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Article: Randomized controlled trials assessing efficacy of brief web-based stress management interventions for college students during the COVID pandemic.

Frazier, Patricia / Liu, Yuchen / Selvey, Alicia / Meredith, Liza / Nguyen-Feng, Viann N

2023 Volume 70, Issue 3, Page(s) 314–324

Abstract: The purpose of this study was to evaluate the efficacy of brief, self-guided web-based interventions for decreasing distress among U.S. college students during the pandemic. Three randomized controlled trials were conducted during the spring (Study 1), ... ...

Abstract	The purpose of this study was to evaluate the efficacy of brief, self-guided web-based interventions for decreasing distress among U.S. college students during the pandemic. Three randomized controlled trials were conducted during the spring (Study 1), summer (Study 2), and fall (Study 3) 2020 terms, and were combined into one sample to increase power (
MeSH term(s)	Humans ; COVID-19 ; Internet-Based Intervention ; Pandemics ; Randomized Controlled Trials as Topic ; Stress, Psychological/prevention & control ; Stress, Psychological/psychology ; Students/psychology
Language	English
Publishing date	2023-01-23
Publishing country	United States
Document type	Journal Article ; Randomized Controlled Trial
ZDB-ID	2066555-6
ISSN	1939-2168 ; 0022-0167
ISSN (online)	1939-2168
ISSN	0022-0167
DOI	10.1037/cou0000652
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Article ; Online: US college student mental health and COVID-19: Comparing pre-pandemic and pandemic timepoints.

Frazier, Patricia / Liu, Yuchen / Asplund, Alexa / Meredith, Liza / Nguyen-Feng, Viann N

Journal of American college health : J of ACH

2021 Volume 71, Issue 9, Page(s) 2686–2696

Abstract: Objective: To assess mental health in US undergraduates during COVID-19; to identify key pandemic-related stressors, perceived control, and coping and their associations with mental health.: Participants: Data collected from a sample of ... ...

Abstract	Objective: To assess mental health in US undergraduates during COVID-19; to identify key pandemic-related stressors, perceived control, and coping and their associations with mental health. Participants: Data collected from a sample of undergraduates in April 2020 ( Methods: Online measures of depression, anxiety, and stress symptoms and perceived control and coping (both samples); pandemic-related stressors and perceived benefits (April 2020). Results: Depression and stress symptoms were higher in April 2020 than in 2017. Most students reported perceiving at least some pandemic-related benefits. Top-rated stressors involved missing seeing friends and school-related stressors. Perceived control and approach coping were lower during the pandemic but related to better mental health; avoidant coping was higher during the pandemic and related to poorer mental health. Conclusions: Findings can inform campuses regarding how to improve student mental health during COVID and beyond.
MeSH term(s)	Humans ; Mental Health ; COVID-19/epidemiology ; Pandemics ; Students ; Universities
Language	English
Publishing date	2021-11-11
Publishing country	United States
Document type	Journal Article
ZDB-ID	604907-2
ISSN	1940-3208 ; 0744-8481
ISSN (online)	1940-3208
ISSN	0744-8481
DOI	10.1080/07448481.2021.1987247
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Article ; Online: Recent insights into the structure and function of coronavirus ribonucleases.

Frazier, Meredith N / Riccio, Amanda A / Wilson, Isha M / Copeland, William C / Stanley, Robin E

FEBS open bio

2022 Volume 12, Issue 9, Page(s) 1567–1583

Abstract: Coronaviruses use approximately two-thirds of their 30-kb genomes to encode nonstructural proteins (nsps) with diverse functions that assist in viral replication and transcription, and evasion of the host immune response. The SARS-CoV-2 pandemic has led ... ...

Abstract	Coronaviruses use approximately two-thirds of their 30-kb genomes to encode nonstructural proteins (nsps) with diverse functions that assist in viral replication and transcription, and evasion of the host immune response. The SARS-CoV-2 pandemic has led to renewed interest in the molecular mechanisms used by coronaviruses to infect cells and replicate. Among the 16 Nsps involved in replication and transcription, coronaviruses encode two ribonucleases that process the viral RNA-an exonuclease (Nsp14) and an endonuclease (Nsp15). In this review, we discuss recent structural and biochemical studies of these nucleases and the implications for drug discovery.
MeSH term(s)	COVID-19 ; Humans ; Mutation ; Ribonucleases ; SARS-CoV-2 ; Viral Nonstructural Proteins/chemistry ; Viral Nonstructural Proteins/genetics ; Viral Nonstructural Proteins/metabolism
Chemical Substances	Viral Nonstructural Proteins ; Ribonucleases (EC 3.1.-)
Language	English
Publishing date	2022-04-29
Publishing country	England
Document type	Journal Article ; Review ; Research Support, N.I.H., Extramural ; Research Support, N.I.H., Intramural
ZDB-ID	2651702-4
ISSN	2211-5463 ; 2211-5463
ISSN (online)	2211-5463
ISSN	2211-5463
DOI	10.1002/2211-5463.13414
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Article: Biochemical Characterization of Emerging SARS-CoV-2 Nsp15 Endoribonuclease Variants.

