Signaling to Chromatin through Histone Modifications

Crystal structure of the nucleosome core particle at 2.8 Å resolution

Luger, K., Mäder, A. W., Richmond, R. K., Sargent, D. F., & Richmond, T. J. (1997) · Nature · doi:10.1038/38444 · Cited by 9,466

DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139

Rogakou, E. P., Pilch, D. R., Orr, A. H., Ivanova, V. S., & Bonner, W. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.10.5858 · Cited by 5,438

Regulation of chromatin structure by site-specific histone H3 methyltransferases

Rea, S., Eisenhaber, F., O'Carroll, D., Strahl, B. D., Sun, Z.-W., Schmid, M., Opravil, S., Mechtler, K., Ponting, C. P., Allis, C. D., et al. (2000) · Nature · doi:10.1038/35020506 · Cited by 2,845

Chromatin Structure: A Repeating Unit of Histones and DNA

Kornberg, R. D. (1974) · Science · doi:10.1126/science.184.4139.868 · Cited by 2,662

Signaling—2000 and Beyond

Hunter, T. (2000) · Cell · doi:10.1016/s0092-8674(00)81688-8 · Cited by 2,586

IAP family proteins---suppressors of apoptosisPreprint

Deveraux, Q. L., & Reed, J. C. (1999) · Genes & Development · doi:10.1101/gad.13.3.239 · Cited by 2,535

Megabase Chromatin Domains Involved in DNA Double-Strand Breaks in Vivo

Rogakou, E. P., Boon, C., Redon, C., & Bonner, W. M. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.146.5.905 · Cited by 2,422

CREB: A Stimulus-Induced Transcription Factor Activated by A Diverse Array of Extracellular Signals

Shaywitz, A. J., & Greenberg, M. E. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.821 · Cited by 2,133

Phosphorylated CREB binds specifically to the nuclear protein CBP

Chrivia, J. C., Kwok, R. P. S., Lamb, N., Hagiwara, M., Montminy, M. R., & Goodman, R. H. (1993) · Nature · doi:10.1038/365855a0 · Cited by 2,052

Mitosis-specific phosphorylation of histone H3 initiates primarily within pericentromeric heterochromatin during G2 and spreads in an ordered fashion coincident with mitotic chromosome condensation

Hendzel, M. J., Wei, Y., Mancini, M. A., Hooser, A. A. V., Ranalli, T. A., Brinkley, B. R., Bazett‐Jones, D. P., & Allis, C. D. (1997) · Chromosoma · doi:10.1007/s004120050256 · Cited by 1,860

Role of Protein Tyrosine Phosphatases in Cancer

Motiwala, T., & Jacob, S. T. (2006) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(06)81008-1 · Cited by 51

HDAC inhibition promotes cardiogenesis and the survival of embryonic stem cells through proteasome‐dependent pathway

Chen, H. P., DeNicola, M., Qin, X., Zhao, Y., Zhang, L., Long, X. L., Zhuang, S., Liu, P. Y., & Zhao, T. C. (2011) · Journal of Cellular Biochemistry · doi:10.1002/jcb.23251 · Cited by 51

Joining the dots: from chromatin remodeling to neuronal plasticity

Zocchi, L., & Sassone‐Corsi, P. (2010) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2010.04.005 · Cited by 51

Valproic acid: Growth inhibition of head and neck cancer by induction of terminal differentiation and senescence

Gan, C. P., Hamid, S., Hor, S. Y., Zain, R. B., Ismail, S. M., Mustafa, W. M. W., Teo, S., Saunders, N. A., & Cheong, S. C. (2011) · Head & Neck · doi:10.1002/hed.21734 · Cited by 51

Histone Deacetylase Modifications by Probiotics in Colorectal Cancer

Farrokhi, A. S., Mohammadlou, M., Abdollahi, M., Eslami, M., & Yousefi, B. (2019) · Journal of Gastrointestinal Cancer · doi:10.1007/s12029-019-00338-2 · Cited by 52

