Involvement of heterogeneous nuclear ribonucleoproteins in viral multiplication

2012 ◽  
Vol 7 (6) ◽  
pp. 575-591 ◽  
Author(s):  
Viviana Castilla ◽  
Luis A Scolaro
Keyword(s):  
Viral Multiplication ◽  
Heterogeneous Nuclear Ribonucleoproteins

A Device for Rapid Removal of Embryos from Fish Eggs

1971 ◽  
Vol 28 (1) ◽  
pp. 100-102 ◽  
Author(s):  
R. M. MacKelvie
Keyword(s):  
Fish Eggs ◽  
Viral Multiplication ◽  
Rapid Removal

An inexpensive and easily constructed device is described whereby embryos were removed from fish eggs for the study of viral multiplication.

scholarly journals Heterogeneous nuclear ribonucleoproteins A1 and A2 modulate expression of Tid1 isoforms and EGFR signaling in non-small cell lung cancer

Oncotarget ◽  
2016 ◽  
Vol 7 (13) ◽  
pp. 16760-16772 ◽  
Author(s):  
Chi-Yuan Chen ◽  
Chia-Ing Jan ◽  
Wen-Chieh Pi ◽  
Wen-Lung Wang ◽  
Pan-Chyr Yang ◽  
...  
Keyword(s):  
Lung Cancer ◽  
Small Cell Lung Cancer ◽  
Cell Lung Cancer ◽  
Small Cell ◽  
Egfr Signaling ◽  
Small Cell Lung ◽  
Heterogeneous Nuclear Ribonucleoproteins

scholarly journals Heterogeneous nuclear ribonucleoproteins R and Q accumulate in pathological inclusions in FTLD-FUS

2019 ◽  
Vol 7 (1) ◽  
Author(s):  
Lauren M. Gittings ◽  
Sandrine C. Foti ◽  
Bridget C. Benson ◽  
Priya Gami-Patel ◽  
Adrian M. Isaacs ◽  
...  
Keyword(s):  
Heterogeneous Nuclear Ribonucleoproteins

scholarly journals Oligomeric amyloid-β induces early and widespread changes to the proteome in human iPSC-derived neurons

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Christopher Sackmann ◽  
Martin Hallbeck
Keyword(s):  
Amyloid Β ◽  
Brain Regions ◽  
Tau Proteins ◽  
Label Free ◽  
Human Neurons ◽  
Associated Proteins ◽  
Proteasome Subunits ◽  
Heterogeneous Nuclear Ribonucleoproteins ◽  
Human Ipsc ◽  
Differential Phosphorylation

AbstractAlzheimer’s disease (AD) is the most common form of dementia globally and is characterized by aberrant accumulations of amyloid-beta (Aβ) and tau proteins. Oligomeric forms of these proteins are believed to be most relevant to disease progression, with oligomeric amyloid-β (oAβ) particularly implicated in AD. oAβ pathology spreads among interconnected brain regions, but how oAβ induces pathology in these previously unaffected neurons requires further study. Here, we use well characterized iPSC-derived human neurons to study the early changes to the proteome and phosphoproteome after 24 h exposure to oAβ 1-42. Using nLC-MS/MS and label-free quantification, we identified several proteins that are differentially regulated in response to acute oAβ challenge. At this early timepoint, oAβ induced the decrease of TDP-43, heterogeneous nuclear ribonucleoproteins (hnRNPs), and coatomer complex I (COPI) proteins. Conversely, increases were observed in 20 S proteasome subunits and vesicle associated proteins VAMP1/2, as well as the differential phosphorylation of tau at serine 208. These changes show that there are widespread alterations to the neuronal proteome within 24 h of oAβ uptake, including proteins previously not shown to be related to neurodegeneration. This study provides new targets for the further study of early mediators of AD pathogenesis.

scholarly journals Glucose Oxidation by Normal and Virus-Infected Mice

1956 ◽  
Vol 184 (2) ◽  
pp. 356-358 ◽  
Author(s):  
Benjamin V. Siegel ◽  
Ann M. Hughes
Keyword(s):  
Glucose Metabolism ◽  
Glucose Oxidation ◽  
Apparent Effect ◽  
Diseased Animal ◽  
Poliomyelitis Virus ◽  
Viral Multiplication

