Trichostatin is a lipid of Polyketides (PK) class. Trichostatin is associated with abnormalities such as Dentatorubral-Pallidoluysian Atrophy, PARAGANGLIOMAS 3, abnormal fragmented structure, Disintegration (morphologic abnormality) and Hyperostosis, Diffuse Idiopathic Skeletal. The involved functions are known as Acetylation, Cell Differentiation process, histone modification, Gene Silencing and Transcriptional Activation. Trichostatin often locates in CD41a, Hematopoietic System, Chromatin Structure, Blood and Endothelium. The associated genes with Trichostatin are SPI1 gene, CELL Gene, Chromatin, CXCR4 gene and DNMT1 gene. The related lipids are Butyrates, Promega, butyrate, Lipopolysaccharides and Steroids. The related experimental models are Knock-out, Mouse Model, Xenograft Model and Cancer Model.
To understand associated biological information of trichostatin A, we collected biological information of abnormalities, associated pathways, cellular/molecular locations, biological functions, related genes/proteins, lipids and common seen animal/experimental models with organized paragraphs from literatures.
trichostatin A is suspected in Infection, Morphologically altered structure, Ureteral obstruction, Photosensitization, Atherosclerosis, Hypertrophic Cardiomyopathy and other diseases in descending order of the highest number of associated sentences.
Disease | Cross reference | Weighted score | Related literature |
---|
We collected disease MeSH terms mapped to the references associated with trichostatin A
Lipid pathways are not clear in current pathway databases. We organized associated pathways with trichostatin A through full-text articles, including metabolic pathways or pathways of biological mechanisms.
Pathway name | Related literatures |
---|
Associated locations are in red color. Not associated locations are in black.
Location | Cross reference | Weighted score | Related literatures |
---|
Function | Cross reference | Weighted score | Related literatures |
---|
Lipid concept | Cross reference | Weighted score | Related literatures |
---|
Gene | Cross reference | Weighted score | Related literatures |
---|
Mouse Model are used in the study 'Regulation of minichromosome maintenance gene family by microRNA-1296 and genistein in prostate cancer.' (Majid S et al., 2010), Mouse Model are used in the study 'Reversal of hypermethylation and reactivation of p16INK4a, RARbeta, and MGMT genes by genistein and other isoflavones from soy.' (Fang MZ et al., 2005) and Mouse Model are used in the study 'Histone deacetylase 3 mediates allergic skin inflammation by regulating expression of MCP1 protein.' (Kim Y et al., 2012).
Xenograft Model are used in the study 'Histone deacetylase inhibitors induce growth arrest and differentiation in uveal melanoma.' (Landreville S et al., 2012), Xenograft Model are used in the study 'Extended treatment with physiologic concentrations of dietary phytochemicals results in altered gene expression, reduced growth, and apoptosis of cancer cells.' (Moiseeva EP et al., 2007) and Xenograft Model are used in the study 'Retinoic acid and the histone deacetylase inhibitor trichostatin a inhibit the proliferation of human renal cell carcinoma in a xenograft tumor model.' (Touma SE et al., 2005).
Cancer Model are used in the study 'Plasma pharmacokinetics and metabolism of the histone deacetylase inhibitor trichostatin a after intraperitoneal administration to mice.' (Sanderson L et al., 2004).