CTD phosphatase: Role in RNA polymerase II cycling and the regulation of transcript elongation

Lin, P. S., Marshall, N. F., & Dahmus, M. E. (2002) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(02)72074-6 · Cited by 51

Genome-Wide Analysis of the Relationship between Transcriptional Regulation by Rpd3p and the Histone H3 and H4 Amino Termini in Budding Yeast

Sabet, N., Volo, S., Yu, C., Madigan, J. P., & Morse, R. H. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.20.8823-8833.2004 · Cited by 51

The role of histone H3 phosphorylation (Ser10 and Ser28) in cell growth and cell transformation

Dong, Z., & Bode, A. M. (2006) · Molecular Carcinogenesis · doi:10.1002/mc.20220 · Cited by 51

Vascular smooth muscle cells in intracranial aneurysms

Wang, Z., Ma, J., Yue, H., Zhang, Z., Fang, F., Wang, G., Liu, X., & Shen, Y. (2023) · Microvascular Research · doi:10.1016/j.mvr.2023.104554 · Cited by 55

Regulation of macrophage cyclooxygenase-2 gene expression by modifications of histone H3

Park, G. Y., Joo, M., Pedchenko, T. V., Blackwell, T. S., & Christman, J. W. (2004) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00338.2003 · Cited by 50

Targeting specific HATs for neurodegenerative disease treatment: translating basic biology to therapeutic possibilities

Pirooznia, S. K., & Elefant, F. (2013) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2013.00030 · Cited by 53

Nuclear Receptor Recruitment of Histone-Modifying Enzymes to Target Gene Promoters

Tsai, C., & Fondell, J. D. (2004) · Vitamins and hormones · doi:10.1016/s0083-6729(04)68003-4 · Cited by 50

Phosphorylation of histone H3 is functionally linked to retinoic acid receptor β promoter activation

Lefebvre, B., Ozato, K., & Lefèbvre, P. (2002) · EMBO Reports · doi:10.1093/embo-reports/kvf066 · Cited by 50

Imatinib induces H2AX phosphorylation and apoptosis in chronic myelogenous leukemia cells in vitro via caspase-3/Mst1 pathway

Zhang, Y., Lu, C., Cao, Y., Luo, Y. M., Bao, R.-F., Yan, S., Xue, M., Zhu, F., Wang, Z., & Duan, L.-N. (2012) · Acta Pharmacologica Sinica · doi:10.1038/aps.2012.9 · Cited by 50

Targeted deletion of NF-κB p50 diminishes the cardioprotection of histone deacetylase inhibition

Zhang, L., Zhao, Y., Cheng, G., Guo, T. L., Chin, Y. E., Liu, P. Y., & Zhao, T. (2010) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01015.2009 · Cited by 49

Phosphorylation of Histone H2B Serine 32 Is Linked to Cell Transformation

Lau, A. T. Y., Lee, S., Xu, Y., Zheng, D., Cho, Y., Zhu, F., Kim, H. G., Li, S.-Q., Zhang, Z., Bode, A. M., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.215590 · Cited by 49

Ultra-High Performance Liquid Chromatography−Mass Spectrometry for the Fast Profiling of Histone Post-Translational Modifications

Contrepois, K., Ezan, É., Mann, C., & Fenaille, F. (2010) · Journal of Proteome Research · doi:10.1021/pr100497a · Cited by 55

Chemical Inhibition of Protein Methyltransferases

Schapira, M. (2016) · Cell chemical biology · doi:10.1016/j.chembiol.2016.07.014 · Cited by 49

HIV-1 Tat protein induces IL-10 production in monocytes by classical and alternative NF-κB pathways

Leghmari, K., Bennasser, Y., & Bahraoui, E. (2008) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2008.06.005 · Cited by 49

Chromatin remodeling in plant cell culture: patterns of DNA methylation and histone H3 and H4 acetylation vary during growth of asynchronous potato cell suspensions

