European Muon Collaboration effect: Nuclear-binding effect or vivid quark signature?

1991 ◽  
Vol 43 (6) ◽  
pp. 2821-2824 ◽  
Author(s):  
Bo-Qiang Ma
Keyword(s):  
Binding Effect ◽  
Nuclear Binding ◽  
European Muon Collaboration

Nuclear binding effect in deep-inelastic lepton scattering

1990 ◽  
Vol 234 (1-2) ◽  
pp. 170-174 ◽  
Author(s):  
S.V. Akulinichev ◽  
S. Shlomo
Keyword(s):  
Binding Effect ◽  
Nuclear Binding

Role of nuclear binding in the European-Muon-Collaboration effect

1992 ◽  
Vol 45 (3) ◽  
pp. 1374-1381 ◽  
Author(s):  
Franz Gross ◽  
S. Liuti
Keyword(s):  
Nuclear Binding ◽  
European Muon Collaboration

Unraveling the action mechanism of Buyang Huanwu Tang (BYHWT) for Cerebral Ischemia by Systematic Pharmacological Methodology

2020 ◽  
Vol 23 ◽  
Author(s):  
Shi-tang Ma ◽  
Ning Zhang ◽  
Ge Hong ◽  
Cheng-tao Feng ◽  
Sheng-wei Hong ◽  
...  
Keyword(s):  
Cerebral Ischemia ◽  
Virtual Screening ◽  
Signaling Pathways ◽  
Bioactive Compounds ◽  
Enrichment Analysis ◽  
Material Base ◽  
Lead Discovery ◽  
Binding Effect ◽  
Bioactive Ingredients ◽  
Compound Target

Background: Buyang Huanwu Tang (BYHWT) and relevant Traditional Chinese medicine (TCM) has its unique advantages in the treatment of cerebral ischemia. However, its pharmacological mechanism have not been fully explained. Objective: Base on the multi-component, also the entire disease network targets, the present study set out to identify major bioactive ingredients, key disease targets, and pathways of BYHWT against cerebral ischemia disease by systematic pharmacological methodology. Methods: Both the bioactive compounds from the BYHWT and the positive drugs against cerebral ischemia were fully investigated. The binding targets of the positive drugs were then obtained. A virtual screening protocol was then used to highlight the compound-target interaction. And network was constructed to visual the compound-target binding effect after docking analysis. Moreover，the targets enrichment analysis for biological processes and pathways were revealed to further explore the function of bio-targets protein gene and its role in the signal pathway. Results: A total of 382 active ingredients of the BYHWT and 23 candidate disease targets were identified. Virtual screening results indicated that multiple bioactive compounds targeted multiple proteins. Each compounds act on one or more targets. The mechanisms were linked to 20 signaling pathways, and the key mechanism was related to serotonergic synapse, calcium signaling pathway and camp signaling pathways. Conclusion: The present study explored the bioactive ingredients and mechanisms of BYHWT against cerebral ischemia by systematic pharmacological methodology. the novel methodology would provide a reference for the lead discovery of precursors, disease mechanism and material base for TCM.

scholarly journals Alteration of hepatic glucocorticoid receptor stability and nuclear binding in vitro by citrate

1983 ◽  
Vol 210 (1) ◽  
pp. 259-263 ◽  
Author(s):  
J Hubbard ◽  
M Kalimi
Keyword(s):  
Glucocorticoid Receptor ◽  
Glucocorticoid Receptors ◽  
Density Gradient Centrifugation ◽  
Gradient Centrifugation ◽  
Deae Cellulose ◽  
Sucrose Density Gradient ◽  
Sucrose Density Gradient Centrifugation ◽  
Nuclear Binding ◽  
Wide Range

Citrate greatly stabilized rat hepatic unbound glucocorticoid receptors in cell-free conditions at 4 degrees C with optimal effectiveness at 5-15 mM. Control receptors were inactivated at 4 degrees C with a half-life of less than 12 h. However, in the presence of 10 mM-citrate, unbound receptors were almost completely stabilized for 48 h at 4 degrees C. Citrate at a concentration of 1-2 mM yielded half-maximal stabilization. The stabilizing effect of citrate was rather specific, as succinate, alpha-oxoglutarate, oxaloacetate, malate and pyruvate had no apparent stabilizing action. Citrate stabilized receptors over a wide range of H+ concentrations, with complete protection between pH 6.5 and 8.5. In addition, citrate appeared to have a significant effect on glucocorticoid-receptor complex activation into a nuclear binding form. Thus 5-10 mM-citrate enhanced nuclear binding, with optimal activation achieved at 10 mM concentration. As analysed by sucrose-density-gradient centrifugation and DEAE-cellulose chromatography, no apparent change was observed in the physical characteristics of the glucocorticoid receptor in the presence of citrate.

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