Model | Cross reference | Weighted score | Related literatures |
---|
Authors | Title | Published | Journal | PubMed Link |
---|---|---|---|---|
Fu J et al. | Discovery of 1H-benzo[d][1,2,3]triazol-1-yl 3,4,5-trimethoxybenzoate as a potential antiproliferative agent by inhibiting histone deacetylase. | 2010 | Bioorg. Med. Chem. | pmid:21067930 |
Saha A et al. | Synthesis and biological evaluation of a targeted DNA-binding transcriptional activator with HDAC8 inhibitory activity. | 2013 | Bioorg. Med. Chem. | pmid:23719282 |
Schäfer S et al. | Phenylalanine-containing hydroxamic acids as selective inhibitors of class IIb histone deacetylases (HDACs). | 2008 | Bioorg. Med. Chem. | pmid:18054239 |
Chen PC et al. | Synthesis and structure-activity relationship of histone deacetylase (HDAC) inhibitors with triazole-linked cap group. | 2008 | Bioorg. Med. Chem. | pmid:18397827 |
Whitehead L et al. | Human HDAC isoform selectivity achieved via exploitation of the acetate release channel with structurally unique small molecule inhibitors. | 2011 | Bioorg. Med. Chem. | pmid:21723733 |
Mukherjee P et al. | Structural insights into the Plasmodium falciparum histone deacetylase 1 (PfHDAC-1): A novel target for the development of antimalarial therapy. | 2008 | Bioorg. Med. Chem. | pmid:18362073 |
Kaldre D et al. | Optimization of histone deacetylase inhibitor activity in non-secosteroidal vitamin D-receptor agonist hybrids. | 2015 | Bioorg. Med. Chem. | pmid:26048026 |
Lee S et al. | Design, synthesis, and evaluation of isoindolinone-hydroxamic acid derivatives as histone deacetylase (HDAC) inhibitors. | 2007 | Bioorg. Med. Chem. Lett. | pmid:17588744 |
Rajak H et al. | 2,5-Disubstituted-1,3,4-oxadiazoles/thiadiazole as surface recognition moiety: design and synthesis of novel hydroxamic acid based histone deacetylase inhibitors. | 2011 | Bioorg. Med. Chem. Lett. | pmid:21875796 |
Vaidya AS et al. | Novel histone deacetylase 8 ligands without a zinc chelating group: exploring an 'upside-down' binding pose. | 2012 | Bioorg. Med. Chem. Lett. | pmid:23010266 |
Wang DF et al. | QSAR studies of PC-3 cell line inhibition activity of TSA and SAHA-like hydroxamic acids. | 2004 | Bioorg. Med. Chem. Lett. | pmid:14741273 |
Hirata Y et al. | Anti-tumor activity of new orally bioavailable 2-amino-5-(thiophen-2-yl)benzamide-series histone deacetylase inhibitors, possessing an aqueous soluble functional group as a surface recognition domain. | 2012 | Bioorg. Med. Chem. Lett. | pmid:22321215 |
Desai D et al. | SelSA, selenium analogs of SAHA as potent histone deacetylase inhibitors. | 2010 | Bioorg. Med. Chem. Lett. | pmid:20167479 |
Jose B et al. | Novel histone deacetylase inhibitors: cyclic tetrapeptide with trifluoromethyl and pentafluoroethyl ketones. | 2004 | Bioorg. Med. Chem. Lett. | pmid:15454224 |
Liao V et al. | Amide-based derivatives of β-alanine hydroxamic acid as histone deacetylase inhibitors: attenuation of potency through resonance effects. | 2012 | Bioorg. Med. Chem. Lett. | pmid:22932316 |
Pabba C et al. | Design and synthesis of aryl ether and sulfone hydroxamic acids as potent histone deacetylase (HDAC) inhibitors. | 2011 | Bioorg. Med. Chem. Lett. | pmid:21109435 |
Gupta PK et al. | Inhibitors selective for HDAC6 in enzymes and cells. | 2010 | Bioorg. Med. Chem. Lett. | pmid:20947351 |
Vasudevan A et al. | Heterocyclic ketones as inhibitors of histone deacetylase. | 2003 | Bioorg. Med. Chem. Lett. | pmid:14592473 |
Charrier C et al. | Antiproliferative activities of a library of hybrids between indanones and HDAC inhibitor SAHA and MS-275 analogues. | 2007 | Bioorg. Med. Chem. Lett. | pmid:17897824 |
Lavoie R et al. | Design and synthesis of a novel class of histone deacetylase inhibitors. | 2001 | Bioorg. Med. Chem. Lett. | pmid:11597413 |