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Article ; Online: Targeting conserved co-opted host factors to block virus replication: Using allosteric inhibitors of the cytosolic Hsp70s to interfere with tomato bushy stunt virus replication.

Molho, Melissa / Prasanth, K Reddisiva / Pogany, Judit / Nagy, Peter D

2021 Volume 563, Page(s) 1–19

Abstract: To further our understanding of the pro-viral roles of the host cytosolic heat shock protein 70 (Hsp70) family, we chose the conserved Arabidopsis thaliana Hsp70-2 and the unique Erd2 (early response to dehydration 2), which contain Hsp70 domains. Based ... ...

Abstract	To further our understanding of the pro-viral roles of the host cytosolic heat shock protein 70 (Hsp70) family, we chose the conserved Arabidopsis thaliana Hsp70-2 and the unique Erd2 (early response to dehydration 2), which contain Hsp70 domains. Based on in vitro studies with purified components, we show that AtHsp70-2 and AtErd2 perform pro-viral functions equivalent to that of the yeast Ssa1 Hsp70. These functions include activation of the tombusvirus RdRp, and stimulation of replicase assembly. Yeast-based complementation studies demonstrate that AtHsp70-2 or AtErd2 are present in the purified tombusvirus replicase. RNA silencing and over-expression studies in Nicotiana benthamiana suggest that both Hsp70-2 and Erd2 are co-opted by tomato bushy stunt virus (TBSV). Moreover, we used allosteric inhibitors of Hsp70s to inhibit replication of TBSV and related plant viruses in plants. Altogether, interfering with the functions of the co-opted Hsp70s could be an effective antiviral approach against tombusviruses in plants.
MeSH term(s)	Arabidopsis/metabolism ; Arabidopsis Proteins/genetics ; Arabidopsis Proteins/metabolism ; Benzothiazoles/pharmacology ; Gene Expression Regulation, Plant/immunology ; Gene Expression Regulation, Viral/drug effects ; Gene Expression Regulation, Viral/physiology ; Gene Knockdown Techniques ; Genetic Complementation Test ; HSP70 Heat-Shock Proteins/genetics ; HSP70 Heat-Shock Proteins/metabolism ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Plant Leaves/metabolism ; Plant Leaves/virology ; Pyridinium Compounds/pharmacology ; RNA, Viral/physiology ; Nicotiana/metabolism ; Nicotiana/virology ; Tombusvirus/physiology ; Two-Hybrid System Techniques ; Viral Proteins/genetics ; Viral Proteins/metabolism ; Virus Replication/drug effects ; Virus Replication/physiology
Chemical Substances	Arabidopsis Proteins ; Benzothiazoles ; ERD2 protein, Arabidopsis ; HSP70 Heat-Shock Proteins ; Membrane Proteins ; Pyridinium Compounds ; RNA, Viral ; Viral Proteins ; YM-01 compound
Language	English
Publishing date	2021-08-06
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	200425-2
ISSN	1096-0341 ; 0042-6822
ISSN (online)	1096-0341
ISSN	0042-6822
DOI	10.1016/j.virol.2021.08.002
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Article ; Online: Dynamic interplay between the co-opted Fis1 mitochondrial fission protein and membrane contact site proteins in supporting tombusvirus replication.

Lin, Wenwu / Feng, Zhike / Prasanth, K Reddisiva / Liu, Yuyan / Nagy, Peter D

PLoS pathogens

2021 Volume 17, Issue 3, Page(s) e1009423

Abstract: Plus-stranded RNA viruses have limited coding capacity and have to co-opt numerous pro-viral host factors to support their replication. Many of the co-opted host factors support the biogenesis of the viral replication compartments and the formation of ... ...