Law, R. D., & Suttle, J. C. (2005) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2005.03.014 · Cited by 51

Cancer molecular biology and strategies for the design of cytotoxic gold( i ) and gold( iii ) complexes: a tutorial review

Westhuizen, D., Bezuidenhout, D. I., & Munro, O. Q. (2021) · Dalton Transactions · doi:10.1039/d1dt02783b · Cited by 49

Effects of hydrogen peroxide on MAPK activation, IL‐8 production and cell viability in primary cultures of human bronchial epithelial cells

Pelaia, G., Cuda, G., Vatrella, A., Gallelli, L., Fratto, D., Gioffrè, V., D’Agostino, B., Caputi, M., Maselli, R., Rossi, F., et al. (2004) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20124 · Cited by 47

Meiotic progression of rat spermatocytes requires mitogen-activated protein kinases of Sertoli cells and close contacts between the germ cells and the Sertoli cells

Godet, M., Sabido, O., Gilleron, J., & Durand, P. (2008) · Developmental Biology · doi:10.1016/j.ydbio.2007.12.019 · Cited by 47

Modulation ofAanatgene transcription in the rat pineal gland

Ho, A. K., & Chik, C. L. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06457.x · Cited by 49

Toward Biochemical Understanding of a Transcriptionally Silenced Chromosomal Domain in Saccharomyces cerevisiae

Fox, C. A., & McConnell, K. H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.r400033200 · Cited by 47

Exposure to novel environment is characterized by an interaction of D1/NMDA receptors underlined by phosphorylation of the NMDA and AMPA receptor subunits and activation of ERK1/2 signaling, leading to epigenetic changes and gene expression in rat hippocampus

Sarantis, K., Antoniou, K., Matsokis, N. A., & Angelatou, F. (2011) · Neurochemistry International · doi:10.1016/j.neuint.2011.10.018 · Cited by 46

Proteomic Interrogation of Human Chromatin

Torrente, M. P., Zee, B. M., Young, N. L., Baliban, R. C., LeRoy, G., Floudas, C. A., Hake, S. B., & Garcia, B. A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0024747 · Cited by 46

Uncovering an IL‐10‐dependent NF‐KB recruitment to the IL‐1ra promoter that is impaired in STAT3 functionally defective patients

Tamassia, N., Castellucci, M., Rossato, M., Gasperini, S., Bosisio, D., Giacomelli, M., Badolato, R., Cassatella, M. A., & Bazzoni, F. (2009) · The FASEB Journal · doi:10.1096/fj.09-145573 · Cited by 45

RSK2 and its binding partners in cell proliferation, transformation and cancer development

Cho, Y. (2016) · Archives of Pharmacal Research · doi:10.1007/s12272-016-0880-z · Cited by 46

Epigenetic dysfunctional diseases and therapy for infection and inflammation

Samanta, S., Rajasingh, S., Cao, T., Dawn, B., & Rajasingh, J. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.11.030 · Cited by 49

The stem-loop binding protein CDL-1 is required for chromosome condensation, progression of cell death and morphogenesis inCaenorhabditis elegans

Kodama, Y., Rothman, J. H., Sugimoto, A., & Yamamoto, M. P. (2002) · Development · doi:10.1242/dev.129.1.187 · Cited by 46

Control of histone H3 phosphorylation by CaMKII δ in response to haemodynamic cardiac stress

Awad, S. M., Al‐Haffar, K. M. A., Marashly, Q., Quijada, P. J., Kunhi, M., Al‐Yacoub, N., Wade, S. F., Mohammed, S. F., Al‐Dayel, F., Sutherland, G. R., et al. (2014) · The Journal of Pathology · doi:10.1002/path.4489 · Cited by 44

Overexpression of Phosphorylated Histone H3 is an Indicator of Poor Prognosis in Gastric Adenocarcinoma Patients

Takahashi, H., Murai, Y., Tsuneyama, K., Nomoto, K., Okada, E., FUJITA, H., & Takano, Y. (2006) · Applied immunohistochemistry & molecular morphology · doi:10.1097/00129039-200609000-00007 · Cited by 45

Glutamate and cortisol—a critical confluence in PTSD?

