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PDBsum entry 1w22

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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
1w22
Jmol
Contents
Protein chains
353 a.a. *
Ligands
NHB ×2
Metals
_ZN ×2
__K ×4
Waters ×280
* Residue conservation analysis
PDB id:
1w22
Name: Hydrolase
Title: Crystal structure of inhibited human hdac8
Structure: Histone deacetylase 8. Chain: a, b. Synonym: hdac8, hd8, cda07. Engineered: yes
Source: Homo sapiens. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Resolution:
2.50Å     R-factor:   0.210     R-free:   0.249
Authors: A.Vannini,C.Volpari,E.Caroli Casavola,S.Di Marco
Key ref:
A.Vannini et al. (2004). Crystal structure of a eukaryotic zinc-dependent histone deacetylase, human HDAC8, complexed with a hydroxamic acid inhibitor. Proc Natl Acad Sci U S A, 101, 15064-15069. PubMed id: 15477595 DOI: 10.1073/pnas.0404603101
Date:
25-Jun-04     Release date:   24-Sep-04    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9BY41  (HDAC8_HUMAN) -  Histone deacetylase 8
Seq:
Struc:
377 a.a.
353 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.5.1.98  - Histone deacetylase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   5 terms 
  Biological process     histone H3 deacetylation   11 terms 
  Biochemical function     hydrolase activity     11 terms  

 

 
DOI no: 10.1073/pnas.0404603101 Proc Natl Acad Sci U S A 101:15064-15069 (2004)
PubMed id: 15477595  
 
 
Crystal structure of a eukaryotic zinc-dependent histone deacetylase, human HDAC8, complexed with a hydroxamic acid inhibitor.
A.Vannini, C.Volpari, G.Filocamo, E.C.Casavola, M.Brunetti, D.Renzoni, P.Chakravarty, C.Paolini, R.De Francesco, P.Gallinari, C.Steinkühler, S.Di Marco.
 
  ABSTRACT  
 
Histone deacetylases (HDACs) are a family of enzymes involved in the regulation of gene expression, DNA repair, and stress response. These processes often are altered in tumors, and HDAC inhibitors have had pronounced antitumor activity with promising results in clinical trials. Here, we report the crystal structure of human HDAC8 in complex with a hydroxamic acid inhibitor. Such a structure of a eukaryotic zinc-dependent HDAC has not be described previously. Similar to bacterial HDAC-like protein, HDAC8 folds in a single alpha/beta domain. The inhibitor and the zinc-binding sites are similar in both proteins. However, significant differences are observed in the length and structure of the loops surrounding the active site, including the presence of two potassium ions in HDAC8 structure, one of which interacts with key catalytic residues. CD data suggest a direct role of potassium in the fold stabilization of HDAC8. Knockdown of HDAC8 by RNA interference inhibits growth of human lung, colon, and cervical cancer cell lines, highlighting the importance of this HDAC subtype for tumor cell proliferation. Our findings open the way for the design and development of selective inhibitors of HDAC8 as possible antitumor agents.
 
  Selected figure(s)  
 
Figure 2.
Fig. 2. Overall HDAC8 structure. (A) Ribbon diagram of the asymmetric unit of human HDAC8 crystals. The two monomers, A and B, are shown in indigo and yellow, respectively. The two inhibitor molecules and residues involved in the head-to-head packing are drawn in stick representation. Red, oxygen; blue, nitrogen; orange, sulfur. Carbon is shown in indigo (molecule A) and yellow (molecule B). Violet spheres, Zn2+ ions; red spheres, K+ ions. The chemical structure of the hydroxamic acid inhibitor is drawn in the upper left. (B) Ribbon diagram of human HDAC8 monomer with -helices and -strands labeled and colored yellow and indigo, respectively. The inhibitor is drawn in stick representation. Red, oxygen; blue, nitrogen; orange, sulfur; green, carbon. (C) Superposition of human HDAC8 (yellow) and HDLP (gray) backbone. Compound 1 and TSA are drawn in stick representation. Oxygen, nitrogen, and sulfur are colored as in A. Carbon is shown in yellow (compound 1) and gray (TSA). Dashed circles highlight structural variations of loops emerging from the core of the two structures.
Figure 3.
