Characterization of the transcript of a new class of retroposon-type repetitive element cloned from the powdery mildew fungus,

1996 ◽  
Vol 250 (4) ◽  
pp. 477 ◽  
Author(s):  
Y. D. Wei ◽  
D. B. Collinge ◽  
Viggo Smedegaard-Petersen ◽  
Hans Thordal-Christensen
Keyword(s):  
Powdery Mildew ◽  
Repetitive Element ◽  
Powdery Mildew Fungus ◽  
New Class

Characterization of the transcript of a new class of retroposon-type repetitive element cloned from the powdery mildew fungus,Erysiphe graminis

1996 ◽  
Vol 250 (4) ◽  
pp. 477-482
Author(s):  
Y. D. Wei ◽  
D. B. Collinge ◽  
V. Smedegaard-Petersen ◽  
H. Thordal-Christensen
Keyword(s):  
Powdery Mildew ◽  
Repetitive Element ◽  
Erysiphe Graminis ◽  
Powdery Mildew Fungus ◽  
New Class

cDNA cloning and characterization of two barley peroxidase transcripts induced differentially by the powdery mildew fungus Erysiphe graminis

1992 ◽  
Vol 40 (6) ◽  
pp. 395-409 ◽  
Author(s):  
Hans Thordal-Christensen ◽  
Jakob Brandt ◽  
Baik Ho Cho ◽  
Søren K. Rasmussen ◽  
Per L. Gregersen ◽  
...  
Keyword(s):  
Powdery Mildew ◽  
Cdna Cloning ◽  
Erysiphe Graminis ◽  
Powdery Mildew Fungus

scholarly journals Molecular Characterization of the Oxalate Oxidase Involved in the Response of Barley to the Powdery Mildew Fungus

1998 ◽  
Vol 117 (1) ◽  
pp. 33-41 ◽  
Author(s):  
Fasong Zhou ◽  
Ziguo Zhang ◽  
Per L. Gregersen ◽  
Jørn D. Mikkelsen ◽  
Eigil de Neergaard ◽  
...  
Keyword(s):  
Powdery Mildew ◽  
Molecular Characterization ◽  
Oxalate Oxidase ◽  
Powdery Mildew Fungus

Cloning and Characterization of a Novel Wheat Glycoside Hydrolase Gene TaGlc2 Induced by Powdery Mildew Pathogen (Erysiphe graminis) Infection

2009 ◽  
Vol 35 (5) ◽  
pp. 786-794
Author(s):  
N PUDAKE Ramesh ◽  
Ming-Ming XIN ◽  
Yu-Jing YIN ◽  
Chao-Jie XIE ◽  
Zhong-Fu NI ◽  
...  
Keyword(s):  
Powdery Mildew ◽  
Glycoside Hydrolase ◽  
Erysiphe Graminis ◽  
Powdery Mildew Pathogen

Targeting IDH Mutations in AML: Wielding the Double-edged Sword of Differentiation

2020 ◽  
Vol 20 (7) ◽  
pp. 490-500 ◽  
Author(s):  
Justin S. Becker ◽  
Amir T. Fathi
Keyword(s):  
Genome Structure ◽  
Cellular Metabolism ◽  
Standard Of Care ◽  
Competitive Inhibitor ◽  
Driver Mutations ◽  
New Class ◽  
Regulatory Enzymes ◽  
Idh Mutations ◽  
Genomic Characterization

