Zobrazeno 1 - 10
of 90
pro vyhledávání: '"Matthew F. Bush"'
Autor:
Guangfeng Zhou, Domnita-Valeria Rusnac, Hahnbeom Park, Daniele Canzani, Hai Minh Nguyen, Lance Stewart, Matthew F. Bush, Phuong Tran Nguyen, Heike Wulff, Vladimir Yarov-Yarovoy, Ning Zheng, Frank DiMaio
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-14 (2024)
Abstract Structure-based virtual screening is a key tool in early drug discovery, with growing interest in the screening of multi-billion chemical compound libraries. However, the success of virtual screening crucially depends on the accuracy of the
Externí odkaz:
https://doaj.org/article/29a1302972a44e30ab683de7520641e9
Autor:
Emily L. Pruitt, Rutan Zhang, Dylan H. Ross, Nathaniel K. Ashford, Xi Chen, Francis Alonzo, Matthew F. Bush, Brian J. Werth, Libin Xu
Publikováno v:
mSphere, Vol 8, Iss 6 (2023)
ABSTRACTStaphylococcus aureus only synthesizes straight-chain saturated fatty acids (SCFAs) or branched-chain saturated fatty acids via the type II fatty acid synthesis (FASII) pathway, but as a highly adaptive pathogen, S. aureus can also utilize ho
Externí odkaz:
https://doaj.org/article/c835f30f3cbf4a7ab932dd1f826ef968
Publikováno v:
ASPET 2023 Annual Meeting Abstract - Drug Metabolism and Disposition (DMD).
Autor:
Theresa A. Gozzo, Matthew F. Bush
Publikováno v:
Mass Spectrometry Reviews.
Publikováno v:
Annual Review of Analytical Chemistry. 16
Recent developments in ion mobility (IM) technology have expanded the capability to separate and characterize gas-phase ions of biomolecules, especially when paired with mass spectrometry. This next generation of IM technology has been ushered in by
Native ion mobility (IM) mass spectrometry (MS) is used to probe the size, shape, and assembly of biomolecular complexes. IM-IM-MS can increase the amount of information available in structural studies by isolating subpopulations of structures for fu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::802bb64525859e4c758527f476aba377
https://doi.org/10.26434/chemrxiv-2023-lsts3
https://doi.org/10.26434/chemrxiv-2023-lsts3
Publikováno v:
Proceedings of the National Academy of Sciences. 120
Small heat-shock proteins (sHSPs) are a widely expressed family of ATP-independent molecular chaperones that are among the first responders to cellular stress. Mechanisms by which sHSPs delay aggregation of client proteins remain undefined. sHSPs hav
Autor:
Christopher N Woods, Lindsey D Ulmer, Maria K Janowska, Natalie L Stone, Ellie I James, Miklos Guttman, Matthew F Bush, Rachel E Klevit
Small heat shock proteins (sHSPs) are chaperones whose importance in protein homeostasis is exemplified by dozens of missense mutations associated with tissue-specific disease states. Despite decades of studies, the structure, dynamics, and mechanism
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::27f957b193fd5e65cd4d4016255409c6
https://doi.org/10.1101/2022.05.30.493970
https://doi.org/10.1101/2022.05.30.493970
Autor:
Abhigya Mookherjee, Sanjit S. Uppal, Matthew F. Bush, Miklos Guttman, Sarah E. Beasley, Rick Harkewicz
Publikováno v:
Anal Chem
Mass spectrometry (MS) has become a primary tool for identifying and quantifying biological molecules. In combination with other orthogonal techniques, such as gas-phase hydrogen/deuterium exchange (gHDX), MS is also capable of probing the structure
Publikováno v:
Anal Chem
Human cells make use of hundreds of unique ubiquitin E3 ligases to ensure proteome fidelity and control cellular functions by promoting protein degradation. These processes require exquisite selectivity, but the individual roles of most E3s remain po