Fig. 3. Molecular surface representation and architecture of HDAC8 active site. Residues relevant for catalysis and involved in inhibitor binding as well as the inhibitor and the modeled acetyllysine are drawn in stick representation. Red, oxygen; blue, nitrogen; orange, sulfur; gray, carbon. Carbon is colored green for the inhibitor and wheat for the docked acetyllysine. Polar interactions are shown as dashed yellow lines. Numbers in parentheses represent the zinc-ligand distances.
 
  Figures were selected by the author.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21377170 G.Li, H.Jiang, M.Chang, H.Xie, and L.Hu (2011).
HDAC6 α-tubulin deacetylase: a potential therapeutic target in neurodegenerative diseases.
  J Neurol Sci, 304, 1-8.  
21334896 W.Tang, T.Luo, E.F.Greenberg, J.E.Bradner, and S.L.Schreiber (2011).
Discovery of histone deacetylase 8 selective inhibitors.
  Bioorg Med Chem Lett, 21, 2601-2605.  
21419152 Y.Zhang, G.Yu, D.Wang, Y.Hu, and W.Lei (2011).
ERK1/2 activation plays important roles in the opposite effects of Trichostatin A in non-cancer and cancer cells.
  Toxicon, 57, 932-937.  
20219112 G.Wu, C.Nan, J.C.Rollo, X.Huang, and J.Tian (2010).
Sodium valproate-induced congenital cardiac abnormalities in mice are associated with the inhibition of histone deacetylase.
  J Biomed Sci, 17, 16.  
20157916 H.Park, S.Kim, Y.E.Kim, and S.J.Lim (2010).
A structure-based virtual screening approach toward the discovery of histone deacetylase inhibitors: identification of promising zinc-chelating groups.
  ChemMedChem, 5, 591-597.  
  20657706 J.M.Hooker, S.W.Kim, D.Alexoff, Y.Xu, C.Shea, A.Reid, N.Volkow, and J.S.Fowler (2010).
Histone deacetylase inhibitor, MS-275, exhibits poor brain penetration: PK studies of [C]MS-275 using Positron Emission Tomography.
  ACS Chem Neurosci, 1, 65-73.  
20142042 K.T.Smith, S.A.Martin-Brown, L.Florens, M.P.Washburn, and J.L.Workman (2010).
Deacetylase inhibitors dissociate the histone-targeting ING2 subunit from the Sin3 complex.
  Chem Biol, 17, 65-74.  
20401613 N.Noureen, H.Rashid, and S.Kalsoom (2010).
Identification of type-specific anticancer histone deacetylase inhibitors: road to success.
  Cancer Chemother Pharmacol, 66, 625-633.  
20029090 S.L.Gantt, C.G.Joseph, and C.A.Fierke (2010).
Activation and inhibition of histone deacetylase 8 by monovalent cations.
  J Biol Chem, 285, 6036-6043.  
20209563 W.J.Huang, C.C.Chen, S.W.Chao, S.S.Lee, F.L.Hsu, Y.L.Lu, M.F.Hung, and C.I.Chang (2010).
Synthesis of N-hydroxycinnamides capped with a naturally occurring moiety as inhibitors of histone deacetylase.
  ChemMedChem, 5, 598-607.  
19349466 A.Bougdour, D.Maubon, P.Baldacci, P.Ortet, O.Bastien, A.Bouillon, J.C.Barale, H.Pelloux, R.Ménard, and M.A.Hakimi (2009).
Drug inhibition of HDAC3 and epigenetic control of differentiation in Apicomplexa parasites.
  J Exp Med, 206, 953-966.  
19093884 A.K.Oyelere, P.C.Chen, W.Guerrant, S.C.Mwakwari, R.Hood, Y.Zhang, and Y.Fan (2009).
Non-peptide macrocyclic histone deacetylase inhibitors.
  J Med Chem, 52, 456-468.  
19169274 A.Zubia, S.Ropero, D.Otaegui, E.Ballestar, M.F.Fraga, M.Boix-Chornet, M.Berdasco, A.Martinez, L.Coll-Mulet, J.Gil, F.P.Cossío, and M.Esteller (2009).
Identification of (1H)-pyrroles as histone deacetylase inhibitors with antitumoral activity.
  Oncogene, 28, 1477-1484.  
18603028 B.C.Smith, and J.M.Denu (2009).
Chemical mechanisms of histone lysine and arginine modifications.
  Biochim Biophys Acta, 1789, 45-57.  