Wilson, Isha M / Frazier, Meredith N / Li, Jian-Liang / Randall, Thomas A / Stanley, Robin E

bioRxiv : the preprint server for biology

2022

Abstract: ... revealed mutations across Nsp15â€™s three structured domains (N-terminal, Middle, EndoU). Selected Nsp15 ...

Abstract	Global sequencing efforts from the ongoing COVID-19 pandemic, caused by the novel coronavirus SARS-CoV-2, continue to provide insight into the evolution of the viral genome. Coronaviruses encode 16 nonstructural proteins, within the first two-thirds of their genome, that facilitate viral replication and transcription as well as evasion of the host immune response. However, many of these viral proteins remain understudied. Nsp15 is a uridine-specific endoribonuclease conserved across all coronaviruses. The nuclease activity of Nsp15 helps the virus evade triggering an innate immune response. Understanding how Nsp15 has changed over the course of the pandemic, and how mutations affect its RNA processing function, will provide insight into the evolution of an oligomerization-dependent endoribonuclease and inform drug design. In combination with previous structural data, bioinformatics analyses of 1.9+ million SARS-CoV-2 sequences revealed mutations across Nsp15â€™s three structured domains (N-terminal, Middle, EndoU). Selected Nsp15 variants were characterized biochemically and compared to wild type Nsp15. We found that mutations to important catalytic residues decreased cleavage activity but increased the hexamer/monomer ratio of the recombinant protein. Many of the highly prevalent variants we analyzed led to decreased nuclease activity as well as an increase in the inactive, monomeric form. Overall, our work establishes how Nsp15 variants seen in patient samples affect nuclease activity and oligomerization, providing insight into the effect of these variants
Language	English
Publishing date	2022-05-12
Publishing country	United States
Document type	Preprint
DOI	10.1101/2022.05.10.491349
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Article ; Online: Biochemical Characterization of Emerging SARS-CoV-2 Nsp15 Endoribonuclease Variants.

Wilson, Isha M / Frazier, Meredith N / Li, Jian-Liang / Randall, Thomas A / Stanley, Robin E

Journal of molecular biology

2022 Volume 434, Issue 20, Page(s) 167796

Abstract: ... revealed mutations across Nsp15's three structured domains (N-terminal, Middle, EndoU). Selected Nsp15 ...

Abstract	Global sequencing efforts from the ongoing COVID-19 pandemic, caused by the novel coronavirus SARS-CoV-2, continue to provide insight into the evolution of the viral genome. Coronaviruses encode 16 nonstructural proteins, within the first two-thirds of their genome, that facilitate viral replication and transcription as well as evasion of the host immune response. However, many of these viral proteins remain understudied. Nsp15 is a uridine-specific endoribonuclease conserved across all coronaviruses. The nuclease activity of Nsp15 helps the virus evade triggering an innate immune response. Understanding how Nsp15 has changed over the course of the pandemic, and how mutations affect its RNA processing function, will provide insight into the evolution of an oligomerization-dependent endoribonuclease and inform drug design. In combination with previous structural data, bioinformatics analyses of 1.9 + million SARS-CoV-2 sequences revealed mutations across Nsp15's three structured domains (N-terminal, Middle, EndoU). Selected Nsp15 variants were characterized biochemically and compared to wild type Nsp15. We found that mutations to important catalytic residues decreased cleavage activity but increased the hexamer/monomer ratio of the recombinant protein. Many of the highly prevalent variants we analyzed led to decreased nuclease activity as well as an increase in the inactive, monomeric form. Overall, our work establishes how Nsp15 variants seen in patient samples affect nuclease activity and oligomerization, providing insight into the effect of these variants in vivo.
MeSH term(s)	COVID-19/virology ; Endoribonucleases/chemistry ; Endoribonucleases/genetics ; Humans ; Recombinant Proteins/chemistry ; SARS-CoV-2/enzymology ; Uridylate-Specific Endoribonucleases/chemistry ; Uridylate-Specific Endoribonucleases/genetics ; Viral Nonstructural Proteins/chemistry ; Viral Nonstructural Proteins/genetics
Chemical Substances	Recombinant Proteins ; Viral Nonstructural Proteins ; Endoribonucleases (EC 3.1.-) ; Uridylate-Specific Endoribonucleases (EC 3.1.-) ; nidoviral uridylate-specific endoribonuclease (EC 3.1.-)
Language	English
Publishing date	2022-08-19
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Intramural
ZDB-ID	80229-3
ISSN	1089-8638 ; 0022-2836
ISSN (online)	1089-8638
ISSN	0022-2836
DOI	10.1016/j.jmb.2022.167796
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Zs.A 867: Show issues

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Article ; Online: Watching real-time endocytosis in living cells.

