scholarly journals Role of Equalized Electronegativity in Modeling HIV-RT Inhibitory Activity

2017 ◽  
Vol Volume-2 (Issue-1) ◽  
pp. 972-984
Author(s):  
Anita K. ◽  
Shweta Sharma ◽  
Suparna Ghosh | Ruchi Dubey Sharma ◽  
Keyword(s):  
Inhibitory Activity ◽  
Hiv Rt

scholarly journals Exploring the role of the α-carboxyphosphonate moiety in the HIV-RT activity of α-carboxy nucleoside phosphonates

2016 ◽  
Vol 14 (8) ◽  
pp. 2454-2465 ◽  
Author(s):  
Nicholas D. Mullins ◽  
Nuala M. Maguire ◽  
Alan Ford ◽  
Kalyan Das ◽  
Eddy Arnold ◽  
...  
Keyword(s):  
Acid Moiety ◽  
Phosphonoacetic Acid ◽  
Hiv Rt

The importance of the α-carboxy phosphonoacetic acid moiety to achieve RT inhibition, without the need for prior phosphorylation, is confirmed.

The Role of Aromatase Enzyme in Hormone Related Diseases and Plant-Based Aromatase Inhibitors as Therapeutic Regimens

2021 ◽  
Vol 21 ◽  
Author(s):  
Kevser Taban Akça ◽  
Murside Ayşe Demirel ◽  
Ipek Süntar
Keyword(s):  
Natural Products ◽  
Aromatase Inhibitors ◽  
Inhibitory Activity ◽  
Chemical Compounds ◽  
Synthesis Methods ◽  
Herbal Drugs ◽  
Drug Discovery And Development ◽  
History Of ◽  
History Of Use

: Medicinal plants have a long history of use as food and remedy in traditional and modern societies, as well as have been used as herbal drugs and sources of novel bioactive compounds. They provide a wide array of chemical compounds, many of which can not be synthesized via current synthesis methods. Natural products may provide aromatase inhibitory activity through various pathways and may act clinically effective for treating pathologies associated with excessive aromatase secretion including breast, ovarian and endometrial cancers, endometriosis, uterine fibroid, benign prostatic hyperplasia (BPH), prostate cancer, infertility, and gynecomastia. Recent studies have shown that natural products with aromatase inhibitory activity, could also be good options against secondary recurrence of breast cancer by exhibiting chemopreventive effects. Therefore, screening for new plant-based aromatase inhibitors may provide novel leads for drug discovery and development, particularly with increased clinical efficacy and decreased side effects.

scholarly journals Interaction between complement proteins C5b-7 and erythrocyte membrane sialic acid.

1996 ◽  
Vol 184 (4) ◽  
pp. 1225-1232 ◽  
Author(s):  
P Marshall ◽  
A Hasegawa ◽  
E A Davidson ◽  
V Nussenzweig ◽  
M Whitlow
Keyword(s):  
Sialic Acid ◽  
Carboxylic Acid ◽  
Cell Membrane ◽  
Inhibitory Activity ◽  
Initial Phase ◽  
Ionic Interaction ◽  
Complement Proteins ◽  
Erythrocyte Surface ◽  
Complement Lysis

The initial phase of membrane attack by complement is the interaction between C5b6, C7, and the cell membrane that leads to the insertion of C5b-7. Here we investigate the role of sialic acid residues in the assembly of C5b-7 intermediates on erythrocyte cell membranes. We find that C5b6 binds to glycophorin, whereas C5 or C6 does not bind, and desialylation of the glycophorin abolishes C5b6 binding. Complement lysis is inhibited by either masking glycophorin sialic acid with F(ab) fragments of an mAb, or by removal of the sialylated region of glycophorin by mild trypsinization. Gangliosides inhibit C5b-7 deposition when added to the aqueous phase. Asialogangliosides and synthetic gangliosides lacking the carboxylic acid residue have no inhibitory activity. We conclude that C5b6 binds to sialylated molecules on the erythrocyte surface. We propose a new model of membrane attack in which C5b6 initially binds to membranes via ionic forces. C7 then binds to C5b6, disrupting the ionic interaction and leading to the exposure of hydrophobic domains. Sialic acid is known to inhibit complement activation. Thus, these findings reveal a paradoxical role for sialic acid in complement attack; the presence of sialic acid inhibits the generation of C5b6, but once the membrane attack pathway is initiated, sialic acid enhances complement lysis.

scholarly journals Inhibition of DNA-dependent transcription by the leader RNA of vesicular stomatitis virus: role of specific nucleotide sequences and cell protein binding.

