Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Kevin Jooss"'
Publikováno v:
Analytical Chemistry. 95:4059-4066
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::443ac07ba0974f4fb90a2a6b99e3589e
https://doi.org/10.1021/acs.analchem.2c04578
https://doi.org/10.1021/acs.analchem.2c04578
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::22d7da3622e779a1476601ae3c828cc2
https://pubmed.ncbi.nlm.nih.gov/35749283
https://pubmed.ncbi.nlm.nih.gov/35749283
Native mass spectrometry is a rapidly emerging technique for fast and sensitive structural analysis of protein constructs, maintaining the protein higher order structure. The coupling with electromigrative separation techniques under native condition
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9d2845f80f616be55a21bad2245e1224
https://doi.org/10.22541/au.167872031.13574357/v1
https://doi.org/10.22541/au.167872031.13574357/v1
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6137bf6daff116ce7d2d6701f37183cd
https://pubmed.ncbi.nlm.nih.gov/36416365
https://pubmed.ncbi.nlm.nih.gov/36416365
Autor:
Zachary B. Gillespie, Neil L. Kelleher, Jonathan D. Licht, Marcus A. Cheek, Amin Sobh, Sarah A. Howard, Michael-Christopher Keogh, Luis F. Schachner, Kevin Jooß, Matthew J. Meiners, Rachel Watson
Publikováno v:
Anal Chem
We report a novel platform [native capillary zone electrophoresis–top-down mass spectrometry (nCZE–TDMS)] for the separation and characterization of whole nucleosomes, their histone subunits, and post-translational modifications (PTMs). As the re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5ac31269a410e4f0c34ce0d226a6478e
https://doi.org/10.1021/acs.analchem.0c04975
https://doi.org/10.1021/acs.analchem.0c04975
Autor:
Bryon S. Drown, Kevin Jooß, Rafael D. Melani, Cameron Lloyd-Jones, Jeannie M. Camarillo, Neil L. Kelleher
Publikováno v:
Journal of proteome research. 21(5)
A functional understanding of the human body requires structure-function studies of proteins at scale. The chemical structure of proteins is controlled at the transcriptional, translational, and post-translational levels, creating a variety of produc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7e130c1f66d68051037cb49f52358226
https://pubmed.ncbi.nlm.nih.gov/35413190
https://pubmed.ncbi.nlm.nih.gov/35413190
Autor:
Friedrich Lottspeich, Kevin Jooß, Neil L. Kelleher, Michael Götze, Betty Friedrich, Ruedi Aebersold
Publikováno v:
Bioanalytik ISBN: 9783662617069
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b4390503926e594195316b54fcce8761
https://doi.org/10.1007/978-3-662-61707-6_42
https://doi.org/10.1007/978-3-662-61707-6_42
Describes the CZE-MS/MS data acquisition procedure for top-down proteomics samples using the Thermo Scientific Orbitrap Eclipse Tribrid mass spectrometer
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::eecd719359ba94ac05ba2c660efaec7b
https://doi.org/10.17504/protocols.io.btxdnpi6
https://doi.org/10.17504/protocols.io.btxdnpi6
Autor:
Marcus A. Cheek, Michael-Christopher Keogh, Kevin Jooss, Sarah A. Howard, Rachel Watson, Matthew J. Meiners, Jonathan D. Licht, Zachary B. Gillespie, Luis F. Schachner, Neil L. Kelleher
We report a novel platform (native capillary zone electrophoresis – top-down mass spectrometry; nCZE-TDMS) for the separation and characterization of whole nucleosomes, their histone subunits, and PTMs. As the repeating unit of chromatin, mononucle
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::844f8f087ef381857f938cc8e0e24cfc
https://doi.org/10.1101/2020.11.25.398925
https://doi.org/10.1101/2020.11.25.398925
Publikováno v:
Electrophoresis
Native mass spectrometry (nMS) is a rapidly growing method for the characterization of large proteins and protein complexes, preserving “native” non-covalent inter- and intramolecular interactions. Direct infusion of purified analytes into a mass
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c3143b3f02b6df7e10b15fa8a5a70cf3
https://doi.org/10.1101/2020.11.02.351247
https://doi.org/10.1101/2020.11.02.351247