HDAC1 (histone deacetylase 1)

2017-08-01 Emanuely Silva Chrun , Filipe Modolo , Filipe Ivan Daniel Affiliation

Federal University of Santa Catarina, Florianopolis, Santa Catarina, emanuely.silva@gmail.com (ESC), Pathology Department, Federal University of Santa Catarina, Florianopolis, SC, Brazil. filipe.modolo@ufsc.br; filipe.daniel@ufsc.br (FM, FID)

Identity

HGNC

HDAC1

LOCATION

1p35.2-p35.1

LOCUSID

3065

ALIAS

GON-10,HD1,KDAC1,RPD3,RPD3L1

Abstract

HDAC1 is a Class I histone deacetylase (HDACs) encoded by this gene. HDACs remove acetyl group from amino-terminal tail of histone lysine recovering the positive charge of histone tail, permitting interactions between negatively charged DNA and histone protein, resulting in chromatin structure condensation which is associated with gene repression. Overexpression of this protein has been related to several malignancies, controlling tumour suppressor genes expression, feasible prognostics factor, and medications target. This paper propound data about HDAC1 gene, its protein encoded and function.

DNA/RNA

Description

Located in chromosome 1. The entire HDAC1 gene is approximately 41,550 bases (start: 32,292,086 and end: 32,333,635 bp; orientation: Plus strand) and contains 14 exons.

Proteins

Expression

Ubiquitously.

Localisation

HDAC1 is found mainly in the nucleus.

Function

HDAC1 is an enzyme responsible for epigenetic alterations leading to modulation of chromatin structure and transcriptional regulation across lysine residues deacetylation on the N-terminal part of the core histones (H2A, H2B, H3 and H4) (Fig. 1). It shows a role in cell cycle regulation and haematopoiesis (Dovey, et al. 2010). Deacetylation of TP53 by HDAC1 is a mechanism that participate of physiological activity of TP53 (Juan, et al. 2000 2000). It was also observed an important participation in cellular proliferation through direct regulation of CDKN1A (p21) gene (Zupkovitz, et al. 2010) 2010. HDAC2 is a HDAC1 homologue that, in part, compensates its loss and has redundant functions (Zupkovitz, et al. 2006 2006). These enzymes act through multiprotein co-repressor complexes such as: SIN3, NuRD, RCOR1 (CoREST) (Kelly and Cowley 2013).

Fig. 1. Chromatin remodeling by histone acetylation changes. HATs catalyse the addition of acetyl groups turning histone tail charge to negative, leading to chromatin opening, while HDACs remove acetyl group from amino-terminal tail of histone lysine recovering its positive charge, closing the chromatin structure.

Homology

HDAC1 shares high homology between diverse species (Table 1).
Table 1. Comparative identity of human HDAC1 and its homologs in other species).

Gene		Identity
H. sapiens vs.	Symbol	Protein	DNA
P. troglogytes	HDAC1	99.8	99.4
P. troglogytes	HDAC1	99.6	99.4
M. mulata	LOC708441	99.8	97.8
C. lupus	HDAC1	99.2	94.1
B. taurus	HDAC1	99.2	93.9
M. musculus	Hdac1	99.4	90.5
R. norvegicus	Hdac1	99.2	90.9
G. gallus	Hdac1	93.3	79.2
D. melanogaster	Rpd3	82.1	72.2
A. gambiae	AgaP_AGAP006511	83.1	72.8
C. elegans	hda-3	69.5	63.5
S. cerevisiae	RPD3	64.8	60.3
K. lactis	KLLA0E01981g	65.4	61.2
E. gossypii	AGOS_AGR395W	65.0	62.2
S. pombe	clr6	64.5	63.2
M. oryzae	MGG_05857	66.7	63.9
N. crassa	NCU00824	66.1	62.8
A. thaliana	HD1	67.6	63.4
O. sativa	Os02g02124900	68.3	64.0
O. sativa	Os06g0583400	69.2	65.4

Mutations

Note

A total of 60 substitution missense, 5 substitution nonsense, 29 substitution synonymous, no insertion frameshift, no deletions inframe, 2 deletion frameshift, none complex and none other mutations are reported in COSMIC (Catalogue of somatic mutations in cancer); it was found 110 mutated samples from a total of 29924 tested samples.

