User:Jlp21k/Acetyltransferase: Difference between revisions
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[[File:Acetyl.svg|thumb|Chemical structure of an acetyl group bound to the remainder R of a molecule.]] |
[[File:Acetyl.svg|thumb|Chemical structure of an acetyl group bound to the remainder R of a molecule. ]] |
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'''Acetyltransferase''' (or '''transacetylase''') is a type of [[transferase]] [[enzyme]] that transfers an [[acetyl]] group, through a process called acetylation. Acetylation serves as a modification that can profoundly transform the functionality of a protein by modifying various properties like hydrophobicity, solubility, and surface attributes. These alterations have the potential to influence the protein's conformation and its interactions with substrates, cofactors, and other macromolecules. |
'''Acetyltransferase''' (or '''transacetylase''') is a type of [[transferase]] [[enzyme]] that transfers an [[acetyl]] group, through a process called [[acetylation]]. Acetylation serves as a modification that can profoundly transform the functionality of a protein by modifying various properties like hydrophobicity, solubility, and surface attributes<ref name=":0">{{Cite journal |last=Marmorstein |first=Ronen |last2=Zhou |first2=Ming-Ming |date=2014-07-01 |title=Writers and readers of histone acetylation: structure, mechanism, and inhibition |url=https://pubmed.ncbi.nlm.nih.gov/24984779/ |journal=Cold Spring Harbor Perspectives in Biology |volume=6 |issue=7 |pages=a018762 |doi=10.1101/cshperspect.a018762 |issn=1943-0264 |pmc=4067988 |pmid=24984779}}</ref>. These alterations have the potential to influence the protein's conformation and its interactions with substrates, cofactors, and other macromolecules<ref name=":0" />. The image to the right shows the basic structure of an acetyl group, where R is a variable indicates the remainder of the molecule to which the acetyl group is attached. |
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|Histone Acetyltransferase |
|Histone Acetyltransferase |
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|Lysine residues on histones< |
|Lysine residues on histones<ref name=":0" /> |
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| ⚫ | |HAT1<ref name=":1">{{Cite journal |last=Verreault |first=A. |last2=Kaufman |first2=P. D. |last3=Kobayashi |first3=R. |last4=Stillman |first4=B. |date=1998-01-15 |title=Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase |url=https://pubmed.ncbi.nlm.nih.gov/9427644/ |journal=Current biology: CB |volume=8 |issue=2 |pages=96–108 |doi=10.1016/s0960-9822(98)70040-5 |issn=0960-9822 |pmid=9427644}}</ref> |
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|HAT1<sup>2</sup> |
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|2q31.1< |
|2q31.1<ref name=":1" /> |
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|Lysine acetyltransferases< |
|Lysine acetyltransferases<ref name=":1" /> |
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|HAT |
|HAT |
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|- |
|- |
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|Choline Acetyltransferase |
|Choline Acetyltransferase |
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|Choline<ref name=":2">{{Cite journal |last=Kim |first=Ae-Ri |last2=Rylett |first2=R. Jane |last3=Shilton |first3=Brian H. |date=2006-12-01 |title=Substrate Binding and Catalytic Mechanism of Human Choline Acetyltransferase , |url=https://pubs.acs.org/doi/10.1021/bi061536l |journal=Biochemistry |language=en |volume=45 |issue=49 |pages=14621–14631 |doi=10.1021/bi061536l |issn=0006-2960}}</ref> |
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|Choline<sup>3</sup> |
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|CHAT<ref name=":3">{{Cite journal |last=Strauss |first=William L. |last2=Kemper |first2=Robert R. |last3=Jayakar |first3=Parul |last4=Kong |first4=Chuang Fong |last5=Hersh |first5=Louis B. |last6=Hilt |first6=Dana C. |last7=Rabin |first7=Mark |date=1991-02-01 |title=Human choline acetyltransferase gene maps to region 10q11–q22.2 by in situ hybridization |url=https://www.sciencedirect.com/science/article/pii/088875439190273H |journal=Genomics |volume=9 |issue=2 |pages=396–398 |doi=10.1016/0888-7543(91)90273-H |issn=0888-7543}}</ref> |
