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.

Cross Reference

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
Neovascularization, Pathologic D009389 39 associated lipids
Adenocarcinoma D000230 166 associated lipids
Breast Neoplasms D001943 24 associated lipids
Neoplasms D009369 13 associated lipids
Autoimmune Diseases D001327 27 associated lipids
Lupus Erythematosus, Systemic D008180 43 associated lipids
Lung Neoplasms D008175 171 associated lipids
Pulmonary Fibrosis D011658 24 associated lipids
Pancreatic Neoplasms D010190 77 associated lipids
Inflammation D007249 119 associated lipids
Reperfusion Injury D015427 65 associated lipids
Colonic Neoplasms D003110 161 associated lipids
Diabetes Mellitus, Experimental D003921 85 associated lipids
Mammary Neoplasms, Experimental D008325 67 associated lipids
Body Weight D001835 333 associated lipids
Arthritis, Experimental D001169 24 associated lipids
Carcinoma D002277 18 associated lipids
Ureteral Obstruction D014517 10 associated lipids
Prostatic Neoplasms D011471 126 associated lipids
Hypersensitivity D006967 22 associated lipids
Osteosarcoma D012516 50 associated lipids
Brain Neoplasms D001932 15 associated lipids
Leukemia, Erythroblastic, Acute D004915 41 associated lipids
Melanoma D008545 69 associated lipids
Muscular Dystrophies D009136 10 associated lipids
Asthma D001249 52 associated lipids
Abnormalities, Multiple D000015 13 associated lipids
Intellectual Disability D008607 13 associated lipids
Glioma D005910 112 associated lipids
Cell Transformation, Neoplastic D002471 126 associated lipids
Hypertension, Pulmonary D006976 32 associated lipids
Endometriosis D004715 29 associated lipids
Uterine Neoplasms D014594 18 associated lipids
Adrenoleukodystrophy D000326 29 associated lipids
Prostatic Hyperplasia D011470 20 associated lipids
Alzheimer Disease D000544 76 associated lipids
Thyroid Neoplasms D013964 33 associated lipids
Leukemia D007938 74 associated lipids
Neuroblastoma D009447 66 associated lipids
Carcinoma, Hepatocellular D006528 140 associated lipids
Liver Cirrhosis D008103 67 associated lipids
Myeloproliferative Disorders D009196 5 associated lipids
Osteoarthritis, Knee D020370 13 associated lipids
Fibrosis D005355 23 associated lipids
Carcinoma, Ductal, Breast D018270 19 associated lipids
Carcinoma, Renal Cell D002292 12 associated lipids
Immunologic Deficiency Syndromes D007153 8 associated lipids
Leukemia, Promyelocytic, Acute D015473 3 associated lipids
Stroke D020521 32 associated lipids
Leukemia, Myeloid D007951 52 associated lipids
Nerve Degeneration D009410 53 associated lipids
Cystic Fibrosis D003550 65 associated lipids
Hypertension D006973 115 associated lipids
Tongue Neoplasms D014062 15 associated lipids
Cytomegalovirus Infections D003586 7 associated lipids
Nasal Polyps D009298 26 associated lipids
Leukemia, Myeloid, Acute D015470 19 associated lipids
Mast-Cell Sarcoma D012515 9 associated lipids
Leukemia, Lymphocytic, Chronic, B-Cell D015451 25 associated lipids
Neoplasms, Hormone-Dependent D009376 23 associated lipids
Coronary Artery Disease D003324 47 associated lipids
Encephalomyelitis, Autoimmune, Experimental D004681 26 associated lipids
Translocation, Genetic D014178 20 associated lipids
Cardiomegaly D006332 31 associated lipids
Leukemia, T-Cell D015458 23 associated lipids
Radiation Injuries D011832 14 associated lipids
Leishmaniasis D007896 19 associated lipids
Enteritis D004751 8 associated lipids
Primary Myelofibrosis D055728 6 associated lipids
Fetal Growth Retardation D005317 9 associated lipids
Chondrosarcoma D002813 9 associated lipids
Osteomalacia D010018 5 associated lipids