Reul, J., & Nutt, D. (2008) · Journal of Psychopharmacology · doi:10.1177/0269881108094617 · Cited by 45

Epigenetics and Chromatin Remodeling in Adult Cardiomyopathy

Awad, S. M., & Poizat, C. I. (2013) · The Journal of Pathology · doi:10.1002/path.4234 · Cited by 46

The histone deacetylase HDAC3 is essential for Purkinje cell function, potentially complicating the use of HDAC inhibitors in SCA1

Venkatraman, A., Hu, Y.-S., Didonna, A., Cvetanović, M., Krbanjevic, A., Bilesimo, P., & Opal, P. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu081 · Cited by 44

DNA methylation in the tumor microenvironment

Zhang, M., Fujiwara, K., Che, X., Zheng, S. S., & Zheng, L. (2017) · Journal of Zhejiang University SCIENCE B · doi:10.1631/jzus.b1600579 · Cited by 44

Trichostatin-A induces differential changes in histone protein dynamics and expression in HeLa cells

Rao, J. P., Bhattacharya, D., Banerjee, B., Sarin, A., & Shivashankar, G. V. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.08.120 · Cited by 45

Altering the chromatin landscape for nucleotide excision repair

Chaudhuri, R. N., & Smerdon, M. J. (2009) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2009.01.002 · Cited by 42

Mass spectrometric analysis of histone posttranslational modifications

Burlingame, A. L., Zhang, X., & Chalkley, R. J. (2005) · Methods · doi:10.1016/j.ymeth.2005.03.009 · Cited by 44

Mass spectrometry-based strategies for characterization of histones and their post-translational modifications

Su, X., Ren, C., & Freitas, M. A. (2007) · Expert Review of Proteomics · doi:10.1586/14789450.4.2.211 · Cited by 43

Regulation of Gene Expression and Pain States by Epigenetic Mechanisms

Géranton, S. M., & Tochiki, K. K. (2015) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2014.11.012 · Cited by 44

Acetylation in hormone signaling and the cell cycle

Fu, M., Wang, C., Wang, J., Zafonte, B. T., Lisanti, M. P., & Pestell, R. G. (2002) · Cytokine & Growth Factor Reviews · doi:10.1016/s1359-6101(02)00003-5 · Cited by 43

Histone acetylation: novel target for the treatment of acute lymphoblastic leukemia

Zhang, C., Zhong, J. F., Stucky, A., Chen, X., Press, M. F., & Zhang, X. (2015) · Clinical Epigenetics · doi:10.1186/s13148-015-0151-8 · Cited by 43

Dynamic regulation of six histone H3 lysine (K) methyltransferases in response to prolonged anoxia exposure in a freshwater turtle

Wijenayake, S., Hawkins, L. J., & Storey, K. B. (2018) · Gene · doi:10.1016/j.gene.2018.01.086 · Cited by 46

Quantitative Assays for Characterization of the Sir2 Family of NAD+-Dependent Deacetylases

Borra, M. T., & Denu, J. M. (2003) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(03)76011-x · Cited by 42

Linking Covalent Histone Modifications to Epigenetics: The Rigidity and Plasticity of the MarksPreprint

Wang, Y., Wysocka, J., Perlin, J. R., Leonelli, L., Allis, C. D., & Coonrod, S. A. (2004) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2004.69.161 · Cited by 44

Epigenetik – ein Epizentrum der Genregulation: Histone und histonmodifizierende Enzyme

Biel, M., Wascholowski, V., & Giannis, A. (2005) · Angewandte Chemie · doi:10.1002/ange.200461346 · Cited by 42

Epigenetic regulation of kallikrein-related peptidases: there is a whole new world out there