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|CHAT<sup>4</sup> |
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|10q11.23< |
|10q11.23<ref name=":3" /> |
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|NA |
|NA |
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|ChAT< |
|ChAT<ref name=":2" /> |
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|Serotonin N-Acetyltransferase |
|Serotonin N-Acetyltransferase |
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|Serotonin |
|Serotonin |
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|AANAT<ref name=":4">{{Cite journal |last=Coon |first=Steven L. |last2=Mazuruk |first2=Krzysztof |last3=Bernard |first3=Marianne |last4=Roseboom |first4=Patrick H. |last5=Klein |first5=David C. |last6=Rodriguez |first6=Ignacio R. |date=1996-05-15 |title=The Human SerotoninN-Acetyltransferase (EC 2.3.1.87) Gene (AANAT): Structure, Chromosomal Localization, and Tissue Expression |url=https://www.sciencedirect.com/science/article/pii/S0888754396902438 |journal=Genomics |volume=34 |issue=1 |pages=76–84 |doi=10.1006/geno.1996.0243 |issn=0888-7543}}</ref> |
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|AANAT<sup>5</sup> |
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|17q25.1< |
|17q25.1<ref name=":4" /> |
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|GCN5 Related N-Acetyltransferases< |
|GCN5 Related N-Acetyltransferases<ref name=":4" /> |
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|AANAT< |
|AANAT<ref name=":4" /> |
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|NatA Acetyltransferase |
|NatA Acetyltransferase |
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|N-terminus of various proteins as they emerge from the ribosome |
|N-terminus of various proteins as they emerge from the ribosome |
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|NAA15<ref name=":5">{{Cite journal |last=Arnesen |first=Thomas |last2=Van Damme |first2=Petra |last3=Polevoda |first3=Bogdan |last4=Helsens |first4=Kenny |last5=Evjenth |first5=Rune |last6=Colaert |first6=Niklaas |last7=Varhaug |first7=Jan Erik |last8=Vandekerckhove |first8=Joël |last9=Lillehaug |first9=Johan R. |last10=Sherman |first10=Fred |last11=Gevaert |first11=Kris |date=2009-05-19 |title=Proteomics analyses reveal the evolutionary conservation and divergence of N-terminal acetyltransferases from yeast and humans |url=https://pnas.org/doi/full/10.1073/pnas.0901931106 |journal=Proceedings of the National Academy of Sciences |language=en |volume=106 |issue=20 |pages=8157–8162 |doi=10.1073/pnas.0901931106 |issn=0027-8424 |pmc=PMC2688859 |pmid=19420222}}</ref> |
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|NAA15<sup>6</sup> |
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|4q31.1< |
|4q31.1<ref name=":5" /> |
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|Armadillo like helical domain containing |
|Armadillo like helical domain containing |
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N-alpha-acetyltransferase subunits< |
N-alpha-acetyltransferase subunits<ref name=":5" /> |
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|NatA< |
|NatA<ref name=":5" /> |
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|NatB Acetyltransferase |
|NatB Acetyltransferase |
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|Peptides starting with Met-Asp/Glu/Asn/Gln<ref>{{Cite journal |last=Hong |first=Haiyan |last2=Cai |first2=Yongfei |last3=Zhang |first3=Shijun |last4=Ding |first4=Hongyan |last5=Wang |first5=Haitao |last6=Han |first6=Aidong |date=2017-04-04 |title=Molecular Basis of Substrate Specific Acetylation by N-Terminal Acetyltransferase NatB |url=https://pubmed.ncbi.nlm.nih.gov/28380339/ |journal=Structure (London, England: 1993) |volume=25 |issue=4 |pages=641–649.e3 |doi=10.1016/j.str.2017.03.003 |issn=1878-4186 |pmid=28380339}}</ref> |
