Zobrazeno 1 - 10
of 78
pro vyhledávání: '"Christine M Dunham"'
Autor:
Eric D Hoffer, Samuel Hong, S Sunita, Tatsuya Maehigashi, Ruben L Gonzalez Jnr, Paul C Whitford, Christine M Dunham
Publikováno v:
eLife, Vol 9 (2020)
Modifications in the tRNA anticodon loop, adjacent to the three-nucleotide anticodon, influence translation fidelity by stabilizing the tRNA to allow for accurate reading of the mRNA genetic code. One example is the N1-methylguanosine modification at
Externí odkaz:
https://doaj.org/article/fb608c54b875484f9b3f925b14cc674c
Autor:
Jeremy Monroe, Daniel E. Eyler, Lili Mitchell, Indrajit Deb, Abigail Bojanowski, Pooja Srinivas, Christine M. Dunham, Bijoyita Roy, Aaron T. Frank, Kristin S. Koutmou
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-11 (2024)
Abstract The ribosome utilizes hydrogen bonding between mRNA codons and aminoacyl-tRNAs to ensure rapid and accurate protein production. Chemical modification of mRNA nucleobases can adjust the strength and pattern of this hydrogen bonding to alter p
Externí odkaz:
https://doaj.org/article/50975c01401849b98fd36770145e907c
Autor:
Neeraja Marathe, Ha An Nguyen, John N. Alumasa, Alexandra B. Kuzmishin Nagy, Michael Vazquez, Christine M. Dunham, Kenneth C. Keiler
Publikováno v:
mBio, Vol 14, Iss 5 (2023)
ABSTRACT trans-Translation is conserved throughout bacteria and is essential in many species. High-throughput screening identified a tetrazole-based trans-translation inhibitor, KKL-55, that has broad-spectrum antibiotic activity. A biotinylated vers
Externí odkaz:
https://doaj.org/article/3798d2a02c844a40a0b3917376c78437
Autor:
Zachary D. Aron, Atousa Mehrani, Eric D. Hoffer, Kristie L. Connolly, Pooja Srinivas, Matthew C. Torhan, John N. Alumasa, Mynthia Cabrera, Divya Hosangadi, Jay S. Barbor, Steven C. Cardinale, Steven M. Kwasny, Lucas R. Morin, Michelle M. Butler, Timothy J. Opperman, Terry L. Bowlin, Ann Jerse, Scott M. Stagg, Christine M. Dunham, Kenneth C. Keiler
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
Antibiotic-resistant bacterial pathogens pose a substantial threat to human health. Here, aided by structural analyses, the authors describe the molecular mechanism behind the activity of a series of compounds that inhibit trans-translation and are e
Externí odkaz:
https://doaj.org/article/65f0e506e42e4cd09c551a4db2d7e630
Autor:
Pooja Srinivas, Meisam Nosrati, Natalia Zelinskaya, Debayan Dey, Lindsay R. Comstock, Christine M. Dunham, Graeme L. Conn
Publikováno v:
bioRxiv
Acquired ribosomal RNA (rRNA) methylation has emerged as a significant mechanism of aminoglycoside resistance in pathogenic bacterial infections. Modification of a single nucleotide in the ribosome decoding center by the aminoglycoside-resistance 16S
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f36a7687d6663ee93546431136a6f16f
https://europepmc.org/articles/PMC10054953/
https://europepmc.org/articles/PMC10054953/
Autor:
William E. Pierson, Eric D. Hoffer, Hannah E. Keedy, Carrie L. Simms, Christine M. Dunham, Hani S. Zaher
Publikováno v:
Cell Reports, Vol 17, Iss 1, Pp 11-18 (2016)
Termination of protein synthesis on the ribosome is catalyzed by release factors (RFs), which share a conserved glycine-glycine-glutamine (GGQ) motif. The glutamine residue is methylated in vivo, but a mechanistic understanding of its contribution to
Externí odkaz:
https://doaj.org/article/5228e4d5939042f3a623ac302f9605bb
Publikováno v:
bioRxiv
Rapid and accurate translation is essential in all organisms to produce properly folded and functional proteins. mRNA codons that define the protein coding sequences are decoded by tRNAs on the ribosome in the aminoacyl (A) binding site. The mRNA cod
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8cf7ee710891464d3871d6e39cd910b5
https://doi.org/10.1101/2023.01.28.526049
https://doi.org/10.1101/2023.01.28.526049
Autor:
Asem Hassan, Sandra Byju, Frederico Campos Freitas, Claude Roc, Nisaa Pender, Kien Nguyen, Evelyn M Kimbrough, Jacob M Mattingly, Ruben L Gonzalez Jr., Ronaldo Junio de Oliveira, Christine M Dunham, Paul C Whitford
Publikováno v:
Nucleic acids research.
Protein synthesis by the ribosome involves large-scale rearrangements of the “small” subunit (SSU; ∼1 MDa), which include inter- and intra-subunit rotational motions. With more than 1000 structures of ribosomes and ribosomal subunits now public
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::30ebc0bd5935557c1b2013f2756e7541
https://pubmed.ncbi.nlm.nih.gov/36583339
https://pubmed.ncbi.nlm.nih.gov/36583339
Publikováno v:
Bioessays
Bacteria use trans-translation to rescue stalled ribosomes and target incomplete proteins for proteolysis. Despite similarities between tRNAs and transfer-messenger RNA (tmRNA), the key molecule for trans-translation, new structural and biochemical d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a715a5c46d827bcdd8602200c388fecc
https://europepmc.org/articles/PMC9308750/
https://europepmc.org/articles/PMC9308750/
Autor:
Zane T, Laughlin, Suparno, Nandi, Debayan, Dey, Natalia, Zelinskaya, Marta A, Witek, Pooja, Srinivas, Ha An, Nguyen, Emily G, Kuiper, Lindsay R, Comstock, Christine M, Dunham, Graeme L, Conn
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 119(14)
Changes in bacterial ribosomal RNA (rRNA) methylation status can alter the activity of diverse groups of ribosome-targeting antibiotics. These modifications are typically incorporated by a single methyltransferase that acts on one nucleotide target a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::08fd42be2df7e73cd6d00fa51f067dd0
https://pubmed.ncbi.nlm.nih.gov/35357969
https://pubmed.ncbi.nlm.nih.gov/35357969