Frazier, Meredith N / Jackson, Lauren P

The Journal of cell biology

2017 Volume 216, Issue 1, Page(s) 9–11

Abstract: The precise sequence of events promoting clathrin-coated vesicle assembly is still debated. In this issue, Kadlecova et al. (2017. J. Cell Biol. https://doi.org/10.1083/jcb.201608071) test structural models using quantitative microscopy in living cells ... ...

Abstract	The precise sequence of events promoting clathrin-coated vesicle assembly is still debated. In this issue, Kadlecova et al. (2017. J. Cell Biol. https://doi.org/10.1083/jcb.201608071) test structural models using quantitative microscopy in living cells to investigate the hierarchy and temporal importance of molecular events required for clathrin-coated pit initiation.
MeSH term(s)	Biological Transport ; Clathrin/chemistry ; Clathrin-Coated Vesicles ; Coated Pits, Cell-Membrane ; Endocytosis ; Humans
Chemical Substances	Clathrin
Language	English
Publishing date	2017--02
Publishing country	United States
Document type	Journal Article ; Comment
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.201611115
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Article: Recent insights into the structure and function of coronavirus ribonucleases

Frazier, Meredith N. / Riccio, Amanda A. / Wilson, Isha M. / Copeland, William C. / Stanley, Robin E.

FEBS Open Bio. 2022 Sept., v. 12, no. 9

2022

Abstract: Coronaviruses use approximately two‐thirds of their 30‐kb genomes to encode nonstructural proteins (nsps) with diverse functions that assist in viral replication and transcription, and evasion of the host immune response. The SARS‐CoV‐2 pandemic has led ... ...

Abstract	Coronaviruses use approximately two‐thirds of their 30‐kb genomes to encode nonstructural proteins (nsps) with diverse functions that assist in viral replication and transcription, and evasion of the host immune response. The SARS‐CoV‐2 pandemic has led to renewed interest in the molecular mechanisms used by coronaviruses to infect cells and replicate. Among the 16 Nsps involved in replication and transcription, coronaviruses encode two ribonucleases that process the viral RNA—an exonuclease (Nsp14) and an endonuclease (Nsp15). In this review, we discuss recent structural and biochemical studies of these nucleases and the implications for drug discovery.
Keywords	Severe acute respiratory syndrome coronavirus 2 ; drugs ; genome ; immune response ; pandemic ; ribonucleases ; virus replication
Language	English
Dates of publication	2022-09
Size	p. 1567-1583.
Publishing place	John Wiley & Sons, Ltd
Document type	Article
Note	REVIEW
ZDB-ID	2651702-4
ISSN	2211-5463
ISSN	2211-5463
DOI	10.1002/2211-5463.13414
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Article ; Online: HEPN RNases - an emerging class of functionally distinct RNA processing and degradation enzymes.

Pillon, Monica C / Gordon, Jacob / Frazier, Meredith N / Stanley, Robin E

Critical reviews in biochemistry and molecular biology

2020 Volume 56, Issue 1, Page(s) 88–108

Abstract: HEPN (Higher Eukaryotes and Prokaryotes Nucleotide-binding) RNases are an emerging class of functionally diverse RNA processing and degradation enzymes. Members are defined by a small α-helical bundle encompassing a short consensus RNase motif. HEPN ... ...

Abstract	HEPN (Higher Eukaryotes and Prokaryotes Nucleotide-binding) RNases are an emerging class of functionally diverse RNA processing and degradation enzymes. Members are defined by a small α-helical bundle encompassing a short consensus RNase motif. HEPN dimerization is a universal requirement for RNase activation as the conserved RNase motifs are precisely positioned at the dimer interface to form a composite catalytic center. While the core HEPN fold is conserved, the organization surrounding the HEPN dimer can support large structural deviations that contribute to their specialized functions. HEPN RNases are conserved throughout evolution and include bacterial HEPN RNases such as CRISPR-Cas and toxin-antitoxin associated nucleases, as well as eukaryotic HEPN RNases that adopt large multi-component machines. Here we summarize the canonical elements of the growing HEPN RNase family and identify molecular features that influence RNase function and regulation. We explore similarities and differences between members of the HEPN RNase family and describe the current mechanisms for HEPN RNase activation and inhibition.
MeSH term(s)	Amino Acid Sequence ; Animals ; CRISPR-Cas Systems ; Catalytic Domain ; Endoribonucleases/chemistry ; Endoribonucleases/genetics ; Endoribonucleases/metabolism ; Humans ; Protein Conformation, alpha-Helical ; Protein Multimerization ; Proteolysis ; RNA Processing, Post-Transcriptional ; RNA Stability ; RNA-Binding Proteins/chemistry ; RNA-Binding Proteins/genetics ; RNA-Binding Proteins/metabolism ; Toxin-Antitoxin Systems
Chemical Substances	RNA-Binding Proteins ; Endoribonucleases (EC 3.1.-)
Language	English
Publishing date	2020-12-22
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Intramural ; Review
ZDB-ID	1000977-2
ISSN	1549-7798 ; 1381-3455 ; 1040-9238
ISSN (online)	1549-7798
ISSN	1381-3455 ; 1040-9238
DOI	10.1080/10409238.2020.1856769
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Article ; Online: Flipped over U: structural basis for dsRNA cleavage by the SARS-CoV-2 endoribonuclease.

