Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Fabian B. H. Rehm"'
Autor:
Junqiao Du, Kuok Yap, Lai Yue Chan, Fabian B. H. Rehm, Fong Yang Looi, Aaron G. Poth, Edward K. Gilding, Quentin Kaas, Thomas Durek, David J. Craik
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-11 (2020)
Asparaginyl endopeptidases (AEPs) catalyze the cyclization step during the biosynthesis of cyclic peptides in plants. Here, the authors report a recombinantly produced AEP that catalyzes the backbone cyclization of a linear cyclotide precursor and an
Externí odkaz:
https://doaj.org/article/2374d960c8e2417095bdec822494ebdd
Publikováno v:
Molecules, Vol 21, Iss 10, p 1370 (2016)
Enzymes are used as biocatalysts in a vast range of industrial applications. Immobilization of enzymes to solid supports or their self-assembly into insoluble particles enhances their applicability by strongly improving properties such as stability i
Externí odkaz:
https://doaj.org/article/eb7c9cbbc3204ec6adac680adc46b3cf
Autor:
Hidde L. Ploegh, Yushu J. Xie, Novalia Pishesha, William Pinney, Weiyi Ma, Fabian B. H. Rehm, Thibault J. Harmand
Publikováno v:
ACS Chemical Biology. 16:1201-1207
Red blood cells (RBCs) can serve as vascular carriers for drugs, proteins, peptides, and nanoparticles. Human RBCs remain in the circulation for ∼120 days, are biocompatible, and are immunologically largely inert. RBCs are cleared by the reticuloen
Autor:
Fabian B. H. Rehm, Simon J. de Veer, Linda H.L. Lua, Shyn Ric Tang, Yan Zhou, Conan K. Wang, Thomas Durek, David J. Craik, Junqiao Du, Kuok Yap, Jing Xie
Publikováno v:
Nature Protocols. 16:1740-1760
Cyclic disulfide-rich peptides have attracted significant interest in drug development and biotechnology. Here, we describe a protocol for producing cyclic peptide precursors in Pichia pastoris that undergo in vitro enzymatic maturation into cyclic p
Publikováno v:
Angewandte Chemie. 133:4050-4054
The use of enzymes for the site-specific modification of proteins/peptides has become a highly accessible, widespread approach to study protein/peptide functions or to generate therapeutic conjugates. Asparaginyl endopeptidases (AEPs) that preferenti
Autor:
Choi Yi Li, Fabian B. H. Rehm, Kuok Yap, Christina N. Zdenek, Maxim D. Harding, Bryan G. Fry, Thomas Durek, David J. Craik, Simon J. de Veer
Publikováno v:
Angewandte Chemie (International ed. in English). 61(19)
Knottins are topologically complex peptides that are stabilised by a cystine knot and have exceptionally diverse functions, including protease inhibition. However, approaches for tuning their activity in situ are limited. Here, we demonstrate separat
Autor:
Quentin Kaas, Edward K. Gilding, David J. Craik, Fong Yang Looi, Lai Yue Chan, Thomas Durek, Kuok Yap, Junqiao Du, Aaron G. Poth, Fabian B. H. Rehm
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-11 (2020)
Nature Communications
Nature Communications
Asparaginyl endopeptidases (AEPs) catalyze the key backbone cyclization step during the biosynthesis of plant-derived cyclic peptides. Here, we report the identification of two AEPs from Momordica cochinchinensis and biochemically characterize MCoAEP
Autor:
David J. Craik, Fabian B. H. Rehm, Anuja R. Bony, Kuok Yap, Shyn Ric Tang, Simon J. de Veer, Junqiao Du, Fong Yang Looi, Conan K. Wang, David J. Adams, Jing Xie, Linda H.L. Lua, Lai Yue Chan, Thomas Durek
Publikováno v:
Green Chemistry. 22:5002-5016
Macrocyclic, disulfide-rich peptides have found widespread applications in drug design and development. Current peptide production strategies rely heavily on solid phase peptide synthesis (SPPS) requiring large amounts of hazardous/toxic reagents and
Autor:
Hidde L. Ploegh, David J. Craik, Thomas Durek, Thibault J. Harmand, Fabian B. H. Rehm, Kuok Yap
Publikováno v:
J Am Chem Soc
Protein ligases of defined substrate specificity are versatile tools for protein engineering. Upon completion of the reaction, the products of currently reported protein ligases contain the amino acid sequence that is recognized by that same ligase,
Publikováno v:
Angewandte Chemie (International ed. in English). 61(11)
Transpeptidase-catalyzed protein and peptide modifications have been widely utilized for generating conjugates of interest for biological investigation or therapeutic applications. However, all known transpeptidases are constrained to ligating in the