Abstract	Plus-stranded RNA viruses have limited coding capacity and have to co-opt numerous pro-viral host factors to support their replication. Many of the co-opted host factors support the biogenesis of the viral replication compartments and the formation of viral replicase complexes on subverted subcellular membrane surfaces. Tomato bushy stunt virus (TBSV) exploits peroxisomal membranes, whereas the closely-related carnation Italian ringspot virus (CIRV) hijacks the outer membranes of mitochondria. How these organellar membranes can be recruited into pro-viral roles is not completely understood. Here, we show that the highly conserved Fis1 mitochondrial fission protein is co-opted by both TBSV and CIRV via direct interactions with the p33/p36 replication proteins. Deletion of FIS1 in yeast or knockdown of the homologous Fis1 in plants inhibits tombusvirus replication. Instead of the canonical function in mitochondrial fission and peroxisome division, the tethering function of Fis1 is exploited by tombusviruses to facilitate the subversion of membrane contact site (MCS) proteins and peroxisomal/mitochondrial membranes for the biogenesis of the replication compartment. We propose that the dynamic interactions of Fis1 with MCS proteins, such as the ER resident VAP tethering proteins, Sac1 PI4P phosphatase and the cytosolic OSBP-like oxysterol-binding proteins, promote the formation and facilitate the stabilization of virus-induced vMCSs, which enrich sterols within the replication compartment. We show that this novel function of Fis1 is exploited by tombusviruses to build nuclease-insensitive viral replication compartment.
MeSH term(s)	Membrane Proteins/metabolism ; Mitochondrial Proteins/metabolism ; Saccharomyces cerevisiae/virology ; Saccharomyces cerevisiae Proteins/metabolism ; Nicotiana/virology ; Tombusvirus/physiology ; Virus Replication/physiology
Chemical Substances	FIS1 protein, S cerevisiae ; Membrane Proteins ; Mitochondrial Proteins ; Saccharomyces cerevisiae Proteins
Language	English
Publishing date	2021-03-16
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7374
ISSN (online)	1553-7374
ISSN	1553-7374
DOI	10.1371/journal.ppat.1009423
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Dynamic interplay between the co-opted Fis1 mitochondrial fission protein and membrane contact site proteins in supporting tombusvirus replication.

Wenwu Lin / Zhike Feng / K Reddisiva Prasanth / Yuyan Liu / Peter D Nagy

PLoS Pathogens, Vol 17, Iss 3, p e

2021 Volume 1009423

Abstract	Plus-stranded RNA viruses have limited coding capacity and have to co-opt numerous pro-viral host factors to support their replication. Many of the co-opted host factors support the biogenesis of the viral replication compartments and the formation of viral replicase complexes on subverted subcellular membrane surfaces. Tomato bushy stunt virus (TBSV) exploits peroxisomal membranes, whereas the closely-related carnation Italian ringspot virus (CIRV) hijacks the outer membranes of mitochondria. How these organellar membranes can be recruited into pro-viral roles is not completely understood. Here, we show that the highly conserved Fis1 mitochondrial fission protein is co-opted by both TBSV and CIRV via direct interactions with the p33/p36 replication proteins. Deletion of FIS1 in yeast or knockdown of the homologous Fis1 in plants inhibits tombusvirus replication. Instead of the canonical function in mitochondrial fission and peroxisome division, the tethering function of Fis1 is exploited by tombusviruses to facilitate the subversion of membrane contact site (MCS) proteins and peroxisomal/mitochondrial membranes for the biogenesis of the replication compartment. We propose that the dynamic interactions of Fis1 with MCS proteins, such as the ER resident VAP tethering proteins, Sac1 PI4P phosphatase and the cytosolic OSBP-like oxysterol-binding proteins, promote the formation and facilitate the stabilization of virus-induced vMCSs, which enrich sterols within the replication compartment. We show that this novel function of Fis1 is exploited by tombusviruses to build nuclease-insensitive viral replication compartment.
Keywords	Immunologic diseases. Allergy ; RC581-607 ; Biology (General) ; QH301-705.5
Subject code	570
Language	English
Publishing date	2021-03-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article: Targeting conserved co-opted host factors to block virus replication: Using allosteric inhibitors of the cytosolic Hsp70s to interfere with tomato bushy stunt virus replication

Molho, Melissa / Prasanth, K. Reddisiva / Pogany, Judit / Nagy, Peter D.

