scholarly journals Glyceraldehyde 3-Phosphate Dehydrogenase Is a Cellular Target of the Insulin Mimic Demethylasterriquinone B1

2007 ◽  
Vol 50 (15) ◽  
pp. 3423-3426 ◽  
Author(s):  
Hyunsoo Kim ◽  
Liu Deng ◽  
Xin Xiong ◽  
William D. Hunter ◽  
Melissa C. Long ◽  
...  
Keyword(s):  
Cellular Target ◽  
Demethylasterriquinone B1 ◽  
Insulin Mimic

scholarly journals The Buzz about ADP-Ribosylation Toxins from Paenibacillus larvae, the Causative Agent of American Foulbrood in Honey Bees

Toxins ◽  
2021 ◽  
Vol 13 (2) ◽  
pp. 151
Author(s):  
Julia Ebeling ◽  
Anne Fünfhaus ◽  
Elke Genersch
Keyword(s):  
Virulence Factors ◽  
Structural Similarity ◽  
Paenibacillus Larvae ◽  
American Foulbrood ◽  
Rho Proteins ◽  
Experimental Proof ◽  
Host Interactions ◽  
B Subunit ◽  
Cellular Target ◽  
B Subunits

The Gram-positive, spore-forming bacterium Paenibacillus larvae is the etiological agent of American Foulbrood, a highly contagious and often fatal honey bee brood disease. The species P. larvae comprises five so-called ERIC-genotypes which differ in virulence and pathogenesis strategies. In the past two decades, the identification and characterization of several P. larvae virulence factors have led to considerable progress in understanding the molecular basis of pathogen-host-interactions during P. larvae infections. Among these virulence factors are three ADP-ribosylating AB-toxins, Plx1, Plx2, and C3larvin. Plx1 is a phage-born toxin highly homologous to the pierisin-like AB-toxins expressed by the whites-and-yellows family Pieridae (Lepidoptera, Insecta) and to scabin expressed by the plant pathogen Streptomyces scabiei. These toxins ADP-ribosylate DNA and thus induce apoptosis. While the presumed cellular target of Plx1 still awaits final experimental proof, the classification of the A subunits of the binary AB-toxins Plx2 and C3larvin as typical C3-like toxins, which ADP-ribosylate Rho-proteins, has been confirmed experimentally. Normally, C3-exoenzymes do not occur together with a B subunit partner, but as single domain toxins. Interestingly, the B subunits of the two P. larvae C3-like toxins are homologous to the B-subunits of C2-like toxins with striking structural similarity to the PA-63 protomer of Bacillus anthracis.

scholarly journals Small molecule induces mitochondrial fusion for neuroprotection via targeting CK2 without affecting its conventional kinase activity

2021 ◽  
Vol 6 (1) ◽  
Author(s):  
Ke-Wu Zeng ◽  
Jing-Kang Wang ◽  
Li-Chao Wang ◽  
Qiang Guo ◽  
Ting-Ting Liu ◽  
...  
Keyword(s):  
Small Molecule ◽  
Nuclear Translocation ◽  
Fusion Gene ◽  
Artery Occlusion ◽  
Mitochondrial Fusion ◽  
Dependent Manner ◽  
Behavioral Deficits ◽  
Α Subunit ◽  
Cellular Target ◽  
Cerebral Artery Occlusion

