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Article ; Online: "The ubiquitin ligase SIAH2 is a female-specific regulator of circadian rhythms and metabolism".

Mekbib, Tsedey / Suen, Ting-Chung / Rollins-Hairston, Aisha / Smith, Kiandra / Armstrong, Ariel / Gray, Cloe / Owino, Sharon / Baba, Kenkichi / Baggs, Julie E / Ehlen, J Christopher / Tosini, Gianluca / DeBruyne, Jason P

PLoS genetics

2022 Volume 18, Issue 7, Page(s) e1010305

Abstract: Circadian clocks enable organisms to predict and align their behaviors and physiologies to constant daily day-night environmental cycle. Because the ubiquitin ligase Siah2 has been identified as a potential regulator of circadian clock function in ... ...

Abstract	Circadian clocks enable organisms to predict and align their behaviors and physiologies to constant daily day-night environmental cycle. Because the ubiquitin ligase Siah2 has been identified as a potential regulator of circadian clock function in cultured cells, we have used SIAH2-deficient mice to examine its function in vivo. Our experiments demonstrate a striking and unexpected sexually dimorphic effect of SIAH2-deficiency on the regulation of rhythmically expressed genes in the liver. The absence of SIAH2 in females, but not in males, altered the expression of core circadian clock genes and drastically remodeled the rhythmic transcriptome in the liver by increasing the number of day-time expressed genes, and flipping the rhythmic expression from nighttime expressed genes to the daytime. These effects are not readily explained by effects on known sexually dimorphic pathways in females. Moreover, loss of SIAH2 in females, not males, preferentially altered the expression of transcription factors and genes involved in regulating lipid and lipoprotein metabolism. Consequently, SIAH2-deficient females, but not males, displayed disrupted daily lipid and lipoprotein patterns, increased adiposity and impaired metabolic homeostasis. Overall, these data suggest that SIAH2 may be a key component of a female-specific circadian transcriptional output circuit that directs the circadian timing of gene expression to regulate physiological rhythms, at least in the liver. In turn, our findings imply that sex-specific transcriptional mechanisms may closely interact with the circadian clock to tailor overt rhythms for sex-specific needs.
MeSH term(s)	Animals ; Circadian Clocks/genetics ; Circadian Rhythm/genetics ; Female ; Lipids ; Lipoproteins ; Male ; Mice ; Ubiquitin ; Ubiquitin-Protein Ligases/genetics
Chemical Substances	Lipids ; Lipoproteins ; Ubiquitin ; Siah2 protein, mouse (EC 2.3.2.27) ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
Language	English
Publishing date	2022-07-05
Publishing country	United States
Document type	Journal Article
ZDB-ID	2186725-2
ISSN	1553-7404 ; 1553-7390
ISSN (online)	1553-7404
ISSN	1553-7390
DOI	10.1371/journal.pgen.1010305
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Article ; Online: Genomics and systems approaches in the mammalian circadian clock.

Baggs, Julie E / Hogenesch, John B

Current opinion in genetics & development

2010 Volume 20, Issue 6, Page(s) 581–587

Abstract: The circadian clock is an endogenous oscillator that regulates daily rhythms in behavior and physiology. In recent years, systems biology and genomics approaches re-shaped our view of the clock. Our understanding of outputs that regulate behavior and ... ...

Abstract	The circadian clock is an endogenous oscillator that regulates daily rhythms in behavior and physiology. In recent years, systems biology and genomics approaches re-shaped our view of the clock. Our understanding of outputs that regulate behavior and physiology has been enhanced through gene expression profiling and proteomic analyses. Systems approaches uncovered underlying principles of transcriptional regulation and robustness of the oscillator through perturbation analysis and synthetic methods. Finally, new clock components and modifiers were identified through cell-based screening efforts and proteomics.
MeSH term(s)	Animals ; Circadian Rhythm ; Genomics ; Humans ; Systems Biology
Language	English
Publishing date	2010-10-06
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	1077312-5
ISSN	1879-0380 ; 0959-437X
ISSN (online)	1879-0380
ISSN	0959-437X
DOI	10.1016/j.gde.2010.08.009
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Article ; Online: Polycystin-1 regulates bone development through an interaction with the transcriptional coactivator TAZ.