Virology. 2021 Nov., v. 563

2021

Abstract	To further our understanding of the pro-viral roles of the host cytosolic heat shock protein 70 (Hsp70) family, we chose the conserved Arabidopsis thaliana Hsp70-2 and the unique Erd2 (early response to dehydration 2), which contain Hsp70 domains. Based on in vitro studies with purified components, we show that AtHsp70-2 and AtErd2 perform pro-viral functions equivalent to that of the yeast Ssa1 Hsp70. These functions include activation of the tombusvirus RdRp, and stimulation of replicase assembly. Yeast-based complementation studies demonstrate that AtHsp70-2 or AtErd2 are present in the purified tombusvirus replicase. RNA silencing and over-expression studies in Nicotiana benthamiana suggest that both Hsp70-2 and Erd2 are co-opted by tomato bushy stunt virus (TBSV). Moreover, we used allosteric inhibitors of Hsp70s to inhibit replication of TBSV and related plant viruses in plants. Altogether, interfering with the functions of the co-opted Hsp70s could be an effective antiviral approach against tombusviruses in plants.
Keywords	Arabidopsis thaliana ; Nicotiana benthamiana ; RNA ; Tomato bushy stunt virus ; heat-shock protein 70 ; virus replication ; yeasts
Language	English
Dates of publication	2021-11
Size	p. 1-19.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	200425-2
ISSN	1096-0341 ; 0042-6822
ISSN (online)	1096-0341
ISSN	0042-6822
DOI	10.1016/j.virol.2021.08.002
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Role of RNA-binding proteins during the late stages of Flavivirus replication cycle.

Diosa-Toro, Mayra / Prasanth, K Reddisiva / Bradrick, Shelton S / Garcia Blanco, Mariano A

Virology journal

2020 Volume 17, Issue 1, Page(s) 60

Abstract: The genus Flavivirus encompasses several worldwide-distributed arthropod-borne viruses including, dengue virus, Japanese encephalitis virus, West Nile virus, yellow fever virus, Zika virus, and tick-borne encephalitis virus. Infection with these viruses ... ...

Abstract	The genus Flavivirus encompasses several worldwide-distributed arthropod-borne viruses including, dengue virus, Japanese encephalitis virus, West Nile virus, yellow fever virus, Zika virus, and tick-borne encephalitis virus. Infection with these viruses manifest with symptoms ranging from febrile illness to life- threatening hypotensive shock and encephalitis. Therefore, flaviviruses pose a great risk to public health. Currently, preventive measures are falling short to control epidemics and there are no antivirals against any Flavivirus.Flaviviruses carry a single stranded positive-sense RNA genome that plays multiple roles in infected cells: it is translated into viral proteins, used as template for genome replication, it is the precursor of the subgenomic flaviviral RNA and it is assembled into new virions. Furthermore, viral RNA genomes are also packaged into extracellular vesicles, e.g. exosomes, which represent an alternate mode of virus dissemination.Because RNA molecules are at the center of Flavivirus replication cycle, viral and host RNA-binding proteins (RBPs) are critical determinants of infection. Numerous studies have revealed the function of RBPs during Flavivirus infection, particularly at the level of RNA translation and replication. These proteins, however, are also critical participants at the late stages of the replication cycle. Here we revise the function of host RBPs and the viral proteins capsid, NS2A and NS3, during the packaging of viral RNA and the assembly of new virus particles. Furthermore, we go through the evidence pointing towards the importance of host RBPs in mediating cellular RNA export with the idea that the biogenesis of exosomes harboring Flavivirus RNA would follow an analogous pathway.
MeSH term(s)	Flavivirus/genetics ; Flavivirus/physiology ; Flavivirus Infections/virology ; Genome, Viral ; Host-Pathogen Interactions/genetics ; Humans ; RNA, Viral/genetics ; RNA-Binding Proteins/genetics ; RNA-Binding Proteins/metabolism ; Viral Proteins/genetics ; Virus Replication
Chemical Substances	RNA, Viral ; RNA-Binding Proteins ; Viral Proteins
Language	English
Publishing date	2020-04-25
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2160640-7
ISSN	1743-422X ; 1743-422X
ISSN (online)	1743-422X
ISSN	1743-422X
DOI	10.1186/s12985-020-01329-7
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Co-opting ATP-generating glycolytic enzyme PGK1 phosphoglycerate kinase facilitates the assembly of viral replicase complexes.

