon S. Drown, Fatma Ayaloglu Butun, Joseph B. Greer, Bryan P. Early, Ryan T. Fellers, Jeffrey M. Spraggins, Julia Laskin, Jeannie M. Camarillo, Jared O. Kafader, Neil L. Kelleher
Imaging of proteoforms in human tissues is hindered by low molecular specificity and limited proteome coverage. Here, we introduce proteoform imaging mass spectrometry (PiMS), which increases the size limit for proteoform detection and identification
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::84625188e5d50a57e1c1d677c03a9789
https://doi.org/10.1101/2021.12.07.471638
https://doi.org/10.1101/2021.12.07.471638
Autor:
Lena Al-Harthi, Young Ah Goo, Neil L. Kelleher, Cameron M. Lloyd-Jones, Rafael D. Melani, Jeannie M. Camarillo, Eleonora Forte, Henrique S. Seckler, Bryon Drown, Richard D. LeDuc, Michael Hollas, Beverly E. Sha, Paul M. Thomas, Pavan P. Bhimalli, Basil Baby Mattamana, Voislav Blagojevic, John P. McGee, Jared O. Kafader, Jeffrey R Schneider, Ryan T. Fellers, Byoung-Kyu Cho, Philip D. Compton, Bryan P. Early, Michelle K Ash, Fernanda Negrão, Benjamin J. Des Soye
Publikováno v:
medRxiv
Journal of Proteome Research
Journal of Proteome Research
Methods of antibody detection are used to assess exposure or immunity to a pathogen. Here, we presentIg-MS, a novel serological readout that captures the immunoglobulin (Ig) repertoire at molecular resolution, including entire variable regions in Ig
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1074d56e3e9640edb88b3e9fb4880306
https://doi.org/10.1101/2021.07.06.21259226
https://doi.org/10.1101/2021.07.06.21259226