Merrick, David / Mistry, Kavita / Wu, Jingshing / Gresko, Nikolay / Baggs, Julie E / Hogenesch, John B / Sun, Zhaoxia / Caplan, Michael J

Human molecular genetics

2018 Volume 28, Issue 1, Page(s) 16–30

Abstract: Polycystin-1 (PC1), encoded by the PKD1 gene that is mutated in the autosomal dominant polycystic kidney disease, regulates a number of processes including bone development. Activity of the transcription factor RunX2, which controls osteoblast ... ...

Abstract	Polycystin-1 (PC1), encoded by the PKD1 gene that is mutated in the autosomal dominant polycystic kidney disease, regulates a number of processes including bone development. Activity of the transcription factor RunX2, which controls osteoblast differentiation, is reduced in Pkd1 mutant mice but the mechanism governing PC1 activation of RunX2 is unclear. PC1 undergoes regulated cleavage that releases its C-terminal tail (CTT), which translocates to the nucleus to modulate transcriptional pathways involved in proliferation and apoptosis. We find that the cleaved CTT of PC1 (PC1-CTT) stimulates the transcriptional coactivator TAZ (Wwtr1), an essential coactivator of RunX2. PC1-CTT physically interacts with TAZ, stimulating RunX2 transcriptional activity in pre-osteoblast cells in a TAZ-dependent manner. The PC1-CTT increases the interaction between TAZ and RunX2 and enhances the recruitment of the p300 transcriptional co-regulatory protein to the TAZ/RunX2/PC1-CTT complex. Zebrafish injected with morpholinos directed against pkd1 manifest severe bone calcification defects and a curly tail phenotype. Injection of messenger RNA (mRNA) encoding the PC1-CTT into pkd1-morphant fish restores bone mineralization and reduces the severity of the curly tail phenotype. These effects are abolished by co-injection of morpholinos directed against TAZ. Injection of mRNA encoding a dominant-active TAZ construct is sufficient to rescue both the curly tail phenotype and the skeletal defects observed in pkd1-morpholino treated fish. Thus, TAZ constitutes a key mechanistic link through which PC1 mediates its physiological functions.
MeSH term(s)	Animals ; Apoptosis ; Bone Development/genetics ; Bone Development/physiology ; Cell Differentiation ; E1A-Associated p300 Protein/physiology ; Gene Expression Regulation ; Genes, Regulator ; HEK293 Cells ; Humans ; Intracellular Signaling Peptides and Proteins/physiology ; Kidney/metabolism ; Models, Animal ; Morpholinos ; Osteoblasts/metabolism ; Osteogenesis/physiology ; Polycystic Kidney, Autosomal Dominant/genetics ; TRPP Cation Channels/genetics ; TRPP Cation Channels/physiology ; Transcription Factors ; Zebrafish/genetics ; Zebrafish Proteins/genetics
Chemical Substances	Intracellular Signaling Peptides and Proteins ; Morpholinos ; TRPP Cation Channels ; Transcription Factors ; WWTR1 protein, human ; WWTR1 protein, zebrafish ; Zebrafish Proteins ; polycystic kidney disease 1 protein ; E1A-Associated p300 Protein (EC 2.3.1.48) ; EP300 protein, human (EC 2.3.1.48)
Language	English
Publishing date	2018-09-17
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	1108742-0
ISSN	1460-2083 ; 0964-6906
ISSN (online)	1460-2083
ISSN	0964-6906
DOI	10.1093/hmg/ddy322
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Zs.A 3469: Show issues

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Article ; Online: The network as the target.

Baggs, Julie E / Hughes, Michael E / Hogenesch, John B

Wiley interdisciplinary reviews. Systems biology and medicine

2010 Volume 2, Issue 2, Page(s) 127–133

Abstract: The conventional target centric model of drug discovery is pinned under the weight of prior success and the traditional problems of safety and efficacy for new molecules. An alternative to target centric drug development is to shift focus to the pathways ...