Prasanth, K Reddisiva / Chuang, Chingkai / Nagy, Peter D

PLoS pathogens

2017 Volume 13, Issue 10, Page(s) e1006689

Abstract: The intricate interactions between viruses and hosts include exploitation of host cells for viral replication by using many cellular resources, metabolites and energy. Tomato bushy stunt virus (TBSV), similar to other (+)RNA viruses, induces major ... ...

Abstract	The intricate interactions between viruses and hosts include exploitation of host cells for viral replication by using many cellular resources, metabolites and energy. Tomato bushy stunt virus (TBSV), similar to other (+)RNA viruses, induces major changes in infected cells that lead to the formation of large replication compartments consisting of aggregated peroxisomal and ER membranes. Yet, it is not known how TBSV obtains the energy to fuel these energy-consuming processes. In the current work, the authors discovered that TBSV co-opts the glycolytic ATP-generating Pgk1 phosphoglycerate kinase to facilitate the assembly of new viral replicase complexes. The recruitment of Pgk1 into the viral replication compartment is through direct interaction with the viral replication proteins. Altogether, we provide evidence that the ATP generated locally within the replication compartment by the co-opted Pgk1 is used to fuel the ATP-requirement of the co-opted heat shock protein 70 (Hsp70) chaperone, which is essential for the assembly of new viral replicase complexes and the activation of functional viral RNA-dependent RNA polymerase. The advantage of direct recruitment of Pgk1 into the virus replication compartment could be that the virus replicase assembly does not need to intensively compete with cellular processes for access to ATP. In addition, local production of ATP within the replication compartment could greatly facilitate the efficiency of Hsp70-driven replicase assembly by providing high ATP concentration within the replication compartment.
MeSH term(s)	Host-Pathogen Interactions/physiology ; Phosphoglycerate Kinase/metabolism ; RNA-Dependent RNA Polymerase/metabolism ; Saccharomyces cerevisiae ; Nicotiana/virology ; Tombusvirus/growth & development ; Virus Assembly/physiology
Chemical Substances	Phosphoglycerate Kinase (EC 2.7.2.3) ; RNA-Dependent RNA Polymerase (EC 2.7.7.48)
Language	English
Publishing date	2017-10-23
Publishing country	United States
Document type	Journal Article
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7374
ISSN (online)	1553-7374
ISSN	1553-7374
DOI	10.1371/journal.ppat.1006689
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: The Glycolytic Pyruvate Kinase Is Recruited Directly into the Viral Replicase Complex to Generate ATP for RNA Synthesis.

Chuang, Chingkai / Prasanth, K Reddisiva / Nagy, Peter D

Cell host & microbe

2017 Volume 22, Issue 5, Page(s) 639–652.e7

Abstract: Viruses accomplish their replication by exploiting many cellular resources, including metabolites and energy. Similarly to other (+)RNA viruses, tomato bushy stunt virus (TBSV) induces major changes in infected cells. However, the source of energy ... ...

