Zobrazeno 1 - 10
of 83
pro vyhledávání: '"D. J. Craik"'
Autor:
M. A. Jackson, E. K. Gilding, T. Shafee, K. S. Harris, Q. Kaas, S. Poon, K. Yap, H. Jia, R. Guarino, L. Y. Chan, T. Durek, M. A. Anderson, D. J. Craik
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-12 (2018)
Asparaginyl endopeptidases (AEPs) are plant proteases that can also function as ligases, catalyzing the production of cyclic plant peptides. Here, the authors identify structural features that govern AEP ligase activity, providing insights to aid the
Externí odkaz:
https://doaj.org/article/1a99ceed0b0643118c6ddef2be35adf9
Autor:
D. J. Craik, J. A. Jarvis
Publikováno v:
Current Medicinal Chemistry. 1:115-144
Abstract: Peptides are responsible for the regulation of a wide range of physiological functions. Their diverse biological roles, ranging from neurotransmitters to hormones, make them ideal targets for novel drug design. To utilize this potential it
Publikováno v:
Molecular pharmacology. 72(6)
The synthetic alpha-conotoxin Vc1.1 is a small disulfide bonded peptide currently in development as a treatment for neuropathic pain. Unlike Vc1.1, the native post-translationally modified peptide vc1a does not act as an analgesic in vivo in rat mode
Autor:
D J, Craik
Publikováno v:
IDrugs : the investigational drugs journal. 2(12)
Autor:
M L, Korsinczky, H J, Schirra, K J, Rosengren, J, West, B A, Condie, L, Otvos, M A, Anderson, D J, Craik
Publikováno v:
Journal of molecular biology. 311(3)
SFTI-1 is a recently discovered cyclic peptide trypsin inhibitor from sunflower seeds comprising 14 amino acid residues. It is the most potent known Bowman-Birk inhibitor and the only naturally occurring cyclic one. The solution structure of SFTI-1 h
Publikováno v:
The Journal of biological chemistry. 276(25)
Much interest has been generated by recent reports on the discovery of circular (i.e. head-to-tail cyclized) proteins in plants. Here we report the three-dimensional structure of one of the newest such circular proteins, MCoTI-II, a novel trypsin inh
Publikováno v:
Journal of molecular biology. 306(1)
A two-domain portion of the proteinase inhibitor precursor from Nicotiana alata (NaProPI) has been expressed and its structure determined by NMR spectroscopy. NaProPI contains six almost identical 53 amino acid repeats that fold into six highly simil
Autor:
N L, Daly, D J, Craik
Publikováno v:
The Journal of biological chemistry. 275(25)
Kalata B1 is a prototypic member of the unique cyclotide family of macrocyclic polypeptides in which the major structural features are a circular peptide backbone, a triple-stranded beta-sheet, and a cystine knot arrangement of three disulfide bonds.
Autor:
N F, Dawson, D J, Craik, A M, McManus, S G, Dashper, E C, Reynolds, G W, Tregear, L, Otvos, J D, Wade
Publikováno v:
Journal of peptide science : an official publication of the European Peptide Society. 6(1)
The 32-residue peptide, RK-1, a novel kidney-derived three disulfide-bonded member of the antimicrobial alpha-defensin family, was synthesized by the continuous flow Fmoc-solid phase method. The crude, cleaved and S-reduced linear peptide was both ef
Publikováno v:
Journal of peptide science : an official publication of the European Peptide Society. 5(10)
An increased degree of utilization of the potential N-glycosylation site in the fourth repeat unit of the human tau protein may be involved in the inability of tau to bind to the corresponding tubulin sequence(s) and in the subsequent development of