19705846 C.A.Olsen, and M.R.Ghadiri (2009).
Discovery of potent and selective histone deacetylase inhibitors via focused combinatorial libraries of cyclic alpha3beta-tetrapeptides.
  J Med Chem, 52, 7836-7846.  
19885462 D.Griffith, M.P.Morgan, and C.J.Marmion (2009).
A novel anti-cancer bifunctional platinum drug candidate with dual DNA binding and histone deacetylase inhibitory activity.
  Chem Commun (Camb), (), 6735-6737.  
19362838 F.Hu, C.J.Chou, and J.M.Gottesfeld (2009).
Design and synthesis of novel hybrid benzamide-peptide histone deacetylase inhibitors.
  Bioorg Med Chem Lett, 19, 3928-3931.  
19528666 H.Nian, W.H.Bisson, W.M.Dashwood, J.T.Pinto, and R.H.Dashwood (2009).
Alpha-keto acid metabolites of organoselenium compounds inhibit histone deacetylase activity in human colon cancer cells.
  Carcinogenesis, 30, 1416-1423.  
18845268 K.T.Smith, and J.L.Workman (2009).
Histone deacetylase inhibitors: anticancer compounds.
  Int J Biochem Cell Biol, 41, 21-25.  
19855427 L.Wang, E.F.de Zoeten, M.I.Greene, and W.W.Hancock (2009).
Immunomodulatory effects of deacetylase inhibitors: therapeutic targeting of FOXP3+ regulatory T cells.
  Nat Rev Drug Discov, 8, 969-981.  
19459166 P.A.Marks, and W.S.Xu (2009).
Histone deacetylase inhibitors: Potential in cancer therapy.
  J Cell Biochem, 107, 600-608.  
19821480 P.Galletti, A.Quintavalla, C.Ventrici, G.Giannini, W.Cabri, S.Penco, G.Gallo, S.Vincenti, and D.Giacomini (2009).
Azetidinones as Zinc-Binding Groups to Design Selective HDAC8 Inhibitors.
  ChemMedChem, 4, 1991-2001.  
19433508 P.H.Lee, K.L.Kuo, P.Y.Chu, E.M.Liu, and J.H.Lin (2009).
SLITHER: a web server for generating contiguous conformations of substrate molecules entering into deep active sites of proteins or migrating through channels in membrane transporters.
  Nucleic Acids Res, 37, W559-W564.  
19388875 S.F.Sleiman, M.Basso, L.Mahishi, A.P.Kozikowski, M.E.Donohoe, B.Langley, and R.R.Ratan (2009).
Putting the 'HAT' back on survival signalling: the promises and challenges of HDAC inhibition in the treatment of neurological conditions.
  Expert Opin Investig Drugs, 18, 573-584.  
19721249 T.Suzuki (2009).
Explorative study on isoform-selective histone deacetylase inhibitors.
  Chem Pharm Bull (Tokyo), 57, 897-906.  
19560043 W.Renthal, and E.J.Nestler (2009).
Histone acetylation in drug addiction.
  Semin Cell Dev Biol, 20, 387-394.  
19822520 Y.Luo, W.Jian, D.Stavreva, X.Fu, G.Hager, J.Bungert, S.Huang, and Y.Qiu (2009).
Trans-regulation of histone deacetylase activities through acetylation.
  J Biol Chem, 284, 34901-34910.  
19029799 A.Abbas, and S.Gupta (2008).
The role of histone deacetylases in prostate cancer.
  Epigenetics, 3, 300-309.  
19099580 A.Ashe, D.K.Morgan, N.C.Whitelaw, T.J.Bruxner, N.K.Vickaryous, L.L.Cox, N.C.Butterfield, C.Wicking, M.E.Blewitt, S.J.Wilkins, G.J.Anderson, T.C.Cox, and E.Whitelaw (2008).
A genome-wide screen for modifiers of transgene variegation identifies genes with critical roles in development.
  Genome Biol, 9, R182.  
18648687 A.I.Anzellotti, and N.P.Farrell (2008).
Zinc metalloproteins as medicinal targets.
  Chem Soc Rev, 37, 1629-1651.  
18181121 A.P.Kozikowski, Y.Chen, A.M.Gaysin, D.N.Savoy, D.D.Billadeau, and K.H.Kim (2008).
Chemistry, biology, and QSAR studies of substituted biaryl hydroxamates and mercaptoacetamides as HDAC inhibitors-nanomolar-potency inhibitors of pancreatic cancer cell growth.
