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Journal articles on the topic 'PROTEIN N'

Author: Grafiati

Published: 11 September 2023

Last updated: 31 July 2025

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1

Duclos, S., P. Da Silva, F. Vovelle, F. Piller, and V. Piller. "Characterization of the UDP-N-acetylgalactosamine binding domain of bovine polypeptide N-acetylgalactosaminyltransferase T1." Protein Engineering Design and Selection 17, no. 8 (2004): 635–46. http://dx.doi.org/10.1093/protein/gzh075.

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2

Koyama, Y., M. Hidaka, M. Nishimoto, and M. Kitaoka. "Directed evolution to enhance thermostability of galacto-N-biose/lacto-N-biose I phosphorylase." Protein Engineering Design and Selection 26, no. 11 (2013): 755–61. http://dx.doi.org/10.1093/protein/gzt049.

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3

Gordon, J. I., R. J. Duronio, D. A. Rudnick, S. P. Adams, and G. W. Gokel. "Protein N-myristoylation." Journal of Biological Chemistry 266, no. 14 (1991): 8647–50. http://dx.doi.org/10.1016/s0021-9258(18)31490-x.

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4

Flanagan, Karen, John Walshaw, Sarah L. Price, and Julia M. Goodfellow. "Solvent interactions with n ring systems in proteins." "Protein Engineering, Design and Selection" 8, no. 2 (1995): 109–16. http://dx.doi.org/10.1093/protein/8.2.109.

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5

Imberty, A., and S. Perez. "Stereochemistry of the N-glycosylation sites in glycoproteins." Protein Engineering Design and Selection 8, no. 7 (1995): 699–709. http://dx.doi.org/10.1093/protein/8.7.699.

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6

Roth, Jürgen, Christian Zuber, Sujin Park, et al. "Protein N-glycosylation, protein folding, and protein quality control." Molecules and Cells 30, no. 6 (2010): 497–506. http://dx.doi.org/10.1007/s10059-010-0159-z.

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7

Hollebeke, Jolien, Petra Van Damme та Kris Gevaert. "N-terminal acetylation and other functions of Nα-acetyltransferases". Biological Chemistry 393, № 4 (2012): 291–98. http://dx.doi.org/10.1515/hsz-2011-0228.

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Abstract Protein N-terminal acetylation by Nα-acetyltransferases (NATs) is an omnipresent protein modification that affects a large number of proteins. The exact biological role of N-terminal acetylation has, however, remained enigmatic for the overall majority of affected proteins, and only for a rather small number of proteins, N-terminal acetylation was linked to various protein features including stability, localization, and interactions. This minireview tries to summarize the recent progress made in understanding the functionality of N-terminal protein acetylation and also focuses on nonc

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8

Hope, John N., Hao-Chia Chen та J. Fidding Hejtmancik. "βA3/Al-crystallin association: role of the N-terminal arm". "Protein Engineering, Design and Selection" 7, № 3 (1994): 445–51. http://dx.doi.org/10.1093/protein/7.3.445.

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9

Wu, Di, Weston B. Struwe, David J. Harvey, Michael A. J. Ferguson, and Carol V. Robinson. "N-glycan microheterogeneity regulates interactions of plasma proteins." Proceedings of the National Academy of Sciences 115, no. 35 (2018): 8763–68. http://dx.doi.org/10.1073/pnas.1807439115.

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Altered glycosylation patterns of plasma proteins are associated with autoimmune disorders and pathogenesis of various cancers. Elucidating glycoprotein microheterogeneity and relating subtle changes in the glycan structural repertoire to changes in protein–protein, or protein–small molecule interactions, remains a significant challenge in glycobiology. Here, we apply mass spectrometry-based approaches to elucidate the global and site-specific microheterogeneity of two plasma proteins: α1-acid glycoprotein (AGP) and haptoglobin (Hp). We then determine the dissociation constants of the anticoag

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10

Doughty, S. W., F. E. Blaney, B. S. Orlek, and W. G. Richards. "A molecular mechanism for toxin block in N-type calcium channels." Protein Engineering Design and Selection 11, no. 2 (1998): 95–99. http://dx.doi.org/10.1093/protein/11.2.95.

