Zobrazeno 1 - 10
of 78
pro vyhledávání: '"John A. W. Kruijtzer"'
Autor:
Bas G J Surewaard, Reindert Nijland, András N Spaan, John A W Kruijtzer, Carla J C de Haas, Jos A G van Strijp
Publikováno v:
PLoS Pathogens, Vol 8, Iss 3, p e1002606 (2012)
Staphylococcus aureus virulence has been associated with the production of phenol soluble modulins (PSM). PSM are known to activate, attract and lyse neutrophils. However, the functional characterizations were generally performed in the absence of hu
Externí odkaz:
https://doaj.org/article/496e1bea6f3e4993b3da77bcf442ec6e
Autor:
Albert J. R. Heck, John A. W. Kruijtzer, Tiehai Li, Tomislav Čaval, Javier Sastre Toraño, Geert-Jan Boons, Ivan A. Gagarinov, Apoorva D. Srivastava
Publikováno v:
Journal of the American Chemical Society. 139:1011-1018
Progress in glycoscience is hampered by a lack of well-defined complex oligosaccharide standards that are needed to fabricate the next generation of microarrays, to develop analytical protocols to determine exact structures of isolated glycans, and t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::01acbf33c85e439cb31bb07438512088
https://doi.org/10.1021/jacs.6b12080
https://doi.org/10.1021/jacs.6b12080
Autor:
Rob M. J. Liskamp, Sebastian A. J. Zaat, H. C. Quarles van Ufford, John A. W. Kruijtzer, Rik T. C. Cleophas, Martijn Riool
Publikováno v:
ACS MACRO LETTERS, 3(5), 477-480. American Chemical Society
This report describes the design and synthesis of a bactericidal poly(ethylene glycol)-based (PEG) hydrogel coating with covalently attached antimicrobial peptides (AMP) stabilized against proteolytic degradation. As such, mimics of the highly active
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::586a0a21cfd6b9cac7de238d1df51475
https://doi.org/10.1021/mz5001465
https://doi.org/10.1021/mz5001465
Autor:
Helmus van de Langemheen, Paul R. Werkhoven, Steffen van der Wal, Rob M. J. Liskamp, John A. W. Kruijtzer
Publikováno v:
Journal of Peptide Science. 20:235-239
Synthetic mimics of discontinuous epitopes may have a wide range of potential applications, including synthetic vaccines and inhibition of protein-protein interactions. However, synthetic access to these relatively complex peptide molecular construct
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1de591e85a3a0bd43879f50ab12879c8
https://doi.org/10.1002/psc.2624
https://doi.org/10.1002/psc.2624
Autor:
Paul R. Werkhoven, H. C. Quarles van Ufford, T. J. Meuleman, Rob M. J. Liskamp, John A. W. Kruijtzer, M. Elwakiel
Publikováno v:
Organic & Biomolecular Chemistry, 14(2), 701. Royal Society of Chemistry
Mimics of discontinuous epitopes of for example bacterial or viral proteins may have considerable potential for the development of synthetic vaccines, especially if conserved epitopes can be mimicked. However, due to the structural complexity and siz
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f6cf75a651385b84f3737dbddcc6ec9
https://dspace.library.uu.nl/handle/1874/328183
https://dspace.library.uu.nl/handle/1874/328183
Autor:
Arwin J. Brouwer, Helmus van de Langemheen, Rob M. J. Liskamp, Johan Kemmink, John A. W. Kruijtzer
Publikováno v:
The Journal of Organic Chemistry. 77:10058-10064
The synthesis of cyclic peptides containing a thioester handle using a sulfo-click linker is reported. These cyclic peptides can be coupled to N-terminal cysteine-containing constructs via native chemical ligation. A successful application of a cycli
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df8583cb2ffb09afb4fa79fa8d8f46b3
https://doi.org/10.1021/jo3015566
https://doi.org/10.1021/jo3015566
Autor:
John A. W. Kruijtzer, Rob M. J. Liskamp, Anton Bunschoten, Börje Sellergren, Sudhirkumar Shinde
Publikováno v:
Angewandte Chemie International Edition. 51:8326-8329
Leaving a lasting impression: Molecularly imprinted polymers (MIPs) featuring neutral binding sites for phosphotyrosine (P) is also shown to have affinity for sulfotyrosine (S) and a sulfotyrosine-containing peptide. The MIPs were capable of selectiv
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::92d5b2f8d293789f1ad49d92a5a0e699
https://doi.org/10.1002/anie.201201314
https://doi.org/10.1002/anie.201201314
Autor:
Bart J. Crielaard, Cristianne J. F. Rijcken, Lingdong Quan, Steffen van der Wal, Isil Altintas, Martin van der Pot, John A. W. Kruijtzer, Rob M. J. Liskamp, Raymond M. Schiffelers, Cornelus F. van Nostrum, Wim E. Hennink, Dong Wang, Twan Lammers, Gert Storm
Publikováno v:
Angewandte Chemie. 124:7366-7370
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::888c4188598c7a4892b6957b47c57318
https://doi.org/10.1002/ange.201202713
https://doi.org/10.1002/ange.201202713
Autor:
Ingrid R. Vetter, Lucas Brunsveld, Herbert Waldmann, Nachiket Vartak, Rob M. J. Liskamp, John A. W. Kruijtzer, Marco Bürger, Gemma Triola, Philippe I. H. Bastiaens, Kristina Görmer
Publikováno v:
ChemBioChem, 13(7), 1017-1023. Wiley-VCH Verlag
A dynamic de-/repalmitoylation cycle determines localization and activity of H- and N-Ras. This combined cellular de- and repalmitoylation machinery has been shown to be substrate tolerant--it accepts variation of amino acid sequence, structure and c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f6ab890bd03da5057cedb4cd225aa457
https://doi.org/10.1002/cbic.201200078
https://doi.org/10.1002/cbic.201200078
Autor:
Monique P. C. Mulder, John A. W. Kruijtzer, Rob M. J. Liskamp, Johan Kemmink, Roland J. Pieters, Eefjan Breukink
Publikováno v:
Bioorganic & Medicinal Chemistry. 19:6505-6517
Echinocandins are a novel class of macrocyclic antifungal peptides that act by inhibiting the β-(1,3)-D-glucan synthase complex, which is not present in mammalian cells. Due to the large number of hydroxyl groups present in these complex macrocyclic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1798dcab9153e3627595dde0bf4f30d5
https://doi.org/10.1016/j.bmc.2011.08.034
https://doi.org/10.1016/j.bmc.2011.08.034