Ацетилювання (Ukrainian Wikipedia)

Analysis of information sources in references of the Wikipedia article "Ацетилювання" in Ukrainian language version.

refsWebsite

Global rank Ukrainian rank

71nih.gov

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43doi.org

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13harvard.edu

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9archive.org

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1web.archive.org

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1caymanchem.com

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1worldcat.org

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archive.org

Arnesen T, Starheim KK, Van Damme P, Evjenth R, Dinh H, Betts MJ, Ryningen A, Vandekerckhove J, Gevaert K, Anderson D (2010). The chaperone-like protein HYPK acts together with NatA in cotranslational N-terminal acetylation and prevention of Huntingtin aggregation. Mol. Cell. Biol. 30 (8): 1898—1909. doi:10.1128/mcb.01199-09. PMC 2849469. PMID 20154145.
Gautschi M, Just S, Mun A, Ross S, Rücknagel P, Dubaquié Y, Ehrenhofer-Murray A, Rospert S (2003). The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides. Mol. Cell. Biol. 23 (20): 7403—7414. doi:10.1128/mcb.23.20.7403-7414.2003. PMC 230319. PMID 14517307.
Starheim KK, Gromyko D, Evjenth R, Ryningen A, Varhaug JE, Lillehaug JR, Arnesen T (2009). Knockdown of human N alpha-terminal acetyltransferase complex C leads to p53-dependent apoptosis and aberrant human Arl8b localization. Mol. Cell. Biol. 29 (13): 3569—3581. doi:10.1128/mcb.01909-08. PMC 2698767. PMID 19398576.
Eddé B, Denoulet P, de Néchaud B, Koulakoff A, Berwald-Netter Y, Gros F (1989). Posttranslational modifications of tubulin in cultured mouse brain neurons and astroglia. Biol. Cell. 65 (2): 109—117. doi:10.1016/0248-4900(89)90018-x. PMID 2736326. {{cite journal}}: |first3= з пропущеним |last3= (довідка)
Maruta H, Greer K, Rosenbaum JL (1986). The acetylation of alpha-tubulin and its relationship to the assembly and disassembly of microtubules. J. Cell Biol. 103 (2): 571—579. doi:10.1083/jcb.103.2.571. PMC 2113826. PMID 3733880.
Alberts, Bruce (March 2002). Molecular Biology of the Cell. Garland Science. ISBN 0815332181.
Kreis, ed. by Thomas; Vale, Ronald (1999). Guidebook to the cytoskeletal and motor proteins (вид. 2.). Oxford [u.a.]: Oxford Univ. Press. ISBN 0198599560.
Fojo, edited by Tito (2008). The role of microtubules in cell biology, neurobiology, and oncology (вид. [Online-Ausg.]). Totowa, N. J.: Humana Press. ISBN 978-1588292940.
Müller-Decker, Friedrich Marks, Ursula Klingmüller, Karin (2009). Cellular signal processing : an introduction to the molecular mechanisms of signal transduction. New York: Garland Science. ISBN 978-0815342151.

caymanchem.com

Brook, Tom. Protein Acetylation: Much More than Histone Acetylation. Cayman Chemical. Архів оригіналу за 28 лютого 2014.

