Relevant bibliographies by topics / Serine octamers

Academic literature on the topic 'Serine octamers'

Author: Grafiati
Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "Serine octamers"

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Nanita, Sergio C., and R. Graham Cooks. "Negatively-Charged Halide Adducts of Homochiral Serine Octamers." Journal of Physical Chemistry B 109, no. 10 (March 2005): 4748–53. http://dx.doi.org/10.1021/jp046653+.

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2

Takats, Zoltan, Sergio C. Nanita, Gitta Schlosser, Karoly Vekey, and R. Graham Cooks. "Atmospheric Pressure Gas-Phase H/D Exchange of Serine Octamers." Analytical Chemistry 75, no. 22 (November 2003): 6147–54. http://dx.doi.org/10.1021/ac034284s.

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Nanita, Sergio C., and R. Graham Cooks. "Serine Octamers: Cluster Formation, Reactions, and Implications for Biomolecule Homochirality." Angewandte Chemie International Edition 45, no. 4 (January 16, 2006): 554–69. http://dx.doi.org/10.1002/anie.200501328.

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Liao, Guanhua, Yijie Yang, and Xianglei Kong. "Chirality effects on proline-substituted serine octamers revealed by infrared photodissociation spectroscopy." Phys. Chem. Chem. Phys. 16, no. 4 (2014): 1554–58. http://dx.doi.org/10.1039/c3cp53469c.

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Yan, C., and T. Mélèse. "Multiple regions of NSR1 are sufficient for accumulation of a fusion protein within the nucleolus." Journal of Cell Biology 123, no. 5 (December 1, 1993): 1081–91. http://dx.doi.org/10.1083/jcb.123.5.1081.

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NSR1, a 67-kD nucleolar protein, was originally identified in our laboratory as a nuclear localization signal binding protein, and has subsequently been found to be involved in ribosome biogenesis. NSR1 has three regions: an acidic/serine-rich NH2 terminus, two RNA recognition motifs, and a glycine/arginine-rich COOH terminus. In this study we show that NSR1 itself has a bipartite nuclear localization sequence. Deletion of either basic amino acid stretch results in the mislocation of NSR1 to the cytoplasm. We further demonstrate that either of two regions, the NH2 terminus or both RNA recognition motifs, are sufficient to localize a bacterial protein, beta-galactosidase, to the nucleolus. Intensive deletion analysis has further defined a specific acidic/serine-rich region within the NH2 terminus as necessary for nucleolar accumulation rather than nucleolar targeting. In addition, deletion of either RNA recognition motif or point mutations in one of the RNP consensus octamers results in the mislocalization of a fusion protein within the nucleus. Although the glycine/arginine-rich region in the COOH terminus is not sufficient to bring beta-galactosidase to the nucleolus, our studies show that this domain is necessary for nucleolar accumulation when an RNP consensus octamer in one of the RNA recognition motifs is mutated. Our findings are consistent with the notion that nucleolar localization is a result of the binding interactions of various domains of NSR1 within the nucleolus rather than the presence of a specific nucleolar targeting signal.
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Vandenbussche, Sophie, Guy Vandenbussche, Jacques Reisse, and Kristin Bartik. "Do Serine Octamers Exist in Solution? Relevance of this Question in the Context of the Origin of Homochirality on Earth." European Journal of Organic Chemistry 2006, no. 14 (July 2006): 3069–73. http://dx.doi.org/10.1002/ejoc.200600370.

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7

Criglar, Jeanette M., Ramakrishnan Anish, Liya Hu, Sue E. Crawford, Banumathi Sankaran, B. V. Venkataram Prasad, and Mary K. Estes. "Phosphorylation cascade regulates the formation and maturation of rotaviral replication factories." Proceedings of the National Academy of Sciences 115, no. 51 (December 3, 2018): E12015—E12023. http://dx.doi.org/10.1073/pnas.1717944115.

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The rotavirus (RV) genome is replicated and packaged into virus progeny in cytoplasmic inclusions called viroplasms, which require interactions between RV nonstructural proteins NSP2 and NSP5. How viroplasms form remains unknown. We previously found two forms of NSP2 in RV-infected cells: a cytoplasmically dispersed dNSP2, which interacts with hypophosphorylated NSP5; and a viroplasm-specific vNSP2, which interacts with hyperphosphorylated NSP5. Other studies report that CK1α, a ubiquitous cellular kinase, hyperphosphorylates NSP5, but requires NSP2 for reasons that are unclear. Here we show that silencing CK1α in cells before RV infection resulted in (i) >90% decrease in RV replication, (ii) disrupted vNSP2 and NSP5 interaction, (iii) dispersion of vNSP2 throughout the cytoplasm, and (iv) reduced vNSP2 protein levels. Together, these data indicate that CK1α directly affects NSP2. Accordingly, an in vitro kinase assay showed that CK1α phosphorylates serine 313 of NSP2 and triggers NSP2 octamers to form a lattice structure as demonstrated by crystallographic analysis. Additionally, a dual-specificity autokinase activity for NSP2 was identified and confirmed by mass spectrometry. Together, our studies show that phosphorylation of NSP2 involving CK1α controls viroplasm assembly. Considering that CK1α plays a role in the replication of other RNA viruses, similar phosphorylation-dependent mechanisms may exist for other virus pathogens that require cytoplasmic virus factories for replication.
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8

Jordan, Jacob S., and Evan R. Williams. "Dissociation of large gaseous serine clusters produces abundant protonated serine octamer." Analyst 146, no. 8 (2021): 2617–25. http://dx.doi.org/10.1039/d1an00273b.

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9

Takáts, Zoltán, and R. Graham Cooks. "Thermal formation of serine octamer ions." Chem. Commun., no. 4 (2004): 444–45. http://dx.doi.org/10.1039/b316768b.

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10

Scutelnic, Valeriu, Marta A. S. Perez, Mateusz Marianski, Stephan Warnke, Aurelien Gregor, Ursula Rothlisberger, Michael T. Bowers, et al. "The Structure of the Protonated Serine Octamer." Journal of the American Chemical Society 140, no. 24 (April 11, 2018): 7554–60. http://dx.doi.org/10.1021/jacs.8b02118.

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Book chapters on the topic "Serine octamers"

1

Schnyder, Thomas, Andreas Engel, Heinz Gross, Hans M. Eppenberger, and Theo Wallimann. "Mitochondrial Creatine Kinase (Mi-CK) Forms Octameric Molecules: Structure-Function Relationship and Implications for the CP-Shuttle." In Springer Series in Biophysics, 39–41. Berlin, Heidelberg: Springer Berlin Heidelberg, 1989. http://dx.doi.org/10.1007/978-3-642-73925-5_6.

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