1985 ◽  
Vol 5 (10) ◽  
pp. 2502-2513 ◽  
Author(s):  
B W Grinnell ◽  
R R Wagner
Keyword(s):  
Nucleotide Sequence ◽  
Hela Cell ◽  
Vesicular Stomatitis Virus ◽  
Inhibitory Activity ◽  
Cell Extract ◽  
Wild Type Virus ◽  
Rich Region ◽  
Vesicular Stomatitis ◽  
Specific Nucleotide

The leader RNA transcript of vesicular stomatitis virus inhibits transcription of the adenovirus major late promoter and virus-associated genes in a soluble HeLa cell transcription system. We examined the specific nucleotide sequence involved and the potential role of leader-protein interactions in this inhibition of RNA polymerase II- and III-directed transcription. Using synthetic oligodeoxynucleotides homologous to regions of the leader RNA molecule, we extend our previous results (B.W. Grinnell and R.R. Wagner, Cell 36:533-543, 1984) that suggest a role for the AU-rich region of the leader RNA or the homologous AT region of a cloned cDNA leader in the inhibition of DNA-dependent transcription. Our results indicate that a short nucleotide sequence (AUUAUUA) or its deoxynucleotide homolog (ATTATTA) appears to be the minimal requirement for the leader RNA to inhibit transcription by both RNA polymerases, but sequences flanking both sides of this region increase the inhibitory activity. Nucleotide changes in the homologous AT-rich region drastically decrease the transcriptional inhibitory activity. Leader RNAs from wild-type virus, but not from a 5'-defective interfering particle, form a ribonuclease-resistant, protease-sensitive ribonucleoprotein complex in the soluble HeLa cell extract. Several lines of evidence suggest that the leader RNA specifically interacts with a 65,000-dalton (65K) cellular protein. In a fractionated cell extract, only those fractions containing this 65K protein could reverse the inhibition of DNA-dependent RNA synthesis by the plus-strand vesicular stomatitis virus leader RNA or by homologous DNA. In studies with synthetic oligodeoxynucleotides homologous to leader RNA sequences, only those oligonucleotides containing the inhibitory sequence were able to bind to a gradient fraction containing the 65K protein.

scholarly journals TrkB induced metastatic potential of cancer by suppression of BMP mediated tumor inhibitory activity

2020 ◽  
Author(s):  
Min Soo Kim ◽  
Wook Jin
Keyword(s):  
Breast Cancer ◽  
Colorectal Cancer ◽  
Inhibitory Activity ◽  
Metastatic Potential ◽  
Bmp Signaling ◽  
Unique Role ◽  
Akt Activation ◽  
Growth Inhibitory ◽  
Growth Inhibitory Activity

AbstractOur previous observations also demonstrate that TrkB expression in breast cancer induces metastatic potential by both JAK2/STAT3 and PI3K/AKT activation and induced metastasis of breast cancer mediated suppression of RUNX3 and KEAP1 expression by TrkB. Also, TrkB induced metastatic potential of cancer and suppressed the growth inhibitory activity in response to BMP signaling by preventing BMRRI/BMPRII complex formation. The previous report BMP-2 and BMP4 trigger tumor inhibitory activity in colorectal cancer by upregulation of RUNX3 expression. Although TrkB may regulate tumor inhibitory activity by BMP-induced upregulation of RUNX3, it is not still fully understood how TrkB signaling adjusts to inhibit BMP signaling-mediated tumor suppression.Our findings provide important molecular insights into TrkB-mediated modulation of BMP signaling has remained unknown, and none of the studies still reported a correlation between TrkB and BMP signaling. Our current study surprisingly showed that unique role of TrkB in the regulation of BMP-induced tumor inhibitory activity and BMP-2-induced RUNX3 expression.

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