Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Henno W. van den Hooven"'
Autor:
Rianne Luderer, Susana Rivas, Thorsten Nürnberger, Benedetta Mattei, Henno W. Van den Hooven, Renier A. L. Van der Hoorn, Tina Romeis, Josa-M. Wehrfritz, Beatrix Blume, Dirk Nennstiel, Douwe Zuidema, Jacques Vervoort, Giulia De Lorenzo, Jonathan D. G. Jones, Pierre J. G. M. De Wit, Matthieu H. A. J. Joosten
Publikováno v:
Molecular Plant-Microbe Interactions, Vol 14, Iss 7, Pp 867-876 (2001)
The gene-for-gene model postulates that for every gene determining resistance in the host plant, there is a corresponding gene conditioning avirulence in the pathogen. On the basis of this relationship, products of resistance (R) genes and matching a
Externí odkaz:
https://doaj.org/article/c8f7b29e5df0491692d113e223f4daba
Autor:
and Antonie J. W. G. Visser, Annechien F. Hengeveld, Carlo P. M. van Mierlo, Aart de Kok, Henno W. van den Hooven
Publikováno v:
Biochemistry 41 (2002)
Biochemistry, 41, 7490-7500
Biochemistry, 41, 7490-7500
A synthetic peptide (Nterm-E1p) is used to characterize the structure and function of the N-terminal region (amino acid residues 4-45) of the pyruvate dehydrogenase component (E1p) from the pyruvate dehydrogenase multienzyme complex (PDHC) from Azoto
Autor:
Roland J. Siezen, Henno W. van den Hooven, Harry S. Rollema, Cornelis W. Hilbers, Oscar P. Kuipers
Publikováno v:
Biochemistry, 36(46), 14137-14145. AMER CHEMICAL SOC
The antimicrobial membrane-interacting polypeptide nisin is a prominent member of the lantibiotic family, the members of which contain thioether-bridged residues called lanthionines. To gain insight into the complex biosynthesis and the structure/fun
Autor:
Cornelis W. Hilbers, Roland J. Siezen, Oscar P. Kuipers, Ruud N.H. Konings, Mart Van De Kamp, Hans-Georg Sahl, Gabriele Bierbaum, Willem M. de Vos, Henno W. van den Hooven, Frank J. M. Van De Ven
Publikováno v:
European Journal of Biochemistry, 230(2). Blackwell Publishing Ltd
Lantibiotics are bacteriocins that contain unusual amino acids such as lanthionines and alpha, beta-didehydro residues generated by posttranslational modification of a ribosomally synthesized precursor protein. The structural gene encoding the novel
Autor:
Angelika Frey, Ruud N.H. Konings, Lennard M. Horstink, Cornelis W. Hilbers, Mart Van De Kamp, Jörg W. Metzger, Henno W. van den Hooven, Frank J. M. Van De Ven, Hans-Georg Sahl
Publikováno v:
European Journal of Biochemistry. 227:757-771
The amino acid sequence of the novel lantibiotic epilancin K7 from Staphylococcus epidermidis K7 was determined by NMR spectroscopy. NMR spectroscopy was used because sequencing by conventional Edman degradation techniques was prohibited by internal
Autor:
Cornelis W. Hilbers, Ruud N.H. Konings, Henno W. van den Hooven, Frank J. M. Van De Ven, Harry S. Rollema, Federico Fogolari
Publikováno v:
FEBS Letters. 319:189-194
The lantibiotic, nisin, which is known to interact with membranes of certain Gram-positive bacteria, was studied in three model systems which mimic a membrane-like environment, i.e. a mixture of trifluoroethanol and water, or micelles of sodium dodec
Autor:
P. Vossen, Ralph Vogelsang, Axel Berg, Jacques Vervoort, Pierre J. G. M. de Wit, Matthieu H. A. J. Joosten, Henno W. van den Hooven
Publikováno v:
FEBS Letters 404 (1997)
FEBS Letters, 404, 153-158
FEBS Letters, 404, 153-158
The secondary structure and global fold of the AVR9 elicitor protein of Cladosporium fulvum has been determined by 2D NMR and distance-geometry protocols. The protein consists of three anti-parallel strands forming a rigid region of β-sheet. On the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::554fbfd616f5d51db1fda3be234e587a
https://research.wur.nl/en/publications/the-race-specific-elicitor-avr9-of-the-tomato-pathogen-cladospori
https://research.wur.nl/en/publications/the-race-specific-elicitor-avr9-of-the-tomato-pathogen-cladospori
Autor:
Cornelis W. Hilbers, Roland J. Siezen, Oscar P. Kuipers, Fija M. Lagerwerf, Harry S. Rollema, Johan Haverkamp, Wigger Heerma, Jean-Christophe Piard, Henno W. van den Hooven
Publikováno v:
FEBS Letters
FEBS Letters, Wiley, 1996, 391 (3), pp.317-322. ⟨10.1016/0014-5793(96)00771-5⟩
FEBS Letters, 391(3). Wiley
FEBS Letters, Wiley, 1996, 391 (3), pp.317-322. ⟨10.1016/0014-5793(96)00771-5⟩
FEBS Letters, 391(3). Wiley
The lantibiotic lacticin 481 is a bacteriocin produced by Lactococcus lactis ssp. lactis. This polypeptide contains 27 amino acids, including the unusual residues dehydrobutyrine and the thioether-bridging lanthionine and 3-methyllanthionine. Lactici
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::deed10fd44140086ed390b02614817c0
https://hal.inrae.fr/hal-03031680
https://hal.inrae.fr/hal-03031680
Autor:
Mart Van De Kamp, Ruud N.H. Konings, Henno W. van den Hooven, Frank J. M. Van De Ven, Cornelis W. Hilbers, Chris A. E. M. Spronk
Publikováno v:
European journal of biochemistry. 235(1-2)
The interaction of nisin, a membrane-interacting cationic polypeptide, with membrane-mimicking micelles of zwitterionic dodecylphosphocholine and of anionic sodium dodecylsulphate was studied. Direct contacts have been established through the observa
Publikováno v:
Bacteriocins, Microcins and Lantibiotics ISBN: 9783642769764
Nisin, a bacteriocin produced by Lactococcus lactis ssp., is a post-translationally modified pentacyclic polypeptide of 34 amino acids. It is a member of the class of bacteriocins, known as lantibiotics, that contain the unusual amino acid lanthionin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::aae7ac6142bb317b5abcd6daced29ab2
https://doi.org/10.1007/978-3-642-76974-0_39
https://doi.org/10.1007/978-3-642-76974-0_39