John Wesley Stuart

Works (3)

Updated: March 10th, 2025 12:14

2003 article

Naturally-occurring Modification Restricts the Anticodon Domain Conformational Space of tRNA Phe

Stuart, J. W., Koshlap, K. M., Guenther, R., & Agris, P. F. (2003, December 1). Journal of Molecular Biology.

By: J. Stuart n, K. Koshlap n, R. Guenther n & P. Agris n

author keywords: methylation; anticodon dynamics; tRNA position 37; codon recognition; frameshifting
MeSH headings : Anticodon; Base Sequence; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Nucleic Acid Conformation; RNA, Transfer, Phe / chemistry
topics (OpenAlex): RNA modifications and cancer; RNA and protein synthesis mechanisms; RNA Research and Splicing
TL;DR: A comparison of the resulting structures indicates that modification of position 37 affects the accuracy of decoding and the maintenance of the mRNA reading frame by restricting anticodon loop conformational space. (via Semantic Scholar)
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Source: Web Of Science
Added: August 6, 2018

2000 article

Functional Anticodon Architecture of Human tRNALys3 Includes Disruption of Intraloop Hydrogen Bonding by the Naturally Occurring Amino Acid Modification, t6A

Stuart, J. W., Gdaniec, Z., Guenther, R., Marszalek, M., Sochacka, E., Malkiewicz, A., & Agris, P. F. (2000, October 10). Biochemistry.

By: J. Stuart n, Z. Gdaniec  n, R. Guenther n, M. Marszalek n, E. Sochacka  n, A. Malkiewicz n, P. Agris n

MeSH headings : Adenosine / analogs & derivatives; Adenosine / chemistry; Adenosine / metabolism; Amino Acid Substitution; Anticodon / chemical synthesis; Anticodon / chemistry; Crystallography, X-Ray; Humans; Hydrogen Bonding; Models, Molecular; Nuclear Magnetic Resonance, Biomolecular / methods; Nucleic Acid Conformation; Protein Binding; Pseudouridine / chemistry; RNA, Transfer, Lys / chemical synthesis; RNA, Transfer, Lys / chemistry; Ribosomal Proteins / chemistry; Thermodynamics; Threonine / chemistry; Threonine / metabolism
topics (OpenAlex): RNA modifications and cancer; RNA and protein synthesis mechanisms; RNA Research and Splicing
TL;DR: From these results, it is concluded that ribosome binding cannot simply be an induced fit of the anticodon stem and loop, otherwise the unmodified ASL(Lys3)(UUU) would bind as well as ASL (Lys 3)(UU U)-t(6)A(37), and the ionized carboxylic acid moiety of t(6), possibly neutralizes the positive charge of A(+)(38). (via Semantic Scholar)
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1997 journal article

Unconventional structure of tRNA(Lys)SUU anticodon explains tRNA's role in bacterial and mammalian ribosomal frameshifting and primer selection by HIV-1

RNA, 3(4), 420–428.

By: P. Agris, R. Guenther, P. Ingram, M. Basti, J. Stuart, E. Sochacka, A. Malkiewicz

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

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