scholarly journals Testing the executability of scenarios in general inhibitor nets

2007 ◽  
Author(s):  
Robert Lorenz ◽  
Sebastian Mauser ◽  
Robin Bergenthum
Keyword(s):  
General Inhibitor

scholarly journals Process semantics of general inhibitor nets

2004 ◽  
Vol 190 (1) ◽  
pp. 18-69 ◽  
Author(s):  
H.C.M. Kleijn ◽  
M. Koutny
Keyword(s):  
General Inhibitor

scholarly journals YM‐254890 is a General Inhibitor of G Proteins

2019 ◽  
Vol 33 (S1) ◽  
Author(s):  
Qianman Peng ◽  
Jianzhong Shen
Keyword(s):  
G Proteins ◽  
General Inhibitor

Ku is a general inhibitor of DNA-protein complex formation and transcription

1996 ◽  
Vol 33 (9) ◽  
pp. 787-796 ◽  
Author(s):  
Masashi Ono ◽  
Philip W. Tucker ◽  
J.Donald Capra
Keyword(s):  
Complex Formation ◽  
Protein Complex ◽  
Protein Complex Formation ◽  
General Inhibitor

Precipitation Reactions Between Components of Plant Tissue Extracts

1975 ◽  
Vol 2 (4) ◽  
pp. 533 ◽  
Author(s):  
MA Jermyn
Keyword(s):  
Concanavalin A ◽  
Carbohydrate Binding ◽  
Exact Nature ◽  
Plant Seeds ◽  
Tissue Extracts ◽  
General Inhibitor ◽  
Precipitation Reactions ◽  
Leguminous Seeds ◽  
Gel Diffusion ◽  
Seed Extracts

Precipitation lines are observed on gel-diffusion plates between many pairs of seed extracts. Interactions involving Canavalia ensiformis depend upon concanavalin A, and a number of extracts from other plant seeds contain a precipitant that mimics that lectin. Methyl a-D-mannopyranoside is a general inhibitor of the precipitation phenomenon and some form of protein-carbohydrate binding seems to be involved in all precipitations, although the exact nature of the macromolecules taking part is obscure. For the leguminous seeds Phaseolus vulgauis, Vicia faba and Cajanus cajan, precipitation reactions occur between extracts of cotyledons and extracts of tissues of the parent plants, even of the testa of the seeds. The nature of these reactions appears to be the same as those of the interspecies ones. Both types of reaction may be examples of ways in which plant cells recognize self from non-self. The material in P. vulgaris that reacts with concanavalin A is a group of globulin-like glycoproteins (5 % carbohydrate), heterogeneous in both charge and molecular weight but similar in overall amino acid analysis.

scholarly journals Mode of inhibition of HIV reverse transcriptase by 2-hexaprenylhydroquinone, a novel general inhibitor of RNA-and DNA-directed DNA polymerases

1997 ◽  
Vol 324 (3) ◽  
pp. 721-727 ◽  
Author(s):  
Shoshana LOYA ◽  
Amira RUDI ◽  
Yoel KASHMAN ◽  
Amnon HIZI
Keyword(s):  
Reverse Transcriptase ◽  
Dna Polymerases ◽  
Competitive Inhibitor ◽  
Polymerization Process ◽  
Hiv Reverse Transcriptase ◽  
Allosteric Site ◽  
Leukaemia Virus ◽  
General Inhibitor ◽  
Hiv 1 ◽  
Rna And Dna

A natural compound from the Red Sea sponge Ircinia sp., 2-hexaprenylhydroquinone (HPH), has been shown to be a general inhibitor of retroviral reverse transcriptases (from HIV-1, HIV-2 and murine leukaemia virus) as well as of cellular DNA polymerases (Escherichia coli DNA polymerase I, and DNA polymerases α and β). The pattern of inhibition was found to be similar for all DNA polymerases tested. Thus the mode of inhibition was studied in detail for HIV-1 reverse transcriptase. HPH is a non-competitive inhibitor and binds the enzyme irreversibly with high affinity (Ki = 0.62 μM). The polar hydroxy groups have been shown to be of key importance. A methylated derivative, mHPH, which is devoid of these polar moieties, showed a significantly decreased capacity to inhibit all DNA polymerases tested. Like the natural product, mHPH binds the enzyme independently at an allosteric site, but with reduced affinity (Ki = 7.4 μM). We show that HPH does not interfere with the first step of the polymerization process, i.e. the physical formation of the reverse-transcriptase–DNA complex. Consequently, we suggest that the natural inhibitor interferes with the subsequent steps of the overall reaction. Since HPH seems not to affect the affinity of dNTP for the enzyme (the Km is unchanged under conditions where the HPH concentration is increased), we speculate that its inhibitory capacity is derived from its effect on the nucleotidyl-transfer catalytic reaction. We suggest that such a mechanism of inhibition is typical of an inhibitor whose mode of inhibition should be common to all RNA- and DNA-directed polymerases.