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11

Li, Hui-Guang, Shi-Zhen Xu, Shen Wu, et al. "Role of Arg163 in the N-glycosidase activity of neo-trichosanthin." Protein Engineering, Design and Selection 12, no. 11 (1999): 999–1004. http://dx.doi.org/10.1093/protein/12.11.999.

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12

Medvedkin, Vyacheslav N., Eugene A. Permyakov, Lyubov V. Klimenko, et al. "Interactions of (Ala*Ala*Lys*Pro)n and (Lys*Lys*Ser*Pro)n with DNA. Proposed coiled-coil structure of AlgR3 and AlgP from Pseudomonas aeruginosa." "Protein Engineering, Design and Selection" 8, no. 1 (1995): 63–70. http://dx.doi.org/10.1093/protein/8.1.63.

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13

Aubol, Brandon E., Ryan M. Plocinik, Malik M. Keshwani, et al. "N-terminus of the protein kinase CLK1 induces SR protein hyperphosphorylation." Biochemical Journal 462, no. 1 (2014): 143–52. http://dx.doi.org/10.1042/bj20140494.

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14

Kumar, Kapila, Sreejith Rajasekharan, Sahil Gulati, et al. "Elucidating the Interacting Domains ofChandipuraVirus Nucleocapsid Protein." Advances in Virology 2013 (2013): 1–9. http://dx.doi.org/10.1155/2013/594319.

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The nucleocapsid (N) protein ofChandipuravirus (CHPV) plays a crucial role in viral life cycle, besides being an important structural component of the virion through proper organization of its interactions with other viral proteins. In a recent study, the authors had mapped the associations among CHPV proteins and shown that N protein interacts with four of the viral proteins: N, phosphoprotein (P), matrix protein (M), and glycoprotein (G). The present study aimed to distinguish the regions of CHPV N protein responsible for its interactions with other viral proteins. In this direction, we have

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15

Munson, Mary, and Nia J. Bryant. "A role for the syntaxin N-terminus." Biochemical Journal 418, no. 1 (2009): e1-e3. http://dx.doi.org/10.1042/bj20082389.

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Intracellular membrane fusion steps in eukaryotes require the syntaxin family of SNARE (soluble N-ethylmaleimide-sensitive fusion protein-attachment protein receptor) proteins. Syntaxins are regulated at several levels through interactions with regulatory proteins, including the SM (Sec1p/Munc18) proteins. Key to understanding this regulation is the characterization of different SM–syntaxin binding interactions at the molecular level and in terms of their contribution to function in vivo. The most conserved SM–syntaxin binding mode is through interaction of the syntaxin's extreme N-terminal pe

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16

Stokes, H. L., A. J. Easton, and A. C. Marriott. "Chimeric pneumovirus nucleocapsid (N) proteins allow identification of amino acids essential for the function of the respiratory syncytial virus N protein." Journal of General Virology 84, no. 10 (2003): 2679–83. http://dx.doi.org/10.1099/vir.0.19370-0.

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The nucleocapsid (N) protein of the pneumovirus respiratory syncytial virus (RSV) is a major structural protein which encapsidates the RNA genome and is essential for replication and transcription of the RSV genome. The N protein of the related virus pneumonia virus of mice (PVM) is functionally unable to replace the RSV N protein in a minigenome replication assay. Using chimeric proteins, in which the immediate C-terminal part of the RSV N protein was replaced with the equivalent region of the PVM N protein, it was shown that six amino acid residues near the C terminus of the N protein (betwe

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17

Mammadova-Bach, Elmina, Jaak Jaeken, Thomas Gudermann, and Attila Braun. "Platelets and Defective N-Glycosylation." International Journal of Molecular Sciences 21, no. 16 (2020): 5630. http://dx.doi.org/10.3390/ijms21165630.

