Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Phillip Zhu"'
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-16 (2024)
Abstract ATP-sensitive potassium (KATP) channels, composed of four pore-lining Kir6.2 subunits and four regulatory sulfonylurea receptor 1 (SUR1) subunits, control insulin secretion in pancreatic β-cells. KATP channel opening is stimulated by PIP2 a
Externí odkaz:
https://doaj.org/article/51943945f40e4fbd84e1af7be3d9f24b
Publikováno v:
Channels, Vol 18, Iss 1 (2024)
ABSTRACTKATP channels are ligand-gated potassium channels that couple cellular energetics with membrane potential to regulate cell activity. Each channel is an eight subunit complex comprising four central pore-forming Kir6 inward rectifier potassium
Externí odkaz:
https://doaj.org/article/ae5b90c7be9645178e9ac3531c0fa733
Publikováno v:
Bio-Protocol, Vol 13, Iss 17 (2023)
Externí odkaz:
https://doaj.org/article/ced81f1388d7422eae586fa558c61647
Publikováno v:
Bio-Protocol, Vol 12, Iss 21 (2022)
This protocol describes the recombinant expression of proteins in E. coli containing phosphoserine (pSer) installed at positions guided by TAG codons. The E. coli strains that can be used here are engineered with a ∆serB genomic knockout to produce
Externí odkaz:
https://doaj.org/article/9665de5b69224d0291bc1705e6139010
Autor:
Phillip Zhu, Stanislau Stanisheuski, Rachel Franklin, Amber Vogel, Cat Hoang Vesely, Patrick Reardon, Nikolai N. Sluchanko, Joseph S. Beckman, P. Andrew Karplus, Ryan A. Mehl, Richard B. Cooley
Publikováno v:
ACS Central Science. 9:816-835
Autor:
Phillip Zhu, Kyle T. Nguyen, Aidan B. Estelle, Nikolai N. Sluchanko, Ryan A. Mehl, Richard B. Cooley
Publikováno v:
Protein Science. 32
14-3-3 proteins are central hub regulators of hundreds of phosphorylated “client” proteins. They are subject to over 60 post-translational modifications (PTMs), yet little is known how these PTMs alter 14-3-3 function and its ability to regulate
Autor:
Kristina V. Tugaeva, Andrey A. Sysoev, Anna A. Kapitonova, Jake L. R. Smith, Phillip Zhu, Richard B. Cooley, Alfred A. Antson, Nikolai N. Sluchanko
Publikováno v:
Journal of Molecular Biology. 435:167891
Phosphorylation of SARS-CoV-2 nucleoprotein recruits human cytosolic 14-3-3 proteins playing a well-recognized role in replication of many viruses. Here we use genetic code expansion to demonstrate that 14-3-3 binding is triggered by phosphorylation
Autor:
Phillip Zhu, Rachel Franklin, Amber Vogel, Stanislau Stanisheuski, Patrick Reardon, Nikolai N. Sluchanko, Joseph S. Beckman, P. Andrew Karplus, Ryan A. Mehl, Richard B. Cooley
Publikováno v:
bioRxiv
article-version (status) pre
article-version (number) 2
article-version (status) pre
article-version (number) 2
Installing stable, functional mimics of phosphorylated amino acids into proteins offers a powerful strategy to study protein regulation. Previously, a genetic code expansion (GCE) system was developed to translationally install non-hydrolyzable phosp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6fb01b8700a08b2f11157475c3349776
https://doi.org/10.1101/2021.10.22.465468
https://doi.org/10.1101/2021.10.22.465468
Autor:
Joaquin Rodriguez Galvan, Phillip Zhu, Amber D. Rolland, Richard B. Cooley, Elisar Barbar, Zhen Yu, Patrick N. Reardon, Heather M. Forsythe, Seth Pinckney, James S. Prell
Publikováno v:
Biophysical Journal
The nucleocapsid phosphoprotein N plays critical roles in multiple processes of the severe acute respiratory syndrome coronavirus 2 infection cycle: it protects and packages viral RNA in N assembly, interacts with the inner domain of spike protein, b
Autor:
Parisa Hosseinzadeh, Jenna N. Beyer, Riley M. Bednar, Ilana Gottfried-Lee, Richard B. Cooley, Elise M. Van Fossen, P. Andrew Karplus, Phillip Zhu, Ryan A. Mehl
Publikováno v:
J Mol Biol
Genetic code expansion (GCE) technologies incorporate non-canonical amino acids (ncAAs) into proteins at amber stop codons. To avoid unwanted truncated protein and improve ncAA-protein yields, genomically recoded strains of Escherichia coli lacking R
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::69128365724b37f137b9f524364e756b
https://europepmc.org/articles/PMC7665880/
https://europepmc.org/articles/PMC7665880/