Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Theodore J. Litberg"'
Autor:
Theodore J. Litberg, Rajesh Kumar Reddy Sannapureddi, Zijue Huang, Ahyun Son, Bharathwaj Sathyamoorthy, Scott Horowitz
Publikováno v:
RNA Biology, Vol 20, Iss 1, Pp 495-509 (2023)
Maintaining a healthy protein folding environment is essential for cellular function. Recently, we found that nucleic acids, G-quadruplexes in particular, are potent chaperones for preventing protein aggregation. With the aid of structure-function an
Externí odkaz:
https://doaj.org/article/ace4afa7131b4629b23d62b1584417cc
Publikováno v:
Proceedings of the National Academy of Sciences. 120
Maintaining the health of the proteome is a critical cellular task. Recently, we found G-quadruplex (G4) nucleic acids are especially potent at preventing protein aggregation in vitro and could at least indirectly improve the protein folding environm
SummaryMaintaining the health of the proteome is a critical cellular task. Recently, we found G-quadruplex (G4) nucleic acids are especially potent at preventing protein aggregation in vitro and could at least indirectly improve the protein folding e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f28a8d55fef785ec05e2062b6a297e79
https://doi.org/10.1101/2022.09.09.507295
https://doi.org/10.1101/2022.09.09.507295
Autor:
Theodore J. Litberg, Rajesh Kumar Reddy Sannapureddi, Zijue Huang, Ahyun Son, Bharathwaj Sathyamoorthy, Scott Horowitz
Maintaining a healthy protein folding environment is essential for cellular function. Recently, we found that nucleic acids, and G-quadruplexes in particular, are potent chaperones for preventing protein aggregation. With the aid of structure-functio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d6451e8d1677c43c6105a941475a2e9a
https://doi.org/10.1101/2022.08.23.504968
https://doi.org/10.1101/2022.08.23.504968
Autor:
Bryan B. Guzman, Ahyun Son, Theodore J. Litberg, Zijue Huang, Daniel Dominguez, Scott Horowitz
Publikováno v:
The FEBS journalReferences.
How nucleic acids interact with proteins, and how they affect protein folding, aggregation, and misfolding is a still-evolving area of research. Considerable effort is now focusing on a particular structure of RNA and DNA, G-quadruplexes, and their r
Autor:
Tadeusz Wroblewski, Adam Begeman, Ahyun Son, Scott Horowitz, Veronica Huizar Cabral, Jennifer N. Bourne, Theodore J. Litberg, Thane Gehring, Zhenyu Xuan
Publikováno v:
EMBO Reports
Maintaining proteome health is important for cell survival. Nucleic acids possess the ability to prevent protein aggregation more efficiently than traditional chaperone proteins. In this study, we explore the sequence specificity of the chaperone act
Maintaining proteome health is important for cell survival. Nucleic acids possess the ability to prevent aggregation up to 300-fold more efficiently than traditional chaperone proteins. In this study, we explore the sequence specificity of the chaper
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f31753bed3475e09f880ae0e3f9cb2c8
https://doi.org/10.1101/850263
https://doi.org/10.1101/850263
Autor:
Brianne E. Docter, Scott Horowitz, Jennifer N. Bourne, Theodore J. Litberg, Michael P. Hughes
Publikováno v:
Biophys J
Previous studies have shown that nucleic acids can nucleate protein aggregation in disease-related proteins, but in other cases, they can act as molecular chaperones that prevent protein aggregation, even under extreme conditions. In this study, we d
Publikováno v:
The Journal of organic chemistry. 81(13)
Previous work on the o-hydroxychalcone/flavanone molecular switching scaffold showed that simple substitutions alter the pH range in which rapid interconversion occurs. Herein, more impactful structural modifications were performed via alteration of