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N-glycans are covalently linked to an asparagine residue in a simple acceptor sequence of proteins, called a sequon. This modification is important for protein folding, enhancing thermodynamic stability, and decreasing abnormal protein aggregation within the endoplasmic reticulum (ER), for the lifetime and for the subcellular localization of proteins besides other functions. Hypoglycosylation is the hallmark of a group of rare genetic diseases called congenital disorders of glycosylation (CDG). These diseases are due to defects in glycan synthesis, processing, and attachment to proteins and li

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18

Van Damme, Petra, Thomas Arnesen, and Kris Gevaert. "Protein alpha-N-acetylation studied by N-terminomics." FEBS Journal 278, no. 20 (2011): 3822–34. http://dx.doi.org/10.1111/j.1742-4658.2011.08230.x.

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19

Gaudry, A., B. Lorber, A. Neuenfeldt, C. Sauter, C. Florentz, and M. Sissler. "Re-designed N-terminus enhances expression, solubility and crystallizability of mitochondrial protein." Protein Engineering Design and Selection 25, no. 9 (2012): 473–81. http://dx.doi.org/10.1093/protein/gzs046.

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20

Wang, M., L. S. Lee, A. Nepomich, et al. "Single-chain Fv with manifold N-glycans as bifunctional scaffolds for immunomolecules." Protein Engineering Design and Selection 11, no. 12 (1998): 1277–83. http://dx.doi.org/10.1093/protein/11.12.1277.

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21

Benito, A., M. Bosch, G. Torrent, M. Ribó, and M. Vilanova. "Stabilization of human pancreatic ribonuclease through mutation at its N-terminal edge." Protein Engineering, Design and Selection 15, no. 11 (2002): 887–93. http://dx.doi.org/10.1093/protein/15.11.887.

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22

De Rosa, Lucia, Rossella Di Stasi, Alessandra Romanelli, and Luca Domenico D’Andrea. "Exploiting Protein N-Terminus for Site-Specific Bioconjugation." Molecules 26, no. 12 (2021): 3521. http://dx.doi.org/10.3390/molecules26123521.

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Although a plethora of chemistries have been developed to selectively decorate protein molecules, novel strategies continue to be reported with the final aim of improving selectivity and mildness of the reaction conditions, preserve protein integrity, and fulfill all the increasing requirements of the modern applications of protein conjugates. The targeting of the protein N-terminal alpha-amine group appears a convenient solution to the issue, emerging as a useful and unique reactive site universally present in each protein molecule. Herein, we provide an updated overview of the methodologies

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23

Boza, Julio J., Olga Martínez-Augustin, Luis Baró, M. Dolores Suarez, and Angel Gil. "Protein v. enzymic protein hydrolysates. Nitrogen utilization in starved rats." British Journal of Nutrition 73, no. 1 (1995): 65–71. http://dx.doi.org/10.1079/bjn19950009.

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The present study was carried out to compare the effects of four isoenergetic and isonitrogenous diets on the N utilization, total serum protein concentration and serum amino acid profile in starved rats at weaning. These diets differed only in the molecular form of two milk proteins (whey protein and casein), which were either native or partly hydrolysed. Male Wistar rats at weaning were fasted for 3 d and then refed with one of the four diets for 48 h. No differences were observed in the body weight gain, protein digestibility and total serum protein concentration between groups after the re

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24

Welke, Robert-William, Hannah Sabeth Sperber, Ronny Bergmann, et al. "Characterization of Hantavirus N Protein Intracellular Dynamics and Localization." Viruses 14, no. 3 (2022): 457. http://dx.doi.org/10.3390/v14030457.