Glioblastoma D005909 27 associated lipids
Keloid D007627 12 associated lipids
Dermatitis, Allergic Contact D017449 20 associated lipids
Medulloblastoma D008527 22 associated lipids
Carcinoma, Non-Small-Cell Lung D002289 72 associated lipids
Lymphatic Metastasis D008207 10 associated lipids
Atherosclerosis D050197 85 associated lipids
Leukemia-Lymphoma, Adult T-Cell D015459 25 associated lipids
Bone Marrow Neoplasms D019046 2 associated lipids
Carcinoma, Pancreatic Ductal D021441 6 associated lipids
Cat Diseases D002371 12 associated lipids
Biliary Tract Neoplasms D001661 7 associated lipids
Neurodegenerative Diseases D019636 32 associated lipids
Polycystic Kidney, Autosomal Dominant D016891 6 associated lipids
Ventricular Remodeling D020257 28 associated lipids
Endometrial Neoplasms D016889 30 associated lipids
Retinoblastoma D012175 12 associated lipids
Genomic Instability D042822 7 associated lipids
Cicatrix, Hypertrophic D017439 4 associated lipids
Carcinoma, Embryonal D018236 8 associated lipids
Mastocytoma D034801 3 associated lipids
Cell Transformation, Viral D002472 26 associated lipids
Nasopharyngeal Neoplasms D009303 4 associated lipids
Fragile X Syndrome D005600 5 associated lipids
Adenocarcinoma, Follicular D018263 3 associated lipids
Hypereosinophilic Syndrome D017681 3 associated lipids
Retinal Neoplasms D019572 3 associated lipids
Progeria D011371 3 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
Malone CS et al. B29 gene silencing in pituitary cells is regulated by its 3' enhancer. 2006 J. Mol. Biol. pmid:16920149
Lee JH et al. Structural and functional studies of the yeast class II Hda1 histone deacetylase complex. 2009 J. Mol. Biol. pmid:19573535
Rincón-Arano H et al. YY1 and GATA-1 interaction modulate the chicken 3'-side alpha-globin enhancer activity. 2005 J. Mol. Biol. pmid:15913647
Lopez-Atalaya JP et al. Histone acetylation deficits in lymphoblastoid cell lines from patients with Rubinstein-Taybi syndrome. 2012 J. Med. Genet. pmid:21984751
Patel V et al. Identification and characterization of small molecule inhibitors of a class I histone deacetylase from Plasmodium falciparum. 2009 J. Med. Chem. pmid:19317450
Olsen CA and Ghadiri MR Discovery of potent and selective histone deacetylase inhibitors via focused combinatorial libraries of cyclic alpha3beta-tetrapeptides. 2009 J. Med. Chem. pmid:19705846
Trapp J et al. Adenosine mimetics as inhibitors of NAD+-dependent histone deacetylases, from kinase to sirtuin inhibition. 2006 J. Med. Chem. pmid:17149860
Liu T et al. Design and synthesis of a potent histone deacetylase inhibitor. 2007 J. Med. Chem. pmid:17419603
Ragno R et al. 3-(4-Aroyl-1-methyl-1H-pyrrol-2-yl)-N-hydroxy-2-propenamides as a new class of synthetic histone deacetylase inhibitors. 3. Discovery of novel lead compounds through structure-based drug design and docking studies. 2004 J. Med. Chem. pmid:14998325
Kim DK et al. Synthesis and biological evaluation of 3-(4-substituted-phenyl)-N-hydroxy-2-propenamides, a new class of histone deacetylase inhibitors. 2003 J. Med. Chem. pmid:14667227
Bergman JA et al. Selective histone deacetylase 6 inhibitors bearing substituted urea linkers inhibit melanoma cell growth. 2012 J. Med. Chem. pmid:23009203
Remiszewski SW et al. Inhibitors of human histone deacetylase: synthesis and enzyme and cellular activity of straight chain hydroxamates. 2002 J. Med. Chem. pmid:11831887
Mai A et al. 3-(4-Aroyl-1-methyl-1H-2-pyrrolyl)-N-hydroxy-2-propenamides as a new class of synthetic histone deacetylase inhibitors. 2. Effect of pyrrole-C2 and/or -C4 substitutions on biological activity. 2004 J. Med. Chem. pmid:14971890