Implicated in

Entity name

Oral squamous cell carcinoma

Note

HDAC1 overexpression was found in 55.10% of 49 mobile tongue squamous cell carcinoma evaluated whereas most of the cells from non-neoplastic epithelium presents negative immunoexpression for HDAC1 (Theocharis, et al. 2011). HDAC1 was overexpressed in 70% of lip squamous cell carcinoma (Fig.2) and in 77% of actinic cheilitis, with immunoexpression increasing in preneoplastic cases with severe epithelial dysplasia, and in neoplastic cases with poor differentiation (Chrun, et al. 2017).

Fig. 2. Immunoexpression of HDAC1 in lip squamous cell carcinoma.

Entity name

Esophageal cancer

Note

Comparing H4 acetylation and HDAC1 expression, it was observed hyperacetylation of H4 and decreased HDAC1 expression from esophageal normal tissue through esophageal carcinoma, suggesting that the equilibrium between HDAC and HAT is interrupted in this carcinoma (Toh, et al. 2003). Few cases of esophageal cancer were reported with HDAC1 overexpression when compared to normal esophageal mucosa (15%) (Nakagawa, et al. 2007). Esophageal adenocarcinoma also presented subexpression in majority of cases and was not associated to prognostic factor (Langer, et al. 2010).

Entity name

Thyroid cancer

Note

HDAC1 immunoexpression was found in 99% of 47 thyroid malignances (papillary, follicular, medullary, and anaplastic thyroid carcinomas) and 23 benign thyroid tumors, with significant relation to tumor size, without difference in expression between malignant and benign thyroid tumors (Giaginis, et al. 2014). Nakagawa and collaborators reported immunoreactivity in all evaluated cases of papillary thyroid tumors (Nakagawa, et al. 2007).

Entity name

Gastric cancer

Note

HDAC1 overexpression was detected by semi-quantitative RT-PCR, immunoblot analysis, and immunohistochemistry in gastric cancer tissues compared to its corresponding normal tissue (Choi, et al. 2001; Nakagawa, et al. 2007). Sudo and colleagues found association between HDAC expression and aggressive behavior of primary gastric cancer. In this study, HDAC1 overexpression was found by quantitative reverse transcription-PCR in gastric cancer tissue in 77% of the cases, with higher expression correlated to lymph vessel and vascular vessel permeations, advanced stage of the disease, and lymph node metastasis (Sudo, et al. 2011).

Entity name

Colorectal cancer

Note

When comparing colorectal carcinoma cells and normal colonic mucosa by reverse transcription (RT)-PCR (Ishihama, et al. 2007) and immunohistochemistry (Nakagawa, et al. 2007) there was a greater HDAC1 expression in cancer than in normal colonic epithelium. Bernard and collaborators evaluated tissue microarray (TMA) with 254 colorectal adenocarcinomas samples and 50 normal colorectal tissues, showing no significant difference between normal and cancerous tissues, but suggested combination of higher HDAC expression and clinical outcomes for these patients (Benard, et al. 2015).

Entity name

Pancreatic cancer

Note

HDAC1 with HDAC2 and SIN3A were recognized as complex silencing regulators of CDH1 (E-cadherin), thus involved in pancreatic adenocarcinoma metastasis (von Burstin, et al. 2009; Aghdassi, et al. 2012). Several HDACs were evaluated in (pNET): higher expression of HDAC1 was observed in high grade pNET and its expression showed positive correlation with mitotic (pHH3) and proliferation (Ki-67) index (Klieser, et al. 2017).

