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Nonenzymic acetylation of histones with acetyl phosphate and acetyl adenylate

Cite this: Biochemistry 1975, 14, 12, 2681–2685
Publication Date (Print):June 17, 1975
https://doi.org/10.1021/bi00683a018
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    Cited By

    This article is cited by 29 publications.

    1. Naixin Li and, R. F. Pratt. Inhibition of Serine β-Lactamases by Acyl Phosph(on)ates:  A New Source of Inert Acyl [and Phosphyl] Enzymes. Journal of the American Chemical Society 1998, 120 (18) , 4264-4268. https://doi.org/10.1021/ja9741537
    2. Linbin Zhou, Danny Siu-Chun Ng, Jason C. Yam, Li Jia Chen, Clement C. Tham, Chi Pui Pang, Wai Kit Chu. Post-translational modifications on the retinoblastoma protein. Journal of Biomedical Science 2022, 29 (1) https://doi.org/10.1186/s12929-022-00818-x
    3. Jürgen Lassak, Alina Sieber, Michael Hellwig. Exceptionally versatile take II: post-translational modifications of lysine and their impact on bacterial physiology. Biological Chemistry 2022, 403 (8-9) , 819-858. https://doi.org/10.1515/hsz-2021-0382
    4. David G. Christensen, Xueshu Xie, Nathan Basisty, James Byrnes, Sean McSweeney, Birgit Schilling, Alan J. Wolfe. Post-translational Protein Acetylation: An Elegant Mechanism for Bacteria to Dynamically Regulate Metabolic Functions. Frontiers in Microbiology 2019, 10 https://doi.org/10.3389/fmicb.2019.01604
    5. Miao-Miao Wang, Di You, Bang-Ce Ye. Site-specific and kinetic characterization of enzymatic and nonenzymatic protein acetylation in bacteria. Scientific Reports 2017, 7 (1) https://doi.org/10.1038/s41598-017-13897-w
    6. Jie Ren, Yu Sang, Jie Lu, Yu-Feng Yao. Protein Acetylation and Its Role in Bacterial Virulence. Trends in Microbiology 2017, 25 (9) , 768-779. https://doi.org/10.1016/j.tim.2017.04.001
    7. Sumana Venkat, Caroline Gregory, Jourdan Sturges, Qinglei Gan, Chenguang Fan. Studying the Lysine Acetylation of Malate Dehydrogenase. Journal of Molecular Biology 2017, 429 (9) , 1396-1405. https://doi.org/10.1016/j.jmb.2017.03.027
    8. Jinzi Wu, Zhen Jin, Liang-Jun Yan. Redox imbalance and mitochondrial abnormalities in the diabetic lung. Redox Biology 2017, 11 , 51-59. https://doi.org/10.1016/j.redox.2016.11.003
    9. Maria Juarez, Holger Bang, Friederike Hammar, Ulf Reimer, Bernard Dyke, Ilfita Sahbudin, Christopher D Buckley, Benjamin Fisher, Andrew Filer, Karim Raza. Identification of novel antiacetylated vimentin antibodies in patients with early inflammatory arthritis. Annals of the Rheumatic Diseases 2016, 75 (6) , 1099-1107. https://doi.org/10.1136/annrheumdis-2014-206785
    10. Xin-Xin Liu, Wei-bing Liu, Bang-Ce Ye, . Regulation of a Protein Acetyltransferase in Myxococcus xanthus by the Coenzyme NADP +. Journal of Bacteriology 2016, 198 (4) , 623-632. https://doi.org/10.1128/JB.00661-15
    11. Xiaoting Luo, Jinzi Wu, Siqun Jing, Liang-Jun Yan. Hyperglycemic Stress and Carbon Stress in Diabetic Glucotoxicity. Aging and disease 2016, 7 (1) , 90. https://doi.org/10.14336/AD.2015.0702
    12. Hong Zheng, Jinzi Wu, Zhen Jin, Liang-Jun Yan. Protein Modifications as Manifestations of Hyperglycemic Glucotoxicity in Diabetes and Its Complications. Biochemistry Insights 2016, 9 , BCI.S36141. https://doi.org/10.4137/BCI.S36141
    13. Vicente Bernal, Sara Castaño-Cerezo, Julia Gallego-Jara, Ana Écija-Conesa, Teresa de Diego, José Luis Iborra, Manuel Cánovas. Regulation of bacterial physiology by lysine acetylation of proteins. New Biotechnology 2014, 31 (6) , 586-595. https://doi.org/10.1016/j.nbt.2014.03.002
    14. Sara Castaño‐Cerezo, Vicente Bernal, Harm Post, Tobias Fuhrer, Salvatore Cappadona, Nerea C Sánchez‐Díaz, Uwe Sauer, Albert JR Heck, AF Maarten Altelaar, Manuel Cánovas. Protein acetylation affects acetate metabolism, motility and acid stress response in Escherichia coli. Molecular Systems Biology 2014, 10 (11) https://doi.org/10.15252/msb.20145227