Baud MG et al. Defining the mechanism of action and enzymatic selectivity of psammaplin A against its epigenetic targets. 2012 J. Med. Chem. pmid:22280363
Remiszewski SW et al. N-hydroxy-3-phenyl-2-propenamides as novel inhibitors of human histone deacetylase with in vivo antitumor activity: discovery of (2E)-N-hydroxy-3-[4-[[(2-hydroxyethyl)[2-(1H-indol-3-yl)ethyl]amino]methyl]phenyl]-2-propenamide (NVP-LAQ824). 2003 J. Med. Chem. pmid:14521422
Jung M et al. Amide analogues of trichostatin A as inhibitors of histone deacetylase and inducers of terminal cell differentiation. 1999 J. Med. Chem. pmid:10579829
He R et al. Synthesis and biological evaluation of triazol-4-ylphenyl-bearing histone deacetylase inhibitors as anticancer agents. 2010 J. Med. Chem. pmid:20055418
Auzzas L et al. Non-natural macrocyclic inhibitors of histone deacetylases: design, synthesis, and activity. 2010 J. Med. Chem. pmid:21073160
Massa S et al. Synthesis and antimicrobial and cytotoxic activities of pyrrole-containing analogues of trichostatin A. 1990 J. Med. Chem. pmid:2213836
Huber K et al. Novel 3-arylideneindolin-2-ones as inhibitors of NAD+ -dependent histone deacetylases (sirtuins). 2010 J. Med. Chem. pmid:20030343
Trunzer M et al. Metabolic soft spot identification and compound optimization in early discovery phases using MetaSite and LC-MS/MS validation. 2009 J. Med. Chem. pmid:19108654
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
Yu CW et al. Quinazolin-4-one derivatives as selective histone deacetylase-6 inhibitors for the treatment of Alzheimer's disease. 2013 J. Med. Chem. pmid:23905680
Wittich S et al. Structure-activity relationships on phenylalanine-containing inhibitors of histone deacetylase: in vitro enzyme inhibition, induction of differentiation, and inhibition of proliferation in Friend leukemic cells. 2002 J. Med. Chem. pmid:12109913
Lu Q et al. Structure-based optimization of phenylbutyrate-derived histone deacetylase inhibitors. 2005 J. Med. Chem. pmid:16107152
Heltweg B et al. Subtype selective substrates for histone deacetylases. 2004 J. Med. Chem. pmid:15456267
Paris M et al. Histone deacetylase inhibitors: from bench to clinic. 2008 J. Med. Chem. pmid:18247554
Xiao J et al. Discovery, synthesis, and biological evaluation of novel SMN protein modulators. 2011 J. Med. Chem. pmid:21819082
Casero RA and Woster PM Recent advances in the development of polyamine analogues as antitumor agents. 2009 J. Med. Chem. pmid:19534534
Mai A et al. Binding mode analysis of 3-(4-benzoyl-1-methyl-1H-2-pyrrolyl)-N-hydroxy-2-propenamide: a new synthetic histone deacetylase inhibitor inducing histone hyperacetylation, growth inhibition, and terminal cell differentiation. 2002 J. Med. Chem. pmid:11960489
Mai A et al. Synthesis and biological properties of novel, uracil-containing histone deacetylase inhibitors. 2006 J. Med. Chem. pmid:17004718
Woo SH et al. Structurally simple trichostatin A-like straight chain hydroxamates as potent histone deacetylase inhibitors. 2002 J. Med. Chem. pmid:12061890
Chen Y et al. A series of potent and selective, triazolylphenyl-based histone deacetylases inhibitors with activity against pancreatic cancer cells and Plasmodium falciparum. 2008 J. Med. Chem. pmid:18494463
Glenn MP et al. Antiproliferative and phenotype-transforming antitumor agents derived from cysteine. 2004 J. Med. Chem. pmid:15163181
Charrier C et al. Synthesis and modeling of new benzofuranone histone deacetylase inhibitors that stimulate tumor suppressor gene expression. 2009 J. Med. Chem. pmid:19385600