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|Peptides starting with Met-Asp/Glu/Asn/Gln<sup>8</sup> |
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|NAA25<ref name=":6">{{Cite journal |last=Van Damme |first=Petra |last2=Lasa |first2=Marta |last3=Polevoda |first3=Bogdan |last4=Gazquez |first4=Cristina |last5=Elosegui-Artola |first5=Alberto |last6=Kim |first6=Duk Soo |last7=De Juan-Pardo |first7=Elena |last8=Demeyer |first8=Kimberly |last9=Hole |first9=Kristine |last10=Larrea |first10=Esther |last11=Timmerman |first11=Evy |last12=Prieto |first12=Jesus |last13=Arnesen |first13=Thomas |last14=Sherman |first14=Fred |last15=Gevaert |first15=Kris |date=2012-07-31 |title=N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB |url=https://pnas.org/doi/full/10.1073/pnas.1210303109 |journal=Proceedings of the National Academy of Sciences |language=en |volume=109 |issue=31 |pages=12449–12454 |doi=10.1073/pnas.1210303109 |issn=0027-8424 |pmc=PMC3412031 |pmid=22814378}}</ref> |
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|NAA25<sup>7</sup> |
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|12q24.13< |
|12q24.13<ref name=":6" /> |
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|N-alpha-acetyltransferase subunits |
|N-alpha-acetyltransferase subunits |
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MicroRNA protein coding host genes< |
MicroRNA protein coding host genes<ref name=":6" /> |
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|NatB< |
|NatB<ref name=":6" /> |
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== 3D structures of acetyltransferase enzymes == |
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[[File:Histoneacetyltransferase.jpg|thumb|3D structure of histone acetyltransferase]] |
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The 3D structure predictions of histone, choline, and serotonin acetyltransferases are shown to the side of this page. The 3D structure of these proteins are essential for interactions between them and their substrates. Alterations to the 3D structures of these enzymes could result in the chemical modifications not being completed. |
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[[File:Protein CHAT PDB 2fy2.png|thumb|3D Structure of choline acetyltransferase]] |
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[[File:SNAT PDB-code 1KUX.png|thumb|3D structure of serotonin N-acetyltransferase]] |
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=== References === |
=== References === |
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1. Marmorstein R, Zhou MM. Writers and readers of histone acetylation: structure, mechanism, and inhibition. Cold Spring Harb Perspect Biol. 2014 Jul 1;6(7):a018762. doi: 10.1101/cshperspect.a018762. PMID: 24984779; PMCID: PMC4067988. |
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| ⚫ | |||
3. Kim, A. R., Rylett, R. J., & Shilton, B. H. (2006). Substrate binding and catalytic mechanism of human choline acetyltransferase. <nowiki>''</nowiki>Biochemistry<nowiki>''</nowiki>, <nowiki>''</nowiki>45<nowiki>''</nowiki>(49), 14621–14631. <nowiki><nowiki>https://doi.org/10.1021/bi061536l</nowiki></nowiki> |
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4. Strauss, W. L., Kemper, R. R., Jayakar, P., Kong, C. F., Hersh, L. B., Hilt, D. C., & Rabin, M. (1991). Human choline acetyltransferase gene maps to region 10q11-q22.2 by in situ hybridization. <nowiki>''</nowiki>Genomics<nowiki>''</nowiki>, <nowiki>''</nowiki>9<nowiki>''</nowiki>(2), 396–398. <nowiki><nowiki>https://doi.org/10.1016/0888-7543(91)90273-h</nowiki></nowiki> |
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5. Coon, S. L., Mazuruk, K., Bernard, M., Roseboom, P. H., Klein, D. C., & Rodriguez, I. R. (1996). The human serotonin N-acetyltransferase (EC 2.3.1.87) gene (AANAT): structure, chromosomal localization, and tissue expression. <nowiki>''</nowiki>Genomics<nowiki>''</nowiki>, <nowiki>''</nowiki>34<nowiki>''</nowiki>(1), 76–84. <nowiki><nowiki>https://doi.org/10.1006/geno.1996.0243</nowiki></nowiki> |
