Yann A.P. Bilbille

Works (4)

Updated: July 5th, 2023 15:50

2015 journal article

NMR-based structural analysis of threonylcarbamoyl-AMP synthase and Its substrate interactions

Journal of Biological Chemistry, 290(33), 20032–20043.

By: K. Harris, B. Bobay, K. Sarachan, A. Sims, Y. Bilbille, C. Deutsch, D. Iwata-Reuyl, P. Agris

Source: NC State University Libraries
Added: August 6, 2018

2012 article

Modifications Modulate Anticodon Loop Dynamics and Codon Recognition of E. coli tRNAArg1,2

Cantara, W. A., Bilbille, Y., Kim, J., Kaiser, R., Leszczyńska, G., Malkiewicz, A., & Agris, P. F. (2012, January 3). Journal of Molecular Biology.

By: W. Cantara n, Y. Bilbille n, J. Kim  n, R. Kaiser*, G. Leszczyńska *, A. Malkiewicz*, P. Agris *

author keywords: 2-thiocytidine; inosine; 2-methyladenosine; RNA structure; RNA function
MeSH headings : Anticodon / chemistry; Base Pairing; Binding Sites; Circular Dichroism; Codon / chemistry; Crystallography, X-Ray; Escherichia coli / genetics; Escherichia coli / metabolism; Escherichia coli Proteins / chemistry; Nucleic Acid Conformation; Protein Conformation; Protein Isoforms / chemistry; Protein Processing, Post-Translational; RNA, Transfer, Arg / chemistry; Thermodynamics
topics (OpenAlex): RNA and protein synthesis mechanisms; RNA modifications and cancer; Genomics and Phylogenetic Studies
TL;DR: The results suggest that, by allowing loop flexibility, the modifications modulate the conformation of the ASL(Arg1,2), which takes one structure free in solution and two others when bound to the cognate arginyl-tRNA synthetase or to codons on the ribosome where modifications reduce or restrict binding to specific codons. (via Semantic Scholar)
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Source: Web Of Science
Added: August 6, 2018

2011 journal article

YrdC exhibits properties expected of a subunit for a tRNA threonylcarbamoyl transferase

RNA, 17(9), 1678–1687.

By: K. Harris, V. Jones, Y. Bilbille, M. Swairjo & P. Agris

Source: NC State University Libraries
Added: August 6, 2018

2009 article

The structure of the human tRNALys3 anticodon bound to the HIV genome is stabilized by modified nucleosides and adjacent mismatch base pairs

Bilbille, Y., Vendeix, F. A. P., Guenther, R., Malkiewicz, A., Ariza, X., Vilarrasa, J., & Agris, P. F. (2009, March 26). Nucleic Acids Research.

By: Y. Bilbille n, F. Vendeix n, R. Guenther n, A. Malkiewicz n, X. Ariza  n, J. Vilarrasa  n, P. Agris n

MeSH headings : Anticodon / chemistry; Base Pair Mismatch; Base Sequence; Carbohydrates / chemistry; Genome, Viral; HIV-1 / genetics; Humans; Models, Molecular; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Protons; Pseudouridine / chemistry; RNA, Transfer, Lys / chemistry; RNA, Viral / chemistry; Thermodynamics; Thiouridine / analogs & derivatives; Thiouridine / chemistry
topics (OpenAlex): RNA and protein synthesis mechanisms; RNA modifications and cancer; RNA Research and Splicing
TL;DR: The thermal stabilities of variously modified tRNA anticodon region sequences bound to the Loop I of viral sub(sero)types G and B were analyzed and the structure of one duplex containing two modified nucleosides was determined using NMR spectroscopy and restrained molecular dynamics. (via Semantic Scholar)
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10. Reduced Inequalities (OpenAlex)
Source: Web Of Science
Added: August 6, 2018

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