  ChemMedChem, 3, 487-501.  
18285338 A.Schuetz, J.Min, A.Allali-Hassani, M.Schapira, M.Shuen, P.Loppnau, R.Mazitschek, N.P.Kwiatkowski, T.A.Lewis, R.L.Maglathin, T.H.McLean, A.Bochkarev, A.N.Plotnikov, M.Vedadi, and C.H.Arrowsmith (2008).
Human HDAC7 harbors a class IIa histone deacetylase-specific zinc binding motif and cryptic deacetylase activity.
  J Biol Chem, 283, 11355-11363.
PDB codes: 3c0y 3c0z 3c10
18568166 A.V.Bieliauskas, and M.K.Pflum (2008).
Isoform-selective histone deacetylase inhibitors.
  Chem Soc Rev, 37, 1402-1413.  
18454196 C.C.Zhu, D.J.Bornemann, D.Zhitomirsky, E.L.Miller, M.B.O'Connor, and J.A.Simon (2008).
Drosophila histone deacetylase-3 controls imaginal disc size through suppression of apoptosis.
  PLoS Genet, 4, e1000009.  
18616420 C.Le Tourneau, and L.L.Siu (2008).
Promising antitumor activity with MGCD0103, a novel isotype-selective histone deacetylase inhibitor.
  Expert Opin Investig Drugs, 17, 1247-1254.  
18398905 C.Yan, Z.Xiu, X.Li, S.Li, C.Hao, and H.Teng (2008).
Comparative molecular dynamics simulations of histone deacetylase-like protein: binding modes and free energy analysis to hydroxamic acid inhibitors.
  Proteins, 73, 134-149.  
18360740 D.P.Dowling, L.Di Costanzo, H.A.Gennadios, and D.W.Christianson (2008).
Evolution of the arginase fold and functional diversity.
  Cell Mol Life Sci, 65, 2039-2055.  
19053282 D.P.Dowling, S.L.Gantt, S.G.Gattis, C.A.Fierke, and D.W.Christianson (2008).
Structural studies of human histone deacetylase 8 and its site-specific variants complexed with substrate and inhibitors.
  Biochemistry, 47, 13554-13563.
PDB codes: 3ew8 3ewf 3ezp 3ezt 3f06 3f07 3f0r
18451556 H.Kobayashi, N.Morisaki, H.Miyachi, and Y.Hashimoto (2008).
Coordination of divalent metal cation to amide group to form adduct ion in FAB mass spectrometry: implication of Zn2+ in enzymatic hydrolysis of amide bond.
  Chem Pharm Bull (Tokyo), 56, 672-676.  
18628250 H.Nian, B.Delage, J.T.Pinto, and R.H.Dashwood (2008).
Allyl mercaptan, a garlic-derived organosulfur compound, inhibits histone deacetylase and enhances Sp3 binding on the P21WAF1 promoter.
  Carcinogenesis, 29, 1816-1824.  
18789133 M.Dejligbjerg, M.Grauslund, T.Litman, L.Collins, X.Qian, M.Jeffers, H.Lichenstein, P.B.Jensen, and M.Sehested (2008).
Differential effects of class I isoform histone deacetylase depletion and enzymatic inhibition by belinostat or valproic acid in HeLa cells.
  Mol Cancer, 7, 70.  
18800048 P.A.Cole (2008).
Chemical probes for histone-modifying enzymes.
  Nat Chem Biol, 4, 590-597.  
18256683 S.Balasubramanian, J.Ramos, W.Luo, M.Sirisawad, E.Verner, and J.J.Buggy (2008).
A novel histone deacetylase 8 (HDAC8)-specific inhibitor PCI-34051 induces apoptosis in T-cell lymphomas.
  Leukemia, 22, 1026-1034.  
18729444 S.V.Weerasinghe, G.Estiu, O.Wiest, and M.K.Pflum (2008).
Residues in the 11 A channel of histone deacetylase 1 promote catalytic activity: implications for designing isoform-selective histone deacetylase inhibitors.
  J Med Chem, 51, 5542-5551.  
18555775 T.Ago, T.Liu, P.Zhai, W.Chen, H.Li, J.D.Molkentin, S.F.Vatner, and J.Sadoshima (2008).
A redox-dependent pathway for regulating class II HDACs and cardiac hypertrophy.
  Cell, 133, 978-993.  