Mai A et al. Class II (IIa)-selective histone deacetylase inhibitors. 1. Synthesis and biological evaluation of novel (aryloxopropenyl)pyrrolyl hydroxyamides. 2005 J. Med. Chem. pmid:15857140
Miller TA et al. Histone deacetylase inhibitors. 2003 J. Med. Chem. pmid:14613312
Day JA and Cohen SM Investigating the selectivity of metalloenzyme inhibitors. 2013 J. Med. Chem. pmid:24074025
Mai A et al. Discovery of (aryloxopropenyl)pyrrolyl hydroxyamides as selective inhibitors of class IIa histone deacetylase homologue HD1-A. 2003 J. Med. Chem. pmid:14584932
Kozikowski AP et al. Use of the nitrile oxide cycloaddition (NOC) reaction for molecular probe generation: a new class of enzyme selective histone deacetylase inhibitors (HDACIs) showing picomolar activity at HDAC6. 2008 J. Med. Chem. pmid:18642892
Suzuki T et al. Synthesis and histone deacetylase inhibitory activity of new benzamide derivatives. 1999 J. Med. Chem. pmid:10425110
Itoh Y et al. Design, synthesis, structure--selectivity relationship, and effect on human cancer cells of a novel series of histone deacetylase 6-selective inhibitors. 2007 J. Med. Chem. pmid:17929798
Neelarapu R et al. Design, synthesis, docking, and biological evaluation of novel diazide-containing isoxazole- and pyrazole-based histone deacetylase probes. 2011 J. Med. Chem. pmid:21548582
Suzuki T et al. Highly potent and selective histone deacetylase 6 inhibitors designed based on a small-molecular substrate. 2006 J. Med. Chem. pmid:16884291
Marek L et al. Histone deacetylase (HDAC) inhibitors with a novel connecting unit linker region reveal a selectivity profile for HDAC4 and HDAC5 with improved activity against chemoresistant cancer cells. 2013 J. Med. Chem. pmid:23252603
Bouchain G et al. Development of potential antitumor agents. Synthesis and biological evaluation of a new set of sulfonamide derivatives as histone deacetylase inhibitors. 2003 J. Med. Chem. pmid:12593661
Nunes MJ et al. Okadaic acid inhibits the trichostatin A-mediated increase of human CYP46A1 neuronal expression in a ERK1/2-Sp3-dependent pathway. 2012 J. Lipid Res. pmid:22693257
Clarke CJ et al. ATRA transcriptionally induces nSMase2 through CBP/p300-mediated histone acetylation. 2016 J. Lipid Res. pmid:27013100
Reddy P Editorial: HDAC inhibition begets more MDSCs. 2012 J. Leukoc. Biol. pmid:22547132
Rosborough BR et al. Histone deacetylase inhibition facilitates GM-CSF-mediated expansion of myeloid-derived suppressor cells in vitro and in vivo. 2012 J. Leukoc. Biol. pmid:22028329
Rossi LE et al. Histone deacetylase inhibitors impair NK cell viability and effector functions through inhibition of activation and receptor expression. 2012 J. Leukoc. Biol. pmid:22124136
Halili MA et al. Differential effects of selective HDAC inhibitors on macrophage inflammatory responses to the Toll-like receptor 4 agonist LPS. 2010 J. Leukoc. Biol. pmid:20200406
Claus R et al. Inhibitors of DNA methylation and histone deacetylation independently relieve AML1/ETO-mediated lysozyme repression. 2006 J. Leukoc. Biol. pmid:17000900
Bosisio D et al. Blocking TH17-polarizing cytokines by histone deacetylase inhibitors in vitro and in vivo. 2008 J. Leukoc. Biol. pmid:18780875
Moldenhauer A et al. Histone deacetylase inhibition improves dendritic cell differentiation of leukemic blasts with AML1-containing fusion proteins. 2004 J. Leukoc. Biol. pmid:15197237
Phelan MW et al. Hypoxia increases thrombospondin-1 transcript and protein in cultured endothelial cells. 1998 J. Lab. Clin. Med. pmid:9851743
Sung TY et al. Innovative in vitro chemo-hormonal drug therapy for refractory thyroid carcinomas. 2012 J. Korean Med. Sci. pmid:22787366
