Results 11 to 20 of about 2,730,472 (338)

DNA polymerase III protein, HolC, helps resolve replication/transcription conflicts

open access: yesMicrobial Cell, 2021
In Escherichia coli, DNA replication is catalyzed by an assembly of proteins, the DNA polymerase III holoenzyme. This complex includes the polymerase and proofreading subunits, the processivity clamp and clamp loader complex.
Susan T. Lovett
doaj   +1 more source

Structure of the RNA-dependent RNA polymerase from COVID-19 virus

open access: yesScience, 2020
The COVID-19 RNA-synthesizing machine Many in the scientific community have mobilized to understand the virus that is causing the global coronavirus disease 2019 (COVID-19) pandemic. Gao et al.
Yan Gao   +27 more
semanticscholar   +1 more source

Structure of the SARS-CoV-2 RNA-dependent RNA polymerase in the presence of favipiravir-RTP

open access: yesProceedings of the National Academy of Sciences of the United States of America, 2021
Significance While the current COVID-19 pandemic continues, the US Food and Drug Administration (FDA) has approved only one drug against the virus—remdesivir.
K. Naydenova   +14 more
semanticscholar   +1 more source

Structural Basis for the Inhibition of the RNA-Dependent RNA Polymerase from SARS-CoV-2 by Remdesivir

open access: yesbioRxiv, 2020
The pandemic of Corona Virus Disease 2019 (COVID-19) caused by SARS-CoV-2 has become a global crisis. The replication of SARS-CoV-2 requires the viral RNA-dependent RNA polymerase (RdRp), a direct target of the antiviral drug, Remdesivir.
W. Yin   +21 more
semanticscholar   +1 more source

Emerging SARS-CoV-2 mutation hot spots include a novel RNA-dependent-RNA polymerase variant

open access: yesJournal of Translational Medicine, 2020
Background SARS-CoV-2 is a RNA coronavirus responsible for the pandemic of the Severe Acute Respiratory Syndrome (COVID-19). RNA viruses are characterized by a high mutation rate, up to a million times higher than that of their hosts.
M. Pachetti   +11 more
semanticscholar   +1 more source

Remdesivir is a direct-acting antiviral that inhibits RNA-dependent RNA polymerase from severe acute respiratory syndrome coronavirus 2 with high potency

open access: yesJournal of Biological Chemistry, 2020
Effective treatments for coronavirus disease 2019 (COVID-19) are urgently needed to control this current pandemic, caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2).
Calvin J. Gordon   +6 more
semanticscholar   +1 more source

Contractions of the C-Terminal Domain of Saccharomyces cerevisiae Rpb1p Are Mediated by Rad5p

open access: yesG3: Genes, Genomes, Genetics, 2020
The C-terminal domain (CTD) is an essential domain of the largest subunit of RNA polymerase II, Rpb1p, and is composed of 26 tandem repeats of a seven-amino acid sequence, YSPTSPS.
Taylor Stewart   +3 more
doaj   +1 more source

The antiviral compound remdesivir potently inhibits RNA-dependent RNA polymerase from Middle East respiratory syndrome coronavirus

open access: yesJournal of Biological Chemistry, 2020
Antiviral drugs for managing infections with human coronaviruses are not yet approved, posing a serious challenge to current global efforts aimed at containing the outbreak of severe acute respiratory syndrome–coronavirus 2 (CoV-2).
Calvin J. Gordon   +4 more
semanticscholar   +1 more source

A roadmap for designing narrow-spectrum antibiotics targeting bacterial pathogens

open access: yesMicrobial Cell, 2022
Clostridioides difficile (Cdiff) infection (CDI) continues to be the leading threat of nosocomial deaths worldwide and a major burden on health-care systems.
Xinyun Cao   +2 more
doaj   +1 more source

Transcription-translation coupling: direct interactions of RNA polymerase with ribosomes and ribosomal subunits. [PDF]

open access: yes, 2017
In prokaryotes, RNA polymerase and ribosomes can bind concurrently to the same RNA transcript, leading to the functional coupling of transcription and translation.
Blaha, Gregor M   +9 more
core   +1 more source

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