User:Jlp21k/Acetyltransferase/Bibliography
You will be compiling your bibliography and creating an outline of the changes you will make in this sandbox.
Bibliography
As you gather the sources for your Wikipedia contribution, think about the following:
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Bibliography
[edit]Examples:
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References
[edit]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.
2. Verreault, A., Kaufman, P. D., Kobayashi, R., & Stillman, B. (1998). Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase. Current biology : CB, 8(2), 96–108. https://doi.org/10.1016/s0960-9822(98)70040-5
3. Kim, A. R., Rylett, R. J., & Shilton, B. H. (2006). Substrate binding and catalytic mechanism of human choline acetyltransferase. Biochemistry, 45(49), 14621–14631. https://doi.org/10.1021/bi061536l
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. Genomics, 9(2), 396–398. https://doi.org/10.1016/0888-7543(91)90273-h
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. Genomics, 34(1), 76–84. https://doi.org/10.1006/geno.1996.0243
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. Proceedings of the National Academy of Sciences of the United States of America, 106(20), 8157–8162. https://doi.org/10.1073/pnas.0901931106
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. Proceedings of the National Academy of Sciences of the United States of America, 109(31), 12449–12454. https://doi.org/10.1073/pnas.1210303109
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. Structure (London, England : 1993), 25(4), 641–649.e3. https://doi.org/10.1016/j.str.2017.03.003
**These are the references for the table**
**Below are references for potential text to be added**
Christensen, D. G., Xie, X., Basisty, N., Byrnes, J., McSweeney, S., Schilling, B., & Wolfe, A. J. (2019). Post-translational Protein Acetylation: An Elegant Mechanism for Bacteria to Dynamically Regulate Metabolic Functions. Frontiers in microbiology, 10, 1604. https://doi.org/10.3389/fmicb.2019.01604
Outline of proposed changes
[edit]Acetyltransferase | Substrate | Gene (Human) | Chromosome Location (Human) | Gene Group | Abbreviation |
Histone Acetyltransferase | Lysine residues on histones1 | HAT12 | 2q31.12 | Lysine acetyltransferases2 | HAT |
Choline Acetyltransferase | Choline3 | CHAT4 | 10q11.234 | NA | ChAT3 |
Serotonin N-Acetyltransferase | Serotonin | AANAT5 | 17q25.15 | GCN5 Related N-Acetyltransferases5 | AANAT5 |
NatA Acetyltransferase | N-terminus of various proteins as they emerge from the ribosome | NAA156 | 4q31.16 | Armadillo like helical domain containing N-alpha-acetyltransferase subunits6 | NatA6 |
NatB Acetyltransferase | Peptides starting with Met-Asp/Glu/Asn/Gln8 | NAA257 | 12q24.137 | N-alpha-acetyltransferase subunits MicroRNA protein coding host genes7 | NatB7 |
After the opening sentences, perhaps add sentence discussing the relevance of acetylation, and how it can impact the chemical properties of the substrate (like below, for example).
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.
Now that you have compiled a bibliography, it's time to plan out how you'll improve your assigned article.
In this section, write up a concise outline of how the sources you've identified will add relevant information to your chosen article. Be sure to discuss what content gap your additions tackle and how these additions will improve the article's quality. Consider other changes you'll make to the article, including possible deletions of irrelevant, outdated, or incorrect information, restructuring of the article to improve its readability or any other change you plan on making. This is your chance to really think about how your proposed additions will improve your chosen article and to vet your sources even further. Note: This is not a draft. This is an outline/plan where you can think about how the sources you've identified will fill in a content gap. |