Jung N et al. Pharmacological unmasking microarray approach-based discovery of novel DNA methylation markers for hepatocellular carcinoma. 2012 J. Korean Med. Sci. pmid:22690089
Tran HT et al. Improved therapeutic effect against leukemia by a combination of the histone methyltransferase inhibitor chaetocin and the histone deacetylase inhibitor trichostatin A. 2013 J. Korean Med. Sci. pmid:23400519
Russell SB et al. Epigenetically altered wound healing in keloid fibroblasts. 2010 J. Invest. Dermatol. pmid:20555348
Tigges J et al. Aryl hydrocarbon receptor repressor (AhRR) function revisited: repression of CYP1 activity in human skin fibroblasts is not related to AhRR expression. 2013 J. Invest. Dermatol. pmid:22951721
Markova NG et al. Inhibition of histone deacetylation promotes abnormal epidermal differentiation and specifically suppresses the expression of the late differentiation marker profilaggrin. 2007 J. Invest. Dermatol. pmid:17195011
Johnson JL et al. The desmosomal protein desmoglein 1 aids recovery of epidermal differentiation after acute UV light exposure. 2014 J. Invest. Dermatol. pmid:24594668
Schauber J et al. Histone acetylation in keratinocytes enables control of the expression of cathelicidin and CD14 by 1,25-dihydroxyvitamin D3. 2008 J. Invest. Dermatol. pmid:17943182
Nakazawa Y et al. Evaluation of long-term transgene expression in piggyBac-modified human T lymphocytes. 2013 J. Immunother. pmid:23211626
Lu L et al. Role of SMAD and non-SMAD signals in the development of Th17 and regulatory T cells. 2010 J. Immunol. pmid:20304828
Lee KY et al. NF-kappaB and activator protein 1 response elements and the role of histone modifications in IL-1beta-induced TGF-beta1 gene transcription. 2006 J. Immunol. pmid:16365456
Bai Y et al. Protein acetylation regulates both PU.1 transactivation and Ig kappa 3' enhancer activity. 2005 J. Immunol. pmid:16210620
Gao B et al. Inhibition of histone deacetylase activity suppresses IFN-γ induction of tripartite motif 22 via CHIP-mediated proteasomal degradation of IRF-1. 2013 J. Immunol. pmid:23729439
Grabiec AM et al. Histone deacetylase inhibitors suppress inflammatory activation of rheumatoid arthritis patient synovial macrophages and tissue. 2010 J. Immunol. pmid:20100935
Bachl J et al. Increased transcription levels induce higher mutation rates in a hypermutating cell line. 2001 J. Immunol. pmid:11290786
Gays F et al. The mouse tumor cell lines EL4 and RMA display mosaic expression of NK-related and certain other surface molecules and appear to have a common origin. 2000 J. Immunol. pmid:10799866
Maës J et al. Chromatin remodeling at the Ig loci prior to V(D)J recombination. 2001 J. Immunol. pmid:11441093
Magner WJ et al. Activation of MHC class I, II, and CD40 gene expression by histone deacetylase inhibitors. 2000 J. Immunol. pmid:11120829
Uhlenbrock F et al. The NKG2D ligand ULBP2 is specifically regulated through an invariant chain-dependent endosomal pathway. 2014 J. Immunol. pmid:25024379
Thomas RM et al. Regulation of mouse mammary tumor virus env transcriptional activator initiated mammary tumor virus superantigen transcripts in lymphomas of SJL/J mice: role of Ikaros, demethylation, and chromatin structural change in the transcriptional activation of mammary tumor virus superantigen. 2003 J. Immunol. pmid:12496403
Serrat N et al. The response of secondary genes to lipopolysaccharides in macrophages depends on histone deacetylase and phosphorylation of C/EBPβ. 2014 J. Immunol. pmid:24307736
Sebastián C et al. Deacetylase activity is required for STAT5-dependent GM-CSF functional activity in macrophages and differentiation to dendritic cells. 2008 J. Immunol. pmid:18424709
