André Padilla
YOU?
Author Swipe
View article: <i>Zymoseptoria tritici</i> Effectors Structurally Related to Killer Proteins <scp>UmV</scp> ‐ <scp>KP4</scp> and <scp>UmV</scp> ‐ <scp>KP6</scp> Inhibit Fungal Growth, and Define Extended Protein Families in Fungi
<i>Zymoseptoria tritici</i> Effectors Structurally Related to Killer Proteins <span>UmV</span> ‐ <span>KP4</span> and <span>UmV</span> ‐ <span>KP6</span> Inhibit Fungal Growth, and Define Extended Protein Families in Fungi Open
Fungal effectors play crucial roles in plant infection. Despite low sequence identity, they were recently discovered to belong to families with similar three‐dimensional structures. In this study, we elucidated the structures of Zt‐NIP1 an…
View article: The <i>Magnaporthe oryzae</i> MAX effector AVR-Pia binds a novel group of rice HMA domain-containing proteins
The <i>Magnaporthe oryzae</i> MAX effector AVR-Pia binds a novel group of rice HMA domain-containing proteins Open
Phytopathogenic fungi secrete effector proteins to promote virulence. MAX ( M agnaporthe A vrs and T oxB-like) effectors form a sequence-diverse family sharing a conserved protein structure. AVR-Pia, a MAX effector from the rice blast fung…
View article: Structure‐guided insights into the biology of fungal effectors
Structure‐guided insights into the biology of fungal effectors Open
Summary Phytopathogenic fungi cause enormous yield losses in many crops, threatening both agricultural production and global food security. To infect plants, they secrete effectors targeting various cellular processes in the host. Putative…
View article: <i>Zymoseptoria tritici</i>effectors structurally related to killer proteins UmV-KP4 and UmV-KP6 are toxic to fungi, and define extended protein families in fungi
<i>Zymoseptoria tritici</i>effectors structurally related to killer proteins UmV-KP4 and UmV-KP6 are toxic to fungi, and define extended protein families in fungi Open
Fungal effectors play crucial roles in plant infection. Despite low sequence identity, effectors were recently classified into structural families. In this study, we have elucidated the structures of Zt-NIP1 and Mycgr3-91409 effectors of t…
View article: The structural landscape and diversity of Pyricularia oryzae MAX effectors revisited
The structural landscape and diversity of Pyricularia oryzae MAX effectors revisited Open
Magnaporthe AVRs and ToxB-like (MAX) effectors constitute a family of secreted virulence proteins in the fungus Pyricularia oryzae (syn . Magnaporthe oryzae) , which causes blast disease on numerous cereals and grasses. In spite of high se…
View article: The structural landscape and diversity of<i>Pyricularia oryzae</i>MAX effectors revisited
The structural landscape and diversity of<i>Pyricularia oryzae</i>MAX effectors revisited Open
Magnaporthe AVRs and ToxB-like (MAX) effectors constitute a family of secreted virulence proteins in the fungus Pyricularia oryzae (syn. Magnaporthe oryzae) , which causes blast disease on numerous cereals and grasses. In spite of high seq…
View article: Adaptive evolution in virulence effectors of the rice blast fungus Pyricularia oryzae
Adaptive evolution in virulence effectors of the rice blast fungus Pyricularia oryzae Open
Plant pathogens secrete proteins called effectors that target host cellular processes to promote disease. Recently, structural genomics has identified several families of fungal effectors that share a similar three-dimensional structure de…
View article: Does a Similar 3D Structure Mean a Similar Folding Pathway? The Presence of a C-Terminal α-Helical Extension in the 3D Structure of MAX60 Drastically Changes the Folding Pathway Described for Other MAX-Effectors from Magnaporthe oryzae
Does a Similar 3D Structure Mean a Similar Folding Pathway? The Presence of a C-Terminal α-Helical Extension in the 3D Structure of MAX60 Drastically Changes the Folding Pathway Described for Other MAX-Effectors from Magnaporthe oryzae Open
Does a similar 3D structure mean a similar folding pathway? This question is particularly meaningful when it concerns proteins sharing a similar 3D structure, but low sequence identity or homology. MAX effectors secreted by the phytopathog…
View article: Adaptive evolution in virulence effectors of the rice blast fungus<i>Pyricularia oryzae</i>
Adaptive evolution in virulence effectors of the rice blast fungus<i>Pyricularia oryzae</i> Open
Plant pathogens secrete proteins called effectors that target host cellular processes to promote disease. Recently, structural genomics has identified several families of fungal effectors that share a similar three-dimensional structure de…
View article: The activity of the <scp>RGA5</scp> sensor <scp>NLR</scp> from rice requires binding of its integrated <scp>HMA</scp> domain to effectors but not <scp>HMA</scp> domain self‐interaction