Abstract	The conventional target centric model of drug discovery is pinned under the weight of prior success and the traditional problems of safety and efficacy for new molecules. An alternative to target centric drug development is to shift focus to the pathways that mediate both biology and pathophysiology. This method has the advantage of not requiring a priori knowledge of the small molecule target, but also comes with it several challenges including target determination. We suggest extending this notion more broadly across the drug discovery process using quantitative network structure-activity relationships (QNSAR), and discuss the steps necessary to test the hypothesis that systems biology approaches can be used to improve the drug discovery process.
MeSH term(s)	Algorithms ; Chemistry, Pharmaceutical/methods ; Drug Discovery ; Genome, Human ; Genomics ; Humans ; Proteomics ; Quantitative Structure-Activity Relationship ; Systems Biology
Language	English
Publishing date	2010-03
Publishing country	United States
Document type	Journal Article
ZDB-ID	2503323-2
ISSN	1939-005X ; 1939-5094
ISSN (online)	1939-005X
ISSN	1939-5094
DOI	10.1002/wsbm.57
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Article ; Online: Ubiquitin ligase Siah2 regulates RevErbα degradation and the mammalian circadian clock.

DeBruyne, Jason P / Baggs, Julie E / Sato, Trey K / Hogenesch, John B

Proceedings of the National Academy of Sciences of the United States of America

2015 Volume 112, Issue 40, Page(s) 12420–12425

Abstract: Regulated degradation of proteins by the proteasome is often critical to their function in dynamic cellular pathways. The molecular clock underlying mammalian circadian rhythms relies on the rhythmic expression and degradation of its core components. ... ...

Abstract	Regulated degradation of proteins by the proteasome is often critical to their function in dynamic cellular pathways. The molecular clock underlying mammalian circadian rhythms relies on the rhythmic expression and degradation of its core components. However, because the tools available for identifying the mechanisms underlying the degradation of a specific protein are limited, the mechanisms regulating clock protein degradation are only beginning to be elucidated. Here we describe a cell-based functional screening approach designed to quickly identify the ubiquitin E3 ligases that induce the degradation of potentially any protein of interest. We screened the nuclear hormone receptor RevErbα (Nr1d1), a key constituent of the mammalian circadian clock, for E3 ligases that regulate its stability and found Seven in absentia2 (Siah2) to be a key regulator of RevErbα stability. Previously implicated in hypoxia signaling, Siah2 overexpression destabilizes RevErbα/β, and siRNA depletion of Siah2 stabilizes endogenous RevErbα. Moreover, Siah2 depletion delays circadian degradation of RevErbα and lengthens period length. These results demonstrate the utility of functional screening approaches for identifying regulators of protein stability and reveal Siah2 as a previously unidentified circadian clockwork regulator that mediates circadian RevErbα turnover.
MeSH term(s)	Animals ; Blotting, Western ; Cell Line ; Cell Line, Tumor ; Cells, Cultured ; Circadian Clocks/genetics ; Embryo, Mammalian/cytology ; Fibroblasts/metabolism ; Gene Expression ; Humans ; Mice ; Microscopy, Fluorescence ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Nuclear Receptor Subfamily 1, Group D, Member 1/genetics ; Nuclear Receptor Subfamily 1, Group D, Member 1/metabolism ; Proteolysis ; RNA Interference ; Reverse Transcriptase Polymerase Chain Reaction ; Ubiquitin-Protein Ligases/genetics ; Ubiquitin-Protein Ligases/metabolism
Chemical Substances	NR1D1 protein, human ; Nuclear Proteins ; Nuclear Receptor Subfamily 1, Group D, Member 1 ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; seven in absentia proteins (EC 2.3.2.27)
Language	English
Publishing date	2015-10-06
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.1501204112
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Zs.A 1148: Show issues

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Article: Functional analysis of nocturnin: a circadian clock-regulated gene identified by differential display.

Baggs, Julie E / Green, Carla B

Methods in molecular biology (Clifton, N.J.)