Entity name

Lymphomas

Note

Hodgkin`s lymphoma exhibited higher immunoexpression of HDAC1 when analysing 283 TMA (Adams, et al. 2010). In diffuse large B-cell lymphomas (DLBCL) HDAC1 immunoexpression was higher in comparison to reactive lymphoid hyperplasia which was correlated to cell proliferation index (Ki67) in the development of DLBCL, and associated with aggressiveness/poor survival of DLBCL patients (Min, et al. 2012). On the other hand, Lee and colleagues found faintly nuclear staining in few cases of 91 DLBCL samples submitted to immunohistochemistry (Lee, et al. 2014).

Entity name

Leukemias

Note

Moreno and collaborators evaluated 94 cases of childhood acute lymphoblastic leukaemia (ALL) and found HDAC1 mRNA increased expression in T-cell ALL when compared to B-cell ALL. Yang et al. also found higher HDAC1 mRNA in ALL. (Moreno, et al. 2010). Quantitative real-time polymerase chain reaction also revealed higher HDAC1 expression in ALL (Yang, et al. 2015). Clinicopathological parameters indicated that overexpression of HDAC1 may be related to unfavourable prognosis of childhood ALL (Gruhn, et al. 2013).

Entity name

Lung cancer

Note

HDAC1 is highly expressed in lung cancer (Nakagawa, et al. 2007). A correlation between HDAC1 mRNA and protein levels showed that HDAC1 gene expression might be involved with lung cancer progression (Sasaki, et al. 2004).

Entity name

Prostate cancer

Note

Up-regulation of HDAC1 in prostate cancer compared to benign prostatic hyperplasia was demonstrated by immunohistochemistry (Patra, et al. 2001; Nakagawa, et al. 2007). Weichert and collaborators achieved immunohistochemistry for Class I HDAC isoforms in prostate carcinomas, showing HDAC1, HDAC2 and HDAC3 stronger expression accompanied by tumor cell proliferation raising (Weichert, et al. 2008). Overexpression of HDAC1 was also related to major increase of hormone refractory in prostate cancer and augmentation of proliferation (Halkidou, et al. 2004).

Entity name

Breast cancer

Note

HDAC1 was evaluated in TMA from 238 patients with primary breast cancer and presented wide variation in positive imunnoexpression (Muller, et al. 2013). While Nakagawa (Nakagawa, et al. 2007) and Ververis (Ververis and Karagiannis 2012) showed higher expression of HDAC1 by immunohistochemistry and immunofluorescence respectively. Suzuki and colleagues detected a decrease in its expression from normal tissue through invasive ductal carcinoma, and from high grade through intermediate/low grade carcinoma (Suzuki, et al. 2009). Higher expression of HDAC1 was related to molecular subtypes (Luminal A, Luminal B, HER overexpressed, and triple-negative) and with improved overall survival (Seo, et al. 2014).

Entity name

Ovarian cancer

Note

HDAC1 immunoexpression showed positive correlation with Ki-67 and inverse correlation with E-cadherin in 115 cases of ovarian tumors, suggesting an important participation of HDAC1 in cellular proliferation. Its overexpression was also associated with poor outcome (Hayashi, et al. 2010). Immunoreactivity for HDAC1 was sighted in 95% of cases evaluated, but without significant difference between histological subtypes of ovarian cancer (Nakagawa, et al. 2007). By immunohistochemistry and qRT-PCR, HDAC1 and DNMT3B revealed positive correlation in ovarian cancer; HDAC1 was highly expressed in comparison to normal ovarian tissue (Gu, et al. 2013). In a population-based cohort of 465 ovarian carcinomas, Weichert and collaborators observed higher level expression of HDAC1 and positive correlation with Ki67, indicating its participation in cell proliferation without significant interference in prognostic (Weichert 2009).

Entity name

Endometrial cancer

Note

Strong HDAC1 immunoexpression was observed in endometrial stromal sarcoma, and it was suggested that this expression is linked to lower than 10 years disease free survival (Baek, et al. 2016). Endometrial adenocarcinomas compared to normal endometrium exhibited reduction in HDAC1 expression (Krusche, et al. 2005). However, in other research, endometrial carcinomas presented higher HDAC1 expression in comparison to normal endometrial tissue (Fakhry, et al. 2010). Weichert and colleagues evaluated 149 endometrial carcinomas and showed a higher level of HDAC1 expression that was positively correlated with cell proliferation indicator (Ki-67) and associated to 10 years survival decrease (Weichert 2009).