Pasic, M. D., Olkhov, E., Bapat, B. V., & Yousef, G. M. (2012) · Biological Chemistry · doi:10.1515/hsz-2011-0273 · Cited by 41

Drawbacks in the use of unconventional hydrophobic anhydrides for histone derivatization in bottom‐up proteomics PTM analysis

Sidoli, S., Yuan, Z., Lin, S., Karch, K. R., Wang, X., Bhanu, N. V., Arnaudo, A. M., Britton, L.-M. P., Cao, X.-J., Gonzales-Cope, M., et al. (2015) · PROTEOMICS · doi:10.1002/pmic.201400483 · Cited by 44

Quantitative proteomics reveals direct and indirect alterations in the histone code following methyltransferase knockdown

Plazas-Mayorca, M. D., Bloom, J. S., Zeißler, U., LeRoy, G., Young, N. L., DiMaggio, P. A., Krugylak, L., Schneider, R., & Garcia, B. A. (2010) · Molecular BioSystems · doi:10.1039/c003307c · Cited by 43

Discovery and synthesis of novel indole derivatives-containing 3-methylenedihydrofuran-2(3H)-one as irreversible LSD1 inhibitors

Liu, H., Suo, F., Li, X., You, Y., Lv, C.-T., Zheng, C.-X., Zhang, G., Liu, Y.-J., Kang, W.-T., Zheng, Y., et al. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.04.065 · Cited by 41

Gcn5p Plays an Important Role in Centromere Kinetochore Function in Budding Yeast

Vernarecci, S., Ornaghi, P., Bâgu, A., Cundari, E., Ballario, P., & Filetici, P. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01366-07 · Cited by 41

Actin allostery again?

Egelman, E. H. (2001) · Nature Structural Biology · doi:10.1038/nsb0901-735 · Cited by 41

Diverse modes of H3K36me3-guided nucleosomal deacetylation by Rpd3S

Guan, H., Wang, P., Zhang, P., Ruan, C., Ou, Y., Peng, B., Zheng, X., Lei, J., Li, B., Yan, C., et al. (2023) · Nature · doi:10.1038/s41586-023-06349-1 · Cited by 40

Valproic acid induces non-apoptotic cell death mechanisms in multiple myeloma cell lines

Schwartz, C., Palissot, V., Aouali, N., Wack, S., Brons, N. H. C., Leners, B., Bosseler, M., & Berchem, G. (2007) · International Journal of Oncology · doi:10.3892/ijo.30.3.573 · Cited by 40

Epigenetic modification in neurons of the mollusc Pomacea canaliculata after immune challenge

Ottaviani, E., Accorsi, A., Rigillo, G., Malagoli, D., Blom, J. M. C., & Tascedda, F. (2013) · Brain Research · doi:10.1016/j.brainres.2013.09.009 · Cited by 42

Silencing CDK4 radiosensitizes breast cancer cells by promoting apoptosis

Hagen, K. R., Zeng, X., Lee, M.-Y., Kahn, S., Pitner, M. K., Zaky, S. S., Liu, Y., O’Regan, R. M., Deng, X., & Saavedra, H. I. (2013) · Cell Division · doi:10.1186/1747-1028-8-10 · Cited by 41

Chromatin remodeling and tissue-selective responses of nuclear hormone receptors.

Hsiao, P., Deroo, B., & Archer, T. (2002) · Biochemistry and cell biology = Biochimie et biologie cellulaire · doi:10.1139/o02-082 · Cited by 42

How to keep V(D)J recombination under control

Oettinger, M. A. (2004) · Immunological Reviews · doi:10.1111/j.0105-2896.2004.00172.x · Cited by 41

Epigenetic regulation in drug addiction.