Ishiguro K et al. Cutting edge: tubulin α functions as an adaptor in NFAT-importin β interaction. 2011 J. Immunol. pmid:21278340
Northrop JK et al. Cutting edge: chromatin remodeling as a molecular basis for the enhanced functionality of memory CD8 T cells. 2008 J. Immunol. pmid:18606637
Schmeck B et al. Histone acetylation and flagellin are essential for Legionella pneumophila-induced cytokine expression. 2008 J. Immunol. pmid:18606645
Zabel MD et al. Lymphoid transcription of the murine CD21 gene is positively regulated by histone acetylation. 1999 J. Immunol. pmid:10453011
Zhang Y et al. Pro-IL-16 recruits histone deacetylase 3 to the Skp2 core promoter through interaction with transcription factor GABP. 2008 J. Immunol. pmid:18097041
Laribee RN and Klemsz MJ Loss of PU.1 expression following inhibition of histone deacetylases. 2001 J. Immunol. pmid:11673528
Mataki H et al. Downregulation of the microRNA-1/133a cluster enhances cancer cell migration and invasion in lung-squamous cell carcinoma via regulation of Coronin1C. 2015 J. Hum. Genet. pmid:25518741
Xu S et al. Abrogation of DUSP6 by hypermethylation in human pancreatic cancer. 2005 J. Hum. Genet. pmid:15824892
Yoshioka H et al. A novel in vitro system for analyzing parental allele-specific histone acetylation in genomic imprinting. 2001 J. Hum. Genet. pmid:11721881
Huang H et al. Expression of P53, P21 in human lung adenocarcinoma A549 cell strains under hypoxia conditions and the effect of TSA on their expression. 2003 J. Huazhong Univ. Sci. Technol. Med. Sci. pmid:15015635
Li C et al. Effect and comparison of sodium butyrate and trichostatin A on the proliferation/differentiation of K562. 2003 J. Huazhong Univ. Sci. Technol. Med. Sci. pmid:14526425
He J et al. Effects of trichostatin A on HDAC8 expression, proliferation and cell cycle of Molt-4 cells. 2006 J. Huazhong Univ. Sci. Technol. Med. Sci. pmid:17219959
Liu H et al. Trichostatin A regulates hGCN5 expression and cell cycle on Daudi cells in vitro. 2006 J. Huazhong Univ. Sci. Technol. Med. Sci. pmid:17219960
Sun C et al. Anticancer activities of trichostatin A on maligant lymphoid cells. 2006 J. Huazhong Univ. Sci. Technol. Med. Sci. pmid:17219961
Hong Z et al. Microarray study of mechanism of trichostatin a inducing apoptosis of Molt-4 cells. 2009 J. Huazhong Univ. Sci. Technol. Med. Sci. pmid:19662360
Li X et al. Regulation of histone acetylation and apoptosis by trichostatin in HL-60 cells. 2004 J. Huazhong Univ. Sci. Technol. Med. Sci. pmid:15791844
Li C et al. Induction of myelogenous leukemia cells with histone deacetylase inhibitors through down-regulating the Daxx protein expression. 2009 J. Huazhong Univ. Sci. Technol. Med. Sci. pmid:19821084
Marquardt JU et al. Curcumin effectively inhibits oncogenic NF-κB signaling and restrains stemness features in liver cancer. 2015 J. Hepatol. pmid:25937435
Rombouts K et al. Actin filament formation, reorganization and migration are impaired in hepatic stellate cells under influence of trichostatin A, a histone deacetylase inhibitor. 2002 J. Hepatol. pmid:12445420
Papeleu P et al. Trichostatin A induces differential cell cycle arrests but does not induce apoptosis in primary cultures of mitogen-stimulated rat hepatocytes. 2003 J. Hepatol. pmid:12927923
Zhang C et al. Epigenetic inactivation of the tumor suppressor gene RIZ1 in hepatocellular carcinoma involves both DNA methylation and histone modifications. 2010 J. Hepatol. pmid:20675009
Chiba T et al. Identification of genes up-regulated by histone deacetylase inhibition with cDNA microarray and exploration of epigenetic alterations on hepatoma cells. 2004 J. Hepatol. pmid:15336447