doi.org

Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M (2009). Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 325 (5942): 834—840. Bibcode:2009Sci...325..834C. doi:10.1126/science.1175371. PMID 19608861.
Fritz KS, Galligan JJ, Hirschey MD, Verdin E, Petersen DR (2012). Mitochondrial acetylome analysis in a mouse model of alcohol-induced liver injury utilizing SIRT3 knockout mice. J. Proteome Res. 11 (3): 1633—1643. doi:10.1021/pr2008384. PMC 3324946. PMID 22309199.
Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL (2010). Regulation of cellular metabolism by protein lysine acetylation. Science. 327 (5968): 1000—1004. Bibcode:2010Sci...327.1000Z. doi:10.1126/science.1179689. PMC 3232675. PMID 20167786. {{cite journal}}: |first3= з пропущеним |last3= (довідка)
Wang, Qijun; Zhang, Yakun; Yang, Chen; Xiong, Hui; Lin, Yan; Yao, Jun; Li, Hong; Xie, Lu; Zhao, Wei (19 лютого 2010). Acetylation of Metabolic Enzymes Coordinates Carbon Source Utilization and Metabolic Flux. Science (англ.). 327 (5968): 1004—1007. Bibcode:2010Sci...327.1004W. doi:10.1126/science.1179687. ISSN 0036-8075. PMC 4183141. PMID 20167787.
Van Damme P, Hole K, Pimenta-Marques A, Helsens K, Vandekerckhove J, Martinho RG, Gevaert K, Arnesen T (2011). NatF contributes to an evolutionary shift in protein N-terminal acetylation and is important for normal chromosome segregation. PLoS Genet. 7 (7): e1002169. doi:10.1371/journal.pgen.1002169. PMC 3131286. PMID 21750686.{{cite journal}}: Обслуговування CS1: Сторінки із непозначеним DOI з безкоштовним доступом (посилання)
Starheim KK, Gevaert K, Arnesen T (2012). Protein N-terminal acetyltransferases: when the start matters. Trends Biochem. Sci. 37 (4): 152—161. doi:10.1016/j.tibs.2012.02.003. PMID 22405572.
Liszczak G, Goldberg JM, Foyn H, Petersson EJ, Arnesen T, Marmorstein R (2013). Molecular basis for N-terminal acetylation by the heterodimeric NatA complex. Nat. Struct. Mol. Biol. 20 (9): 1098—105. doi:10.1038/nsmb.2636. PMC 3766382. PMID 23912279.
Starheim KK, Gromyko D, Velde R, Varhaug JE, Arnesen T (2009). Composition and biological significance of the human Nalpha-terminal acetyltransferases. BMC Proceedings. 3 Suppl 6 (Suppl 6): S3. doi:10.1186/1753-6561-3-s6-s3. PMC 2722096. PMID 19660096.{{cite journal}}: Обслуговування CS1: Сторінки із непозначеним DOI з безкоштовним доступом (посилання)
Arnesen T, Van Damme P, Polevoda B, Helsens K, Evjenth R, Colaert N, Varhaug JE, Vandekerckhove J, Lillehaug JR, Sherman F, Gevaert K (2009). Proteomics analyses reveal the evolutionary conservation and divergence of N-terminal acetyltransferases from yeast and humans. Proc. Natl. Acad. Sci. U.S.A. 106 (20): 8157—8162. Bibcode:2009PNAS..106.8157A. doi:10.1073/pnas.0901931106. PMC 2688859. PMID 19420222. {{cite journal}}: |first3= з пропущеним |last3= (довідка)
Arnesen T, Starheim KK, Van Damme P, Evjenth R, Dinh H, Betts MJ, Ryningen A, Vandekerckhove J, Gevaert K, Anderson D (2010). The chaperone-like protein HYPK acts together with NatA in cotranslational N-terminal acetylation and prevention of Huntingtin aggregation. Mol. Cell. Biol. 30 (8): 1898—1909. doi:10.1128/mcb.01199-09. PMC 2849469. PMID 20154145.
Hole K, Van Damme P, Dalva M, Aksnes H, Glomnes N, Varhaug JE, Lillehaug JR, Gevaert K, Arnesen T (2011). The human N-alpha-acetyltransferase 40 (hNaa40p/hNatD) is conserved from yeast and N-terminally acetylates histones H2A and H4. PLoS ONE. 6 (9): e24713. Bibcode:2011PLoSO...624713H. doi:10.1371/journal.pone.0024713. PMC 3174195. PMID 21935442.{{cite journal}}: Обслуговування CS1: Сторінки із непозначеним DOI з безкоштовним доступом (посилання)
Gautschi M, Just S, Mun A, Ross S, Rücknagel P, Dubaquié Y, Ehrenhofer-Murray A, Rospert S (2003). The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides. Mol. Cell. Biol. 23 (20): 7403—7414. doi:10.1128/mcb.23.20.7403-7414.2003. PMC 230319. PMID 14517307.
Van Damme P, Hole K, Pimenta-Marques A та ін. (July 2011). NatF contributes to an evolutionary shift in protein N-terminal acetylation and is important for normal chromosome segregation. PLoS Genet. 7: e1002169. doi:10.1371/journal.pgen.1002169. PMC 3131286. PMID 21750686.{{cite journal}}: Обслуговування CS1: Сторінки із непозначеним DOI з безкоштовним доступом (посилання)