Article Bibliography

Pubmed ID	Last Year	Title	Authors
20415600	2010	Class I histone deacetylases 1, 2 and 3 are highly expressed in classical Hodgkin's lymphoma.	Adams H et al
22147512	2012	Recruitment of histone deacetylases HDAC1 and HDAC2 by the transcriptional repressor ZEB1 downregulates E-cadherin expression in pancreatic cancer.	Aghdassi A et al
27127168	2016	Immunohistochemical Characterization of Histone Deacetylase as a Potential Prognostic Marker and Therapeutic Target in Endometrial Stromal Sarcoma.	Baek MH et al
25307864	2015	Nuclear expression of histone deacetylases and their histone modifications predicts clinical outcome in colorectal cancer.	Benard A et al
11749695	2001	Expression profile of histone deacetylase 1 in gastric cancer tissues.	Choi JH et al
28107582	2017	Immunoexpression of HDAC1, HDAC2, and HAT1 in actinic cheilitis and lip squamous cell carcinoma.	Chrun ES et al
20404188	2010	Histone deacetylase 1 (HDAC1), but not HDAC2, controls embryonic stem cell differentiation.	Dovey OM et al
20178884	2010	Immunohistochemical detection of histone deacetylases in endometrial carcinoma: involvement of histone deacetylase 2 in the proliferation of endometrial carcinoma cells.	Fakhry H et al
23873102	2014	Clinical significance of histone deacetylase (HDAC)-1, HDAC-2, HDAC-4, and HDAC-6 expression in human malignant and benign thyroid lesions.	Giaginis C et al
23948281	2013	The expression of histone deacetylase 4 is associated with prednisone poor-response in childhood acute lymphoblastic leukemia.	Gruhn B et al
23420051	2013	Investigation of the expression patterns and correlation of DNA methyltransferases and class I histone deacetylases in ovarian cancer tissues.	Gu Y et al
15042618	2004	Upregulation and nuclear recruitment of HDAC1 in hormone refractory prostate cancer.	Halkidou K et al
20049841	2010	Type-specific roles of histone deacetylase (HDAC) overexpression in ovarian carcinoma: HDAC1 enhances cell proliferation and HDAC3 stimulates cell migration with downregulation of E-cadherin.	Hayashi A et al
17720775	2007	Expression of HDAC1 and CBP/p300 in human colorectal carcinomas.	Ishihama K et al
10777477	2000	Histone deacetylases specifically down-regulate p53-dependent gene activation.	Juan LJ et al
23697933	2013	The physiological roles of histone deacetylase (HDAC) 1 and 2: complex co-stars with multiple leading parts.	Kelly RD et al
15770522	2005	Histone deacetylase-1 and -3 protein expression in human breast cancer: a tissue microarray analysis.	Krusche CA et al
20924032	2010	Expression of class I histone deacetylases (HDAC1 and HDAC2) in oesophageal adenocarcinomas: an immunohistochemical study.	Langer R et al
25076845	2014	Expression of histone deacetylases in diffuse large B-cell lymphoma and its clinical significance.	Lee SH et al
23627572	2013	Differential expression of histone deacetylases HDAC1, 2 and 3 in human breast cancer--overexpression of HDAC2 and HDAC3 is associated with clinicopathological indicators of disease progression.	Müller BM et al
23109994	2012	Expression of HAT1 and HDAC1, 2, 3 in Diffuse Large B-Cell Lymphomas, Peripheral T-Cell Lymphomas, and NK/T-Cell Lymphomas.	Min SK et al
20636436	2010	Differential expression of HDAC3, HDAC7 and HDAC9 is associated with prognosis and survival in childhood acute lymphoblastic leukaemia.	Moreno DA et al
17786334	2007	Expression profile of class I histone deacetylases in human cancer tissues.	Nakagawa M et al
11563853	2001	Histone deacetylase and DNA methyltransferase in human prostate cancer.	Patra SK et al
15474665	2004	Histone deacetylase 1 mRNA expression in lung cancer.	Sasaki H et al
25548579	2014	Expression of Histone Deacetylases HDAC1, HDAC2, HDAC3, and HDAC6 in Invasive Ductal Carcinomas of the Breast.	Seo J et al
21725604	2011	Histone deacetylase 1 expression in gastric cancer.	Sudo T et al
19383825	2009	Protein acetylation and histone deacetylase expression associated with malignant breast cancer progression.	Suzuki J et al
21457345	2011	Histone deacetylase-1 and -2 expression in mobile tongue squamous cell carcinoma: associations with clinicopathological parameters and patients survival.	Theocharis S et al
12579268	2003	Histone H4 acetylation and histone deacetylase 1 expression in esophageal squamous cell carcinoma.	Toh Y et al
22347520	2012	An atlas of histone deacetylase expression in breast cancer: fluorescence methodology for comparative semi-quantitative analysis.	Ververis K et al
19103471	2009	HDAC expression and clinical prognosis in human malignancies.	Weichert W et al
18212746	2008	Histone deacetylases 1, 2 and 3 are highly expressed in prostate cancer and HDAC2 expression is associated with shorter PSA relapse time after radical prostatectomy.	Weichert W et al
25944469	2015	Analysis of class I and II histone deacetylase gene expression in human leukemia.	Yang H et al
16940178	2006	Negative and positive regulation of gene expression by mouse histone deacetylase 1.	Zupkovitz G et al
19362090	2009	E-cadherin regulates metastasis of pancreatic cancer in vivo and is suppressed by a SNAIL/HDAC1/HDAC2 repressor complex.	von Burstin J et al

