Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Jo E. Lomax"'
Publikováno v:
Journal of the American Chemical Society. 139:14396-14398
Cloaking its carboxyl groups with a hydrophobic moiety is shown to enable a protein to enter the cytosol of a mammalian cell. Diazo compounds derived from (p-methylphenyl)glycine were screened for the ability to esterify the green fluorescent protein
Autor:
David Gailani, Ronald T. Raines, Bassem M. Mohammed, Emily Garnett, Jo E. Lomax, John P. Sheehan
Publikováno v:
RNA
Biological roles for extracellular RNA (eRNA) have become apparent. For example, eRNA can induce contact activation in blood via activation of the plasma proteases factor XII (FXII) and factor XI (FXI). We sought to reveal the biological role of the
Publikováno v:
ACS Chemical Biology. 11:319-323
The use of exogenous proteins as intracellular probes and chemotherapeutic agents is in its infancy. A major hurdle has been the delivery of native proteins to an intracellular site of action. Herein, we report on a compact delivery vehicle that empl
Publikováno v:
Chemical Science. 6:752-755
A diazo compound is shown to convert carboxylic acids to esters efficiently in an aqueous environment. The basicity of the diazo compound is critical: low basicity does not lead to a reaction but high basicity leads to hydrolysis. This reactivity ext
Pancreatic-type ribonucleases (ptRNases) comprise a class of highly conserved secretory endoribonucleases in vertebrates. The prototype of this enzyme family is ribonuclease 1 (RNase 1). Understanding the physiological roles of RNase 1 is becoming in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae101c280ab79c74b0dd8049db84dabf
https://europepmc.org/articles/PMC5660862/
https://europepmc.org/articles/PMC5660862/
Publikováno v:
The Journal of biological chemistry. 289(38)
Mounting evidence suggests that human pancreatic ribonuclease (RNase 1) plays important roles in vivo, ranging from regulating blood clotting and inflammation to directly counteracting tumorigenic cells. Understanding these putative roles has been pu
Autor:
George N. Phillips, Aram Chang, Jo E. Lomax, Brian G. Fox, Christopher M. Bianchetti, Ronald T. Raines
Publikováno v:
Journal of molecular biology. 426(17)
Ribonuclease inhibitor (RI) is a conserved protein of the mammalian cytosol. RI binds with high affinity to diverse secretory ribonucleases (RNases) and inhibits their enzymatic activity. Although secretory RNases are found in all vertebrates, the ex
Mammalian pancreatic-type ribonucleases (ptRNases) comprise an enzyme family that is remarkably well suited for therapeutic exploitation. ptRNases are robust and prodigious catalysts of RNA cleavage that can naturally access the cytosol. Instilling c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4867af0e935e4391c5c705852cc5dfab
https://europepmc.org/articles/PMC3304445/
https://europepmc.org/articles/PMC3304445/
Autor:
McGrath, Nicholas A., Andersen, Kristen A., Davis, Amy K. F., Lomax, Jo E., Raines, Ronald T.
Publikováno v:
Chemical Science; 2015, Vol. 6 Issue 1, p752-755, 4p
Publikováno v:
Protein Science: A Publication of the Protein Society; Jul2014 Supplement, Vol. 23, p1-284, 284p