Frazier, Meredith N / Wilson, Isha M / Krahn, Juno M / Butay, Kevin John / Dillard, Lucas B / Borgnia, Mario J / Stanley, Robin E

Nucleic acids research

2022 Volume 50, Issue 14, Page(s) 8290–8301

Abstract: Coronaviruses generate double-stranded (ds) RNA intermediates during viral replication that can activate host immune sensors. To evade activation of the host pattern recognition receptor MDA5, coronaviruses employ Nsp15, which is a uridine-specific ... ...

Abstract	Coronaviruses generate double-stranded (ds) RNA intermediates during viral replication that can activate host immune sensors. To evade activation of the host pattern recognition receptor MDA5, coronaviruses employ Nsp15, which is a uridine-specific endoribonuclease. Nsp15 is proposed to associate with the coronavirus replication-transcription complex within double-membrane vesicles to cleave these dsRNA intermediates. How Nsp15 recognizes and processes dsRNA is poorly understood because previous structural studies of Nsp15 have been limited to small single-stranded (ss) RNA substrates. Here we present cryo-EM structures of SARS-CoV-2 Nsp15 bound to a 52nt dsRNA. We observed that the Nsp15 hexamer forms a platform for engaging dsRNA across multiple protomers. The structures, along with site-directed mutagenesis and RNA cleavage assays revealed critical insight into dsRNA recognition and processing. To process dsRNA Nsp15 utilizes a base-flipping mechanism to properly orient the uridine within the active site for cleavage. Our findings show that Nsp15 is a distinctive endoribonuclease that can cleave both ss- and dsRNA effectively.
MeSH term(s)	COVID-19 ; Endoribonucleases/metabolism ; Humans ; RNA, Double-Stranded/genetics ; SARS-CoV-2/genetics ; Uridine ; Viral Nonstructural Proteins/metabolism
Chemical Substances	RNA, Double-Stranded ; Viral Nonstructural Proteins ; Endoribonucleases (EC 3.1.-) ; Uridine (WHI7HQ7H85)
Language	English
Publishing date	2022-07-08
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Intramural
ZDB-ID	186809-3
ISSN	1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
ISSN (online)	1362-4962 ; 1362-4954
ISSN	0301-5610 ; 0305-1048
DOI	10.1093/nar/gkac589
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Article: Flipped Over U: Structural Basis for dsRNA Cleavage by the SARS-CoV-2 Endoribonuclease.

Frazier, Meredith N / Wilson, Isha M / Krahn, Juno M / Butay, Kevin John / Dillard, Lucas B / Borgnia, Mario J / Stanley, Robin E

bioRxiv : the preprint server for biology

2022

Abstract	Coronaviruses generate double-stranded (ds) RNA intermediates during viral replication that can activate host immune sensors. To evade activation of the host pattern recognition receptor MDA5, coronaviruses employ Nsp15, which is uridine-specific endoribonuclease. Nsp15 is proposed to associate with the coronavirus replication-transcription complex within double-membrane vesicles to cleave these dsRNA intermediates. How Nsp15 recognizes and processes dsRNA is poorly understood because previous structural studies of Nsp15 have been limited to small single-stranded (ss) RNA substrates. Here we present cryo-EM structures of SARS-CoV-2 Nsp15 bound to a 52nt dsRNA. We observed that the Nsp15 hexamer forms a platform for engaging dsRNA across multiple protomers. The structures, along with site-directed mutagenesis and RNA cleavage assays revealed critical insight into dsRNA recognition and processing. To process dsRNA Nsp15 utilizes a base-flipping mechanism to properly orient the uridine within the active site for cleavage. Our findings show that Nsp15 is a distinctive endoribonuclease that can cleave both ss- and dsRNA effectively.
Language	English
Publishing date	2022-03-02
Publishing country	United States
Document type	Preprint
DOI	10.1101/2022.03.02.480688
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