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6. Arnesen, T., Van Damme, P., Polevoda, B., Helsens, K., Evjenth, R., Colaert, N., Varhaug, J. E., Vandekerckhove, J., Lillehaug, J. R., Sherman, F., & Gevaert, K. (2009). Proteomics analyses reveal the evolutionary conservation and divergence of N-terminal acetyltransferases from yeast and humans. <nowiki>''</nowiki>Proceedings of the National Academy of Sciences of the United States of America<nowiki>''</nowiki>, <nowiki>''</nowiki>106<nowiki>''</nowiki>(20), 8157–8162. <nowiki><nowiki>https://doi.org/10.1073/pnas.0901931106</nowiki></nowiki> |
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7. Van Damme, P., Lasa, M., Polevoda, B., Gazquez, C., Elosegui-Artola, A., Kim, D. S., De Juan-Pardo, E., Demeyer, K., Hole, K., Larrea, E., Timmerman, E., Prieto, J., Arnesen, T., Sherman, F., Gevaert, K., & Aldabe, R. (2012). N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. <nowiki>''</nowiki>Proceedings of the National Academy of Sciences of the United States of America<nowiki>''</nowiki>, <nowiki>''</nowiki>109<nowiki>''</nowiki>(31), 12449–12454. <nowiki><nowiki>https://doi.org/10.1073/pnas.1210303109</nowiki></nowiki> |
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8. Hong, H., Cai, Y., Zhang, S., Ding, H., Wang, H., & Han, A. (2017). Molecular Basis of Substrate Specific Acetylation by N-Terminal Acetyltransferase NatB. <nowiki>''</nowiki>Structure (London, England : 1993)<nowiki>''</nowiki>, <nowiki>''</nowiki>25<nowiki>''</nowiki>(4), 641–649.e3. |
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[[Category:Wikipedia Student Program]] |
[[Category:Wikipedia Student Program]] |
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Latest revision as of 15:31, 7 December 2023
Acetyltransferase (or transacetylase) is a type of transferase enzyme that transfers an acetyl group, through a process called acetylation. Acetylation serves as a modification that can profoundly transform the functionality of a protein by modifying various properties like hydrophobicity, solubility, and surface attributes[1]. These alterations have the potential to influence the protein's conformation and its interactions with substrates, cofactors, and other macromolecules[1]. The image to the right shows the basic structure of an acetyl group, where R is a variable indicates the remainder of the molecule to which the acetyl group is attached.
| Acetyltransferases | Substrate | Gene | Chromosome Location | Gene Group | Abbreviation |
| Histone Acetyltransferase | Lysine residues on histones[1] | HAT1[2] | 2q31.1[2] | Lysine acetyltransferases[2] | HAT |
| Choline Acetyltransferase | Choline[3] | CHAT[4] | 10q11.23[4] | NA | ChAT[3] |
| Serotonin N-Acetyltransferase | Serotonin | AANAT[5] | 17q25.1[5] | GCN5 Related N-Acetyltransferases[5] | AANAT[5] |
| NatA Acetyltransferase | N-terminus of various proteins as they emerge from the ribosome | NAA15[6] | 4q31.1[6] | Armadillo like helical domain containing
N-alpha-acetyltransferase subunits[6] |
NatA[6] |
| NatB Acetyltransferase | Peptides starting with Met-Asp/Glu/Asn/Gln[7] | NAA25[8] | 12q24.13[8] | N-alpha-acetyltransferase subunits
MicroRNA protein coding host genes[8] |
NatB[8] |
3D structures of acetyltransferase enzymes
[edit]
The 3D structure predictions of histone, choline, and serotonin acetyltransferases are shown to the side of this page. The 3D structure of these proteins are essential for interactions between them and their substrates. Alterations to the 3D structures of these enzymes could result in the chemical modifications not being completed.
Additional examples include:
See also
[edit]External links
[edit]- Acetyltransferases at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
 | This enzyme-related article is a stub. You can help Wikipedia by expanding it. |
 | This is the sandbox page where you will draft your initial Wikipedia contribution.