    15. Misty L. Kuhn, Bozena Zemaitaitis, Linda I. Hu, Alexandria Sahu, Dylan Sorensen, George Minasov, Bruno P. Lima, Michael Scholle, Milan Mrksich, Wayne F. Anderson, Bradford W. Gibson, Birgit Schilling, Alan J. Wolfe, . Structural, Kinetic and Proteomic Characterization of Acetyl Phosphate-Dependent Bacterial Protein Acetylation. PLoS ONE 2014, 9 (4) , e94816. https://doi.org/10.1371/journal.pone.0094816
    16. Byoung-Joon Song, Mohammed Akbar, Mohamed A. Abdelmegeed, Kyunghee Byun, Bonghee Lee, Seung Kew Yoon, James P. Hardwick. Mitochondrial dysfunction and tissue injury by alcohol, high fat, nonalcoholic substances and pathological conditions through post-translational protein modifications. Redox Biology 2014, 3 , 109-123. https://doi.org/10.1016/j.redox.2014.10.004
    17. Casey Cook, Jeannette N Stankowski, Yari Carlomagno, Caroline Stetler, Leonard Petrucelli. Acetylation: a new key to unlock tau’s role in neurodegeneration. Alzheimer's Research & Therapy 2014, 6 (3) , 29. https://doi.org/10.1186/alzrt259
    18. Katrina Owens, Ji H. Park, Rosemary Schuh, Tibor Kristian. Mitochondrial Dysfunction and NAD+ Metabolism Alterations in the Pathophysiology of Acute Brain Injury. Translational Stroke Research 2013, 4 (6) , 618-634. https://doi.org/10.1007/s12975-013-0278-x
    19. Brian T. Weinert, Vytautas Iesmantavicius, Sebastian A. Wagner, Christian Schölz, Bertil Gummesson, Petra Beli, Thomas Nyström, Chunaram Choudhary. Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Molecular Cell 2013, 51 (2) , 265-272. https://doi.org/10.1016/j.molcel.2013.06.003
    20. Jing-Yi Huang, Matthew D. Hirschey, Tadahiro Shimazu, Linh Ho, Eric Verdin. Mitochondrial sirtuins. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 2010, 1804 (8) , 1645-1651. https://doi.org/10.1016/j.bbapap.2009.12.021
    21. Paolo Paoli, Francesca Sbrana, Bruno Tiribilli, Anna Caselli, Barbara Pantera, Paolo Cirri, Alina De Donatis, Lucia Formigli, Daniele Nosi, Giampaolo Manao, Guido Camici, Giampietro Ramponi. Protein N-Homocysteinylation Induces the Formation of Toxic Amyloid-Like Protofibrils. Journal of Molecular Biology 2010, 400 (4) , 889-907. https://doi.org/10.1016/j.jmb.2010.05.039
    22. W.A. Krajewski, A.N. Luchnik. Relationship of histone acetylation to DNA topology and transcription. Molecular and General Genetics MGG 1991, 230 (3) , 442-448. https://doi.org/10.1007/BF00280301
    23. W. A. Krajewski, A. N. Luchnik. High rotational mobility of DNA in animal cells and its modulation by histone acetylation. Molecular and General Genetics MGG 1991, 231 (1) , 17-21. https://doi.org/10.1007/BF00293816
    24. Vincent G. Allfrey, Eugene A. Di Paola, Richard Sterner. Protein side-chain acetylations. 1984, 224-240. https://doi.org/10.1016/0076-6879(84)07014-2
    25. Donald M. Kirschenbaum. Nonenzymic protein modification: A general phenomenon?. Medical Hypotheses 1982, 8 (5) , 491-493. https://doi.org/10.1016/0306-9877(82)90010-X
    26. Bennett N. COHEN, William T. BLUE, Thomas E. WAGNER. Chemically Induced Gene Expression. European Journal of Biochemistry 1980, 107 (2) , 511-518. https://doi.org/10.1111/j.1432-1033.1980.tb06058.x
    27. C.Kimball Shewmaker, Bennett N. Cohen, Thomas E. Wagner. Chemically induced gene activation: Selective increase in DNAase I susceptibility in chromatin acetylated with acetyl adenylate. Biochemical and Biophysical Research Communications 1978, 84 (2) , 342-349. https://doi.org/10.1016/0006-291X(78)90176-6
    28. B.K. Shashiprabha, S.K. Podder. Mode of action of antitumour antibiotics-III: Modulation of permeability of nuclear membrane in the presence of the antibiotics. Biochemical and Biophysical Research Communications 1978, 83 (3) , 933-940. https://doi.org/10.1016/0006-291X(78)91485-7
    29. Woon Ki Paik, Hyang Woo Lee, Sangduk Kim. Non‐enzymatic methylation of proteins with S‐adenosyl‐L‐methionine. FEBS Letters 1975, 58 (1-2) , 39-42. https://doi.org/10.1016/0014-5793(75)80220-1

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