2006 Volume 317, Page(s) 243–254

Abstract: Within the retina there is a circadian clock that controls the 24-h timing of processes such as hormone release, cell movement, and gene transcription. In an effort to better understand the molecular nature of this retinal clock, a differential display ( ... ...

Abstract	Within the retina there is a circadian clock that controls the 24-h timing of processes such as hormone release, cell movement, and gene transcription. In an effort to better understand the molecular nature of this retinal clock, a differential display (DD) screen was performed to isolate a gene with high amplitude circadian rhythmicity in the Xenopus retina. A novel gene expressed in the early evening in photoreceptor cells was isolated and named nocturnin for night factor. This article outlines the steps we took to study a protein of unknown function, particularly highlighting the analyses one can perform when little more than the primary sequence of a gene is known. In addition, we describe the results of sequence analysis that assisted in predicting the function of nocturnin. We have shown that nocturnin acts as a deadenylase in vitro, removing the poly(A) tail from a mature messenger RNA in a process that either leads to degradation or translational silencing of a message. Although the role of nocturnin in the retina is unknown, future studies to identify target mRNAs that are deadenylated by nocturnin will assist in elucidating its physiological role in this tissue.
MeSH term(s)	Animals ; COS Cells ; Cercopithecus aethiops ; Circadian Rhythm ; Edetic Acid/chemistry ; Gene Expression Profiling/methods ; Gene Expression Regulation ; Green Fluorescent Proteins/metabolism ; In Vitro Techniques ; Nuclear Proteins ; Promoter Regions, Genetic ; Protein Structure, Tertiary ; Proteins/chemistry ; Proteins/genetics ; Proteins/metabolism ; RNA, Messenger/metabolism ; Retina/metabolism ; Saccharomyces cerevisiae/metabolism ; Transcription Factors ; Transcription, Genetic ; Xenopus
Chemical Substances	Nuclear Proteins ; Proteins ; RNA, Messenger ; Transcription Factors ; nocturnin ; Green Fluorescent Proteins (147336-22-9) ; Edetic Acid (9G34HU7RV0)
Language	English
Publishing date	2006
Publishing country	United States
Document type	Journal Article
ISSN	1064-3745
ISSN	1064-3745
DOI	10.1385/1-59259-968-0:243
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Article ; Online: High throughput genomic screen identifies multiple factors that promote cooperative Wnt signaling.

Miller, Mayumi F / Cohen, Ethan David / Baggs, Julie E / Hogenesch, John B / Morrisey, Edward E

PloS one

2013 Volume 8, Issue 1, Page(s) e55782

Abstract: Previous studies have demonstrated that certain Wnt ligands can promote high levels of cooperative signaling in a cell type specific manner. To explore the underlying mechanism of this cooperative Wnt signaling, we performed a high-throughput screen of ... ...

Abstract	Previous studies have demonstrated that certain Wnt ligands can promote high levels of cooperative signaling in a cell type specific manner. To explore the underlying mechanism of this cooperative Wnt signaling, we performed a high-throughput screen of more than 14,000 cDNAs to identify genes that promote cooperative Wnt signaling in the context of a single Wnt ligand, Wnt2. This screen identified several homeobox factors including Msx2, Nkx5.2, and Esx1, in addition to other factors known to promote Wnt signaling including Pias4. Generation of dominant-active or dominant-negative forms of Msx2 indicate that the mechanism by which homeobox factors cooperatively promote Wnt signaling is through their ability to repress gene transcription. These data identify a broad homeobox code, which acts to increase Wnt signaling through transcriptional repression.
MeSH term(s)	Cell Line ; Gene Expression Profiling ; Gene Expression Regulation ; Genomics/methods ; High-Throughput Screening Assays ; Homeodomain Proteins/genetics ; Homeodomain Proteins/metabolism ; Humans ; Ligands ; Protein Binding ; Transcription Factors/genetics ; Transcription Factors/metabolism ; Transcription, Genetic ; Wnt Proteins/metabolism ; Wnt Signaling Pathway
Chemical Substances	Homeodomain Proteins ; Ligands ; Transcription Factors ; Wnt Proteins
Language	English
Publishing date	2013-01-31
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0055782
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Article ; Online: Soluble syntaxin 3 functions as a transcriptional regulator.