Rathore, Om Singh; Faustino, Alexandra; Prudêncio, Pedro; Van Damme, Petra; Cox, Cymon J.; Martinho, Rui Gonçalo (2016). Absence of N-terminal acetyltransferase diversification during evolution of eukaryotic organisms. Scientific Reports. 6: 21304. Bibcode:2016NatSR...621304R. doi:10.1038/srep21304. PMC 4748286. PMID 26861501.
Aksnes (3 березня 2015). An Organellar Nα-Acetyltransferase, Naa60, Acetylates Cytosolic N Termini of Transmembrane Proteins and Maintains Golgi Integrity. Cell Reports. 10 (8): 1362—74. doi:10.1016/j.celrep.2015.01.053. PMID 25732826.
Aksnes, Henriette; Goris, Marianne; Strømland, Øyvind; Drazic, Adrian; Waheed, Qaiser; Reuter, Nathalie; Arnesen, Thomas (2017). Molecular determinants of the N-terminal acetyltransferase Naa60 anchoring to the Golgi membrane. Journal of Biological Chemistry. 292 (16): 6821—6837. doi:10.1074/jbc.M116.770362. PMC 5399128. PMID 28196861.{{cite journal}}: Обслуговування CS1: Сторінки із непозначеним DOI з безкоштовним доступом (посилання)
Drazic A, Aksnes H, Marie M, Boczkowska M, Varland S, Timmerman E, Foyn H, Glomnes N, Rebowski G, Impens F, Gevaert K, Dominguez R, and Arnesen T (2018). NAA80 is actin's N-terminal acetyltransferase and regulates cytoskeleton assembly and cell motility. Proc Natl Acad Sci U S A. 115 (17): 4399—4404. doi:10.1073/pnas.1718336115. PMC 5924898. PMID 29581253.
Hollebeke J, Van Damme P, Gevaert K (2012). N-terminal acetylation and other functions of Nα-acetyltransferases. Biol. Chem. 393 (4): 291—8. doi:10.1515/hsz-2011-0228. PMID 22718636.
Hershko A, Heller H, Eytan E, Kaklij G, Rose IA (1984). Role of the alpha-amino group of protein in ubiquitin-mediated protein breakdown. Proc. Natl. Acad. Sci. U.S.A. 81 (22): 7021—5. Bibcode:1984PNAS...81.7021H. doi:10.1073/pnas.81.22.7021. PMC 392068. PMID 6095265.
Hwang CS, Shemorry A, Varshavsky A (2010). N-terminal acetylation of cellular proteins creates specific degradation signals. Science. 327 (5968): 973—977. Bibcode:2010Sci...327..973H. doi:10.1126/science.1183147. PMC 4259118. PMID 20110468.
Behnia R, Panic B, Whyte JR, Munro S (2004). Targeting of the Arf-like GTPase Arl3p to the Golgi requires N-terminal acetylation and the membrane protein Sys1p. Nat. Cell Biol. 6 (5): 405—413. doi:10.1038/ncb1120. PMID 15077113.
Starheim KK, Gromyko D, Evjenth R, Ryningen A, Varhaug JE, Lillehaug JR, Arnesen T (2009). Knockdown of human N alpha-terminal acetyltransferase complex C leads to p53-dependent apoptosis and aberrant human Arl8b localization. Mol. Cell. Biol. 29 (13): 3569—3581. doi:10.1128/mcb.01909-08. PMC 2698767. PMID 19398576.
Gromyko D, Arnesen T, Ryningen A, Varhaug JE, Lillehaug JR (2010). Depletion of the human Nα-terminal acetyltransferase A induces p53-dependent apoptosis and p53-independent growth inhibition. Int. J. Cancer. 127 (12): 2777—2789. doi:10.1002/ijc.25275. PMID 21351257.
Yi CH, Pan H, Seebacher J, Jang IH, Hyberts SG, Heffron GJ, Vander Heiden MG, Yang R, Li F, Locasale JW, Sharfi H, Zhai B, Rodriguez-Mias R, Luithardt H, Cantley LC, Daley GQ, Asara JM, Gygi SP, Wagner G, Liu CF, Yuan J (2011). Metabolic regulation of protein N-alpha-acetylation by Bcl-xL promotes cell survival. Cell. 146 (4): 607—620. doi:10.1016/j.cell.2011.06.050. PMC 3182480. PMID 21854985.
Kamita M, Kimura Y, Ino Y, Kamp RM, Polevoda B, Sherman F, Hirano H (2011). N(α)-Acetylation of yeast ribosomal proteins and its effect on protein synthesis. J Proteomics. 74 (4): 431—441. doi:10.1016/j.jprot.2010.12.007. PMID 21184851.
Yu M, Gong J, Ma M, Yang H, Lai J, Wu H, Li L, Li L, Tan D (2009). Immunohistochemical analysis of human arrest-defective-1 expressed in cancers in vivo. Oncol. Rep. 21 (4): 909—15. doi:10.3892/or_00000303. PMID 19287988.
Kalvik TV, Arnesen T (2013). Protein N-terminal acetyltransferases in cancer. Oncogene. 32 (3): 269—276. doi:10.1038/onc.2012.82. PMID 22391571.
Sadoul K, Boyault C, Pabion M, Khochbin S (2008). Regulation of protein turnover by acetyltransferases and deacetylases. Biochimie. 90 (2): 306—12. doi:10.1016/j.biochi.2007.06.009. PMID 17681659.
