Zobrazeno 1 - 10
of 135
pro vyhledávání: '"Albert E. Dahlberg"'
Autor:
Stephen W. Mamber, Steven Krakowka, Jeffrey Osborn, Lloyd Saberski, Ryan G. Rhodes, Albert E. Dahlberg, Sunthorn Pond-Tor, Kara Fitzgerald, Neal Wright, Sarah Beseme, John McMichael
Publikováno v:
mSphere, Vol 5, Iss 3 (2020)
ABSTRACT Severe acute respiratory syndrome coronavirus 2 (SARS coronavirus 2, or SARS-CoV-2) is the cause of the respiratory infection known as COVID-19. From an immunopathological standpoint, coronaviruses such as SARS-CoV-2 induce increased levels
Externí odkaz:
https://doaj.org/article/81da9025ab0c4ccba0540c14f25f6b2a
Autor:
Steven Krakowka, Kara Fitzgerald, Ryan G. Rhodes, Sunthorn Pond-Tor, John Mcmichael, Jeffrey L. Osborn, Albert E. Dahlberg, Sarah Beseme, Lloyd Saberski, Stephen W. Mamber, Neal Wright
Publikováno v:
mSphere
mSphere, Vol 5, Iss 3 (2020)
mSphere, Vol 5, Iss 3, p e00288-20 (2020)
mSphere, Vol 5, Iss 3 (2020)
mSphere, Vol 5, Iss 3, p e00288-20 (2020)
Severe acute respiratory syndrome coronavirus 2 (SARS coronavirus 2, or SARS-CoV-2) is the cause of the respiratory infection known as COVID-19. From an immunopathological standpoint, coronaviruses such as SARS-CoV-2 induce increased levels of a vari
Autor:
Jennifer F. Carr, Steven T. Gregory, Gerwald Jogl, Jacqueline L. Connetti, Albert E. Dahlberg
Publikováno v:
Journal of Bacteriology. 196:3776-3783
During protein synthesis, the ribosome undergoes conformational transitions between functional states, requiring communication between distant structural elements of the ribosome. Despite advances in ribosome structural biology, identifying the prote
Autor:
Frank V. Murphy, Eileen L. Murphy, Jacqueline L. Connetti, Steven T. Gregory, Gerwald Jogl, Hasan DeMirci, Albert E. Dahlberg
Publikováno v:
Antimicrobial Agents and Chemotherapy. 58:4308-4317
Streptomycin is a bactericidal antibiotic that induces translational errors. It binds to the 30S ribosomal subunit, interacting with ribosomal protein S12 and with 16S rRNA through contacts with the phosphodiester backbone. To explore the structural
Autor:
Hasan DeMirci, Steven T. Gregory, Jennifer F. Carr, Albert E. Dahlberg, Eileen L. Murphy, Gerwald Jogl, Leyi Wang, Frank V. Murphy, Scott C. Blanchard
Publikováno v:
RNA. 19:1791-1801
The ribosome decodes mRNA by monitoring the geometry of codon–anticodon base-pairing using a set of universally conserved 16S rRNA nucleotides within the conformationally dynamic decoding site. By applying single-molecule FRET and X-ray crystallogr
Capreomycin susceptibility is increased by TlyA-directed 2′-O-methylation on both ribosomal subunits
Publikováno v:
Molecular Microbiology. 85:1194-1203
The binding site of the cyclic peptide antibiotics capreomycin and viomycin is located on the ribosomal subunit interface close to nucleotides C1409 in 16S rRNA and C1920 in 23S rRNA. In Mycobacterium tuberculosis, the 2'-hydroxyls of both nucleotide
Autor:
Gerwald Jogl, Jennifer F. Carr, Albert E. Dahlberg, Hannah J. Lee, Joshua B. Jaspers, Steven T. Gregory
The bacterial ribosome and its associated translation factors are frequent targets of antibiotics, and antibiotic resistance mutations have been found in a number of these components. Such mutations can potentially interact with one another in unpred
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9df58d5abd934a56132aae4b0210e0b4
https://europepmc.org/articles/PMC4542173/
https://europepmc.org/articles/PMC4542173/
Publikováno v:
Cellular Signalling. 23:1972-1977
Streptolysin O (SLO) is a protein cytotoxin derived from Group A beta-hemolytic streptococci that associates with membranes and permeabilizes cells. Oxidation inactivates SLO, eliminating the characteristic hemolytic and cytotoxic activities. However
Autor:
Hasan DeMirci, Venki Ramakrishnan, Albert E. Dahlberg, Steven T. Gregory, Riccardo Belardinelli, Gerwald Jogl, Frank V. Murphy, Ann C. Kelley
Publikováno v:
RNA. 16:2319-2324
All organisms incorporate post-transcriptional modifications into ribosomal RNA, influencing ribosome assembly and function in ways that are poorly understood. The most highly conserved modification is the dimethylation of two adenosines near the 3
Autor:
Albert E. Dahlberg, Gerwald Jogl, Steven T. Gregory, Claudio O. Gualerzi, Riccardo Belardinelli, Hasan DeMirci, Tanakarn Monshupanee
Publikováno v:
RNA. 15:1693-1704
The RsmG methyltransferase is responsible for N7 methylation of G527 of 16S rRNA in bacteria. Here, we report the identification of the Thermus thermophilus rsmG gene, the isolation of rsmG mutants, and the solution of RsmG X-ray crystal structures a