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Hantaviruses are enveloped viruses that possess a tri-segmented, negative-sense RNA genome. The viral S-segment encodes the multifunctional nucleocapsid protein (N), which is involved in genome packaging, intracellular protein transport, immunoregulation, and several other crucial processes during hantavirus infection. In this study, we generated fluorescently tagged N protein constructs derived from Puumalavirus (PUUV), the dominant hantavirus species in Central, Northern, and Eastern Europe. We comprehensively characterized this protein in the rodent cell line CHO-K1, monitoring the dynamics

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25

Wallin, E., and G. von Heijne. "Properties of N-terminal tails in G-protein coupled receptors: a statistical study." Protein Engineering Design and Selection 8, no. 7 (1995): 693–98. http://dx.doi.org/10.1093/protein/8.7.693.

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26

Werten, Paul J. L., John A. Carver, Rainer Jaenicke та Wilfried W. de Jong. "The elusive role of the N-terminal extension of βA3- and βAl-crystallin". "Protein Engineering, Design and Selection" 9, № 11 (1996): 1021–28. http://dx.doi.org/10.1093/protein/9.11.1021.

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27

Kwan, Emily M., Alisdair B. Boraston, Bradley W. McLean, Douglas G. Kilburn, and R. Antony J. Warren. "N-Glycosidase–carbohydrate-binding module fusion proteins as immobilized enzymes for protein deglycosylation." Protein Engineering, Design and Selection 18, no. 10 (2005): 497–501. http://dx.doi.org/10.1093/protein/gzi055.

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28

Ishikawa, N., T. Chiba, L. T. Chen, A. Shimizu, M. Ikeguchi, and S. Sugai. "Remarkable destabilization of recombinant alpha-lactalbumin by an extraneous N-terminal methionyl residue." Protein Engineering Design and Selection 11, no. 5 (1998): 333–35. http://dx.doi.org/10.1093/protein/11.5.333.

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29

Lins, L., C. Flore, L. Chapelle, P. J. Talmud, A. Thomas, and R. Brasseur. "Lipid-interacting properties of the N-terminal domain of human apolipoprotein C-III." Protein Engineering, Design and Selection 15, no. 6 (2002): 513–20. http://dx.doi.org/10.1093/protein/15.6.513.

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30

Clerc, Florent, Karli R. Reiding, Bas C. Jansen, Guinevere S. M. Kammeijer, Albert Bondt, and Manfred Wuhrer. "Human plasma protein N-glycosylation." Glycoconjugate Journal 33, no. 3 (2015): 309–43. http://dx.doi.org/10.1007/s10719-015-9626-2.

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31

Kumar, Raj. "N-Myristoyltransferase: A Novel Therapeutic Target for Cancer, Inflammation and Radiation Response Modifications." Advances in Clinical Toxicology 9, no. 1 (2024): 1–20. http://dx.doi.org/10.23880/act-16000297.

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N-Myristoyltransferase (NMT) is a well conserved monomeric protein that catalyzes myristoyl group transfer to various target proteins carrying consensus amino acid sequence motif GXXXS/T (where ‘X’ is any amino acid). NMT mediated myristoylation promotes protein-protein and protein-membrane interactions, leading to diverse signaling including cell proliferation, carcinogenesis, inflammation and immune responses. However, inter-networking linkage between NMT over-expression and protein myristoylation under oxidative stress coupled with inflammation and carcinogenesis is completely missing and n

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32

Zhang, Qingling, Jubin Wang, Xi Zhang, Yingtian Deng, and Feng Li. "A Conserved, Serine-Rich Protein Plays Opposite Roles in N-Mediated Immunity against TMV and N-Triggered Cell Death." Viruses 15, no. 1 (2022): 26. http://dx.doi.org/10.3390/v15010026.