Other Information

Locus ID:

NCBI: 3065
MIM: 601241
HGNC: 4852
Ensembl: ENSG00000116478

Variants:

dbSNP: 3065
ClinVar: 3065
TCGA: ENSG00000116478
COSMIC: HDAC1

RNA/Proteins

Gene ID	Transcript ID	Uniprot
ENSG00000116478	ENST00000373548	Q13547
ENSG00000116478	ENST00000373548	Q6IT96
ENSG00000116478	ENST00000428704	Q5TEE2

Expression (GTEx)

100

150

200

250

Adipose - Subcutaneous

Adipose - Visceral

Adrenal Gland

Artery - Aorta

Artery - Tibial

Bladder

Brain - Amygdala

Brain - Anterior cingulate cortex

Brain - Caudate

Brain - Cerebellar Hemisphere

Brain - Cerebellum

Brain - Cortex

Brain - Frontal Cortex

Brain - Hippocampus

Brain - Hypothalamus

Brain - Nucleus accumbens

Brain - Putamen

Brain - Spinal cord

Brain - Substantia nigra

Breast - Mammary Tissue

Cells - Cultured fibroblasts

Cells - EBV - transformed lymphocytes

Cervix - Ectocervix

Cervix - Endocervix

Colon - Sigmoid

Colon - Transverse

Esophagus - Gastroesophageal Junction

Esophagus - Mucosa

Esophagus - Muscularis

Fallopian Tube

Heart - Atrial Appendage

Heart - Left Ventricle

Kidney - Cortex

Kidney - Medulla

Liver

Lung

Minor Salivary Gland

Muscle - Skeletal

Nerve - Tibial

Ovary

Pancreas

Pituitary

Prostate

Skin - Not Sun Exposed

Skin - Sun Exposed

Small Intestine - Terminal Ileum

Spleen

Stomach

Testis

Thyroid

Uterus

Vagina

Whole Blood

Pathways

Pathway	Source	External ID
Cell cycle	KEGG	ko04110
Notch signaling pathway	KEGG	ko04330
Huntington's disease	KEGG	ko05016
Chronic myeloid leukemia	KEGG	ko05220
Cell cycle	KEGG	hsa04110
Notch signaling pathway	KEGG	hsa04330
Huntington's disease	KEGG	hsa05016
Pathways in cancer	KEGG	hsa05200
Chronic myeloid leukemia	KEGG	hsa05220
Transcriptional misregulation in cancer	KEGG	ko05202
Transcriptional misregulation in cancer	KEGG	hsa05202
Amphetamine addiction	KEGG	hsa05031
Amphetamine addiction	KEGG	ko05031
Epstein-Barr virus infection	KEGG	hsa05169
Alcoholism	KEGG	hsa05034
Epstein-Barr virus infection	KEGG	ko05169
Alcoholism	KEGG	ko05034
Viral carcinogenesis	KEGG	hsa05203
Viral carcinogenesis	KEGG	ko05203
MicroRNAs in cancer	KEGG	hsa05206
MicroRNAs in cancer	KEGG	ko05206
Thyroid hormone signaling pathway	KEGG	hsa04919
Disease	REACTOME	R-HSA-1643685
Diseases of signal transduction	REACTOME	R-HSA-5663202
Signaling by NOTCH1 in Cancer	REACTOME	R-HSA-2644603
Signaling by NOTCH1 PEST Domain Mutants in Cancer	REACTOME	R-HSA-2644602
Constitutive Signaling by NOTCH1 PEST Domain Mutants	REACTOME	R-HSA-2644606
Signaling by NOTCH1 HD+PEST Domain Mutants in Cancer	REACTOME	R-HSA-2894858
Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants	REACTOME	R-HSA-2894862
Hemostasis	REACTOME	R-HSA-109582
Factors involved in megakaryocyte development and platelet production	REACTOME	R-HSA-983231
Signal Transduction	REACTOME	R-HSA-162582
Signalling by NGF	REACTOME	R-HSA-166520
p75 NTR receptor-mediated signalling	REACTOME	R-HSA-193704
p75NTR negatively regulates cell cycle via SC1	REACTOME	R-HSA-193670
Signaling by TGF-beta Receptor Complex	REACTOME	R-HSA-170834
Transcriptional activity of SMAD2/SMAD3:SMAD4 heterotrimer	REACTOME	R-HSA-2173793
SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription	REACTOME	R-HSA-2173796
Downregulation of SMAD2/3:SMAD4 transcriptional activity	REACTOME	R-HSA-2173795
Signaling by NOTCH	REACTOME	R-HSA-157118
Signaling by NOTCH1	REACTOME	R-HSA-1980143
NOTCH1 Intracellular Domain Regulates Transcription	REACTOME	R-HSA-2122947
Signaling by Wnt	REACTOME	R-HSA-195721
Degradation of beta-catenin by the destruction complex	REACTOME	R-HSA-195253
Repression of WNT target genes	REACTOME	R-HSA-4641265
TCF dependent signaling in response to WNT	REACTOME	R-HSA-201681
Formation of the beta-catenin:TCF transactivating complex	REACTOME	R-HSA-201722
Deactivation of the beta-catenin transactivating complex	REACTOME	R-HSA-3769402
Gene Expression	REACTOME	R-HSA-74160
Generic Transcription Pathway	REACTOME	R-HSA-212436
Transcriptional Regulation by TP53	REACTOME	R-HSA-3700989
RNA Polymerase I, RNA Polymerase III, and Mitochondrial Transcription	REACTOME	R-HSA-504046
RNA Polymerase I Transcription	REACTOME	R-HSA-73864
RNA Polymerase I Promoter Clearance	REACTOME	R-HSA-73854
RNA Polymerase I Transcription Initiation	REACTOME	R-HSA-73762
Epigenetic regulation of gene expression	REACTOME	R-HSA-212165
Negative epigenetic regulation of rRNA expression	REACTOME	R-HSA-5250941
NoRC negatively regulates rRNA expression	REACTOME	R-HSA-427413
Cell Cycle	REACTOME	R-HSA-1640170
Cell Cycle, Mitotic	REACTOME	R-HSA-69278
Mitotic G1-G1/S phases	REACTOME	R-HSA-453279
G0 and Early G1	REACTOME	R-HSA-1538133
Chromatin organization	REACTOME	R-HSA-4839726
Chromatin modifying enzymes	REACTOME	R-HSA-3247509
HDACs deacetylate histones	REACTOME	R-HSA-3214815
Positive epigenetic regulation of rRNA expression	REACTOME	R-HSA-5250913
Longevity regulating pathway - multiple species	KEGG	ko04213
Longevity regulating pathway - multiple species	KEGG	hsa04213
Regulation of TP53 Activity	REACTOME	R-HSA-5633007
Regulation of TP53 Activity through Acetylation	REACTOME	R-HSA-6804758
ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression	REACTOME	R-HSA-427389