Giovannone, Adrian J / Winterstein, Christine / Bhattaram, Pallavi / Reales, Elena / Low, Seng Hui / Baggs, Julie E / Xu, Mimi / Lalli, Matthew A / Hogenesch, John B / Weimbs, Thomas

The Journal of biological chemistry

2018 Volume 293, Issue 15, Page(s) 5478–5491

Abstract: Syntaxins are a conserved family of SNARE proteins and contain C-terminal transmembrane anchors required for their membrane fusion activity. Here we show that Stx3 (syntaxin 3) unexpectedly also functions as a nuclear regulator of gene expression. We ... ...

Abstract	Syntaxins are a conserved family of SNARE proteins and contain C-terminal transmembrane anchors required for their membrane fusion activity. Here we show that Stx3 (syntaxin 3) unexpectedly also functions as a nuclear regulator of gene expression. We found that alternative splicing creates a soluble isoform that we termed Stx3S, lacking the transmembrane anchor. Soluble Stx3S binds to the nuclear import factor RanBP5 (RAN-binding protein 5), targets to the nucleus, and interacts physically and functionally with several transcription factors, including ETV4 (ETS variant 4) and ATF2 (activating transcription factor 2). Stx3S is differentially expressed in normal human tissues, during epithelial cell polarization, and in breast cancer
MeSH term(s)	Adenovirus E1A Proteins/genetics ; Adenovirus E1A Proteins/metabolism ; Animals ; COS Cells ; Caco-2 Cells ; Cell Nucleus/genetics ; Cell Nucleus/metabolism ; Cell Proliferation ; Chlorocebus aethiops ; Dogs ; Gene Expression Regulation ; HEK293 Cells ; HeLa Cells ; Humans ; Madin Darby Canine Kidney Cells ; Protein Binding ; Proto-Oncogene Proteins/genetics ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-ets ; Qa-SNARE Proteins/genetics ; Qa-SNARE Proteins/metabolism ; Signal Transduction ; Solubility ; beta Karyopherins/genetics ; beta Karyopherins/metabolism
Chemical Substances	Adenovirus E1A Proteins ; ETV4 protein, human ; IPO5 protein, human ; Proto-Oncogene Proteins ; Proto-Oncogene Proteins c-ets ; Qa-SNARE Proteins ; beta Karyopherins
Language	English
Publishing date	2018-02-23
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.RA117.000874
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Article: Nocturnin, a deadenylase in Xenopus laevis retina: a mechanism for posttranscriptional control of circadian-related mRNA.

Baggs, Julie E / Green, Carla B

Current biology : CB

2003 Volume 13, Issue 3, Page(s) 189–198

Abstract: Background: Different types of regulation are utilized to produce a robust circadian clock, including regulation at the transcriptional, posttranscriptional, and translational levels. A screen for rhythmic messages that may be involved in such circadian ...