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Plant nucleotide-binding, leucine-rich, repeat-containing proteins (NLRs) play important roles in plant immunity. NLR expression and function are tightly regulated by multiple mechanisms. In this study, a conserved serine/arginine-rich protein (SR protein) was identified through the yeast one-hybrid screening of a tobacco cDNA library using DNA fragments from the N gene, an NLR that confers immunity to tobacco mosaic virus (TMV). This SR protein showed an interaction with a 3′ genomic regulatory sequence (GRS) and has a potential role in regulating the alternative splicing of N. Thus, it was n

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33

Rampoldi, Francesca, Martin Boehm, Wolf Lehmann, Hermann-Josef Gröne, and Stefan Porubsky. "Protein N-myristoylation is indispensable for T-cell development and activation (LYM7P.720)." Journal of Immunology 192, no. 1_Supplement (2014): 193.8. http://dx.doi.org/10.4049/jimmunol.192.supp.193.8.

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Abstract Protein N-myristoylation refers to an irreversible attachment of myristic acid to the N-terminal glycine of proteins. This modification promotes protein-protein and protein-membrane interactions. Thymus represents an organ with a high degree of protein N-myristoylation. Our aim was to elucidate the role of protein N-myristoylation in T-cell development and in T-cell receptor (TCR) signaling in vivo. To this end, mice with a T-cell specific deletion of both genes responsible for protein N-myristoylation (N-myristoyltransferase, Nmt, 1 and 2) were generated. Abrogation of protein N-myri

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34

Sou, Yu-shin, Junji Yamaguchi, Keisuke Masuda, Yasuo Uchiyama, Yusuke Maeda, and Masato Koike. "Golgi pH homeostasis stabilizes the lysosomal membrane throughN-glycosylation of membrane proteins." Life Science Alliance 7, no. 10 (2024): e202402677. http://dx.doi.org/10.26508/lsa.202402677.

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Protein glycosylation plays a vital role in various cellular functions, many of which occur within the Golgi apparatus. The Golgi pH regulator (GPHR) is essential for the proper functioning of the Golgi apparatus. The lysosomal membrane contains highly glycosylated membrane proteins in abundance. This study investigated the role of the Golgi luminal pH inN-glycosylation of lysosomal membrane proteins and the effect of this protein modification on membrane stability usingGphr-deficient MEFs. We showed thatGphrdeficiency causes an imbalance in the Golgi luminal pH, resulting in abnormal proteinN

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35

Scheys, Freja, Els J. M. Van Damme, Jarne Pauwels, An Staes, Kris Gevaert, and Guy Smagghe. "N-glycosylation Site Analysis Reveals Sex-related Differences in Protein N-glycosylation in the Rice Brown Planthopper (Nilaparvata lugens)." Molecular & Cellular Proteomics 19, no. 3 (2020): 529–39. http://dx.doi.org/10.1074/mcp.ra119.001823.

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Glycosylation is a common modification of proteins and critical for a wide range of biological processes. Differences in protein glycosylation between sexes have already been observed in humans, nematodes and trematodes, and have recently also been reported in the rice pest insect Nilaparvata lugens. Although protein N-glycosylation in insects is nowadays of high interest because of its potential for exploitation in pest control strategies, the functionality of differential N-glycosylation between sexes is yet unknown. In this study, therefore, the occurrence and role of sex-related protein N-

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36

Ruboyianes, Mark V., Min Chen, Mathew S. Dubrava, James E. Cherwa та Bentley A. Fane. "The Expression of N-Terminal Deletion DNA Pilot Proteins Inhibits the Early Stages of φX174 Replication". Journal of Virology 83, № 19 (2009): 9952–56. http://dx.doi.org/10.1128/jvi.01077-09.

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ABSTRACT The φX174 DNA pilot protein H contains four predicted C-terminal coiled-coil domains. The region of the gene encoding these structures was cloned, expressed in vivo, and found to strongly inhibit wild-type replication. DNA and protein synthesis was investigated in the absence of de novo H protein synthesis and in wild-type-infected cells expressing the inhibitory proteins (ΔH). The expression of the ΔH proteins interfered with early stages of DNA replication, which did not require de novo H protein synthesis, suggesting that the inhibitory proteins interfere with the wild-type H prote

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37

Khramtsov, Yuri V., Alexey V. Ulasov, Tatiana N. Lupanova, et al. "Intracellular Degradation of SARS-CoV-2 N-Protein Caused by Modular Nanotransporters Containing Anti-N-Protein Monobody and a Sequence That Recruits the Keap1 E3 Ligase." Pharmaceutics 16, no. 1 (2023): 4. http://dx.doi.org/10.3390/pharmaceutics16010004.