Glozak MA, Sengupta N, Zhang X, Seto E (2005). Acetylation and deacetylation of non-histone proteins. Gene. 363: 15—23. doi:10.1016/j.gene.2005.09.010. PMID 16289629.
Yang XJ, Seto E (2008). Lysine acetylation: codified crosstalk with other posttranslational modifications. Mol. Cell. 31 (4): 449—61. doi:10.1016/j.molcel.2008.07.002. PMC 2551738. PMID 18722172.
Eddé B, Denoulet P, de Néchaud B, Koulakoff A, Berwald-Netter Y, Gros F (1989). Posttranslational modifications of tubulin in cultured mouse brain neurons and astroglia. Biol. Cell. 65 (2): 109—117. doi:10.1016/0248-4900(89)90018-x. PMID 2736326. {{cite journal}}: |first3= з пропущеним |last3= (довідка)
Maruta H, Greer K, Rosenbaum JL (1986). The acetylation of alpha-tubulin and its relationship to the assembly and disassembly of microtubules. J. Cell Biol. 103 (2): 571—579. doi:10.1083/jcb.103.2.571. PMC 2113826. PMID 3733880.
Brooks CL, Gu W (2011). The impact of acetylation and deacetylation on the p53 pathway. Protein Cell. 2 (6): 456—462. doi:10.1007/s13238-011-1063-9. PMC 3690542. PMID 21748595.
Tang Y, Zhao W, Chen Y, Zhao Y, Gu W (2008). Acetylation is indispensable for p53 activation. Cell. 133 (4): 612—626. doi:10.1016/j.cell.2008.03.025. PMC 2914560. PMID 18485870.
Yamaguchi H, Woods NT, Piluso LG, Lee HH, Chen J, Bhalla KN, Monteiro A, Liu X, Hung MC, Wang HG (2009). p53 acetylation is crucial for its transcription-independent proapoptotic functions. J. Biol. Chem. 284 (17): 11171—11183. doi:10.1074/jbc.M809268200. PMC 2670122. PMID 19265193.{{cite journal}}: Обслуговування CS1: Сторінки із непозначеним DOI з безкоштовним доступом (посилання)
Vassilev LT, Vu BT, Graves B, Carvajal D, Podlaski F, Filipovic Z, Kong N, Kammlott U, Lukacs C, Klein C, Fotouhi N, Liu EA (2004). In vivo activation of the p53 pathway by small-molecule antagonists of MDM2. Science. 303 (5659): 844—848. Bibcode:2004Sci...303..844V. doi:10.1126/science.1092472. PMID 14704432.
Shangary S, Wang S (2009). Small-molecule inhibitors of the MDM2-p53 protein-protein interaction to reactivate p53 function: a novel approach for cancer therapy. Annu. Rev. Pharmacol. Toxicol. 49 (1): 223—241. doi:10.1146/annurev.pharmtox.48.113006.094723. PMC 2676449. PMID 18834305.
Zajkowicz A, Krześniak M, Matuszczyk I, Głowala-Kosińska M, Butkiewicz D, Rusin M (2013). Nutlin-3a, an MDM2 antagonist and p53 activator, helps to preserve the replicative potential of cancer cells treated with a genotoxic dose of resveratrol. Mol. Biol. Rep. 40 (8): 5013—5026. doi:10.1007/s11033-013-2602-7. PMC 3723979. PMID 23666059.
Kumamoto K, Spillare EA, Fujita K, Horikawa I, Yamashita T, Appella E, Nagashima M, Takenoshita S, Yokota J, Harris CC (2008). Nutlin-3a activates p53 to both down-regulate inhibitor of growth 2 and up-regulate mir-34a, mir-34b, and mir-34c expression, and induce senescence. Cancer Res. 68 (9): 3193—3203. doi:10.1158/0008-5472.CAN-07-2780. PMC 2440635. PMID 18451145.
Friedmann DR, Aguilar A, Fan J, Nachury MV, Marmorstein R (2012). Structure of the α-tubulin acetyltransferase, αTAT1, and implications for tubulin-specific acetylation. Proc. Natl. Acad. Sci. U.S.A. 109 (48): 19655—19660. Bibcode:2012PNAS..10919655F. doi:10.1073/pnas.1209357109. PMC 3511727. PMID 23071314.
Hubbert C, Guardiola A, Shao R, Kawaguchi Y, Ito A, Nixon A, Yoshida M, Wang XF, Yao TP (2002). HDAC6 is a microtubule-associated deacetylase. Nature. 417 (6887): 455—458. Bibcode:2002Natur.417..455H. doi:10.1038/417455a. PMID 12024216.
Yuan ZL, Guan YJ, Chatterjee D, Chin YE (2005). Stat3 dimerization regulated by reversible acetylation of a single lysine residue. Science. 307 (5707): 269—273. Bibcode:2005Sci...307..269Y. doi:10.1126/science.1105166. PMID 15653507.
Lee H, Zhang P, Herrmann A, Yang C, Xin H, Wang Z, Hoon DS, Forman SJ, Jove R, Riggs AD, Yu H (2012). Acetylated STAT3 is crucial for methylation of tumor-suppressor gene promoters and inhibition by resveratrol results in demethylation. Proc. Natl. Acad. Sci. U.S.A. 109 (20): 7765—7769. Bibcode:2012PNAS..109.7765L. doi:10.1073/pnas.1205132109. PMC 3356652. PMID 22547799.