AbstractMitochondrial fusion/fission dynamics plays a fundamental role in neuroprotection; however, there is still a severe lack of therapeutic targets for this biological process. Here, we found that the naturally derived small molecule echinacoside (ECH) significantly promotes mitochondrial fusion progression. ECH selectively binds to the previously uncharacterized casein kinase 2 (CK2) α′ subunit (CK2α′) as a direct cellular target, and genetic knockdown of CK2α′ abolishes ECH-mediated mitochondrial fusion. Mechanistically, ECH allosterically regulates CK2α′ conformation to recruit basic transcription factor 3 (BTF3) to form a binary protein complex. Then, the CK2α′/BTF3 complex facilitates β-catenin nuclear translocation to activate TCF/LEF transcription factors and stimulate transcription of the mitochondrial fusion gene Mfn2. Strikingly, in a mouse middle cerebral artery occlusion (MCAO) model, ECH administration was found to significantly improve cerebral injuries and behavioral deficits by enhancing Mfn2 expression in wild-type but not CK2α′+/− mice. Taken together, our findings reveal, for the first time, that CK2 is essential for promoting mitochondrial fusion in a Wnt/β-catenin-dependent manner and suggest that pharmacologically targeting CK2 is a promising therapeutic strategy for ischemic stroke.

Rapid Evaluation of Small Molecule Cellular Target Engagement with a Luminescent Thermal Shift Assay

2021 ◽  
Author(s):  
Jonathan D. Mortison ◽  
Ivan Cornella-Taracido ◽  
Gireedhar Venkatchalam ◽  
Anthony W. Partridge ◽  
Nirodhini Siriwardana ◽  
...  
Keyword(s):  
Small Molecule ◽  
Rapid Evaluation ◽  
Target Engagement ◽  
Thermal Shift Assay ◽  
Cellular Target ◽  
Thermal Shift

scholarly journals Evaluation of the binding affinity of E3 ubiquitin ligase ligands by cellular target engagement and in-cell ELISA assay

2021 ◽  
Vol 2 (1) ◽  
pp. 100288
Author(s):  
Ka Yang ◽  
Yaxian Zhou ◽  
Brett L. Roberts ◽  
Xueqing Nie ◽  
Weiping Tang
Keyword(s):  
Binding Affinity ◽  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
Elisa Assay ◽  
Target Engagement ◽  
Cellular Target ◽  
Cell Elisa

scholarly journals Nutrient-Deprivation Autophagy Factor-1 (NAF-1): Biochemical Properties of a Novel Cellular Target for Anti-Diabetic Drugs

PLoS ONE ◽  
2013 ◽  
Vol 8 (5) ◽  
pp. e61202 ◽  
Author(s):  
Sagi Tamir ◽  
John A. Zuris ◽  
Lily Agranat ◽  
Colin H. Lipper ◽  
Andrea R. Conlan ◽  
...  
Keyword(s):  
Biochemical Properties ◽  
Nutrient Deprivation ◽  
Cellular Target

scholarly journals Identifying the Cellular Target of a Cordyheptapeptide A and Synthetic Derivatives

2021 ◽  
Author(s):  
Victoria G. Klein ◽  
Walter M. Bray ◽  
Hao-Yuan Wang ◽  
Quinn Edmondson ◽  
Joshua Schwochert ◽  
...  
Keyword(s):  
Cellular Target ◽  
Synthetic Derivatives

scholarly journals Ivermectin effectively inhibits hepatitis E virus replication, requiring the host nuclear transport protein importin α1

2021 ◽  
Author(s):  
Yunlong Li ◽  
Zhijiang Miao ◽  
Pengfei Li ◽  
Ruyi Zhang ◽  
Denis E. Kainov ◽  
...  
Keyword(s):  
Hepatitis E Virus ◽  
Nuclear Transport ◽  
Hepatitis E ◽  
Term Treatment ◽  
Cellular Target ◽  
Long Term Treatment ◽  
Culture Models ◽  
Transport Complex ◽  
Cell Culture Models

AbstractWe show that ivermectin, an FDA-approved anti-parasitic drug, effectively inhibits infection with hepatitis E virus (HEV) genotypes 1 and 3 in a range of cell culture models, including hepatic and extrahepatic cells. Long-term treatment showed no clear evidence of the development of drug resistance. Gene silencing of importin-α1, a cellular target of ivermectin and a key member of the host nuclear transport complex, inhibited viral replication and largely abolished the anti-HEV effect of ivermectin.

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