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The proper viral assembly relies on both nucleic acids and structural viral proteins. Thus a biologically active agent that provides the degradation of one of these key proteins and/or destroys the viral factory could suppress viral replication efficiently. The nucleocapsid protein (N-protein) is a key protein for the SARS-CoV-2 virus. As a bioactive agent, we offer a modular nanotransporter (MNT) developed by us, which, in addition to an antibody mimetic to the N-protein, contains an amino acid sequence for the attraction of the Keap1 E3 ubiquitin ligase. This should lead to the subsequent de

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38

Eldeeb, Mohamed A., Richard P. Fahlman, Mohamed A. Ragheb, and Mansoore Esmaili. "Does N‐Terminal Protein Acetylation Lead to Protein Degradation?" BioEssays 41, no. 11 (2019): 1800167. http://dx.doi.org/10.1002/bies.201800167.

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39

Gaunitz, Stefan, Lars O. Tjernberg, and Sophia Schedin-Weiss. "What Can N-glycomics and N-glycoproteomics of Cerebrospinal Fluid Tell Us about Alzheimer Disease?" Biomolecules 11, no. 6 (2021): 858. http://dx.doi.org/10.3390/biom11060858.

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Proteomics—large-scale studies of proteins—has over the last decade gained an enormous interest for studies aimed at revealing proteins and pathways involved in disease. To fully understand biological and pathological processes it is crucial to also include post-translational modifications in the “omics”. To this end, glycomics (identification and quantification of glycans enzymatically or chemically released from proteins) and glycoproteomics (identification and quantification of peptides/proteins with the glycans still attached) is gaining interest. The study of protein glycosylation require

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40

Naidoo, K. J., D. Denysyk, and J. W. Brady. "Molecular dynamics simulations of the N-linked oligosaccharide of the lectin from Erythrina corallodendron." Protein Engineering Design and Selection 10, no. 11 (1997): 1249–61. http://dx.doi.org/10.1093/protein/10.11.1249.

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41

Ray, L. Bryan. "Providing for protein synthesis." Science 372, no. 6545 (2021): 929.14–929. http://dx.doi.org/10.1126/science.372.6545.929-n.

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42

Szuromi, Phil. "Probing protein-nanorod aggregates." Science 365, no. 6460 (2019): 1414.14–1416. http://dx.doi.org/10.1126/science.365.6460.1414-n.

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43

Eldeeb, Mohamed A., Luana C. A. Leitao, and Richard P. Fahlman. "Emerging branches of the N-end rule pathways are revealing the sequence complexities of N-termini dependent protein degradation." Biochemistry and Cell Biology 96, no. 3 (2018): 289–94. http://dx.doi.org/10.1139/bcb-2017-0274.

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The N-end rule links the identity of the N-terminal amino acid of a protein to its in vivo half-life, as some N-terminal residues confer metabolic instability to a protein via their recognition by the cellular machinery that targets them for degradation. Since its discovery, the N-end rule has generally been defined as set of rules of whether an N-terminal residue is stabilizing or not. However, recent studies are revealing that the N-terminal code of amino acids conferring protein instability is more complex than previously appreciated, as recent investigations are revealing that the identity

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44

Mefleh, Marina, Rosella Motzo, Marie-Franҫoise Samson, Marie-Hélène Morel, and Francesco Giunta. "N Partitioning between Gluten Fractions in a Set of Italian Durum Wheat Cultivars: Role of the Grain N Content." Foods 9, no. 11 (2020): 1684. http://dx.doi.org/10.3390/foods9111684.