harvard.edu

ui.adsabs.harvard.edu

Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M (2009). Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 325 (5942): 834—840. Bibcode:2009Sci...325..834C. doi:10.1126/science.1175371. PMID 19608861.
Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL (2010). Regulation of cellular metabolism by protein lysine acetylation. Science. 327 (5968): 1000—1004. Bibcode:2010Sci...327.1000Z. doi:10.1126/science.1179689. PMC 3232675. PMID 20167786. {{cite journal}}: |first3= з пропущеним |last3= (довідка)
Wang, Qijun; Zhang, Yakun; Yang, Chen; Xiong, Hui; Lin, Yan; Yao, Jun; Li, Hong; Xie, Lu; Zhao, Wei (19 лютого 2010). Acetylation of Metabolic Enzymes Coordinates Carbon Source Utilization and Metabolic Flux. Science (англ.). 327 (5968): 1004—1007. Bibcode:2010Sci...327.1004W. doi:10.1126/science.1179687. ISSN 0036-8075. PMC 4183141. PMID 20167787.
Arnesen T, Van Damme P, Polevoda B, Helsens K, Evjenth R, Colaert N, Varhaug JE, Vandekerckhove J, Lillehaug JR, Sherman F, Gevaert K (2009). Proteomics analyses reveal the evolutionary conservation and divergence of N-terminal acetyltransferases from yeast and humans. Proc. Natl. Acad. Sci. U.S.A. 106 (20): 8157—8162. Bibcode:2009PNAS..106.8157A. doi:10.1073/pnas.0901931106. PMC 2688859. PMID 19420222. {{cite journal}}: |first3= з пропущеним |last3= (довідка)
Hole K, Van Damme P, Dalva M, Aksnes H, Glomnes N, Varhaug JE, Lillehaug JR, Gevaert K, Arnesen T (2011). The human N-alpha-acetyltransferase 40 (hNaa40p/hNatD) is conserved from yeast and N-terminally acetylates histones H2A and H4. PLoS ONE. 6 (9): e24713. Bibcode:2011PLoSO...624713H. doi:10.1371/journal.pone.0024713. PMC 3174195. PMID 21935442.{{cite journal}}: Обслуговування CS1: Сторінки із непозначеним DOI з безкоштовним доступом (посилання)
Rathore, Om Singh; Faustino, Alexandra; Prudêncio, Pedro; Van Damme, Petra; Cox, Cymon J.; Martinho, Rui Gonçalo (2016). Absence of N-terminal acetyltransferase diversification during evolution of eukaryotic organisms. Scientific Reports. 6: 21304. Bibcode:2016NatSR...621304R. doi:10.1038/srep21304. PMC 4748286. PMID 26861501.
Hershko A, Heller H, Eytan E, Kaklij G, Rose IA (1984). Role of the alpha-amino group of protein in ubiquitin-mediated protein breakdown. Proc. Natl. Acad. Sci. U.S.A. 81 (22): 7021—5. Bibcode:1984PNAS...81.7021H. doi:10.1073/pnas.81.22.7021. PMC 392068. PMID 6095265.
Hwang CS, Shemorry A, Varshavsky A (2010). N-terminal acetylation of cellular proteins creates specific degradation signals. Science. 327 (5968): 973—977. Bibcode:2010Sci...327..973H. doi:10.1126/science.1183147. PMC 4259118. PMID 20110468.
Vassilev LT, Vu BT, Graves B, Carvajal D, Podlaski F, Filipovic Z, Kong N, Kammlott U, Lukacs C, Klein C, Fotouhi N, Liu EA (2004). In vivo activation of the p53 pathway by small-molecule antagonists of MDM2. Science. 303 (5659): 844—848. Bibcode:2004Sci...303..844V. doi:10.1126/science.1092472. PMID 14704432.
Friedmann DR, Aguilar A, Fan J, Nachury MV, Marmorstein R (2012). Structure of the α-tubulin acetyltransferase, αTAT1, and implications for tubulin-specific acetylation. Proc. Natl. Acad. Sci. U.S.A. 109 (48): 19655—19660. Bibcode:2012PNAS..10919655F. doi:10.1073/pnas.1209357109. PMC 3511727. PMID 23071314.
Hubbert C, Guardiola A, Shao R, Kawaguchi Y, Ito A, Nixon A, Yoshida M, Wang XF, Yao TP (2002). HDAC6 is a microtubule-associated deacetylase. Nature. 417 (6887): 455—458. Bibcode:2002Natur.417..455H. doi:10.1038/417455a. PMID 12024216.
Yuan ZL, Guan YJ, Chatterjee D, Chin YE (2005). Stat3 dimerization regulated by reversible acetylation of a single lysine residue. Science. 307 (5707): 269—273. Bibcode:2005Sci...307..269Y. doi:10.1126/science.1105166. PMID 15653507.
Lee H, Zhang P, Herrmann A, Yang C, Xin H, Wang Z, Hoon DS, Forman SJ, Jove R, Riggs AD, Yu H (2012). Acetylated STAT3 is crucial for methylation of tumor-suppressor gene promoters and inhibition by resveratrol results in demethylation. Proc. Natl. Acad. Sci. U.S.A. 109 (20): 7765—7769. Bibcode:2012PNAS..109.7765L. doi:10.1073/pnas.1205132109. PMC 3356652. PMID 22547799.

