Zobrazeno 1 - 10
of 28
pro vyhledávání: '"Masa Cemazar"'
Publikováno v:
Expert Opinion on Drug Discovery. 7:179-194
Cyclotides are plant-made defence proteins with a head-to-tail cyclic backbone combined with a conserved, six cystine knot. They have a range of biological activities, including uterotonic and anti-HIV activity, which have attracted attention to thei
Publikováno v:
Biopolymers. 92:35-43
We recently isolated a protein disulfide isomerase (PDI) from the Rubiaceae (coffee family) plant Oldenlandia affinis (OaPDI) and demonstrated that it facilitates the production of disulfide-knotted defense proteins called cyclotides. PDIs are major
Publikováno v:
Antioxidants & Redox Signaling. 10:103-112
Cyclic cystine knot proteins are small but topologically complex molecules that occur naturally in plants and have a wide range of bioactivities that make them interesting from a pharmaceutical perspective. Their remarkable stability is dependent on
Autor:
Rosemary F Renda, Marilyn A. Anderson, David J. Craik, Richard J. Clark, Masa Cemazar, Christian W. Gruber, Tomohisa Horibe
Publikováno v:
Journal of Biological Chemistry. 282:20435-20446
We have isolated a protein-disulfide isomerase (PDI) from Oldenlandia affinis (OaPDI), a coffee family (Rubiaceae) plant that accumulates knotted circular proteins called cyclotides. The novel plant PDI appears to be involved in the biosynthesis of c
Autor:
Kai Pong Lo, David J. Craik, Norelle L. Daly, Masa Cemazar, Sara Häggblad, Ernie Yulyaningsih
Publikováno v:
Journal of Biological Chemistry. 281:8224-8232
The aim of this work was to elucidate the oxidative folding mechanism of the macrocyclic cystine knot protein MCoTI-II. We aimed to investigate how the six-cysteine residues distributed on the circular backbone of the reduced unfolded peptide recogni
Publikováno v:
Journal of Biological Chemistry. 279:16697-16705
Oxidative folding is the fusion of native disulfide bond formation with conformational folding. This complex process is guided by two types of interactions: first, covalent interactions between cysteine residues, which transform into native disulfide
Autor:
Christopher M. Dobson, P. J. Hore, Masa Cemazar, Charles E. Lyon, Jakob J. Lopez, Kiminori Maeda
Publikováno v:
Journal of Biomolecular NMR. 16:235-244
Two new techniques offering considerable improvements in the quality of 1H photo-CIDNP spectra of proteins are demonstrated. Both focus on the problem of progressive photo-degradation of the flavin dye used to generate polarization in exposed tryptop
Autor:
Sotir Zahariev, Ilona Hudáky, Zoltán Gáspári, Sándor Pongor, András Perczel, Oliviero Carugo, Masa Cemazar
Publikováno v:
Protein Engineering Design and Selection. 16:637-639
The formation of a disulfide bond between adjacent cysteine residues is accompanied by the formation of a tight turn of the protein backbone. In nearly 90% of the structures analyzed a type VIII turn was found. The peptide bond between the two cystei
Publikováno v:
Current topics in medicinal chemistry. 12(14)
Cyclic peptides typically have much higher stability and improved biopharmaceutical properties over their linear counterparts. Our work focuses on the discovery of naturally occurring disulfide-rich cyclic peptides and their applications in drug desi
Autor:
David J. Craik, K. Johan Rosengren, Masa Cemazar, Conan K. Wang, Peta J. Harvey, Richard J. Clark
Publikováno v:
Biochemistry. 50(19)
Cyclotides are a family of plant defense proteins with a unique cyclic backbone and cystine knot. Their remarkable stability under harsh thermal, enzymatic, and chemical conditions, combined with their range of bioactivities, including anti-HIV activ