Academic literature on the topic 'Cinnamyl-hydroxamate'

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Journal articles on the topic "Cinnamyl-hydroxamate"

1

Joshi, Mit, Neetinkumar D. Reddy, Nitesh Kumar, Suhani Sumalatha, and Mallikarjuna Rao Chamallamudi. "Cinnamyl Sulfonamide Hydroxamate Derivatives Inhibited LPS-Stimulated NF-kB Expression in RAW 264.7 Cells In Vitro and Mitigated Experimental Colitis in Wistar Rats In Vivo." Current Pharmaceutical Design 26, no. 38 (2020): 4934–43. http://dx.doi.org/10.2174/1381612826666200625101442.

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Background: Histone deacetylase (HDAC) inhibition has been found to be effective in the treatment of inflammatory bowel disease. Previous studies have reported that Cinnamyl sulfonamide hydroxamate derivatives possess non-selective HDAC inhibition. Objective: The present study was designed to screen three selected Cinnamyl sulfonamide hydroxamate derivatives, NMJ-1, NMJ-2, and NMJ3, for in vitro anti-inflammatory response by assessing the expression of pNF-κB in lipopolysaccharide (LPS)-induced inflammatory changes on RAW 264.7 cells, and in vivo anti-inflammatory response in acetic acid (AA)
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2

Tavares, Maurício Temotheo, Larissa Costa de Almeida, Thales Kronenberger, et al. "Structure-activity relationship and mechanistic studies for a series of cinnamyl hydroxamate histone deacetylase inhibitors." Bioorganic & Medicinal Chemistry 35 (April 2021): 116085. http://dx.doi.org/10.1016/j.bmc.2021.116085.

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3

Reddy, Neetinkumar D., M. H. Shoja, B. S. Jayashree, et al. "In vitro and in vivo evaluation of novel cinnamyl sulfonamide hydroxamate derivative against colon adenocarcinoma." Chemico-Biological Interactions 233 (May 2015): 81–94. http://dx.doi.org/10.1016/j.cbi.2015.03.015.

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4

Reddy, Neetinkumar D., M. H. Shoja, Subhankar Biswas, Pawan G. Nayak, Nitesh Kumar, and C. Mallikarjuna Rao. "An appraisal of cinnamyl sulfonamide hydroxamate derivatives (HDAC inhibitors) for anti-cancer, anti-angiogenic and anti-metastatic activities in human cancer cells." Chemico-Biological Interactions 253 (June 2016): 112–24. http://dx.doi.org/10.1016/j.cbi.2016.05.008.

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5

Tavares, Maurício Temotheo, Almeida Larissa Costa de, Thales Kronenberger, et al. "Structure-Activity Relationship and Mechanistic Studies for a Series of Cinnamylhydroxamate Derived Histone Deacetylase (HDAC) Inhibitors." October 3, 2020. https://doi.org/10.5281/zenodo.4064775.

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HDAC1 molecular dynamics simulations with co-crystallized ligand and proposed novel cinnamyl-hydroxamate anticancer agents. Details regarding the simulation method can be found in the respective publication.
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6

C K, Swaliha, Jayachandran T P, and Shadiya C K. "Evaluation of Anti-inflammatory Activity of Novel HDAC Inhibitors using in vitro Methods." Research Journal of Pharmacy and Technology, December 24, 2022, 5455–58. http://dx.doi.org/10.52711/0974-360x.2022.00919.

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Inflammation is a neighborhood reaction to cell injury that is set apart by fine enlargement, leukocytic invasion, redness, heat, agony, expanding and loss of function. HDAC inhibitors play crucial role in regulation of inflammatory gene expression. The point of the investigation was to assess the anti-inflammatory activity of novel HDAC inhibitors having cinnamyl moiety. In the present study, two cinnamyl sulfonamide hydroxamate (CSH) derivatives (4a and 4b) were evaluated for their anti-inflammatory activity by in vitro methods, includes COX, LOX inhibitory assay, iNOS, MPO and determination
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7

Tavares, Maurício T., Arne Krüger, Sun L. Rei Yan, et al. "1,3-Diphenylureido hydroxamate as a promising scaffold for generation of potent antimalarial histone deacetylase inhibitors." Scientific Reports 13, no. 1 (2023). http://dx.doi.org/10.1038/s41598-023-47959-z.

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AbstractWe report a series of 1,3-diphenylureido hydroxamate HDAC inhibitors evaluated against sensitive and drug-resistant P. falciparum strains. Compounds 8a–d show potent antiplasmodial activity, indicating that a phenyl spacer allows improved potency relative to cinnamyl and di-hydrocinnamyl linkers. In vitro, mechanistic studies demonstrated target activity for PfHDAC1 on a recombinant level, which agreed with cell quantification of the acetylated histone levels. Compounds 6c, 7c, and 8c, identified as the most active in phenotypic assays and PfHDAC1 enzymatic inhibition. Compound 8c stan
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