nih.gov

pubmed.ncbi.nlm.nih.gov

Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M (2009). Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 325 (5942): 834—840. Bibcode:2009Sci...325..834C. doi:10.1126/science.1175371. PMID 19608861.
Fritz KS, Galligan JJ, Hirschey MD, Verdin E, Petersen DR (2012). Mitochondrial acetylome analysis in a mouse model of alcohol-induced liver injury utilizing SIRT3 knockout mice. J. Proteome Res. 11 (3): 1633—1643. doi:10.1021/pr2008384. PMC 3324946. PMID 22309199.
Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL (2010). Regulation of cellular metabolism by protein lysine acetylation. Science. 327 (5968): 1000—1004. Bibcode:2010Sci...327.1000Z. doi:10.1126/science.1179689. PMC 3232675. PMID 20167786. {{cite journal}}: |first3= з пропущеним |last3= (довідка)
Wang, Qijun; Zhang, Yakun; Yang, Chen; Xiong, Hui; Lin, Yan; Yao, Jun; Li, Hong; Xie, Lu; Zhao, Wei (19 лютого 2010). Acetylation of Metabolic Enzymes Coordinates Carbon Source Utilization and Metabolic Flux. Science (англ.). 327 (5968): 1004—1007. Bibcode:2010Sci...327.1004W. doi:10.1126/science.1179687. ISSN 0036-8075. PMC 4183141. PMID 20167787.
Van Damme P, Hole K, Pimenta-Marques A, Helsens K, Vandekerckhove J, Martinho RG, Gevaert K, Arnesen T (2011). NatF contributes to an evolutionary shift in protein N-terminal acetylation and is important for normal chromosome segregation. PLoS Genet. 7 (7): e1002169. doi:10.1371/journal.pgen.1002169. PMC 3131286. PMID 21750686.{{cite journal}}: Обслуговування CS1: Сторінки із непозначеним DOI з безкоштовним доступом (посилання)
Starheim KK, Gevaert K, Arnesen T (2012). Protein N-terminal acetyltransferases: when the start matters. Trends Biochem. Sci. 37 (4): 152—161. doi:10.1016/j.tibs.2012.02.003. PMID 22405572.
Liszczak G, Goldberg JM, Foyn H, Petersson EJ, Arnesen T, Marmorstein R (2013). Molecular basis for N-terminal acetylation by the heterodimeric NatA complex. Nat. Struct. Mol. Biol. 20 (9): 1098—105. doi:10.1038/nsmb.2636. PMC 3766382. PMID 23912279.
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Rathore, Om Singh; Faustino, Alexandra; Prudêncio, Pedro; Van Damme, Petra; Cox, Cymon J.; Martinho, Rui Gonçalo (2016). Absence of N-terminal acetyltransferase diversification during evolution of eukaryotic organisms. Scientific Reports. 6: 21304. Bibcode:2016NatSR...621304R. doi:10.1038/srep21304. PMC 4748286. PMID 26861501.
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ncbi.nlm.nih.gov

