Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Svetlana Rogulina"'
Publikováno v:
Molecular Systems Biology, Vol 19, Iss 8, Pp n/a-n/a (2023)
Abstract Over the past two decades, synthetic biological systems have revolutionized the study of cellular physiology. The ability to site‐specifically incorporate biologically relevant non‐standard amino acids using orthogonal translation system
Externí odkaz:
https://doaj.org/article/85d65118eae1479585f4602431d54ea4
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-14 (2022)
Protein phosphorylation is a ubiquitous post-translational modification used to regulate cellular processes and proteome architecture by modulating protein-protein interactions. Here the authors optimize genetically encoded phosphothreonine to study
Externí odkaz:
https://doaj.org/article/4524495ba12546348e670f788fe32025
Publikováno v:
bioRxiv
Interactions between proteins from intracellular pathogens and host proteins in an infected cell are often mediated by post-translational modifications encoded in the host proteome. Identifying protein modifications, such as phosphorylation, that dic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::23bd1c8d659679c1561f55636ec94b3a
https://europepmc.org/articles/PMC9536036/
https://europepmc.org/articles/PMC9536036/
Publikováno v:
Nature communications. 13(1)
Protein phosphorylation is a ubiquitous post-translational modification used to regulate cellular processes and proteome architecture by modulating protein-protein interactions. The identification of phosphorylation events through proteomic surveilla
Over the past twenty years, the development of orthogonal biological systems has sparked a revolution in our ability to study cellular physiology. Orthogonal translation systems (OTSs) enable site-specific incorporation of hundreds of non-standard am
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8965104e7eb4a9473c42c3fc204ce92c
https://doi.org/10.1101/2021.05.20.444985
https://doi.org/10.1101/2021.05.20.444985
Autor:
Mark Gerstein, Jeffrey R. Sampson, Farren J. Isaacs, Jesse Rinehart, Karl W. Barber, Richard V Szeligowski, Paul R. Muir, Svetlana Rogulina
Publikováno v:
Nature biotechnology
Post-translational phosphorylation is essential to human cellular processes, but the transient, heterogeneous nature of this modification complicates its study in native systems. We developed an approach to interrogate phosphorylation and its role in
Autor:
Pierre A. Miranda-Herrera, Sagar R. Shah, Alfredo Quinones-Hinojosa, Andre Levchenko, Hugo Guerrero-Cazares, Natanael Zarco, Onur Kilic, William Hungerford, Farren J. Isaacs, Kyle Mohler, Denton Hoyer, Laura Abriola, Benjamin E. Turk, Natasha L. Pirman, Jesse Rinehart, Svetlana Rogulina, Paula Schiapparelli, Chad J. Miller
Publikováno v:
Cell reports
SUMMARY Advances in genetic code expansion have enabled the production of proteins containing site-specific, authentic post-translational modifications. Here, we use a recoded bacterial strain with an expanded genetic code to encode phosphoserine int
Publikováno v:
ACS Chemical Biology
Adding nonstandard amino acids to the genetic code of E. coli expands the chemical and biological functional space for proteins. This is accomplished with engineered, orthogonal aminoacyl-tRNA synthetase and tRNA pairs that require a nonstandard amin
Autor:
Adrian D. Haimovich, Svetlana Rogulina, Natasha L. Pirman, Farren J. Isaacs, Karl W. Barber, Natalie J. Ma, Jesse Rinehart, Hans R. Aerni
Publikováno v:
Nature Communications
Biochemical investigation of protein phosphorylation events is limited by inefficient production of the phosphorylated and non-phosphorylated forms of full-length proteins. Here using a genomically recoded strain of E. coli with a flexible UAG codon
Autor:
Matthew B. Amrofell, Karl W. Barber, Charlotte M. ter Haar, Svetlana Rogulina, Farren J. Isaacs, Natasha L. Pirman, Javin P. Oza, Michael C. Jewett, Jesse Rinehart, Hans R. Aerni
Publikováno v:
Nature Communications
Understanding the functional and structural consequences of site-specific protein phosphorylation has remained limited by our inability to produce phosphoproteins at high yields. Here we address this limitation by developing a cell-free protein synth