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UnknownStructural Basis of Host Autophagy-related Protein 8 (ATG8) Binding by the Irish Potato Famine Pathogen Effector Protein PexRD54.
Not available
S-EPMC5025708 | biostudies-literature
ProteomicsBiochemical specialization of an ATG8 isoform in Nicotiana benthamiana
ATG8 is a highly-conserved ubiquitin-like protein that modulates autophagy pathways by binding autophagic membranes and numerous proteins, including cargo receptors and core autophagy components. Throughout plant evolution, ATG8 has expanded from a single protein in algae to multiple isoforms in hig...
ORGANISM(S): Nicotiana benthamiana 
2019-11-12 | PXD011484 | Pride
Atg8 Phytophthora infestans Pexrd54 Autophagy Nicotiana benthamiana 
UnknownAn oomycete effector subverts host vesicle trafficking to channel starvation-induced autophagy to the pathogen interface.
Not available
S-EPMC8382295 | biostudies-literature
UnknownRegressive evolution of an effector following a host jump in the Irish potato famine pathogen lineage.
Not available
S-EPMC9642902 | biostudies-literature
UnknownAn effector of the Irish potato famine pathogen antagonizes a host autophagy cargo receptor.
Not available
S-EPMC4775223 | biostudies-literature
UnknownHost autophagy machinery is diverted to the pathogen interface to mediate focal defense responses against the Irish potato famine pathogen.
Not available
S-EPMC6029844 | biostudies-literature
ProteomicsProtein-protein interaction of Phytophthora infestans RxLR effector AvrCap1 by immunoafinity enrichment in planta
In plants, NLR (nucleotide-binding domain and leucine-rich repeat-containing) proteins can form receptor networks to confer hypersensitive cell death and innate immunity. One class of NLRs, known as NRCs (NLR required for cell death), are central nodes in a complex network that protects against mult...
ORGANISM(S): Phytophthora infestans 
2021-03-03 | PXD023178 | Pride
Avrcap1 Rxlr effector Phytophthora infestans Rd54 
UnknownN-terminal β-strand underpins biochemical specialization of an ATG8 isoform.
Not available
S-EPMC6675122 | biostudies-literature
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