Discussione:Istone

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Riordino bibliografia[modifica wikitesto]

Pubblico qui in discussione la bibliografia troppo lunga per stare in voce. Siccome mi sembrano quasi tutti articoli, sarebbe bene che qualcuno più nel settore di me li sistemi come note, più che come bibliografia che ho riorganizzato con i soli libri usati come fonte.

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  • Roth EB et al (2006): Antibodies against transglutaminases, peptidylarginine deiminase and citrulline in rheumatoid arthritis—new pathways to epitope spreading. Clin Exp Rheumatol.2006 Jan-Feb; 24(1):12-8.
  • Morita Y et al (2008): Anti-cyclic citrullinated peptide antibody in systemic sclerosis. Clin Exp Rheumatol. 2008 Jul-Aug; 26(4):542-7.
  • Shilatifard A. (2006): Chromatin modifications by methylation and ubiquitination: implications in the regulation of gene expression. Annu Rev Biochem. 2006; 75:243-69. Review.
  • Vossennar ER et al (2003): Citrullination of synovial proteins in murine models of rheumatoid arthritis. Arthritis Rheum.; 48(9):2489-500.
  • Hagiwara T et al (2002): Deimination of arginine residues in nucleophosmin/B23 and histones in HL-60 granulocytes. Biochem Biophys Res Commun.; 290(3):979-83.
  • Hagiwara T et al (2005): Deimination of histone H2A and H4 at arginine 3 in HL-60 granulocytes. Biochemistry. 2005 Apr 19;44(15):5827-34.
  • Knuckley B et al (2010): Haloacetamidine-based inactivators of protein arginine deiminase 4 (PAD4): evidence that general acid catalysis promotes efficient inactivation. Chembiochem. 2010 Jan 25; 11(2):161-5.
  • Thompson PR, Fast W. (2006): Histone citrullination by protein arginine deiminase: is arginine methylation a green light or a roadblock? ACS Chem. Biol..; 1(7):433-41.
  • Cuthbert GL et al (2004): Histone deimination antagonizes arginine methylation. Cell. 2004 Sep 3;1 18(5):545-53.
  • Zhou W et al (2008): Histone H2A monoubiquitination represses transcription by inhibiting RNA polymerase II transcriptional elongation. Mol Cell. 2008 Jan 18; 29(1):69-80.
  • Zhou W et al (2009): Histone H2A ubiquitination in transcriptional regulation and DNA damage repair. Int J Biochem Cell Biol.; 41(1):12-15.
  • Weake VM, Workman JL. (2008): Histone ubiquitination: triggering gene activity. Mol Cell. 2008 Mar 28; 29(6):653-663.
  • Wang Y et al (2004):Human PAD4 regulates histone arginine methylation levels via demethylimination. Science; 306(5694):279-283.
  • Mastronardi FG et al (2006): Increased citrullination of histone H3 in multiple sclerosis brain and animal models of demyelination: a role for tumor necrosis factor-induced peptidylarginine deiminase 4 translocation. J Neurosci. 2006 Nov 1; 26(44):11387-396.
  • Luo Y et al (2006): Inhibitors and inactivators of protein arginine deiminase 4: functional and structural characterization. Biochemistry. 2006 Oct 3; 45(39):11727-736.
  • Kearnery PL et al (2005): Kinetic characterization of protein arginine deiminase 4: a transcriptional corepressor implicated in the onset and progression of rheumatoid arthritis. Biochemistry. 2005 Aug 9; 44(31):10570-82.
  • Raijmakers R et al (2007): Methylation of arginine residues interferes with citrullination by peptidylarginine deiminases in vitro. J Mol Biol. 2007 Apr 6; 367(4):1118-1129.
  • Hidaka Y et al (2005): Methylation of the guanidino group of arginine residues prevents citrullination by peptidylarginine deiminase IV. FEBS Lett.; 579(19):4088-92.
  • Auger I et al (2009): New autoantigens in rheumatoid arthritis (RA): screening 8268 protein arrays with sera from patients with RA. Ann Rheum Dis.; 68(4):591-594.