18292778 X.J.Yang, and E.Seto (2008).
The Rpd3/Hda1 family of lysine deacetylases: from bacteria and yeast to mice and men.
  Nat Rev Mol Cell Biol, 9, 206-218.  
  17868168 A.J.Vegas, J.E.Bradner, W.Tang, O.M.McPherson, E.F.Greenberg, A.N.Koehler, and S.L.Schreiber (2007).
Fluorous-based small-molecule microarrays for the discovery of histone deacetylase inhibitors.
  Angew Chem Int Ed Engl, 46, 7960-7964.  
17956988 A.Lahm, C.Paolini, M.Pallaoro, M.C.Nardi, P.Jones, P.Neddermann, S.Sambucini, M.J.Bottomley, P.Lo Surdo, A.Carfí, U.Koch, R.De Francesco, C.Steinkühler, and P.Gallinari (2007).
Unraveling the hidden catalytic activity of vertebrate class IIa histone deacetylases.
  Proc Natl Acad Sci U S A, 104, 17335-17340.  
18059533 A.Sekhavat, J.M.Sun, and J.R.Davie (2007).
Competitive inhibition of histone deacetylase activity by trichostatin A and butyrate.
  Biochem Cell Biol, 85, 751-758.  
17307359 A.V.Bieliauskas, S.V.Weerasinghe, and M.K.Pflum (2007).
Structural requirements of HDAC inhibitors: SAHA analogs functionalized adjacent to the hydroxamic acid.
  Bioorg Med Chem Lett, 17, 2216-2219.  
17721440 A.Vannini, C.Volpari, P.Gallinari, P.Jones, M.Mattu, A.Carfí, R.De Francesco, C.Steinkühler, and S.Di Marco (2007).
Substrate binding to histone deacetylases as shown by the crystal structure of the HDAC8-substrate complex.
  EMBO Rep, 8, 879-884.
PDB codes: 2v5w 2v5x
17377789 C.Hildmann, D.Riester, and A.Schwienhorst (2007).
Histone deacetylases--an important class of cellular regulators with a variety of functions.
  Appl Microbiol Biotechnol, 75, 487-497.  
17227860 C.M.Salisbury, and B.F.Cravatt (2007).
Activity-based probes for proteomic profiling of histone deacetylase complexes.
  Proc Natl Acad Sci U S A, 104, 1171-1176.  
17351388 C.Monneret (2007).
Histone deacetylase inhibitors for epigenetic therapy of cancer.
  Anticancer Drugs, 18, 363-370.  
17383217 H.Hess-Stumpp, T.U.Bracker, D.Henderson, and O.Politz (2007).
MS-275, a potent orally available inhibitor of histone deacetylases--the development of an anticancer agent.
  Int J Biochem Cell Biol, 39, 1388-1405.  
18000499 J.Arts, P.Angibaud, A.Mariën, W.Floren, B.Janssens, P.King, J.van Dun, L.Janssen, T.Geerts, R.W.Tuman, D.L.Johnson, L.Andries, M.Jung, M.Janicot, and K.van Emelen (2007).
R306465 is a novel potent inhibitor of class I histone deacetylases with broad-spectrum antitumoral activity against solid and haematological malignancies.
  Br J Cancer, 97, 1344-1353.  
17562323 L.Di Costanzo, M.Moulin, M.Haertlein, F.Meilleur, and D.W.Christianson (2007).
Expression, purification, assay, and crystal structure of perdeuterated human arginase I.
  Arch Biochem Biophys, 465, 82-89.
PDB code: 2pll
17458893 L.Sigalotti, E.Fratta, S.Coral, E.Cortini, A.Covre, H.J.Nicolay, L.Anzalone, L.Pezzani, A.M.Di Giacomo, E.Fonsatti, F.Colizzi, M.Altomonte, L.Calabrò, and M.Maio (2007).
Epigenetic drugs as pleiotropic agents in cancer treatment: biomolecular aspects and clinical applications.
  J Cell Physiol, 212, 330-344.  
17694086 M.Martin, R.Kettmann, and F.Dequiedt (2007).
Class IIa histone deacetylases: regulating the regulators.
  Oncogene, 26, 5450-5467.  
17325692 P.Gallinari, S.Di Marco, P.Jones, M.Pallaoro, and C.Steinkühler (2007).
HDACs, histone deacetylation and gene transcription: from molecular biology to cancer therapeutics.