The genomic characterization of acute myeloid leukemia (AML) by DNA sequencing has illuminated subclasses of the disease, with distinct driver mutations, that might be responsive to targeted therapies. Approximately 15-23% of AML genomes harbor mutations in one of two isoforms of isocitrate dehydrogenase (IDH1 or IDH2). These enzymes are constitutive mediators of basic cellular metabolism, but their mutated forms in cancer synthesize an abnormal metabolite, 2- hydroxyglutarate, that in turn acts as a competitive inhibitor of multiple gene regulatory enzymes. As a result, leukemic IDH mutations cause changes in genome structure and gene activity, culminating in an arrest of normal myeloid differentiation. These discoveries have motivated the development of a new class of selective small molecules with the ability to inhibit the mutant IDH enzymes while sparing normal cellular metabolism. These agents have shown promising anti-leukemic activity in animal models and early clinical trials, and are now entering Phase 3 study. This review will focus on the growing preclinical and clinical data evaluating IDH inhibitors for the treatment of IDH-mutated AML. These data suggest that inducing cellular differentiation is central to the mechanism of clinical efficacy for IDH inhibitors, while also mediating toxicity for patients who experience IDH Differentiation Syndrome. Ongoing trials are studying the efficacy of IDH inhibitors in combination with other AML therapies, both to evaluate potential synergistic combinations as well as to identify the appropriate place for IDH inhibitors within existing standard-of-care regimens.

Spectral characterization of fungal diseases downy mildew, powdery mildew, black-foot and Petri disease on Vitis vinifera leaves

2021 ◽  
Vol 42 (15) ◽  
pp. 5680-5697
Author(s):  
Pâmela A. Pithan ◽  
Jorge R. Ducati ◽  
Lucas R. Garrido ◽  
Diniz C. Arruda ◽  
Adriane B. Thum ◽  
...  
Keyword(s):  
Powdery Mildew ◽  
Vitis Vinifera ◽  
Downy Mildew ◽  
Fungal Diseases ◽  
Spectral Characterization ◽  
Petri Disease ◽  
Black Foot

scholarly journals Disruption of barley immunity to powdery mildew by an in-frame Lys-Leu deletion in the essential protein SGT1

Genetics ◽  
2020 ◽  
Vol 217 (2) ◽  
Author(s):  
Antony V E Chapman ◽  
Matthew Hunt ◽  
Priyanka Surana ◽  
Valeria Velásquez-Zapata ◽  
Weihui Xu ◽  
...  
Keyword(s):  
Powdery Mildew ◽  
Fungal Pathogens ◽  
Novel Mutation ◽  
Exome Capture ◽  
Resistance Locus ◽  
Hordeum Vulgare L ◽  
Powdery Mildew Fungus ◽  
Pathogen Effectors ◽  
Cell Processes ◽  
Disease Resistances

Abstract Barley (Hordeum vulgare L.) Mla (Mildew resistance locus a) and its nucleotide-binding, leucine-rich-repeat receptor (NLR) orthologs protect many cereal crops from diseases caused by fungal pathogens. However, large segments of the Mla pathway and its mechanisms remain unknown. To further characterize the molecular interactions required for NLR-based immunity, we used fast-neutron mutagenesis to screen for plants compromised in MLA-mediated response to the powdery mildew fungus, Blumeria graminis f. sp. hordei. One variant, m11526, contained a novel mutation, designated rar3 (required for Mla6 resistance3), that abolishes race-specific resistance conditioned by the Mla6, Mla7, and Mla12 alleles, but does not compromise immunity mediated by Mla1, Mla9, Mla10, and Mla13. This is analogous to, but unique from, the differential requirement of Mla alleles for the co-chaperone Rar1 (required for Mla12 resistance1). We used bulked-segregant-exome capture and fine mapping to delineate the causal mutation to an in-frame Lys-Leu deletion within the SGS domain of SGT1 (Suppressor of G-two allele of Skp1, Sgt1ΔKL308–309), the structural region that interacts with MLA proteins. In nature, mutations to Sgt1 usually cause lethal phenotypes, but here we pinpoint a unique modification that delineates its requirement for some disease resistances, while unaffecting others as well as normal cell processes. Moreover, the data indicate that the requirement of SGT1 for resistance signaling by NLRs can be delimited to single sites on the protein. Further study could distinguish the regions by which pathogen effectors and host proteins interact with SGT1, facilitating precise editing of effector incompatible variants.

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