  • Nakashima K, Hagiwara T, Yamada M. (2002): Nuclear localization of peptidylarginine deiminase V and histone deimination in granulocytes. J Biol Chem.; 277(51):49562-568.
  • Denman RB et al (2005): PAD: the smoking gun behind arginine methylation signaling? Bioessays. 2005 Mar;27(3):242-46.
  • Anzilotti C et al (2010): Peptidylarginine deiminase 4 and citrullination in health and disease. Autoimmun Rev. 2010 Jan; 9(3):158-60. Review.
  • Zhao J et al (2008): Prevalence and significance of anti-peptidylarginine deiminase 4 antibodies in rheumatoid arthritis. J Rheumatol. 2008 Jun; 35(6):969-74.
  • Wang H et al.: Role of histone H2A ubiquitination in Polycomb silencing. Nature. 2004 Oct 14; 431(7010):873-78.
  • Elvorsen EH et al (2008): Serum IgG antibodies to peptidylarginine deiminase 4 in rheumatoid arthritis and associations with disease severity. Ann Rheum Dis.; 67(3):414-17.
  • Chen Y et al (2007): Lysine propionylation and butyrylation are novel post-translational modifications in histones. Mol Cell Proteomics. 2007 May;6(5):812-9.
  • Cheng Z et al (2009): Molecular characterization of propionyllysines in non-histone proteins. Mol Cell Proteomics. 2009 Jan; 8(1):45-52.
  • Zhang K (2009): Identification and verification of lysine propionylation and butyrylation in yeast core histones using PTMap software. J Proteome Res.; 8(2):900-906.
  • Liu B et al (2009: Identification and characterization of propionylation at histone H3 lysine 23 in mammalian cells. J Biol Chem. 2009 Nov 20; 284(47):32288-295.
  • Hymes J, Fleischhauer K, Wolf B.: Biotinylation of histones by human serum biotinidase: assessment of biotinyl-transferase activity in sera from normal individuals and children with biotinidase deficiency. Biochem Mol Med. 1995 Oct; 56(1):76-83.
  • Hymes J, Wolf B.: Human biotinidase isn't just for recycling biotin. J Nutr. 1999 Feb; 129(2S Suppl):485S-489S.
  • Stanley JS et al: Biotinylation of histones in human cells. Effects of cell proliferation. Eur J Biochem. 2001 Oct; 268(20):5424-29.
  • Ballard TD et al: Biotinidase catalyzes debiotinylation of histones. Eur J Nutr. 2002 Apr; 41(2):78-84.
  • Peters DM et al: Exposure to UV light causes increased biotinylation of histones in Jurkat cells. Am J Physiol Cell Physiol. 2002 Sep; 283(3):C878-84.
  • Narang MA et al: Reduced histone biotinylation in multiple carboxylase deficiency patients: a nuclear role for holocarboxylase synthetase. Hum Mol Genet. 2004 Jan 1; 13(1):15-23.
  • Rodriguez-Melendez R, Zempleni J. (2003): Regulation of gene expression by biotin (review). J Nutr Biochem.; 14(12):680-90.
  • Camporeale G et al (2004): K8 and K12 are biotinylated in human histone H4. Eur J Biochem.; 271(11):2257-63.
  • Kobza K et al: K4, K9 and K18 in human histone H3 are targets for biotinylation by biotinidase. FEBS J. 2005 Aug; 272(16):4249-59.
  • Chew YC et al: Lysine residues in N-terminal and C-terminal regions of human histone H2A are targets for biotinylation by biotinidase. J Nutr Biochem. 2006 Apr;17(4):225-33.
  • Hassan YI, Zempleni J. (2006): Epigenetic regulation of chromatin structure and gene function by biotin. J Nutr.; 136(7):1763-65.
  • Camporeale G et al (2007): K12-biotinylated histone H4 marks heterochromatin in human lymphoblastoma cells. J Nutr Biochem; 18(11):760-68.
  • Che YC et al. (2008): Biotinylation of histones represses transposable elements in human and mouse cells and cell lines and in Drosophila melanogaster. J Nutr.; 138(12):2316-22.
  • Wijeratne SS, Camporeale G, Zempleni J. (2010): K12-biotinylated histone H4 is enriched in telomeric repeats from human lung IMR-90 fibroblasts. J Nutr Biochem; 21(4):310-6.