Abstract	Viruses accomplish their replication by exploiting many cellular resources, including metabolites and energy. Similarly to other (+)RNA viruses, tomato bushy stunt virus (TBSV) induces major changes in infected cells. However, the source of energy required to fuel TBSV replication is unknown. We find that TBSV co-opts the cellular glycolytic ATP-generating pyruvate kinase (PK) directly into the viral replicase complex to boost progeny RNA synthesis. The co-opted PK generates high levels of ATP within the viral replication compartment at the expense of a reduction in cytosolic ATP pools. The ATP generated by the co-opted PK is used to promote the helicase activity of recruited cellular DEAD-box helicases, which are involved in the production of excess viral (+)RNA progeny. Altogether, recruitment of PK and local production of ATP within the replication compartment allow the virus replication machinery an access to plentiful ATP, facilitating robust virus replication.
MeSH term(s)	Adenosine Triphosphate/metabolism ; DEAD-box RNA Helicases/metabolism ; Escherichia coli ; Gene Knockdown Techniques ; Gene Silencing ; Glycolysis/physiology ; Host-Pathogen Interactions/physiology ; Plant Leaves/genetics ; Plant Leaves/metabolism ; Plant Leaves/virology ; Plasmids ; Proteomics ; Pyruvate Kinase/metabolism ; RNA Viruses/enzymology ; RNA Viruses/genetics ; RNA Viruses/metabolism ; RNA, Viral/metabolism ; RNA-Dependent RNA Polymerase/genetics ; RNA-Dependent RNA Polymerase/metabolism ; Recombinant Proteins/genetics ; Saccharomyces cerevisiae/genetics ; Nicotiana/genetics ; Nicotiana/metabolism ; Nicotiana/virology ; Tombusvirus/enzymology ; Tombusvirus/genetics ; Tombusvirus/metabolism ; Virus Replication/genetics ; Virus Replication/physiology
Chemical Substances	RNA, Viral ; Recombinant Proteins ; Adenosine Triphosphate (8L70Q75FXE) ; Pyruvate Kinase (EC 2.7.1.40) ; RNA-Dependent RNA Polymerase (EC 2.7.7.48) ; DEAD-box RNA Helicases (EC 3.6.4.13)
Language	English
Publishing date	2017-11-05
Publishing country	United States
Document type	Journal Article
ZDB-ID	2278004-X
ISSN	1934-6069 ; 1931-3128
ISSN (online)	1934-6069
ISSN	1931-3128
DOI	10.1016/j.chom.2017.10.004
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Zs.A 6578: Show issues

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Article ; Online: Co-opting ATP-generating glycolytic enzyme PGK1 phosphoglycerate kinase facilitates the assembly of viral replicase complexes.

K Reddisiva Prasanth / Chingkai Chuang / Peter D Nagy

PLoS Pathogens, Vol 13, Iss 10, p e

2017 Volume 1006689

Abstract	The intricate interactions between viruses and hosts include exploitation of host cells for viral replication by using many cellular resources, metabolites and energy. Tomato bushy stunt virus (TBSV), similar to other (+)RNA viruses, induces major changes in infected cells that lead to the formation of large replication compartments consisting of aggregated peroxisomal and ER membranes. Yet, it is not known how TBSV obtains the energy to fuel these energy-consuming processes. In the current work, the authors discovered that TBSV co-opts the glycolytic ATP-generating Pgk1 phosphoglycerate kinase to facilitate the assembly of new viral replicase complexes. The recruitment of Pgk1 into the viral replication compartment is through direct interaction with the viral replication proteins. Altogether, we provide evidence that the ATP generated locally within the replication compartment by the co-opted Pgk1 is used to fuel the ATP-requirement of the co-opted heat shock protein 70 (Hsp70) chaperone, which is essential for the assembly of new viral replicase complexes and the activation of functional viral RNA-dependent RNA polymerase. The advantage of direct recruitment of Pgk1 into the virus replication compartment could be that the virus replicase assembly does not need to intensively compete with cellular processes for access to ATP. In addition, local production of ATP within the replication compartment could greatly facilitate the efficiency of Hsp70-driven replicase assembly by providing high ATP concentration within the replication compartment.
Keywords	Immunologic diseases. Allergy ; RC581-607 ; Biology (General) ; QH301-705.5
Subject code	570
Language	English
Publishing date	2017-10-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article: Role of RNA-binding proteins during the late stages of Flavivirus replication cycle

Diosa-Toro, Mayra / Prasanth, K. Reddisiva / Bradrick, Shelton S / Garcia Blanco, Mariano A

