Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Mason J. Appel"'
Autor:
Mason J. Appel, Scott A. Longwell, Maurizio Morri, Norma Neff, Daniel Herschlag, Polly M. Fordyce
Publikováno v:
ACS Omega, Vol 6, Iss 45, Pp 30542-30554 (2021)
Externí odkaz:
https://doaj.org/article/ab1df1c264c84e64b0e78e94148d3976
Publikováno v:
Curr Opin Struct Biol
Accurate predictions from models based on physical principles are the ultimate metric of our biophysical understanding. Although there has been stunning progress toward structure prediction, quantitative prediction of enzyme function has remained cha
Autor:
Norma Neff, Daniel Herschlag, Maurizio Morri, Mason J. Appel, Polly M. Fordyce, Scott A. Longwell
Publikováno v:
ACS Omega, Vol 6, Iss 45, Pp 30542-30554 (2021)
ACS Omega
ACS Omega
New high-throughput biochemistry techniques complement selection-based approaches and provide quantitative kinetic and thermodynamic data for thousands of protein variants in parallel. With these advances, library generation rather than data collecti
Autor:
Julien Lafrance-Vanasse, Mason J. Appel, Hyeongtaek Lim, Carolyn R. Bertozzi, Chi Lin Tsai, John A. Tainer, Katlyn K. Meier, Britt Hedman, Edward I. Solomon, Keith O. Hodgson
Publikováno v:
Proceedings of the National Academy of Sciences. 116:5370-5375
The formylglycine-generating enzyme (FGE) is required for the posttranslational activation of type I sulfatases by oxidation of an active-site cysteine to C α -formylglycine. FGE has emerged as an enabling biotechnology tool due to the robust utilit
Autor:
Polly M. Fordyce, Chiara Sabatti, Daniel A. Mokhtari, Scott A. Longwell, Daniel Herschlag, Mason J. Appel, Eyal Akiva, Fanny Sunden, Craig J. Markin
Go big or you'll get lost Rational mutagenesis is a common approach to investigating or engineering enzyme function in vitro, but the ease with which one can manipulate protein sequences belies many pitfalls in connecting sparse activity data to an e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2b174ff564afcbe0f4b6ac5f5b291826
https://doi.org/10.1101/2020.11.24.383182
https://doi.org/10.1101/2020.11.24.383182
Autor:
Angelo Solania, Mason J. Appel, Peter V. Robinson, Brian Belardi, Carolyn R. Bertozzi, Jason E. Hudak
Publikováno v:
Bioorganic & Medicinal Chemistry. 24:4791-4800
The generation of homogeneously glycosylated proteins is essential for defining glycoform-specific activity and improving protein-based therapeutics. We present a novel glycodendron prosthetic which can be site-selectively appended to recombinant pro
Formylglycine-generating enzyme binds substrate directly at a mononuclear Cu(I) center to initiate O
Autor:
Mason J, Appel, Katlyn K, Meier, Julien, Lafrance-Vanasse, Hyeongtaek, Lim, Chi-Lin, Tsai, Britt, Hedman, Keith O, Hodgson, John A, Tainer, Edward I, Solomon, Carolyn R, Bertozzi
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 116(12)
The formylglycine-generating enzyme (FGE) is required for the posttranslational activation of type I sulfatases by oxidation of an active-site cysteine to C(α)-formylglycine. FGE has emerged as an enabling biotechnology tool due to the robust utilit
Autor:
Polly M. Fordyce, Craig J. Markin, Daniel A. Mokhtari, Daniel Herschlag, Fanny Sunden, Mason J. Appel
Publikováno v:
Biophysical Journal. 118:535a
Autor:
Mason J. Appel, Lalit Ponnala, Elden Rowland, Anton Poliakov, Ryan P. McQuinn, Giulia Friso, Qi Sun, Peter K. Lundquist, Stuart B. Krasnoff, L. Giacomelli, Klaas J. van Wijk
Publikováno v:
The Plant Cell. 25:1818-1839
Plastoglobules (PGs) are plastid lipid-protein particles. This study examines the function of PG-localized kinases ABC1K1 and ABC1K3 in Arabidopsis thaliana. Several lines of evidence suggested that ABC1K1 and ABC1K3 form a protein complex. Null muta
Autor:
Mason J. Appel, Carolyn R. Bertozzi
Publikováno v:
ACS chemical biology. 10(1)
Formylglycine (fGly) is a catalytically essential residue found almost exclusively in the active sites of type I sulfatases. Formed by post-translational oxidation of cysteine or serine side chains, this aldehyde-functionalized residue participates i