Fritz KS, Galligan JJ, Hirschey MD, Verdin E, Petersen DR (2012). Mitochondrial acetylome analysis in a mouse model of alcohol-induced liver injury utilizing SIRT3 knockout mice. J. Proteome Res. 11 (3): 1633—1643. doi:10.1021/pr2008384. PMC 3324946. PMID 22309199.
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Van Damme P, Hole K, Pimenta-Marques A, Helsens K, Vandekerckhove J, Martinho RG, Gevaert K, Arnesen T (2011). NatF contributes to an evolutionary shift in protein N-terminal acetylation and is important for normal chromosome segregation. PLoS Genet. 7 (7): e1002169. doi:10.1371/journal.pgen.1002169. PMC 3131286. PMID 21750686.{{cite journal}}: Обслуговування CS1: Сторінки із непозначеним DOI з безкоштовним доступом (посилання)
Liszczak G, Goldberg JM, Foyn H, Petersson EJ, Arnesen T, Marmorstein R (2013). Molecular basis for N-terminal acetylation by the heterodimeric NatA complex. Nat. Struct. Mol. Biol. 20 (9): 1098—105. doi:10.1038/nsmb.2636. PMC 3766382. PMID 23912279.
Starheim KK, Gromyko D, Velde R, Varhaug JE, Arnesen T (2009). Composition and biological significance of the human Nalpha-terminal acetyltransferases. BMC Proceedings. 3 Suppl 6 (Suppl 6): S3. doi:10.1186/1753-6561-3-s6-s3. PMC 2722096. PMID 19660096.{{cite journal}}: Обслуговування CS1: Сторінки із непозначеним DOI з безкоштовним доступом (посилання)
Arnesen T, Van Damme P, Polevoda B, Helsens K, Evjenth R, Colaert N, Varhaug JE, Vandekerckhove J, Lillehaug JR, Sherman F, Gevaert K (2009). Proteomics analyses reveal the evolutionary conservation and divergence of N-terminal acetyltransferases from yeast and humans. Proc. Natl. Acad. Sci. U.S.A. 106 (20): 8157—8162. Bibcode:2009PNAS..106.8157A. doi:10.1073/pnas.0901931106. PMC 2688859. PMID 19420222. {{cite journal}}: |first3= з пропущеним |last3= (довідка)
Arnesen T, Starheim KK, Van Damme P, Evjenth R, Dinh H, Betts MJ, Ryningen A, Vandekerckhove J, Gevaert K, Anderson D (2010). The chaperone-like protein HYPK acts together with NatA in cotranslational N-terminal acetylation and prevention of Huntingtin aggregation. Mol. Cell. Biol. 30 (8): 1898—1909. doi:10.1128/mcb.01199-09. PMC 2849469. PMID 20154145.
Hole K, Van Damme P, Dalva M, Aksnes H, Glomnes N, Varhaug JE, Lillehaug JR, Gevaert K, Arnesen T (2011). The human N-alpha-acetyltransferase 40 (hNaa40p/hNatD) is conserved from yeast and N-terminally acetylates histones H2A and H4. PLoS ONE. 6 (9): e24713. Bibcode:2011PLoSO...624713H. doi:10.1371/journal.pone.0024713. PMC 3174195. PMID 21935442.{{cite journal}}: Обслуговування CS1: Сторінки із непозначеним DOI з безкоштовним доступом (посилання)
Gautschi M, Just S, Mun A, Ross S, Rücknagel P, Dubaquié Y, Ehrenhofer-Murray A, Rospert S (2003). The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides. Mol. Cell. Biol. 23 (20): 7403—7414. doi:10.1128/mcb.23.20.7403-7414.2003. PMC 230319. PMID 14517307.
Van Damme P, Hole K, Pimenta-Marques A та ін. (July 2011). NatF contributes to an evolutionary shift in protein N-terminal acetylation and is important for normal chromosome segregation. PLoS Genet. 7: e1002169. doi:10.1371/journal.pgen.1002169. PMC 3131286. PMID 21750686.{{cite journal}}: Обслуговування CS1: Сторінки із непозначеним DOI з безкоштовним доступом (посилання)
Rathore, Om Singh; Faustino, Alexandra; Prudêncio, Pedro; Van Damme, Petra; Cox, Cymon J.; Martinho, Rui Gonçalo (2016). Absence of N-terminal acetyltransferase diversification during evolution of eukaryotic organisms. Scientific Reports. 6: 21304. Bibcode:2016NatSR...621304R. doi:10.1038/srep21304. PMC 4748286. PMID 26861501.
Aksnes, Henriette; Goris, Marianne; Strømland, Øyvind; Drazic, Adrian; Waheed, Qaiser; Reuter, Nathalie; Arnesen, Thomas (2017). Molecular determinants of the N-terminal acetyltransferase Naa60 anchoring to the Golgi membrane. Journal of Biological Chemistry. 292 (16): 6821—6837. doi:10.1074/jbc.M116.770362. PMC 5399128. PMID 28196861.{{cite journal}}: Обслуговування CS1: Сторінки із непозначеним DOI з безкоштовним доступом (посилання)
Drazic A, Aksnes H, Marie M, Boczkowska M, Varland S, Timmerman E, Foyn H, Glomnes N, Rebowski G, Impens F, Gevaert K, Dominguez R, and Arnesen T (2018). NAA80 is actin's N-terminal acetyltransferase and regulates cytoskeleton assembly and cell motility. Proc Natl Acad Sci U S A. 115 (17): 4399—4404. doi:10.1073/pnas.1718336115. PMC 5924898. PMID 29581253.