  • Chwang B et al: ERK/MAPK regulates hippocampal histone phosphorylation following contextual fear conditioning. Learn Mem. 2006 May-Jun; 13(3):322-8.
  • Chandramohan Y et al: The forced swimming-induced behavioural immobility response involves histone H3 phospho-acetylation and c-Fos induction in dentate gyrus granule neurons via activation of the N-methyl-D-aspartate/extracellular signal-regulated kinase/mitogen- and stress-activated kinase signalling pathway. Eur J Neurosci. 2008 May; 27(10):2701-13.
  • Collins A et al: Exercise improves cognitive responses to psychological stress through enhancement of epigenetic mechanisms and gene expression in the dentate gyrus. PLoS One. 2009; 4(1):e4330.
  • Bilang-Bleuel A et al: Psychological stress increases histone H3 phosphorylation in adult dentate gyrus granule neurons: involvement in a glucocorticoid receptor-dependent behavioural response. Eur J Neurosci. 2005 Oct; 22(7):1691-700.
  • Teng H et al: Phosphorylation of histone H3 by protein kinase C signaling plays a critical role in the regulation of the developmentally important TBX2 gene. J Biol Chem. 2009 Sep 25; 284(39):26368-76.
  • Espino PS et al: Genomic instability and histone H3 phosphorylation induction by the Ras-mitogen activated protein kinase pathway in pancreatic cancer cells. Int J Cancer. 2009 Feb 1; 124(3):562-67.
  • Ge Z et al: Mitogen-activated protein kinase cascade-mediated histone H3 phosphorylation is critical for telomerase reverse transcriptase expression/telomerase activation induced by proliferation. Mol Cell Biol. 2006 Jan; 26(1):230-237.
  • Ke Q. et al: Nickel compounds induce phosphorylation of histone H3 at serine 10 by activating JNK-MAPK pathway. Carcinogenesis. 2008 Jun; 29(6):1276-81.
  • He Z et al: Regulation of ultraviolet B-induced phosphorylation of histone H3 at serine 10 by Fyn kinase. J Biol Chem. 2005 Jan 28; 280(4):2446-54.
  • Zhong S et al: Ultraviolet B-induced phosphorylation of histone H3 at serine 28 is mediated by MSK1. J Biol Chem. 2001 Aug 31; 276(35):33213-219.
  • Thomson S et al: The nucleosomal response associated with immediate-early gene induction is mediated via alternative MAP kinase cascades: MSK1 as a potential histone H3/HMG-14 kinase. EMBO J. 1999 Sep 1; 18(17):4779-93.
  • Choi HS et al: Phosphorylation of histone H3 at serine 10 is indispensable for neoplastic cell transformation. Cancer Res. 2005 Jul 1; 65(13):5818-27.
  • Lee YJ, Shukla SD.: Histone H3 phosphorylation at serine 10 and serine 28 is mediated by p38 MAPK in rat hepatocytes exposed to ethanol and acetaldehyde. Eur J Pharmacol. 2007 Nov 14; 573(1-3):29-38.
  • Brami-Cherrier K et al: Glutamate induces histone H3 phosphorylation but not acetylation in striatal neurons: role of mitogen- and stress-activated kinase-1. J Neurochem. 2007 May; 101(3):697-708.
  • Portela A. Esteller M.: Epigenetic modifications and human disease. Nature biotechnology. 2010 Oct; 28:1061.
  • Martin C, Zhang Y. : The diverse functions of histone lysine methylation.
  • Hansen 2002: Hansen, Jeffrey C., Conformational dynamics of the chromatin fiber in solution: determinants, mechanisms, and functions, "Annual review of biophysics and biomolecular structure", 31, 2002, pp. 361-392

--Da uno, già due (dan1gia2) 16:38, 12 ott 2013 (CEST)[rispondi]

Istone deacetilasi[modifica wikitesto]

Nella sezione Istone#Alterazioni dell'acetilazione si dice che l'iperespressione delle deacetilasi può causare alcuni tipi di tumore. Questa notizia pare stravagante e difatti non ne ho trovato conferma in alcun dove. Qualcuno ha la possibilità d controllare la fonte riportata?