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
Porcine Reproductive and Respiratory Syndrome D019318 4 associated lipids
Cicatrix, Hypertrophic D017439 4 associated lipids
Spinocerebellar Ataxias D020754 4 associated lipids
Nasopharyngeal Neoplasms D009303 4 associated lipids
Neuroendocrine Tumors D018358 4 associated lipids
Myeloproliferative Disorders D009196 5 associated lipids
Opioid-Related Disorders D009293 5 associated lipids
Osteomalacia D010018 5 associated lipids
Fragile X Syndrome D005600 5 associated lipids
Carcinoma, Pancreatic Ductal D021441 6 associated lipids
Primary Myelofibrosis D055728 6 associated lipids
Leukemia, Myelomonocytic, Acute D015479 6 associated lipids
Polycystic Kidney, Autosomal Dominant D016891 6 associated lipids
Genomic Instability D042822 7 associated lipids
Biliary Tract Neoplasms D001661 7 associated lipids
Cytomegalovirus Infections D003586 7 associated lipids
Enteritis D004751 8 associated lipids
Carcinoma, Embryonal D018236 8 associated lipids
Immunologic Deficiency Syndromes D007153 8 associated lipids
Mast-Cell Sarcoma D012515 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?

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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?

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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
Nielsen AL et al. Interaction with members of the heterochromatin protein 1 (HP1) family and histone deacetylation are differentially involved in transcriptional silencing by members of the TIF1 family. 1999 EMBO J. pmid:10562550
Habeck M Gelsolin: a new marker for breast cancer? 1999 Mol Med Today pmid:10562712
Saunders N et al. Histone deacetylase inhibitors as potential anti-skin cancer agents. 1999 Cancer Res. pmid:9927053
O'Neill LP et al. A developmental switch in H4 acetylation upstream of Xist plays a role in X chromosome inactivation. 1999 EMBO J. pmid:10329635
Strouboulis J et al. Transcriptional repression by XPc1, a new Polycomb homolog in Xenopus laevis embryos, is independent of histone deacetylase. 1999 Mol. Cell. Biol. pmid:10330136
Cameron EE et al. Synergy of demethylation and histone deacetylase inhibition in the re-expression of genes silenced in cancer. 1999 Nat. Genet. pmid:9916800
Olsson TG et al. Transient inhibition of histone deacetylase activity overcomes silencing in the mating-type region in fission yeast. 1999 Curr. Genet. pmid:10079326
Collas P et al. Active transgenes in zebrafish are enriched in acetylated histone H4 and dynamically associate with RNA Pol II and splicing complexes. 1999 J. Cell. Sci. pmid:10198286
Saito A et al. A synthetic inhibitor of histone deacetylase, MS-27-275, with marked in vivo antitumor activity against human tumors. 1999 Proc. Natl. Acad. Sci. U.S.A. pmid:10200307
Dang VD et al. A new member of the Sin3 family of corepressors is essential for cell viability and required for retroelement propagation in fission yeast. 1999 Mol. Cell. Biol. pmid:10022921
Murphy M et al. Transcriptional repression by wild-type p53 utilizes histone deacetylases, mediated by interaction with mSin3a. 1999 Genes Dev. pmid:10521394
Lin RJ et al. Role of the histone deacetylase complex in acute promyelocytic leukaemia. 1998 Nature pmid:9486654
Grignani F et al. Fusion proteins of the retinoic acid receptor-alpha recruit histone deacetylase in promyelocytic leukaemia. 1998 Nature pmid:9486655
Wong J et al. Distinct requirements for chromatin assembly in transcriptional repression by thyroid hormone receptor and histone deacetylase. 1998 EMBO J. pmid:9430643
Magnaghi-Jaulin L et al. Retinoblastoma protein represses transcription by recruiting a histone deacetylase. 1998 Nature pmid:9468140
Waterborg JH Dynamics of histone acetylation in Chlamydomonas reinhardtii. 1998 J. Biol. Chem. pmid:9765294
Madisen L et al. The immunoglobulin heavy chain locus control region increases histone acetylation along linked c-myc genes. 1998 Mol. Cell. Biol. pmid:9774645
Eden S et al. DNA methylation models histone acetylation. 1998 Nature pmid:9732866
Phelan MW et al. Hypoxia increases thrombospondin-1 transcript and protein in cultured endothelial cells. 1998 J. Lab. Clin. Med. pmid:9851743
Ciana P et al. Leukemic transformation by the v-ErbA oncoprotein entails constitutive binding to and repression of an erythroid enhancer in vivo. 1998 EMBO J. pmid:9857194