Hershko A, Heller H, Eytan E, Kaklij G, Rose IA (1984). Role of the alpha-amino group of protein in ubiquitin-mediated protein breakdown. Proc. Natl. Acad. Sci. U.S.A. 81 (22): 7021—5. Bibcode:1984PNAS...81.7021H. doi:10.1073/pnas.81.22.7021. PMC 392068. PMID 6095265.
Hwang CS, Shemorry A, Varshavsky A (2010). N-terminal acetylation of cellular proteins creates specific degradation signals. Science. 327 (5968): 973—977. Bibcode:2010Sci...327..973H. doi:10.1126/science.1183147. PMC 4259118. PMID 20110468.
Starheim KK, Gromyko D, Evjenth R, Ryningen A, Varhaug JE, Lillehaug JR, Arnesen T (2009). Knockdown of human N alpha-terminal acetyltransferase complex C leads to p53-dependent apoptosis and aberrant human Arl8b localization. Mol. Cell. Biol. 29 (13): 3569—3581. doi:10.1128/mcb.01909-08. PMC 2698767. PMID 19398576.
Yi CH, Pan H, Seebacher J, Jang IH, Hyberts SG, Heffron GJ, Vander Heiden MG, Yang R, Li F, Locasale JW, Sharfi H, Zhai B, Rodriguez-Mias R, Luithardt H, Cantley LC, Daley GQ, Asara JM, Gygi SP, Wagner G, Liu CF, Yuan J (2011). Metabolic regulation of protein N-alpha-acetylation by Bcl-xL promotes cell survival. Cell. 146 (4): 607—620. doi:10.1016/j.cell.2011.06.050. PMC 3182480. PMID 21854985.
Yang XJ, Seto E (2008). Lysine acetylation: codified crosstalk with other posttranslational modifications. Mol. Cell. 31 (4): 449—61. doi:10.1016/j.molcel.2008.07.002. PMC 2551738. PMID 18722172.
Maruta H, Greer K, Rosenbaum JL (1986). The acetylation of alpha-tubulin and its relationship to the assembly and disassembly of microtubules. J. Cell Biol. 103 (2): 571—579. doi:10.1083/jcb.103.2.571. PMC 2113826. PMID 3733880.
Brooks CL, Gu W (2011). The impact of acetylation and deacetylation on the p53 pathway. Protein Cell. 2 (6): 456—462. doi:10.1007/s13238-011-1063-9. PMC 3690542. PMID 21748595.
Tang Y, Zhao W, Chen Y, Zhao Y, Gu W (2008). Acetylation is indispensable for p53 activation. Cell. 133 (4): 612—626. doi:10.1016/j.cell.2008.03.025. PMC 2914560. PMID 18485870.
Yamaguchi H, Woods NT, Piluso LG, Lee HH, Chen J, Bhalla KN, Monteiro A, Liu X, Hung MC, Wang HG (2009). p53 acetylation is crucial for its transcription-independent proapoptotic functions. J. Biol. Chem. 284 (17): 11171—11183. doi:10.1074/jbc.M809268200. PMC 2670122. PMID 19265193.{{cite journal}}: Обслуговування CS1: Сторінки із непозначеним DOI з безкоштовним доступом (посилання)
Shangary S, Wang S (2009). Small-molecule inhibitors of the MDM2-p53 protein-protein interaction to reactivate p53 function: a novel approach for cancer therapy. Annu. Rev. Pharmacol. Toxicol. 49 (1): 223—241. doi:10.1146/annurev.pharmtox.48.113006.094723. PMC 2676449. PMID 18834305.
Zajkowicz A, Krześniak M, Matuszczyk I, Głowala-Kosińska M, Butkiewicz D, Rusin M (2013). Nutlin-3a, an MDM2 antagonist and p53 activator, helps to preserve the replicative potential of cancer cells treated with a genotoxic dose of resveratrol. Mol. Biol. Rep. 40 (8): 5013—5026. doi:10.1007/s11033-013-2602-7. PMC 3723979. PMID 23666059.
Kumamoto K, Spillare EA, Fujita K, Horikawa I, Yamashita T, Appella E, Nagashima M, Takenoshita S, Yokota J, Harris CC (2008). Nutlin-3a activates p53 to both down-regulate inhibitor of growth 2 and up-regulate mir-34a, mir-34b, and mir-34c expression, and induce senescence. Cancer Res. 68 (9): 3193—3203. doi:10.1158/0008-5472.CAN-07-2780. PMC 2440635. PMID 18451145.
Friedmann DR, Aguilar A, Fan J, Nachury MV, Marmorstein R (2012). Structure of the α-tubulin acetyltransferase, αTAT1, and implications for tubulin-specific acetylation. Proc. Natl. Acad. Sci. U.S.A. 109 (48): 19655—19660. Bibcode:2012PNAS..10919655F. doi:10.1073/pnas.1209357109. PMC 3511727. PMID 23071314.
Lee H, Zhang P, Herrmann A, Yang C, Xin H, Wang Z, Hoon DS, Forman SJ, Jove R, Riggs AD, Yu H (2012). Acetylated STAT3 is crucial for methylation of tumor-suppressor gene promoters and inhibition by resveratrol results in demethylation. Proc. Natl. Acad. Sci. U.S.A. 109 (20): 7765—7769. Bibcode:2012PNAS..109.7765L. doi:10.1073/pnas.1205132109. PMC 3356652. PMID 22547799.

web.archive.org

Brook, Tom. Protein Acetylation: Much More than Histone Acetylation. Cayman Chemical. Архів оригіналу за 28 лютого 2014.

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Wang, Qijun; Zhang, Yakun; Yang, Chen; Xiong, Hui; Lin, Yan; Yao, Jun; Li, Hong; Xie, Lu; Zhao, Wei (19 лютого 2010). Acetylation of Metabolic Enzymes Coordinates Carbon Source Utilization and Metabolic Flux. Science (англ.). 327 (5968): 1004—1007. Bibcode:2010Sci...327.1004W. doi:10.1126/science.1179687. ISSN 0036-8075. PMC 4183141. PMID 20167787.