Austin B Moyle
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Explore the profile of Austin B Moyle including associated specialties, affiliations and a list of published articles.
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10
Citations
134
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Recent Articles
1.
Wagner W, Moyle A, Wagner N, Rempel D, Gross M
Anal Chem
. 2024 May;
96(23):9693-9703.
PMID: 38815160
Specific amino acid footprinting mass spectrometry (MS) is an increasingly utilized method for elucidating protein higher order structure (HOS). It does this by adding to certain amino acid residues a...
2.
Lin Y, Moyle A, Beaumont V, Liu L, Polleck S, Liu H, et al.
Anal Chem
. 2023 Nov;
95(46):16840-16849.
PMID: 37933954
Characterizing changes in the higher order structure (HOS) of monoclonal antibodies upon stressed conditions is critical to gaining a better understanding of the product and process. One single biophysical approach...
3.
Wu C, Wagner N, Moyle A, Feng A, Sharma N, Stubbs S, et al.
J Mol Biol
. 2023 Aug;
435(20):168241.
PMID: 37598728
Viral inclusion bodies (IBs) are potential sites of viral replication and assembly. How viral IBs form remains poorly defined. Here we describe a combined biophysical and cellular approach to identify...
4.
Moyle A, Wagner N, Wagner W, Cheng M, Gross M
Anal Chem
. 2023 Jun;
95(26):10119-10126.
PMID: 37351860
Protein footprinting mass spectrometry probes protein higher order structure and dynamics by labeling amino acid side-chains or backbone amides as a function of solvent accessibility. One category of footprinting uses...
5.
Wagner N, Moyle A, Rincon Pabon J, Gross M
Anal Chem
. 2022 Jul;
94(29):10314-10319.
PMID: 35830607
Protein footprinting is a mass spectrometry (MS)-based approach to measure protein conformational changes. One approach, specific amino acid labeling, imparts often an irreversible modification to protein side chains but requires...
6.
Moyle A, Cheng M, Wagner N, Gross M
Anal Chem
. 2022 Jan;
94(3):1520-1524.
PMID: 35019278
Protein footprinting mass spectrometry (MS), an emerging approach to elucidate higher-order structure (HOS) and binding, benefits from the iterative development of reaction strategies to expand the covalent labeling toolbox. Herein,...
7.
Wu C, Qavi A, Moyle A, Wagner N, Hachim A, Kavian N, et al.
STAR Protoc
. 2021 Oct;
2(4):100906.
PMID: 34642671
Nucleocapsid proteins are essential for SARS-CoV-2 life cycle. Here, we describe protocols to gather domain-specific insights about essential properties of nucleocapsids. These assays include dynamic light scattering to characterize oligomerization,...
8.
Ganaie S, Schwarz M, McMillen C, Price D, Feng A, Albe J, et al.
Cell
. 2021 Sep;
184(20):5163-5178.e24.
PMID: 34559985
Rift Valley fever virus (RVFV) is a zoonotic pathogen with pandemic potential. RVFV entry is mediated by the viral glycoprotein (Gn), but host entry factors remain poorly defined. Our genome-wide...
9.
Wu C, Qavi A, Hachim A, Kavian N, Cole A, Moyle A, et al.
iScience
. 2021 Jun;
24(6):102681.
PMID: 34095780
Nucleocapsid (N) encoded by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) plays key roles in the replication cycle and is a critical serological marker. Here, we characterize essential biochemical properties...
10.
Wu C, Qavi A, Hachim A, Kavian N, Cole A, Moyle A, et al.
bioRxiv
. 2020 Dec;
PMID: 33269347
Nucleocapsid protein (N) is the most abundant viral protein encoded by SARS-CoV-2, the causative agent of COVID-19. N plays key roles at different steps in the replication cycle and is...