Protein levels (Protein atlas)

Not detected

Low

Medium

High

PharmGKB

Entity ID	Name	Type	Evidence	Association	PD	PMIDs
PA10832	corticosteroids	Chemical	ClinicalAnnotation	associated	PD	24307847
PA443450	Asthma	Disease	ClinicalAnnotation	associated	PD	24307847
PA451846	valproic acid	Chemical	Pathway	associated		23407051

References

Pubmed ID	Year	Title	Citations
38254102	2024	HDAC1/2 control mesothelium/ovarian cancer adhesive interactions impacting on Talin-1-α5β1-integrin-mediated actin cytoskeleton and extracellular matrix protein remodeling.	0
38329647	2024	ZNF787 and HDAC1 Mediate Blood-Brain Barrier Permeability in an In Vitro Model of Alzheimer's Disease Microenvironment.	0
38505872	2024	HDAC1-Mediated Downregulation of NEU1 Exacerbates the Aggressiveness of Cervical Cancer.	0
38812060	2024	Unveiling the role of HP1α-HDAC1-STAT1 axis as a therapeutic target for HP1α-positive intrahepatic cholangiocarcinoma.	1
38254102	2024	HDAC1/2 control mesothelium/ovarian cancer adhesive interactions impacting on Talin-1-α5β1-integrin-mediated actin cytoskeleton and extracellular matrix protein remodeling.	0
38329647	2024	ZNF787 and HDAC1 Mediate Blood-Brain Barrier Permeability in an In Vitro Model of Alzheimer's Disease Microenvironment.	0
38505872	2024	HDAC1-Mediated Downregulation of NEU1 Exacerbates the Aggressiveness of Cervical Cancer.	0
38812060	2024	Unveiling the role of HP1α-HDAC1-STAT1 axis as a therapeutic target for HP1α-positive intrahepatic cholangiocarcinoma.	1
36287107	2023	HDAC1 regulates the chromatin landscape to control transcriptional dependencies in chronic lymphocytic leukemia.	3
36346011	2023	Regulation of osteogenesis in bone marrow-derived mesenchymal stem cells via histone deacetylase 1 and 2 co-cultured with human gingival fibroblasts and periodontal ligament cells.	4
36587730	2023	Proteomics-based trapping with single or multiple inactive mutants reproducibly profiles histone deacetylase 1 substrates.	0
37121053	2023	HDAC1 mediates epithelial-mesenchymal transition and promotes cancer cell invasion in glioblastoma.	3
37661113	2023	Evaluation of epigenetic-related gene expression (DNMT, HDAC1) in Iranian patients with systemic lupus erythematosus.	0
37737560	2023	BCL11B and the NuRD complex cooperatively guard T-cell fate and inhibit OPA1-mediated mitochondrial fusion in T cells.	1
37878419	2023	GSE1 links the HDAC1/CoREST co-repressor complex to DNA damage.	0

Citation

Emanuely Silva Chrun ; Filipe Modolo ; Filipe Ivan Daniel

HDAC1 (histone deacetylase 1)

Atlas Genet Cytogenet Oncol Haematol. 2017-08-01

Online version: http://atlasgeneticsoncology.org/gene/40802