  Cell Res, 17, 195-211.  
17555985 R.H.Dashwood, and E.Ho (2007).
Dietary histone deacetylase inhibitors: from cells to mice to man.
  Semin Cancer Biol, 17, 363-369.  
17694092 S.C.Hodawadekar, and R.Marmorstein (2007).
Chemistry of acetyl transfer by histone modifying enzymes: structure, mechanism and implications for effector design.
  Oncogene, 26, 5528-5540.  
17984971 S.Lall (2007).
Primers on chromatin.
  Nat Struct Mol Biol, 14, 1110-1115.  
  17401192 T.K.Nielsen, C.Hildmann, D.Riester, D.Wegener, A.Schwienhorst, and R.Ficner (2007).
Complex structure of a bacterial class 2 histone deacetylase homologue with a trifluoromethylketone inhibitor.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 63, 270-273.
PDB code: 2gh6
17694093 W.S.Xu, R.B.Parmigiani, and P.A.Marks (2007).
Histone deacetylase inhibitors: molecular mechanisms of action.
  Oncogene, 26, 5541-5552.  
16809764 H.Lee, N.Sengupta, A.Villagra, N.Rezai-Zadeh, and E.Seto (2006).
Histone deacetylase 8 safeguards the human ever-shorter telomeres 1B (hEST1B) protein from ubiquitin-mediated degradation.
  Mol Cell Biol, 26, 5259-5269.  
16955068 J.E.Bolden, M.J.Peart, and R.W.Johnstone (2006).
Anticancer activities of histone deacetylase inhibitors.
  Nat Rev Drug Discov, 5, 769-784.  
  17219959 J.He, H.Liu, and Y.Chen (2006).
Effects of trichostatin A on HDAC8 expression, proliferation and cell cycle of molt-4 cells.
  J Huazhong Univ Sci Technolog Med Sci, 26, 531-533.  
16432198 M.V.Simonini, L.M.Camargo, E.Dong, E.Maloku, M.Veldic, E.Costa, and A.Guidotti (2006).
The benzamide MS-275 is a potent, long-lasting brain region-selective inhibitor of histone deacetylases.
  Proc Natl Acad Sci U S A, 103, 1587-1592.  
17022812 N.Kamath, P.Karwowska-Desaulniers, and M.K.Pflum (2006).
Limited proteolysis of human histone deacetylase 1.
  BMC Biochem, 7, 22.  
16988654 R.Butler, and G.P.Bates (2006).
Histone deacetylase inhibitors as therapeutics for polyglutamine disorders.
  Nat Rev Neurosci, 7, 784-796.  
16397526 S.Minucci, and P.G.Pelicci (2006).
Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer.
  Nat Rev Cancer, 6, 38-51.  
16434199 W.Gu, I.Nusinzon, R.D.Smith, C.M.Horvath, and R.B.Silverman (2006).
Carbonyl- and sulfur-containing analogs of suberoylanilide hydroxamic acid: Potent inhibition of histone deacetylases.
  Bioorg Med Chem, 14, 3320-3329.  
16762839 Y.Qiu, Y.Zhao, M.Becker, S.John, B.S.Parekh, S.Huang, A.Hendarwanto, E.D.Martinez, Y.Chen, H.Lu, N.L.Adkins, D.A.Stavreva, M.Wiench, P.T.Georgel, R.L.Schiltz, and G.L.Hager (2006).
HDAC1 acetylation is linked to progressive modulation of steroid receptor-induced gene transcription.
  Mol Cell, 22, 669-679.  
16187233 A.Thakur, H.Xu, Y.Wang, A.Bollig, H.Biliran, and J.D.Liao (2005).
The role of X-linked genes in breast cancer.
  Breast Cancer Res Treat, 93, 135-143.  
15878665 K.Vanommeslaeghe, F.De Proft, S.Loverix, D.Tourwé, and P.Geerlings (2005).
Theoretical study revealing the functioning of a novel combination of catalytic motifs in histone deacetylase.
  Bioorg Med Chem, 13, 3987-3992.  
16300464 P.J.Barnes (2005).
Targeting histone deacetylase 2 in chronic obstructive pulmonary disease treatment.
  Expert Opin Ther Targets, 9, 1111-1121.  
16041839 S.Schäfer, and M.Jung (2005).
Chromatin modifications as targets for new anticancer drugs.
  Arch Pharm (Weinheim), 338, 347-357.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.