Nutrition and Somatomedin. VIM. The "Somatomedin Inhibitor" in Diabetic Rat Serum is a General Inhibitor of Growing Cartilage

Diabetes ◽  
1979 ◽  
Vol 28 (10) ◽  
pp. 919-924 ◽  
Author(s):  
L. S. Phillips ◽  
R. Vassilopoulou-Sellin ◽  
L. A. Reichard
Keyword(s):  
Diabetic Rat ◽  
Rat Serum ◽  
General Inhibitor

p58IPK is an inhibitor of the eIF2α kinase GCN2 and its localization and expression underpin protein synthesis and ER processing capacity

2015 ◽  
Vol 465 (2) ◽  
pp. 213-225 ◽  
Author(s):  
Anne Roobol ◽  
Jo Roobol ◽  
Amandine Bastide ◽  
John R. P. Knight ◽  
Anne E. Willis ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Synthesis ◽  
Cellular Stress ◽  
Processing Capacity ◽  
General Inhibitor ◽  
Eif2α Kinase

We show that p58IPK is a general inhibitor of the eIF2α kinases and its expression and localization are important in the capacity of the cells to respond to cellular stress by controlling protein synthesis rates and subsequent folding in the endoplasmic reticulum.

Processing of the Drosophila Sog protein creates a novel BMP inhibitory activity

Development ◽  
2000 ◽  
Vol 127 (10) ◽  
pp. 2143-2154 ◽  
Author(s):  
K. Yu ◽  
S. Srinivasan ◽  
O. Shimmi ◽  
B. Biehs ◽  
K.E. Rashka ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
Bmp Signaling ◽  
Developmentally Regulated ◽  
Biologically Relevant ◽  
Adult Wing ◽  
General Inhibitor ◽  
Extracellular Factor ◽  
Mutant Phenotypes

Structurally unrelated neural inducers in vertebrate and invertebrate embryos have been proposed to function by binding to BMP4 or Dpp, respectively, and preventing these homologous signals from activating their receptor(s). In this study, we investigate the functions of various forms of the Drosophila Sog protein using the discriminating assay of Drosophila wing development. We find that misexpression of Drosophila Sog, or its vertebrate counterpart Chordin, generates a very limited vein-loss phenotype. This sog misexpression phenotype is very similar to that of viable mutants of glass-bottom boat (gbb), which encodes a BMP family member. Consistent with Sog selectively interfering with Gbb signaling, Sog can block the effect of misexpressing Gbb, but not Dpp in the wing. In contrast to the limited BMP inhibitory activity of Sog, we have identified carboxy-truncated forms of Sog, referred to as Supersog, which when misexpressed cause a broad range of dpp(−) mutant phenotypes. In line with its phenotypic effects, Supersog can block the effects of both misexpressing Dpp and Gbb in the wing. Vertebrate Noggin, on the other hand, acts as a general inhibitor of Dpp signaling, which can interfere with the effect of overexpressing Dpp, but not Gbb. We present evidence that Sog processing occurs in vivo and is biologically relevant. Overexpression of intact Sog in embryos and adult wing primordia leads to the developmentally regulated processing of Sog. This in vivo processing of Sog can be duplicated in vitro by treating Sog with a combination of the metalloprotease Tolloid (Tld) plus Twisted Gastrulation (Tsg), another extracellular factor involved in Dpp signaling. In accord with this result, coexpression of intact Sog and Tsg in developing wings generates a phenotype very similar to that of Supersog. Finally, we provide evidence that tsg functions in the embryo to generate a Supersog-like activity, since Supersog can partially rescue tsg(−) mutants. Consistent with this finding, sog(−)and tsg(−) mutants exhibit similar dorsal patterning defects during early gastrulation. These results indicate that differential processing of Sog generates a novel BMP inhibitory activity during development and, more generally, that BMP antagonists play distinct roles in regulating the quality as well as the magnitude of BMP signaling.

scholarly journals Apoptosis in Candida biofilms exposed to amphotericin B

2010 ◽  
Vol 59 (2) ◽  
pp. 149-157 ◽  
Author(s):  
Rawya S. Al-Dhaheri ◽  
L. Julia Douglas
Keyword(s):  
Amphotericin B ◽  
Antifungal Agents ◽  
Candida Parapsilosis ◽  
Candida Krusei ◽  
Clinical Use ◽  
Caspase Activity ◽  
Persister Cells ◽  
Specific Staining ◽  
General Inhibitor ◽  
Staining Methods

Candida biofilms are resistant to a range of antifungal agents in current clinical use. The basis of this drug resistance is not clear, but in some cases it could be due to the presence of a small number of drug-tolerant or persister cells. In this study, specific staining methods were used to investigate the existence of persisters and apoptosis in Candida biofilms subjected to different concentrations of amphotericin B. Fluorescein diacetate staining revealed the presence of persisters in biofilms of one of two strains of Candida albicans tested, and in biofilms of Candida krusei and Candida parapsilosis. Caspase activity, indicative of apoptosis, was detected with SR-FLICA and (aspartyl)2-rhodamine 110 fluorochrome-based staining reagents in all of these biofilms. The general inhibitor of mammalian caspases, Z-VAD-FMK, when used at a low concentration (2.5 μM), increased the viability of drug-treated biofilms up to 11.5-fold (P <0.001 %). Seven specific caspase inhibitors had different effects on C. albicans biofilm viability, but inhibitors of caspases-1, −9, −5, −3 and −2 all significantly increased cell survival (40-fold, 8-fold, 3.5-fold, 1.9-fold and 1.7-fold, respectively). However, histone deacetylase (HDA) inhibitors enhanced the activity of amphotericin B for biofilms of all three Candida species. Sodium butyrate and sodium valproate, for example, when added concurrently with amphotericin B, completely eliminated biofilm populations of C. albicans. Overall, our results demonstrate an apoptotic process in amphotericin-treated biofilms of three Candida species. They also indicate that HDA inhibitors can enhance the action of the drug and in some cases even eradicate persister subpopulations, suggesting that histone acetylation might activate apoptosis in these cells.

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