Zobrazeno 1 - 10
of 37
pro vyhledávání: '"Justin P. Lomont"'
Autor:
Nicole M. Ralbovsky, Randal J. Soukup, Justin P. Lomont, Mackenzie L. Lauro, Amanda Gulasarian, Anumita Saha-Shah, Michael A. Winters, Douglas D. Richardson, Sheng-Ching Wang, Ian Mangion, Joseph P. Smith
Publikováno v:
The Analyst. 147:378-386
Process analytical technology was used to monitor formation of a stable emulsion product, with results providing improved understanding of emulsion-based vaccine adjuvant formation processes.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3464034c66f72fd9bf2e651c423534a5
https://doi.org/10.1039/d1an01797g
https://doi.org/10.1039/d1an01797g
Autor:
Nicole M. Ralbovsky, Justin P. Lomont, Xiaodong Bu, Jennifer V. Obligacion, Zachary E. X. Dance, Joseph P. Smith, Benjamin F. Mann
Publikováno v:
Organic Process Research & Development. 25:1402-1413
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::92ff55d89c92e06d94e64bed12f4383f
https://doi.org/10.1021/acs.oprd.1c00091
https://doi.org/10.1021/acs.oprd.1c00091
Autor:
Erin R. Birdsall, Vivek Saraswat, Joshua S. Ostrander, Benjamin R. Feingold, Michael S. Arnold, Justin P. Lomont, Martin T. Zanni, Megan K. Petti, Kacie L. Rich
Publikováno v:
The Journal of Physical Chemistry Letters. 10:3836-3842
Immunosensors use antibodies to detect and quantify biomarkers of disease, though the sensors often lack structural information. We create a surface-sensitive two-dimensional infrared (2D IR) spectroscopic immunosensor for studying protein structures
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b406f83a8302e8bc73d58bb75371ce33
https://doi.org/10.1021/acs.jpclett.9b01267
https://doi.org/10.1021/acs.jpclett.9b01267
Autor:
Justin P, Lomont, Joseph P, Smith
Publikováno v:
Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy. 274:121068
Cysteine serves a wide range of important biological and chemical functions and may have an association to neurodegenerative disease and cancer. Rapid, accurate analytical methods for cysteine detection are thus highly desirable. In this work, we rep
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2bd49d9efc28be9eb924e17b155789da
https://doi.org/10.1016/j.saa.2022.121068
https://doi.org/10.1016/j.saa.2022.121068
Publikováno v:
J Phys Chem Lett
There is enormous interest in measuring amyloid fibril structures, but most structural studies measure fibril formation in vitro using aqueous buffer. Ideally, one would like to measure fibril structure and mechanism under more physiological conditio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b8d0bc0341b7ec3dfaf1e5c8a592ab2
https://europepmc.org/articles/PMC7968077/
https://europepmc.org/articles/PMC7968077/
Autor:
Ian Mangion, Patrick Mchugh, Nicole M. Ralbovsky, Janelle Konietzko, Serge Ruccolo, Justin P. Lomont, Sheng-Ching Wang, Joseph P. Smith
Publikováno v:
International Journal of Pharmaceutics. 611:121324
The use of protection groups to shield a functional group during a synthesis is employed throughout many reactions and organic syntheses. The role of a protection group can be vital to the success of a reaction, as well as increase reaction yield and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2cc395fc917f77da683aaabf3da4c35f
https://doi.org/10.1016/j.ijpharm.2021.121324
https://doi.org/10.1016/j.ijpharm.2021.121324
Publikováno v:
The Journal of Physical Chemistry B. 122:1771-1780
Two-dimensional spectroscopy is a powerful tool for extracting structural and dynamic information from a wide range of chemical systems. We provide a brief overview of the ways in which two-dimensional visible and infrared spectroscopies are being ap
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::55ec5f677f08c277a52fca5aa51bfbdd
https://doi.org/10.1021/acs.jpcb.7b11370
https://doi.org/10.1021/acs.jpcb.7b11370
Publikováno v:
Chemical Science
Human islet amyloid polypeptide (hIAPP) aggregates into fibrils through oligomers that have been postulated to contain α-helices as well as β-sheets.
Human islet amyloid polypeptide (hIAPP) aggregates into fibrils through oligomers that have b
Human islet amyloid polypeptide (hIAPP) aggregates into fibrils through oligomers that have b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1b7720b453dbd778f4b41c98bd9777cb
https://doi.org/10.1039/c7sc03789a
https://doi.org/10.1039/c7sc03789a
Publikováno v:
Journal of the American Chemical Society, vol 139, iss 46
Transiently populated oligomers formed en route to amyloid fibrils may constitute the most toxic aggregates associated with many amyloid-associated diseases. Most nucleation theories used to describe amyloid aggregation predict low oligomer concentra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cb0cf329de45f20483a74a48fb9abd17
https://doi.org/10.1021/jacs.7b08830
https://doi.org/10.1021/jacs.7b08830
Publikováno v:
The Journal of Physical Chemistry B. 121:8935-8945
We report the transition dipole strengths and frequencies of the amyloid β-sheet amide I mode for the aggregated proteins amyloid-β1–40, calcitonin, α-synuclein, and glucagon. According to standard vibrational coupling models for proteins, the f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::94e804b3ee4a04e5542ac7f413f4525a
https://doi.org/10.1021/acs.jpcb.7b06826
https://doi.org/10.1021/acs.jpcb.7b06826