trichostatin A

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.

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Introduction

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.

What diseases are associated with trichostatin A?

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.

Related references are mostly published in these journals:

Disease Cross reference Weighted score Related literature
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Possible diseases from mapped MeSH terms on references

We collected disease MeSH terms mapped to the references associated with trichostatin A

MeSH term MeSH ID Detail
Conjunctival Neoplasms D003230 3 associated lipids
Coronary Artery Disease D003324 47 associated lipids
Cystic Fibrosis D003550 65 associated lipids
Cytomegalovirus Infections D003586 7 associated lipids
Diabetes Mellitus, Experimental D003921 85 associated lipids
Encephalomyelitis, Autoimmune, Experimental D004681 26 associated lipids
Endometriosis D004715 29 associated lipids
Enteritis D004751 8 associated lipids
Leukemia, Erythroblastic, Acute D004915 41 associated lipids
Fetal Growth Retardation D005317 9 associated lipids
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PubChem Associated disorders and diseases

What pathways are 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.

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Pathway name Related literatures
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PubChem Biomolecular Interactions and Pathways

Link to PubChem Biomolecular Interactions and Pathways

What cellular locations are associated with trichostatin A?

Related references are published most in these journals:

Location Cross reference Weighted score Related literatures
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What functions are associated with trichostatin A?


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Function Cross reference Weighted score Related literatures

What lipids are associated with trichostatin A?

Related references are published most in these journals:

Lipid concept Cross reference Weighted score Related literatures
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What genes are associated with trichostatin A?

Related references are published most in these journals:


Gene Cross reference Weighted score Related literatures

What common seen animal models are associated with trichostatin A?

Mouse Model

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

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

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).

Related references are published most in these journals:

Model Cross reference Weighted score Related literatures
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NCBI Entrez Crosslinks

All references with trichostatin A

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Per page 10 20 50 100 | Total 3126
Authors Title Published Journal PubMed Link
Amann JM et al. ETO, a target of t(8;21) in acute leukemia, makes distinct contacts with multiple histone deacetylases and binds mSin3A through its oligomerization domain. 2001 Mol. Cell. Biol. pmid:11533236
Marianna P et al. Valproic acid, trichostatin and their combination with hemin preferentially enhance gamma-globin gene expression in human erythroid liquid cultures. 2001 Haematologica pmid:11454524
Cho JH et al. DNA methylation regulates placental lactogen I gene expression. 2001 Endocrinology pmid:11459782
Walker GE et al. Butyrate, a histone deacetylase inhibitor, activates the human IGF binding protein-3 promoter in breast cancer cells: molecular mechanism involves an Sp1/Sp3 multiprotein complex. 2001 Endocrinology pmid:11517158
Jorgensen JS and Nilson JH AR suppresses transcription of the alpha glycoprotein hormone subunit gene through protein-protein interactions with cJun and activation transcription factor 2. 2001 Mol. Endocrinol. pmid:11518798
Phiel CJ et al. Histone deacetylase is a direct target of valproic acid, a potent anticonvulsant, mood stabilizer, and teratogen. 2001 J. Biol. Chem. pmid:11473107
Sundqvist A et al. Functional knockout of the corepressor CtBP by the second exon of adenovirus E1a relieves repression of transcription. 2001 Exp. Cell Res. pmid:11478854
Maës J et al. Chromatin remodeling at the Ig loci prior to V(D)J recombination. 2001 J. Immunol. pmid:11441093
Wang H et al. Methylation of histone H4 at arginine 3 facilitating transcriptional activation by nuclear hormone receptor. 2001 Science pmid:11387442
Klar AJ et al. A histone deacetylation inhibitor and mutant promote colony-type switching of the human pathogen Candida albicans. 2001 Genetics pmid:11404352
Massa S et al. 3-(4-aroyl-1H-pyrrol-2-yl)-N-hydroxy-2-propenamides, a new class of synthetic histone deacetylase inhibitors. 2001 J. Med. Chem. pmid:11405644
Setlow JK et al. Evidence for gene silencing in Haemophilus influenzae. 2001 Mutat. Res. pmid:11406170
Feng YQ et al. Position effects are influenced by the orientation of a transgene with respect to flanking chromatin. 2001 Mol. Cell. Biol. pmid:11113204
Mehra-Chaudhary R et al. Msx3 protein recruits histone deacetylase to down-regulate the Msx1 promoter. 2001 Biochem. J. pmid:11115394
Kosugi H et al. In vivo effects of a histone deacetylase inhibitor, FK228, on human acute promyelocytic leukemia in NOD / Shi-scid/scid mice. 2001 Jpn. J. Cancer Res. pmid:11376562
Lizcano F et al. Cell type-specific roles of histone deacetylase in TR ligand-independent transcriptional repression. 2001 Mol. Cell. Endocrinol. pmid:11165035
Nervi C et al. Inhibition of histone deacetylase activity by trichostatin A modulates gene expression during mouse embryogenesis without apparent toxicity. 2001 Cancer Res. pmid:11245412
Zhu WG et al. DNA methyltransferase inhibition enhances apoptosis induced by histone deacetylase inhibitors. 2001 Cancer Res. pmid:11245429
Muth V et al. Acetylation of TAF(I)68, a subunit of TIF-IB/SL1, activates RNA polymerase I transcription. 2001 EMBO J. pmid:11250901
Laribee RN and Klemsz MJ Loss of PU.1 expression following inhibition of histone deacetylases. 2001 J. Immunol. pmid:11673528