Abstract	Background: Different types of regulation are utilized to produce a robust circadian clock, including regulation at the transcriptional, posttranscriptional, and translational levels. A screen for rhythmic messages that may be involved in such circadian control identified nocturnin, a novel gene that displays high-amplitude circadian expression in the Xenopus laevis retina, with peak mRNA levels in the early night. Expression of nocturnin mRNA is confined to the clock-containing photoreceptor cell layer within the retina. Results: In these studies, we show that nocturnin removes the poly(A) tail from a synthetic RNA substrate in a process known as deadenylation. Nocturnin nuclease activity is magnesium dependent, as the addition of EDTA or mutation of the residue predicted to bind magnesium disrupts deadenylation. Substrate preference studies show that nocturnin is an exonuclease that specifically degrades the 3' poly(A) tail. While nocturnin is rhythmically expressed in the cytoplasm of the retinal photoreceptor cells, the only other described vertebrate deadenylase, PARN, is constitutively present in most retinal cells, including the photoreceptors. Conclusions: The distinct spatial and temporal expression of nocturnin and PARN suggests that there may be specific mRNA targets of each deadenylase. Since deadenylation regulates mRNA decay and/or translational silencing, we propose that nocturnin deadenylates clock-related transcripts in a novel mechanism for posttranscriptional regulation in the circadian clock or its outputs.
MeSH term(s)	Animals ; Biological Clocks/physiology ; Circadian Rhythm/physiology ; Exoribonucleases/genetics ; Exoribonucleases/metabolism ; Eye Proteins/genetics ; Eye Proteins/metabolism ; Gene Expression Regulation ; Humans ; Magnesium/metabolism ; Nuclear Proteins ; Proteins/genetics ; Proteins/metabolism ; RNA Processing, Post-Transcriptional ; RNA, Messenger/metabolism ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism ; Retina/enzymology ; Retinal Cone Photoreceptor Cells/cytology ; Retinal Cone Photoreceptor Cells/metabolism ; Retinal Rod Photoreceptor Cells/cytology ; Retinal Rod Photoreceptor Cells/metabolism ; Transcription Factors ; Xenopus laevis
Chemical Substances	Eye Proteins ; Nuclear Proteins ; Proteins ; RNA, Messenger ; Recombinant Fusion Proteins ; Transcription Factors ; nocturnin ; Exoribonucleases (EC 3.1.-) ; poly(A)-specific ribonuclease (EC 3.1.13.4) ; Magnesium (I38ZP9992A)
Language	English
Publishing date	2003-02-04
Publishing country	England
Document type	Journal Article
ZDB-ID	1071731-6
ISSN	1879-0445 ; 0960-9822
ISSN (online)	1879-0445
ISSN	0960-9822
DOI	10.1016/s0960-9822(03)00014-9
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Article ; Online: Safety Monitoring of COVID-19 mRNA Vaccine Second Booster Doses Among Adults Aged ≥50 Years - United States, March 29, 2022-July 10, 2022.

Hause, Anne M / Baggs, James / Marquez, Paige / Abara, Winston E / Baumblatt, Jane / Blanc, Phillip G / Su, John R / Hugueley, Brandon / Parker, Casey / Myers, Tanya R / Gee, Julianne / Shimabukuro, Tom T / Shay, David K

MMWR. Morbidity and mortality weekly report

2022 Volume 71, Issue 30, Page(s) 971–976

Abstract: ... after receipt of a second mRNA booster dose during March 29-July 10, 2022. V-safe is a voluntary ... managed by CDC and FDA (3). During March 29-July 10, 2022, approximately 16.8 million persons ...

Abstract	The Advisory Committee on Immunization Practices (ACIP) recommends that all persons aged ≥5 years receive 1 booster dose of a COVID-19 vaccine after completion of their primary series.* On March 29, 2022, the Food and Drug Administration (FDA) authorized a second mRNA booster dose ≥4 months after receipt of a first booster dose for adults aged ≥50 years and persons aged ≥12 years with moderate to severe immunocompromise (1,2). To characterize the safety of a second mRNA booster dose among persons aged ≥50 years, CDC reviewed adverse events and health impact assessments reported to v-safe and the Vaccine Adverse Event Reporting System (VAERS) after receipt of a second mRNA booster dose during March 29-July 10, 2022. V-safe is a voluntary smartphone-based U.S. active surveillance system that monitors adverse events occurring after COVID-19 vaccination. VAERS is a U.S. passive surveillance system for monitoring adverse events after vaccination, managed by CDC and FDA (3). During March 29-July 10, 2022, approximately 16.8 million persons in the United States aged ≥50 years received a fourth dose.
MeSH term(s)	Adverse Drug Reaction Reporting Systems ; COVID-19/prevention & control ; COVID-19 Vaccines/adverse effects ; Humans ; Middle Aged ; mRNA Vaccines/adverse effects
Chemical Substances	COVID-19 Vaccines ; mRNA Vaccines
Language	English
Publishing date	2022-07-29
Publishing country	United States
Document type	Journal Article
ZDB-ID	412775-4
ISSN	1545-861X ; 0149-2195
ISSN (online)	1545-861X
ISSN	0149-2195
DOI	10.15585/mmwr.mm7130a4
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