The oxidation of uniformly labeled C14-glucose by normal mice and mice infected with strain MEF1 poliomyelitis virus was determined in an apparatus designed to measure respiratory radioactivity excretion. The respiration of normal and virus-infected mice was found to be essentially the same over a 10-day period of infection, although the production of virus in the diseased animal during this time was considerable. It is concluded that the rate and extent of viral multiplication in poliomyelitis is without apparent effect on the rate and extent of glucose metabolism by the infected intact host.

scholarly journals RNA-binding proteins with prion-like domains in health and disease

2017 ◽  
Vol 474 (8) ◽  
pp. 1417-1438 ◽  
Author(s):  
Alice Ford Harrison ◽  
James Shorter
Keyword(s):  
Phase Transitions ◽  
Binding Proteins ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Binding Protein ◽  
Low Complexity ◽  
Fused In Sarcoma ◽  
Heterogeneous Nuclear Ribonucleoproteins ◽  
Health And Disease ◽  
Lateral Sclerosis

Approximately 70 human RNA-binding proteins (RBPs) contain a prion-like domain (PrLD). PrLDs are low-complexity domains that possess a similar amino acid composition to prion domains in yeast, which enable several proteins, including Sup35 and Rnq1, to form infectious conformers, termed prions. In humans, PrLDs contribute to RBP function and enable RBPs to undergo liquid–liquid phase transitions that underlie the biogenesis of various membraneless organelles. However, this activity appears to render RBPs prone to misfolding and aggregation connected to neurodegenerative disease. Indeed, numerous RBPs with PrLDs, including TDP-43 (transactivation response element DNA-binding protein 43), FUS (fused in sarcoma), TAF15 (TATA-binding protein-associated factor 15), EWSR1 (Ewing sarcoma breakpoint region 1), and heterogeneous nuclear ribonucleoproteins A1 and A2 (hnRNPA1 and hnRNPA2), have now been connected via pathology and genetics to the etiology of several neurodegenerative diseases, including amyotrophic lateral sclerosis, frontotemporal dementia, and multisystem proteinopathy. Here, we review the physiological and pathological roles of the most prominent RBPs with PrLDs. We also highlight the potential of protein disaggregases, including Hsp104, as a therapeutic strategy to combat the aberrant phase transitions of RBPs with PrLDs that likely underpin neurodegeneration.

scholarly journals Roles of Splicing Factors in Hormone-Related Cancer Progression

2020 ◽  
Vol 21 (5) ◽  
pp. 1551 ◽  
Author(s):  
Toshihiko Takeiwa ◽  
Yuichi Mitobe ◽  
Kazuhiro Ikeda ◽  
Kuniko Horie-Inoue ◽  
Satoshi Inoue
Keyword(s):  
Cancer Progression ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Mrna Isoforms ◽  
Targeting Therapy ◽  
Biological Phenomena ◽  
New Strategy ◽  
Heterogeneous Nuclear Ribonucleoproteins ◽  
Prostate Cancers ◽  
Mrna Precursor

Splicing of mRNA precursor (pre-mRNA) is a mechanism to generate multiple mRNA isoforms from a single pre-mRNA, and it plays an essential role in a variety of biological phenomena and diseases such as cancers. Previous studies have demonstrated that cancer-specific splicing events are involved in various aspects of cancers such as proliferation, migration and response to hormones, suggesting that splicing-targeting therapy can be promising as a new strategy for cancer treatment. In this review, we focus on the splicing regulation by RNA-binding proteins including Drosophila behavior/human splicing (DBHS) family proteins, serine/arginine-rich (SR) proteins and heterogeneous nuclear ribonucleoproteins (hnRNPs) in hormone-related cancers, such as breast and prostate cancers.

scholarly journals Binding of an RNA Trafficking Response Element to Heterogeneous Nuclear Ribonucleoproteins A1 and A2

2000 ◽  
Vol 275 (49) ◽  
pp. 38286-38295 ◽  
Author(s):  
Jianguo Shan ◽  
Kim Moran-Jones ◽  
Trent P. Munro ◽  
Grahame J. Kidd ◽  
Donald J. Winzor ◽  
...  
Keyword(s):  
Response Element ◽  
Rna Trafficking ◽  
Heterogeneous Nuclear Ribonucleoproteins
Sign in / Sign up

Export Citation Format

Share Document