The activity of the <span>RGA5</span> sensor <span>NLR</span> from rice requires binding of its integrated <span>HMA</span> domain to effectors but not <span>HMA</span> domain self‐interaction Open
The rice nucleotide‐binding (NB) and leucine‐rich repeat (LRR) domain immune receptors (NLRs) RGA4 and RGA5 form a helper NLR/sensor NLR (hNLR/sNLR) pair that specifically recognizes the effectors AVR‐Pia and AVR1‐CO39 from the blast fungu…
View article: Combining High-Pressure NMR and Geometrical Sampling to Obtain a Full Topological Description of Protein Folding Landscapes: Application to the Folding of Two MAX Effectors from Magnaporthe oryzae
Combining High-Pressure NMR and Geometrical Sampling to Obtain a Full Topological Description of Protein Folding Landscapes: Application to the Folding of Two MAX Effectors from Magnaporthe oryzae Open
Despite advances in experimental and computational methods, the mechanisms by which an unstructured polypeptide chain regains its unique three-dimensional structure remains one of the main puzzling questions in biology. Single-molecule tec…
View article: Design of a new effector recognition specificity in a plant NLR immune receptor by molecular engineering of its integrated decoy domain
Design of a new effector recognition specificity in a plant NLR immune receptor by molecular engineering of its integrated decoy domain Open
SUMMARY Plant nucleotide-binding and leucine-rich repeat domain proteins (NLRs) are immune sensors that specifically recognize pathogen effectors and induce immune responses. Designing artificial NLRs with new effector recognition specific…
View article: Structural genomics applied to the rust fungus Melampsora larici-populina reveals two candidate effector proteins adopting cystine knot and NTF2-like protein folds
Structural genomics applied to the rust fungus Melampsora larici-populina reveals two candidate effector proteins adopting cystine knot and NTF2-like protein folds Open
Rust fungi are plant pathogens that secrete an arsenal of effector proteins interfering with plant functions and promoting parasitic infection. Effectors are often species-specific, evolve rapidly, and display low sequence similarities wit…
View article: Structural genomic applied on the rust fungus <i>Melampsora larici-populina</i> reveals two candidate effector proteins adopting cystine-knot and nuclear transport factor 2-like protein folds
Structural genomic applied on the rust fungus <i>Melampsora larici-populina</i> reveals two candidate effector proteins adopting cystine-knot and nuclear transport factor 2-like protein folds Open
Rust fungi are plant pathogens that secrete an arsenal of effector proteins interfering with plant functions and promoting parasitic infection. Effectors are often species-specific, evolve rapidly, and display low sequence similarities wit…
View article: Specific recognition of two MAX effectors by integrated HMA domains in plant immune receptors involves distinct binding surfaces
Specific recognition of two MAX effectors by integrated HMA domains in plant immune receptors involves distinct binding surfaces Open
The structurally conserved but sequence-unrelated MAX ( Magnaporthe oryzae avirulence and ToxB-like) effectors AVR1-CO39 and AVR-PikD from the blast fungus M. oryzae are recognized by the rice nucleotide-binding domain and leucine-rich rep…
View article: Recognition of the <i>Magnaporthe oryzae</i> Effector AVR-Pia by the Decoy Domain of the Rice NLR Immune Receptor RGA5
Recognition of the <i>Magnaporthe oryzae</i> Effector AVR-Pia by the Decoy Domain of the Rice NLR Immune Receptor RGA5 Open
Nucleotide binding domain and leucine-rich repeat proteins (NLRs) are important receptors in plant immunity that allow recognition of pathogen effectors. The rice (Oryza sativa) NLR RGA5 recognizes the Magnaporthe oryzae effector AVR-Pia t…
View article: The molecular bases of recognition of the M. Oryzae effector protein AVR-Pia by the rice immune receptor RGA5
The molecular bases of recognition of the M. Oryzae effector protein AVR-Pia by the rice immune receptor RGA5 Open
BGPI : équipe 4
View article: DNPH1 inhibition by cytokinin ribosides 5’-monophosphates and <i>N</i><sup>6</sup>-substituted AMP.
DNPH1 inhibition by cytokinin ribosides 5’-monophosphates and <i>N</i><sup>6</sup>-substituted AMP. Open
DNPH1 inhibition by cytokinin ribosides 5’-monophosphates and N6-substituted AMP.
View article: Structure Analysis Uncovers a Highly Diverse but Structurally Conserved Effector Family in Phytopathogenic Fungi
Structure Analysis Uncovers a Highly Diverse but Structurally Conserved Effector Family in Phytopathogenic Fungi Open
Phytopathogenic ascomycete fungi possess huge effector repertoires that are dominated by hundreds of sequence-unrelated small secreted proteins. The molecular function of these effectors and the evolutionary mechanisms that generate this t…