Virology journal. 2020 Dec., v. 17, no. 1

2020

Abstract	The genus Flavivirus encompasses several worldwide-distributed arthropod-borne viruses including, dengue virus, Japanese encephalitis virus, West Nile virus, yellow fever virus, Zika virus, and tick-borne encephalitis virus. Infection with these viruses manifest with symptoms ranging from febrile illness to life- threatening hypotensive shock and encephalitis. Therefore, flaviviruses pose a great risk to public health. Currently, preventive measures are falling short to control epidemics and there are no antivirals against any Flavivirus.Flaviviruses carry a single stranded positive-sense RNA genome that plays multiple roles in infected cells: it is translated into viral proteins, used as template for genome replication, it is the precursor of the subgenomic flaviviral RNA and it is assembled into new virions. Furthermore, viral RNA genomes are also packaged into extracellular vesicles, e.g. exosomes, which represent an alternate mode of virus dissemination.Because RNA molecules are at the center of Flavivirus replication cycle, viral and host RNA-binding proteins (RBPs) are critical determinants of infection. Numerous studies have revealed the function of RBPs during Flavivirus infection, particularly at the level of RNA translation and replication. These proteins, however, are also critical participants at the late stages of the replication cycle. Here we revise the function of host RBPs and the viral proteins capsid, NS2A and NS3, during the packaging of viral RNA and the assembly of new virus particles. Furthermore, we go through the evidence pointing towards the importance of host RBPs in mediating cellular RNA export with the idea that the biogenesis of exosomes harboring Flavivirus RNA would follow an analogous pathway.
Keywords	Dengue virus ; Flavivirus infections ; Japanese encephalitis virus ; RNA ; RNA transport ; Tick-borne encephalitis virus ; West Nile virus ; Yellow fever virus ; Zika virus ; antiviral agents ; biogenesis ; capsid ; encephalitis ; exosomes ; genome ; public health ; risk ; virology
Language	English
Dates of publication	2020-12
Size	p. 60.
Publishing place	BioMed Central
Document type	Article
Note	NAL-AP-2-clean ; Review
ISSN	1743-422X
DOI	10.1186/s12985-020-01329-7
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: A rapid and simple quantitative method for specific detection of smaller coterminal RNA by PCR (DeSCo-PCR): application to the detection of viral subgenomic RNAs.

Kanodia, Pulkit / Prasanth, K Reddisiva / Roa-Linares, Vicky C / Bradrick, Shelton S / Garcia-Blanco, Mariano A / Miller, W Allen

RNA (New York, N.Y.)

2020 Volume 26, Issue 7, Page(s) 888–901

Abstract: RNAs that are 5'-truncated versions of a longer RNA but share the same 3' terminus can be generated by alternative promoters in transcription of cellular mRNAs or by replicating RNA viruses. These truncated RNAs cannot be distinguished from the longer ... ...

Abstract	RNAs that are 5'-truncated versions of a longer RNA but share the same 3' terminus can be generated by alternative promoters in transcription of cellular mRNAs or by replicating RNA viruses. These truncated RNAs cannot be distinguished from the longer RNA by a simple two-primer RT-PCR because primers that anneal to the cDNA from the smaller RNA also anneal to-and amplify-the longer RNA-derived cDNA. Thus, laborious methods, such as northern blot hybridization, are used to distinguish shorter from longer RNAs. For rapid, low-cost, and specific detection of these truncated RNAs, we report
MeSH term(s)	Alternative Splicing/genetics ; Cell Line, Tumor ; DNA, Complementary/genetics ; Evaluation Studies as Topic ; Genome, Viral/genetics ; HeLa Cells ; Humans ; Nucleic Acid Conformation ; Polymerase Chain Reaction/methods ; Promoter Regions, Genetic/genetics ; RNA Viruses/genetics ; RNA, Messenger/genetics ; RNA, Viral/genetics ; Tombusviridae/genetics ; Zika Virus/genetics ; Zika Virus Infection/virology
Chemical Substances	DNA, Complementary ; RNA, Messenger ; RNA, Viral
Language	English
Publishing date	2020-04-01
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1241540-6
ISSN	1469-9001 ; 1355-8382
ISSN (online)	1469-9001
ISSN	1355-8382
DOI	10.1261/rna.074963.120
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