Biliński, P., Wojtyła, A., Kapka‐Skrzypczak, L., Chwedorowicz, R., Cyranka, M., & Studziński, T. (2012) · PubMed · Cited by 39

The effect of ovine oocyte vitrification on expression of subset of genes involved in epigenetic modifications during oocyte maturation and early embryo development

Shirazi, A., Naderi, M. M., Hassanpour, H., Heidari, M., Borjian-Boroujeni, S., Sarvari, A., & Akhondi, M. M. (2016) · Theriogenology · doi:10.1016/j.theriogenology.2016.07.005 · Cited by 39

Histone Deacetylase Inhibitors as Multitarget-Directed Epi-Drugs in Blocking PI3K Oncogenic Signaling: A Polypharmacology Approach

Ranganna, K., Selvam, C., Shivachar, A. C., & Yousefipour, Z. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218198 · Cited by 40

Commonalities of optic nerve injury and glaucoma-induced neurodegeneration: Insights from transcriptome-wide studies

Wang, J., Struebing, F. L., & Geisert, E. E. (2021) · Experimental Eye Research · doi:10.1016/j.exer.2021.108571 · Cited by 38

Cell Cycle-dependent Binding of HMGN Proteins to Chromatin

Cherukuri, S., Hock, R., Ueda, T., Catez, F., Rochman, M., & Bustin, M. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-10-1018 · Cited by 39

Overlapping CRE and E Box Motifs in the Enhancer Sequences of the Bovine Leukemia Virus 5′ Long Terminal Repeat Are Critical for Basal and Acetylation-Dependent Transcriptional Activity of the Viral Promoter: Implications for Viral Latency

Calomme, C., Dekoninck, A., Nizet, S., Adam, E., Nguyên, T. L.-A., den Broeke, A. V., Willems, L., Kettmann, R., Burny, A., & Lint, C. M. V. (2004) · Journal of Virology · doi:10.1128/jvi.78.24.13848-13864.2004 · Cited by 39

Distinct epigenetic and gene expression changes in rat hippocampal neurons after Morris water maze training

Carter, S. D., Mifsud, K. R., & Reul, J. M. H. M. (2015) · Frontiers in Behavioral Neuroscience · doi:10.3389/fnbeh.2015.00156 · Cited by 41

L‐type voltage‐dependent calcium channels facilitate acetylation of histone H3 through PKCγ phosphorylation in mice with methamphetamine‐induced place preference

Shibasaki, M., Mizuno, K., Kurokawa, K., & Ohkuma, S. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07387.x · Cited by 38

Single molecule and single cell epigenomics

Hyun, B., McElwee, J. L., & Soloway, P. D. (2014) · Methods · doi:10.1016/j.ymeth.2014.08.015 · Cited by 38

Pleckstrin homology domain leucine-rich repeat protein phosphatases set the amplitude of receptor tyrosine kinase output

Reyes, G. X., Niederst, M. J., Cohen‐Katsenelson, K., Stender, J. D., Kunkel, M. T., Chen, M., Brognard, J., Sierecki, E., Gao, T., Nowak, D. G., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1404221111 · Cited by 38

Histone tyrosine phosphorylation comes of age

Singh, R. K., & Gunjan, A. (2011) · Epigenetics · doi:10.4161/epi.6.2.13589 · Cited by 40

Hormesis: A promising strategy to sustain endogenous neuronal survival pathways against neurodegenerative disorders

Marini, A. M., Jiang, H., Pan, H., Wu, X., & Lipsky, R. H. (2007) · Ageing Research Reviews · doi:10.1016/j.arr.2007.07.003 · Cited by 38

The proteasome and epigenetics: zooming in on histone modifications

Bach, S. V., & Hegde, A. N. (2016) · BioMolecular Concepts · doi:10.1515/bmc-2016-0016 · Cited by 37

Chromatin-modifying enzymes as therapeutic targets – Part 2

Keppler, B. R., & Archer, T. (2008) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.12.11.1457 · Cited by 38

Recruitment of a Repressosome Complex at the Growth Hormone Receptor Promoter and Its Potential Role in Diabetic Nephropathy

