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
Rubinstein-Taybi Syndrome D012415 1 associated lipids
Retinoblastoma D012175 12 associated lipids
Radiation Injuries D011832 14 associated lipids
Pulmonary Fibrosis D011658 24 associated lipids
Prostatic Neoplasms D011471 126 associated lipids
Prostatic Hyperplasia D011470 20 associated lipids
Progeria D011371 3 associated lipids
Pancreatic Neoplasms D010190 77 associated lipids
Osteomalacia D010018 5 associated lipids
Neuroblastoma D009447 66 associated lipids
Nerve Degeneration D009410 53 associated lipids
Neovascularization, Pathologic D009389 39 associated lipids
Neoplasms, Hormone-Dependent D009376 23 associated lipids
Neoplasms D009369 13 associated lipids
Nasopharyngeal Neoplasms D009303 4 associated lipids
Nasal Polyps D009298 26 associated lipids
Opioid-Related Disorders D009293 5 associated lipids
Myeloproliferative Disorders D009196 5 associated lipids
Muscular Dystrophies D009136 10 associated lipids
Intellectual Disability D008607 13 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.

Related references are published most in these journals:

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?


Related references are published most in these journals:

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
Plant KE et al. Intergenic transcription in the human beta-globin gene cluster. 2001 Mol. Cell. Biol. pmid:11533239
Chen Lf W et al. Duration of nuclear NF-kappaB action regulated by reversible acetylation. 2001 Science pmid:11533489
Vinatzer U et al. The leukaemia-associated transcription factors EVI-1 and MDS1/EVI1 repress transcription and interact with histone deacetylase. 2001 Br. J. Haematol. pmid:11552981
Sawa H et al. Histone deacetylase inhibitors such as sodium butyrate and trichostatin A induce apoptosis through an increase of the bcl-2-related protein Bad. 2001 Brain Tumor Pathol pmid:11908866
Seth KA and Majzoub JA Repressor element silencing transcription factor/neuron-restrictive silencing factor (REST/NRSF) can act as an enhancer as well as a repressor of corticotropin-releasing hormone gene transcription. 2001 J. Biol. Chem. pmid:11278361
Matsuda E et al. Targeting of Krüppel-associated box-containing zinc finger proteins to centromeric heterochromatin. Implication for the gene silencing mechanisms. 2001 J. Biol. Chem. pmid:11278721
Kim MS et al. Histone deacetylases induce angiogenesis by negative regulation of tumor suppressor genes. 2001 Nat. Med. pmid:11283670
Vigushin DM et al. Trichostatin A is a histone deacetylase inhibitor with potent antitumor activity against breast cancer in vivo. 2001 Clin. Cancer Res. pmid:11309348
Magdinier F and Wolffe AP Selective association of the methyl-CpG binding protein MBD2 with the silent p14/p16 locus in human neoplasia. 2001 Proc. Natl. Acad. Sci. U.S.A. pmid:11309512
Grande A et al. A functionally active RARalpha nuclear receptor is expressed in retinoic acid non responsive early myeloblastic cell lines. 2001 Cell Death Differ. pmid:11313705
Wu Y et al. Negative regulation of bcl-2 expression by p53 in hematopoietic cells. 2001 Oncogene pmid:11313951
Greenberg VL et al. Histone deacetylase inhibitors promote apoptosis and differential cell cycle arrest in anaplastic thyroid cancer cells. 2001 Thyroid pmid:11349829
Chen C et al. Evidence that silencing of the HPRT promoter by DNA methylation is mediated by critical CpG sites. 2001 J. Biol. Chem. pmid:11013250
Arthur JL et al. Herpes simplex virus type 1 promoter activity during latency establishment, maintenance, and reactivation in primary dorsal root neurons in vitro. 2001 J. Virol. pmid:11264377
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
Biade S et al. Chemical agents that promote chromatin compaction radiosensitize tumour cells. 2001 Int. J. Radiat. Biol. pmid:11682008
Mishra SK et al. Dynamic chromatin remodeling on the HER2 promoter in human breast cancer cells. 2001 FEBS Lett. pmid:11682064