scispace - formally typeset
J

Jack H. Vossen

Researcher at Wageningen University and Research Centre

Publications -  65
Citations -  4930

Jack H. Vossen is an academic researcher from Wageningen University and Research Centre. The author has contributed to research in topics: Phytophthora infestans & R gene. The author has an hindex of 32, co-authored 62 publications receiving 4285 citations. Previous affiliations of Jack H. Vossen include University of Amsterdam & Radboud University Nijmegen.

Papers
More filters
Journal ArticleDOI

The Tomato R Gene Products I-2 and Mi-1 Are Functional ATP Binding Proteins with ATPase Activity

TL;DR: It is shown that the NBS of R proteins forms a functional nucleotide binding pocket and it is proposed that they all are capable of binding and hydrolyzing ATP.
Journal ArticleDOI

Understanding and exploiting late blight resistance in the age of effectors

TL;DR: Genome-wide catalogs of P. infestans effectors are available, enabling effectoromics approaches that accelerate R gene cloning and specificity profiling and monitoring effector allelic diversity in pathogen populations can assist in R gene deployment in agriculture.
Journal ArticleDOI

In silicio identification of glycosyl-phosphatidylinositol-anchored plasma-membrane and cell wall proteins of Saccharomyces cerevisiae

TL;DR: Use of the Von Heijne algorithm allowed the identification of 686 open reading frames (ORFs) in the genome of Saccharomyces cerevisiae that encode proteins with a potential N‐terminal signal sequence for entering the secretory pathway.
Journal ArticleDOI

The novel Cladosporium fulvum lysin motif effector Ecp6 is a virulence factor with orthologues in other fungal species

TL;DR: Heterologous expression of ECP6 significantly increased the virulence of the vascular pathogen Fusarium oxysporum on tomato, and by RNA interference (RNAi)‐mediated gene silencing it is demonstrated that Ecp6 is instrumental for C.’fulvum virulence on tomato.
Journal ArticleDOI

Mutations in the NB-ARC domain of I-2 that impair ATP hydrolysis cause autoactivation.

TL;DR: It is proposed that the NB-ARC domain of I-2, and likely of related R proteins, functions as a molecular switch whose state (on/off) depends on the nucleotide bound (ATP/ADP).