If you're starting a new article, you can develop it here until it's ready to go live. If you're working on improvements to an existing article, copy only one section at a time of the article to this sandbox to work on, and be sure to use an edit summary linking to the article you copied from. Do not copy over the entire article. You can find additional instructions here. Remember to save your work regularly using the "Publish page" button. (It just means 'save'; it will still be in the sandbox.) You can add bold formatting to your additions to differentiate them from existing content. |
Article Draft
[edit]Lead
[edit]Article body
[edit]References
[edit]- ^ a b c Marmorstein, Ronen; Zhou, Ming-Ming (2014-07-01). "Writers and readers of histone acetylation: structure, mechanism, and inhibition". Cold Spring Harbor Perspectives in Biology. 6 (7): a018762. doi:10.1101/cshperspect.a018762. ISSN 1943-0264. PMC 4067988. PMID 24984779.
- ^ a b c Verreault, A.; Kaufman, P. D.; Kobayashi, R.; Stillman, B. (1998-01-15). "Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase". Current biology: CB. 8 (2): 96–108. doi:10.1016/s0960-9822(98)70040-5. ISSN 0960-9822. PMID 9427644.
- ^ a b Kim, Ae-Ri; Rylett, R. Jane; Shilton, Brian H. (2006-12-01). "Substrate Binding and Catalytic Mechanism of Human Choline Acetyltransferase ,". Biochemistry. 45 (49): 14621–14631. doi:10.1021/bi061536l. ISSN 0006-2960.
- ^ a b Strauss, William L.; Kemper, Robert R.; Jayakar, Parul; Kong, Chuang Fong; Hersh, Louis B.; Hilt, Dana C.; Rabin, Mark (1991-02-01). "Human choline acetyltransferase gene maps to region 10q11–q22.2 by in situ hybridization". Genomics. 9 (2): 396–398. doi:10.1016/0888-7543(91)90273-H. ISSN 0888-7543.
- ^ a b c d Coon, Steven L.; Mazuruk, Krzysztof; Bernard, Marianne; Roseboom, Patrick H.; Klein, David C.; Rodriguez, Ignacio R. (1996-05-15). "The Human SerotoninN-Acetyltransferase (EC 2.3.1.87) Gene (AANAT): Structure, Chromosomal Localization, and Tissue Expression". Genomics. 34 (1): 76–84. doi:10.1006/geno.1996.0243. ISSN 0888-7543.
- ^ a b c d Arnesen, Thomas; Van Damme, Petra; Polevoda, Bogdan; Helsens, Kenny; Evjenth, Rune; Colaert, Niklaas; Varhaug, Jan Erik; Vandekerckhove, Joël; Lillehaug, Johan R.; Sherman, Fred; Gevaert, Kris (2009-05-19). "Proteomics analyses reveal the evolutionary conservation and divergence of N-terminal acetyltransferases from yeast and humans". Proceedings of the National Academy of Sciences. 106 (20): 8157–8162. doi:10.1073/pnas.0901931106. ISSN 0027-8424. PMC 2688859. PMID 19420222.
{{cite journal}}: CS1 maint: PMC format (link) - ^ Hong, Haiyan; Cai, Yongfei; Zhang, Shijun; Ding, Hongyan; Wang, Haitao; Han, Aidong (2017-04-04). "Molecular Basis of Substrate Specific Acetylation by N-Terminal Acetyltransferase NatB". Structure (London, England: 1993). 25 (4): 641–649.e3. doi:10.1016/j.str.2017.03.003. ISSN 1878-4186. PMID 28380339.
- ^ a b c d Van Damme, Petra; Lasa, Marta; Polevoda, Bogdan; Gazquez, Cristina; Elosegui-Artola, Alberto; Kim, Duk Soo; De Juan-Pardo, Elena; Demeyer, Kimberly; Hole, Kristine; Larrea, Esther; Timmerman, Evy; Prieto, Jesus; Arnesen, Thomas; Sherman, Fred; Gevaert, Kris (2012-07-31). "N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB". Proceedings of the National Academy of Sciences. 109 (31): 12449–12454. doi:10.1073/pnas.1210303109. ISSN 0027-8424. PMC 3412031. PMID 22814378.
{{cite journal}}: CS1 maint: PMC format (link)