Gowri, P. M., Yu, J. H., Shaufl, A. L., Sperling, M. A., & Menon, R. K. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.3.815-825.2003 · Cited by 38

Chromatin Remodeling and Circadian Control: Master Regulator CLOCK Is an EnzymePreprint

Grimaldi, B., Nakahata, Y., Sahar, S., Kaluzová, M., Gauthier, D., Pham, K. T. N., Patel, N., Hirayama, J., & Sassone‐Corsi, P. (2007) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2007.72.049 · Cited by 38

Epigenetics of Drug AddictionPreprint

Stewart, A. F., Fulton, S. L., & Maze, I. S. (2020) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a040253 · Cited by 40

Neuronal extracellular signal-regulated kinase (ERK) activity as marker and mediator of alcohol and opioid dependence

Zamora-Martinez, E. R., & Edwards, S. (2014) · Frontiers in Integrative Neuroscience · doi:10.3389/fnint.2014.00024 · Cited by 37

Post-translational modifications in neurodegeneration

Didonna, A., & Benetti, F. (2015) · AIMS Biophysics · doi:10.3934/biophy.2016.1.27 · Cited by 36

Epigenetic Changes Associated with the Expression of Amyotrophic Lateral Sclerosis (ALS) Causing Genes

Masala, A., Sanna, S., Esposito, S., Rassu, M., Galioto, M., Zinellu, A., Carru, C., Carrì, M. T., Iaccarino, C., & Crosio, C. (2018) · Neuroscience · doi:10.1016/j.neuroscience.2018.08.009 · Cited by 38

Transgenic overexpression of active HDAC4 in the heart attenuates cardiac function and exacerbates remodeling in infarcted myocardium

Zhang, L. X., Du, J., Zhao, Y., Wang, J., Zhang, S., Dubielecka, P. M., Wei, L., Zhuang, S., Qin, G., Chin, Y. E., et al. (2018) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00006.2018 · Cited by 37

Inhibition of Histone Deacetylase by Butyrate Protects Rat Liver from Ischemic Reperfusion Injury

Sun, J. L., Wu, Q., Sun, H., & Qiao, Y. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms151121069 · Cited by 37

Estrogen Mediates Phosphorylation of Histone H3 in Ovarian Follicle and Mammary Epithelial Tumor Cells via the Mitotic Kinase, Aurora B

Ruiz-Cortés, Z. T., Kimmins, S., Monaco, L., Burns, K. H., Sassone‐Corsi, P., & Murphy, B. D. (2005) · Molecular Endocrinology · doi:10.1210/me.2004-0441 · Cited by 37

Metastable Macromolecular Complexes Containing High Mobility Group Nucleosome-binding Chromosomal Proteins in HeLa Nuclei

Lim, J., Bustin, M., Ogryzko, V. V., & Postnikov, Y. V. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200404200 · Cited by 37

The role of global histone post-translational modifications during mammalian hibernation

Tessier, S. N., Luu, B. E., Smith, J. C., & Storey, K. B. (2017) · Cryobiology · doi:10.1016/j.cryobiol.2017.02.008 · Cited by 41

Phosphorylation of TOPK at Y74, Y272 by Src increases the stability of TOPK and promotes tumorigenesis of colon

Xiao, J., Duan, Q., Wang, Z., Yan, W., Sun, H., Xue, P., Fan, X., Zeng, X., Chen, J., Shao, C., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.8231 · Cited by 36

Post-translational Modifications are Required for Circadian Clock Regulation in Vertebrates

Okamoto‐Uchida, Y., Izawa, J., Nishimura, A., Hattori, A., Suzuki, N., & Hirayama, J. (2019) · Current Genomics · doi:10.2174/1389202919666191014094349 · Cited by 37

GCN5 and p300 share essential functions during early embryogenesis

Phan, H., Xu, A. W., Coco, C., Srajer, G., Wyszomierski, S. L., Evrard, Y. A., Eckner, R., & Dent, S. (2005) · Developmental Dynamics · doi:10.1002/dvdy.20445 · Cited by 36

