about
A role in immunity for Arabidopsis cysteine protease RD21, the ortholog of the tomato immune protease C14.Enzyme-inhibitor interactions at the plant-pathogen interface.Proteasome Activity Profiling Uncovers Alteration of Catalytic β2 and β5 Subunits of the Stress-Induced Proteasome during Salinity Stress in Tomato Roots.Papain-like cysteine proteases as hubs in plant immunity.Subunit-selective proteasome activity profiling uncovers uncoupled proteasome subunit activities during bacterial infections.Activity profiling reveals changes in the diversity and activity of proteins in Arabidopsis roots in response to nematode infection.Activity profiling of vacuolar processing enzymes reveals a role for VPE during oomycete infection.Subfamily-Specific Fluorescent Probes for Cysteine Proteases Display Dynamic Protease Activities during Seed Germination.Pseudomonas syringae colonizes distant tissues in Nicotiana benthamiana through xylem vessels.The apoplast as battleground for plant-microbe interactions.A fungal substrate mimicking molecule suppresses plant immunity via an inter-kingdom conserved motifProteases Underground: Analysis of the Maize Root Apoplast Identifies Organ Specific Papain-Like Cysteine Protease ActivityProteasome activity imaging and profiling characterizes bacterial effector syringolin ASNARE-RNAi results in higher terpene emission from ectopically expressed caryophyllene synthase in Nicotiana benthamianaDynamic hydrolase activities precede hypersensitive tissue collapse in tomato seedlingsDynamic hydrolase labelling as a marker for seed quality in Arabidopsis seedsMolecular Interactions Between Smut Fungi and Their Host Plants
P50
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P50
description
investigador
@es
researcher
@en
wetenschapper
@nl
name
Johana C Misas-Villamil
@en
Johana C Misas-Villamil
@nl
type
label
Johana C Misas-Villamil
@en
Johana C Misas-Villamil
@nl
prefLabel
Johana C Misas-Villamil
@en
Johana C Misas-Villamil
@nl
P108
P31
P496
0000-0002-9623-0710