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 journal article

Modifications Modulate Anticodon Loop Dynamics and Codon Recognition of E. coli tRNA (Arg1,2)

JOURNAL OF MOLECULAR BIOLOGY, 416(4), 579–597.

By: W. Cantara n, Y. Bilbille n, J. Kim n, R. Kaiser*, G. Leszczynska*, 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
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)
UN Sustainable Development Goal Categories
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 journal article

The structure of the human tRNA(Lys3) anticodon bound to the HIV genome is stabilized by modified nucleosides and adjacent mismatch base pairs

NUCLEIC ACIDS RESEARCH, 37(10), 3342–3353.

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
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)
UN Sustainable Development Goal Categories
10. Reduced Inequalities (OpenAlex)
Source: Web Of Science
Added: August 6, 2018

Citation Index includes data from a number of different sources. If you have questions about the sources of data in the Citation Index or need a set of data which is free to re-distribute, please contact us.

Certain data included herein are derived from the Web of Science© and InCites© (2024) of Clarivate Analytics. All rights reserved. You may not copy or re-distribute this material in whole or in part without the prior written consent of Clarivate Analytics.