Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Nicholas B. Borotto"'
Publikováno v:
The Analyst. 148:1534-1542
Here, we demonstrate that protein ions can be dissociated prior to mobility analysis in a trapped ion mobility spectrometry device. Generated product ions are mobility separated enabling facile assignment of near isobaric ions.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4db9f76e168927961c8cfc3f240b3151
https://doi.org/10.1039/d2an01682f
https://doi.org/10.1039/d2an01682f
Publikováno v:
Journal of the American Society for Mass Spectrometry. 33:83-89
Native mass spectrometry and collision-induced unfolding (CIU) workflows continue to grow in utilization due to their ability to rapidly characterize protein conformation and stability. To perform these experiments, the instrument must be capable of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fbf4c3fefcdbad460d9388c4e911da4b
https://doi.org/10.1021/jasms.1c00273
https://doi.org/10.1021/jasms.1c00273
Publikováno v:
Analytical Chemistry. 93:9959-9964
Ion mobility separations (IMS) have increasingly been coupled with mass spectrometry to increase peak capacity and deconvolute complex mass spectra in proteomics workflows. IMS separations can be integrated prior to or following the collisional activ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9b6c93d42289c141894594f3b78fcc35
https://doi.org/10.1021/acs.analchem.1c01188
https://doi.org/10.1021/acs.analchem.1c01188
Native mass spectrometry and collision-induced unfolding (CIU) workflows continue to grow in utilization due to their abil-ity to rapidly characterize protein conformation and stability. To perform these experiments, the instrument must be capa-ble o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cf0f5ce37e27bd23d82041cd48c3e4be
https://doi.org/10.33774/chemrxiv-2021-r72x1-v2
https://doi.org/10.33774/chemrxiv-2021-r72x1-v2
Autor:
Christine Akiki, Nicholas B. Borotto, Blaise G. Arden, William Warren, Brittney Burant, Richard W. Vachet
Publikováno v:
Anal Chem
Obtaining kinetic and thermodynamic information for protein amyloid formation can yield new insight into the mechanistic details of this biomedically important process. The kinetics of the structural change that initiates the amyloid pathway, however
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6451dd41dac7b6414993266ef1560e8c
https://europepmc.org/articles/PMC7206453/
https://europepmc.org/articles/PMC7206453/
Publikováno v:
Biochemistry. 56:1095-1104
β-2-Microglobulin (β2m) forms amyloid fibrils in the joints of patients undergoing dialysis treatment as a result of kidney failure. One of the ways in which β2m can be induced to form amyloid fibrils in vitro is via incubation with stoichiometric
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::25028089afe550139e0f4b13a5a5bcf1
https://doi.org/10.1021/acs.biochem.6b01198
https://doi.org/10.1021/acs.biochem.6b01198
Publikováno v:
J Am Soc Mass Spectrom
Hydrogen/deuterium exchange coupled with mass spectrometry (HDX MS) has become a powerful method to characterize protein conformational dynamics. Workflows typically utilize pepsin digestion prior to MS analysis to yield peptide level structural reso
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::41abdb60895a0443b8c82051fdf63c4d
https://pubmed.ncbi.nlm.nih.gov/30805882
https://pubmed.ncbi.nlm.nih.gov/30805882
Autor:
Brent R. Martin, Nicholas B. Borotto, Christina A T M B Tom, Kristina Håkansson, Kevin M Ileka
Tandem mass spectrometry (MS/MS) is the primary method for discovering, identifying, and localizing post-translational modifications (PTMs) in proteins. However, conventional positive ion mode collision induced dissociation (CID)-based MS/MS often fa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::481fadcbc38ea0c8766233636c0a50e0
https://europepmc.org/articles/PMC6235672/
https://europepmc.org/articles/PMC6235672/
Investigating Therapeutic Protein Structure with Diethylpyrocarbonate Labeling and Mass Spectrometry
Autor:
Richard W. Vachet, Robert C. Vaughan, Nicholas B. Borotto, John E. Hale, Stephen R. Hollingsworth, Eric M. Graban, Yuping Zhou
Publikováno v:
Analytical Chemistry. 87:10627-10634
Protein therapeutics are rapidly transforming the pharmaceutical industry. Unlike for small molecule therapeutics, current technologies are challenged to provide the rapid, high resolution analyses of protein higher order structures needed to ensure
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c8cdc0c45fef665f8450081f5bd66c3b
https://doi.org/10.1021/acs.analchem.5b03180
https://doi.org/10.1021/acs.analchem.5b03180
Publikováno v:
Analytical chemistry. 89(16)
Protein S-sulfinylation (R-SO2−) and S-sulfonylation (R-SO3−) are irreversible oxidative post-translational modifications of cysteine residues. Greater than 5% of cysteines are reported to occupy these higher oxidation states, which effectively i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff7a8f54720a3c4bcde016790412ebf3
https://pubmed.ncbi.nlm.nih.gov/28708386
https://pubmed.ncbi.nlm.nih.gov/28708386