Chromatin supraorganization and extensibility in mouse hepatocytes with development and aging

Moraes, A. D. S., Guaraldo, A. M. A., & Mello, M. L. S. (2007) · Cytometry Part A · doi:10.1002/cyto.a.20356 · Cited by 36

Data Processing Algorithms for Analysis of High Resolution MSMS Spectra of Peptides with Complex Patterns of Posttranslational Modifications

Guan, S., & Burlingame, A. L. (2009) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m900431-mcp200 · Cited by 36

Shigella flexneri type III secreted effector OspF reveals new crosstalks of proinflammatory signaling pathways during bacterial infection

Reiterer, V., Grossniklaus, L., Tschon, T., Kasper, C. A., Sorg, I., & Arrieumerlou, C. (2011) · Cellular Signalling · doi:10.1016/j.cellsig.2011.03.006 · Cited by 35

Glucose-dependent Insulinotropic Polypeptide and Glucagon-like Peptide-1 Modulate β-Cell Chromatin Structure

Kim, S., Nian, C., & McIntosh, C. H. S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809046200 · Cited by 35

Mass spectrometry analysis of dynamic post-translational modifications of TH2B during spermatogenesis

Lu, S., Xie, Y., Li, X., Luo, J., Shi, X. Q., Hong, X., Pan, Y. H., & Ma, X. (2009) · Molecular Human Reproduction · doi:10.1093/molehr/gap028 · Cited by 35

Regulation if NF-κB Transcriptional Activity

Vermeulen, L., Berghe, W. V., & Haegeman, G. (2006) · Cancer treatment and research · doi:10.1007/0-387-26283-0_4 · Cited by 35

HMGN dynamics and chromatin function

Catez, F., Lim, J., Hock, R., Postnikov, Y. V., & Bustin, M. (2003) · Biochemistry and Cell Biology · doi:10.1139/o03-040 · Cited by 35

Chromatin assembly and organization

Ridgway, P., & Almouzni, G. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.15.2711 · Cited by 35

Pin1 promotes histone H1 dephosphorylation and stabilizes its binding to chromatin

Raghuram, N., Strickfaden, H., McDonald, D., Williams, K., He, F., Mizzen, C. A., Hayes, J. J., Th'ng, J. P. H., & Hendzel, M. J. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201305159 · Cited by 34

The mechanism of stem cell differentiation into smooth muscle cells

Wang, G., Luo, Z., Xu, Q., & Xiao, Q. (2010) · Thrombosis and Haemostasis · doi:10.1160/th09-11-0794 · Cited by 35

Signalling to chromatin through post-translational modifications of HMGN

Pogna, E. A., Clayton, A. L., & Mahadevan, L. C. (2009) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2009.11.018 · Cited by 34

Epigenetic Regulation of the Molecular Clockwork

Eckel‐Mahan, K. L., & Sassone‐Corsi, P. (2013) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-396971-2.00002-6 · Cited by 35

Signal transduction from cell surface to nucleus in development and disease

Karin, M. (1992) · The FASEB Journal · doi:10.1096/fasebj.6.8.1317309 · Cited by 243

Transcriptional Regulation by Extracellular signals: Mechanisms and Specificity

Hill, C. S., & Treisman, R. (1995) · Cell · doi:10.1016/0092-8674(95)90403-4 · Cited by 1,012

Signal transduction and gene control

Karin, M. (1991) · Current Opinion in Cell Biology · doi:10.1016/0955-0674(91)90075-a · Cited by 94

Histone Phosphorylation

Lau, P. N. I., & Cheung, P. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-374145-5.00288-6 · Cited by 3

Signal transduction from the cell surface to the nucleus through the phosphorylation of transcription factors

Karin, M. (1994) · Current Opinion in Cell Biology · doi:10.1016/0955-0674(94)90035-3 · Cited by 389