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Mashup Score: 0
A structural model of a K-Ras nanocluster that promotes the stability and accessibility of active K-Ras and creates composite interfaces that facilitate Raf binding provides a framework to unravel MAPK signaling.
Categories: Latest Headlines, Oncologists2Tweet
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Mashup Score: 108Mechanism of molnupiravir-induced SARS-CoV-2 mutagenesis - Nature Structural & Molecular Biology - 3 year(s) ago
Quantitative biochemical assays and high-resolution cryo-EM analysis reveal how the COVID-19 antiviral drug candidate molnupiravir causes lethal viral mutagenesis by the RNA-dependent RNA polymerase (RdRp) of SARS-CoV-2.
Categories: Infectious Disease, Latest HeadlinesTweet-
Mechanism of molnupiravir-induced SARS-CoV-2 mutagenesis Excellent paper summarizing the very interesting proposed mechanism of action @NatureSMB https://t.co/omXcQdqt0x
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Mashup Score: 233
Molnupiravir, a wide-spectrum antiviral that is currently in phase 2/3 clinical trials for the treatment of COVID-19, is proposed to inhibit viral replication by a mechanism known as ‘lethal mutagenesis’. Two recently published studies reveal the biochemical and structural bases of how molnupiravir disrupts the fidelity of SARS-CoV-2 genome replication and prevents viral propagation by fostering…
Categories: Expert Picks, Latest HeadlinesTweet-
Molnupiravir is a broad spectrum anti-viral that achieves "lethal mutagenesis" of #SARSCoV2. Unlike remdesivir, it's a pill, it's not repurposed, had solid data from a Phase 2 trial supporting potency + safety vs Covid https://t.co/TpDUE3Ty1e @nature The mechanism of action 👇 https://t.co/jWET5JJKrJ
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Mashup Score: 24
The frameshift stimulation element (FSE) of coronaviruses is an RNA structure that is required for balanced expression of viral proteins and is thus a promising drug target. A structure of the SARS-CoV-2 FSE serves as a guide for the development of antisense oligonucleotides that impair virus replication.
Categories: General Medicine Journals and Societies, Latest HeadlinesTweet-
A structure of the SARS-CoV-2 frameshift stimulation element serves as a guide for the development of antisense oligonucleotides that impair virus replication, according to a @NatureSMB. paper https://t.co/K24JvzH1sD https://t.co/tEhEpezgfa
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Mashup Score: 42Mechanism of molnupiravir-induced SARS-CoV-2 mutagenesis - Nature Structural & Molecular Biology - 3 year(s) ago
Quantitative biochemical assays and high-resolution cryo-EM analysis reveal how the COVID-19 antiviral drug candidate molnupiravir causes lethal viral mutagenesis by the RNA-dependent RNA polymerase (RdRp) of SARS-CoV-2.
Categories: General Medicine Journals and Societies, Latest HeadlinesTweet-
A study in @NatureSMB reveals how the COVID-19 antiviral drug candidate molnupiravir causes lethal viral mutagenesis by the RNA-dependent RNA polymerase (RdRp) of SARS-CoV-2. https://t.co/s6wkd2vu1D https://t.co/aGJZv8PxxT
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Mashup Score: 9
The folding of ribosomal RNAs is central to the biogenesis of the mitoribosome and is a complex, stepwise process. Five recent cryo-EM studies detail the late steps of the folding and maturation of the human mitoribosomal large subunit RNA that forms the catalytic core of the ribosome: the peptidyl transferase center (PTC).
Categories: General Medicine News, Latest HeadlinesTweet-
An @NatureSMB News and Views article by @Hashemyaser4 and @SisslerM, covering recent insights into mitoribosome assembly (including four @NatureComms papers). https://t.co/I1pIQeIwLo https://t.co/uBzm1M6XPO
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Mashup Score: 20
The folding of ribosomal RNAs is central to the biogenesis of the mitoribosome and is a complex, stepwise process. Five recent cryo-EM studies detail the late steps of the folding and maturation of the human mitoribosomal large subunit RNA that forms the catalytic core of the ribosome: the peptidyl transferase center (PTC).
Categories: General Medicine News, Latest HeadlinesTweet-
An @NatureSMB News and Views article by @Hashemyaser4 and @SisslerM, covering recent insights into mitoribosome assembly (including four @NatureComms papers). https://t.co/I1pIQeIwLo https://t.co/CmHbNeWQHr
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Mashup Score: 42Effect of SARS-CoV-2 B.1.1.7 mutations on spike protein structure and function - Nature Structural & Molecular Biology - 3 year(s) ago
Cryo-EM structures and functional analyses of the SARS-CoV-2 B.1.1.7 variant spike protein reveal that the A570D mutation creates a molecular switch to regulate up-down conformations of the ACE2 receptor-binding domain through a pedal-bin-like mechanism.
Categories: General Medicine Journals and Societies, Latest HeadlinesTweet-
Analyses of the SARS-CoV-2 B.1.1.7 variant spike protein published in @NatureSMB reveal that the A570D mutation creates a molecular switch to regulate up-down conformations of the ACE2 receptor-binding domain through a pedal-bin-like mechanism. https://t.co/G1Q7vYqLsu https://t.co/VHQT6goalx
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Mashup Score: 68Mechanism of molnupiravir-induced SARS-CoV-2 mutagenesis - Nature Structural & Molecular Biology - 3 year(s) ago
Quantitative biochemical assays and high-resolution cryo-EM analysis reveal how the COVID-19 antiviral drug candidate molnupiravir causes lethal viral mutagenesis by the RNA-dependent RNA polymerase (RdRp) of SARS-CoV-2.
Categories: General Medicine Journals and Societies, Latest HeadlinesTweet-
A study in @NatureSMB reveals how the COVID-19 antiviral drug candidate molnupiravir causes lethal viral mutagenesis by the RNA-dependent RNA polymerase (RdRp) of SARS-CoV-2. https://t.co/s2saMQZueN https://t.co/iLaW0ep5hI
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Mashup Score: 1Cryo-EM structure of SARS-CoV-2 ORF3a in lipid nanodiscs - 3 year(s) ago
A cryo-EM structure of SARS-CoV-2 ORF3a reveals a new fold conserved in coronaviruses, and functional experiments show ion channel activity that may be important for viral infectivity.
Categories: General Medicine Journals and Societies, Latest HeadlinesTweet-
A cryo-EM structure of SARS-CoV-2 ORF3a reveals a new fold conserved in coronaviruses, and functional experiments show ion channel activity that may be important for viral infectivity, according to a @NatureSMB paper. https://t.co/5nkqqcckwk https://t.co/GpppQw6VCa
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A structural model of a Ras–Raf signalosome | Nature Structural & Molecular Biology https://t.co/84Neqjd6YY