Zobrazeno 1 - 10
of 69
pro vyhledávání: '"David S Burz"'
Publikováno v:
PLoS ONE, Vol 15, Iss 4, p e0232015 (2020)
Transient, site-specific, or so-called quinary, interactions are omnipresent in live cells and modulate protein stability and activity. Quinary intreactions are readily detected by in-cell NMR spectroscopy as severe broadening of the NMR signals. Int
Externí odkaz:
https://doaj.org/article/4df97fac55fe4660adefe76eaa44b24b
Publikováno v:
PLoS ONE, Vol 8, Iss 9, p e74576 (2013)
The Mycobacterium tuberculosis proteasome is required for maximum virulence and to resist killing by the host immune system. The prokaryotic ubiquitin-like protein, Pup-GGE, targets proteins for proteasome-mediated degradation. We demonstrate that Pu
Externí odkaz:
https://doaj.org/article/6ed04d052bc44f2f977170003555ade9
Publikováno v:
PLoS ONE, Vol 8, Iss 6, p e65180 (2013)
Peptide aptamers are small proteins containing a randomized peptide sequence embedded into a stable protein scaffold, such as Thioredoxin. We developed a robust method for building a Combinatorial Library of Improved Peptide aptamers (CLIPs) of high
Externí odkaz:
https://doaj.org/article/4f258d2221a34cfe809aac64924a08e1
Autor:
Nathaniel C Cady, Kurt A McKean, Jason Behnke, Roman Kubec, Aaron P Mosier, Stephen H Kasper, David S Burz, Rabi A Musah
Publikováno v:
PLoS ONE, Vol 7, Iss 6, p e38492 (2012)
Using a microplate-based screening assay, the effects on Pseudomonas aeruginosa PAO1 biofilm formation of several S-substituted cysteine sulfoxides and their corresponding disulfide derivatives were evaluated. From our library of compounds, S-phenyl-
Externí odkaz:
https://doaj.org/article/fc1dd0c4f0b34daf88b75398dc1509d4
Autor:
David S Burz, Alexander Shekhtman
Publikováno v:
PLoS ONE, Vol 3, Iss 7, p e2571 (2008)
Biochemistry and structural biology are undergoing a dramatic revolution. Until now, mostly in vitro techniques have been used to study subtle and complex biological processes under conditions usually remote from those existing in the cell. We develo
Externí odkaz:
https://doaj.org/article/399d283899af45b6bd9e67c9901d5daa
Autor:
Nicholas Sciolino, Anna Liu, Leonard Breindel, David S. Burz, Todd Sulchek, Alexander Shekhtman
Publikováno v:
Communications Biology, Vol 5, Iss 1, Pp 1-1 (2022)
Externí odkaz:
https://doaj.org/article/217a73240739488fa89c1f488a3fcd01
Autor:
Nicholas, Sciolino, Sergey, Reverdatto, Aaron, Premo, Leonard, Breindel, Jianchao, Yu, Gregory, Theophall, David S, Burz, Anna, Liu, Todd, Sulchek, Ann Marie, Schmidt, Ravichandran, Ramasamy, Alexander, Shekhtman
Publikováno v:
Scientific Reports. 12
Analytical tools to study cell physiology are critical for optimizing drug-host interactions. Real time pulse chase NMR spectroscopy, RTPC-NMR, was introduced to monitor the kinetics of metabolite production in HEK 293T cells treated with COVID-19 va
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e1da07b3d3ff394469be5717bd9b99a
https://doi.org/10.1038/s41598-022-26444-z
https://doi.org/10.1038/s41598-022-26444-z
Autor:
Nicholas Sciolino, Anna Liu, Leonard Breindel, David S. Burz, Todd Sulchek, Alexander Shekhtman
Publikováno v:
Communications Biology. 5
High-resolution structural studies of proteins and protein complexes in a native eukaryotic environment present a challenge to structural biology. In-cell NMR can characterize atomic resolution structures but requires high concentrations of labeled p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::61a1e42d898f99d46af4e731a9b50970
https://doi.org/10.1038/s42003-022-03412-x
https://doi.org/10.1038/s42003-022-03412-x
Autor:
Devin B. Busch, Aaron Premo, Qishan Lin, Lisa M. Ramirez, Alexander Shekhtman, Jianchao Yu, David S. Burz
Publikováno v:
Biochemistry. 60(24)
NMR spectroscopy was used to investigate the phenomenon of ribosome-amplified metabolism or RAMBO between pyruvate kinase and ribosomes. Because the concentration of ribosomes increases as the cell grows, ribosome binding interactions may regulate me
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::56e524b150d66fd36fd26598ee9173e7
https://pubmed.ncbi.nlm.nih.gov/34081430
https://pubmed.ncbi.nlm.nih.gov/34081430
Publikováno v:
Communications Biology, Vol 3, Iss 1, Pp 1-9 (2020)
Communications Biology
Communications Biology
Protein–protein interactions, PPIs, underlie most cellular processes, but many PPIs depend on a particular metabolic state that can only be observed in live, actively metabolizing cells. Real time in-cell NMR spectroscopy, RT-NMR, utilizes a biorea
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b8a850192448020f0091d02be911fc49
https://doi.org/10.1038/s42003-020-0976-3
https://doi.org/10.1038/s42003-020-0976-3