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Grain protein content constitutes a key quality trait for durum wheat end-products and may also impact grain protein composition. A total of sixteen durum wheat cultivars were analyzed in a field trial during two seasons at two nitrogen (N) levels to evaluate whether and to what extent the variation in total grain N was associated with variation in the quantity of the various protein fractions and grain quality parameters. Genotypic variation in grain N content correlated with the variation in the content of all three protein fractions, although the strength of the correlation with gliadin and

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45

Rezwan, Mandana, and Daniel Auerbach. "Yeast “N”-hybrid systems for protein–protein and drug–protein interaction discovery." Methods 57, no. 4 (2012): 423–29. http://dx.doi.org/10.1016/j.ymeth.2012.06.006.

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46

Kainz, Elke, Andreas Gallmetzer, Christian Hatzl, et al. "N-Glycan Modification in Aspergillus Species." Applied and Environmental Microbiology 74, no. 4 (2007): 1076–86. http://dx.doi.org/10.1128/aem.01058-07.

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ABSTRACT The production by filamentous fungi of therapeutic glycoproteins intended for use in mammals is held back by the inherent difference in protein N-glycosylation and by the inability of the fungal cell to modify proteins with mammalian glycosylation structures. Here, we report protein N-glycan engineering in two Aspergillus species. We functionally expressed in the fungal hosts heterologous chimeric fusion proteins containing different localization peptides and catalytic domains. This strategy allowed the isolation of a strain with a functional α-1,2-mannosidase producing increased amou

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47

Valentine, William M., Venkataraman Amarnath, Kalyani Amarnath, Fred Rimmele, and Doyle G. Graham. "Carbon Disulfide Mediated Protein Crosslinking by N,N-Diethyldithiocarbamate." Chemical Research in Toxicology 8, no. 1 (1995): 96–102. http://dx.doi.org/10.1021/tx00043a013.

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48

Parks, Anastacia R., and Jorge C. Escalante-Semerena. "Modulation of the bacterial CobB sirtuin deacylase activity by N-terminal acetylation." Proceedings of the National Academy of Sciences 117, no. 27 (2020): 15895–901. http://dx.doi.org/10.1073/pnas.2005296117.

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In eukaryotic cells, the N-terminal amino moiety of many proteins is modified by N-acetyltransferases (NATs). This protein modification can alter the folding of the target protein; can affect binding interactions of the target protein with substrates, allosteric effectors, or other proteins; or can trigger protein degradation. In prokaryotes, only ribosomal proteins are known to be N-terminally acetylated, and the acetyltransferases responsible for this modification belong to the Rim family of proteins. Here, we report that, inSalmonella enterica, the sirtuin deacylase CobB long isoform (CobBL

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49

Yancey, Paul H. "Trimethylamine N-Oxide (TMAO): a Unique Counteracting Osmolyte?" Paracelsus Proceedings of Experimental Medicine 2, S1 (2023): 67–91. http://dx.doi.org/10.33594/000000661.

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Cells of many organisms facing osmotic shrinkage or swelling undergo homeostatic volume regulation using osmolytes—inorganic ions (Na+, K+, Cl-) in transient disturbances, but special organic osmolytes in long-term disturbances. Neutral amino acids, methylamines and polyols are key examples. Widely termed 'compatible' cosolutes/cosolvents, they—unlike inorganic ions—do not perturb membrane potential nor (supposedly) macromolecules. Indeed, most enhance protein stability in part through preferential exclusion; i.e., they 'dissolve' poorly in proteins' hydration layer and reduce water availabili

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Utsumi, Toshihikto, Masahiro Sato, and Rumi Ishisaka. "Analysis of N-terminal sequence requirements for protein N-myristoylation and protein N-acetylation by in vitro translation system." Biochemical Society Transactions 28, no. 5 (2000): A355. http://dx.doi.org/10.1042/bst028a355b.

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