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Article: siRNAs: a new wave of RNA-based therapeutics.

Coburn, Glen A / Cullen, Bryan R

The Journal of antimicrobial chemotherapy

2003 Volume 51, Issue 4, Page(s) 753–756

MeSH term(s)	Antiviral Agents/pharmacology ; RNA Interference/drug effects ; RNA Interference/physiology ; RNA, Small Interfering ; RNA, Viral/genetics ; RNA, Viral/physiology ; Virus Replication/drug effects
Chemical Substances	Antiviral Agents ; RNA, Small Interfering ; RNA, Viral
Language	English
Publishing date	2003-04
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	191709-2
ISSN	1460-2091 ; 0305-7453
ISSN (online)	1460-2091
ISSN	0305-7453
DOI	10.1093/jac/dkg166
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Zs.A 1197: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
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Article: Potent and specific inhibition of human immunodeficiency virus type 1 replication by RNA interference.

Coburn, Glen A / Cullen, Bryan R

Journal of virology

2001 Volume 76, Issue 18, Page(s) 9225–9231

Abstract: Synthetic small interfering RNAs (siRNAs) have been shown to induce the degradation of specific mRNA targets in human cells by inducing RNA interference (RNAi). Here, we demonstrate that siRNA duplexes targeted against the essential Tat and Rev ... ...

Abstract	Synthetic small interfering RNAs (siRNAs) have been shown to induce the degradation of specific mRNA targets in human cells by inducing RNA interference (RNAi). Here, we demonstrate that siRNA duplexes targeted against the essential Tat and Rev regulatory proteins encoded by human immunodeficiency virus type 1 (HIV-1) can specifically block Tat and Rev expression and function. More importantly, we show that these same siRNAs can effectively inhibit HIV-1 gene expression and replication in cell cultures, including those of human T-cell lines and primary lymphocytes. These observations demonstrate that RNAi can effectively block virus replication in human cells and raise the possibility that RNAi could provide an important innate protective response, particularly against viruses that express double-stranded RNAs as part of their replication cycle.
MeSH term(s)	Cell Line ; Cells, Cultured ; Gene Expression Regulation, Viral ; Gene Products, rev/genetics ; Gene Products, rev/metabolism ; Gene Products, tat/genetics ; Gene Products, tat/metabolism ; Genes, rev ; Genes, tat ; HIV-1/drug effects ; HIV-1/genetics ; HIV-1/physiology ; Humans ; Jurkat Cells ; Leukocytes, Mononuclear/virology ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; RNA, Small Interfering ; RNA, Untranslated/chemical synthesis ; RNA, Untranslated/metabolism ; RNA, Untranslated/pharmacology ; T-Lymphocytes/virology ; Virus Replication/drug effects ; Virus Replication/physiology ; rev Gene Products, Human Immunodeficiency Virus ; tat Gene Products, Human Immunodeficiency Virus
Chemical Substances	Gene Products, rev ; Gene Products, tat ; RNA, Messenger ; RNA, Small Interfering ; RNA, Untranslated ; rev Gene Products, Human Immunodeficiency Virus ; tat Gene Products, Human Immunodeficiency Virus
Language	English
Publishing date	2001-05-07
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/jvi.76.18.9225-9231.2002
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Article ; Online: Preparation of the Escherichia coli RNase E protein and reconstitution of the RNA degradosome.

Mackie, George A / Coburn, Glen A / Miao, Xin / Briant, Douglas J / Prud'homme-Généreux, Annie / Stickney, Leigh M / Hankins, Janet S

Methods in enzymology

2008 Volume 447, Page(s) 199–213

Abstract: The RNA degradosome is a multienzyme complex that plays a key role in the processing of stable RNAs, the degradation of mRNAs, and the action of small regulatory RNAs. Initially discovered in Escherichia coli, similar or related complexes are found in ... ...

Abstract	The RNA degradosome is a multienzyme complex that plays a key role in the processing of stable RNAs, the degradation of mRNAs, and the action of small regulatory RNAs. Initially discovered in Escherichia coli, similar or related complexes are found in other bacteria. The core of the RNA degradosome is the essential endoribonuclease, RNase E. The C-terminus of this enzyme serves as a scaffold to which other components of the RNA degradosome bind. These ligands include the phosphorolytic 3'-exonuclease, polynucleotide phosphorylase, the DEAD-box RNA helicase, RhlB, and the glycolytic enzyme, enolase. In addition, the DEAD-box RNA helicases CsdA and RhlE and the RNA binding protein, Hfq, may bind to RNase E in place of one or more of the prototypical components. This chapter describes purification of RNase E (the Rne protein), reconstitution of a minimal degradosome that recapitulates the activity of authentic degradosomes, and methods for the assay of the reconstituted complex.
MeSH term(s)	Base Sequence ; Electrophoresis, Polyacrylamide Gel ; Endoribonucleases/metabolism ; Escherichia coli/enzymology ; Escherichia coli/growth & development ; Hydrolysis ; Molecular Sequence Data ; Nucleic Acid Conformation ; RNA/chemistry ; RNA/metabolism
Chemical Substances	RNA (63231-63-0) ; Endoribonucleases (EC 3.1.-) ; ribonuclease E (EC 3.1.4.-)
Language	English
Publishing date	2008
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1557-7988 ; 0076-6879
ISSN (online)	1557-7988
ISSN	0076-6879
DOI	10.1016/S0076-6879(08)02211-8
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Article ; Online: Novel small-molecule inhibitors of hepatitis C virus entry block viral spread and promote viral clearance in cell culture.

Coburn, Glen A / Fisch, Danielle N / Moorji, Sameer M / de Muys, Jean-Marc / Murga, Jose D / Paul, Dorothy / Provoncha, Kathleen P / Rotshteyn, Yakov / Han, Amy Q / Qian, Dapeng / Maddon, Paul J / Olson, William C

PloS one

2012 Volume 7, Issue 4, Page(s) e35351

Abstract: Combinations of direct-acting anti-virals offer the potential to improve the efficacy, tolerability and duration of the current treatment regimen for hepatitis C virus (HCV) infection. Viral entry represents a distinct therapeutic target that has been ... ...

Abstract	Combinations of direct-acting anti-virals offer the potential to improve the efficacy, tolerability and duration of the current treatment regimen for hepatitis C virus (HCV) infection. Viral entry represents a distinct therapeutic target that has been validated clinically for a number of pathogenic viruses. To discover novel inhibitors of HCV entry, we conducted a high throughput screen of a proprietary small-molecule compound library using HCV pseudoviral particle (HCVpp) technology. We independently discovered and optimized a series of 1,3,5-triazine compounds that are potent, selective and non-cytotoxic inhibitors of HCV entry. Representative compounds fully suppress both cell-free virus and cell-to-cell spread of HCV in vitro. We demonstrate, for the first time, that long term treatment of an HCV cell culture with a potent entry inhibitor promotes sustained viral clearance in vitro. We have confirmed that a single amino acid variant, V719G, in the transmembrane domain of E2 is sufficient to confer resistance to multiple compounds from the triazine series. Resistance studies were extended by evaluating both the fusogenic properties and growth kinetics of drug-induced and natural amino acid variants in the HCVpp and HCV cell culture assays. Our results indicate that amino acid variations at position 719 incur a significant fitness penalty. Introduction of I719 into a genotype 1b envelope sequence did not affect HCV entry; however, the overall level of HCV replication was reduced compared to the parental genotype 1b/2a HCV strain. Consistent with these findings, I719 represents a significant fraction of the naturally occurring genotype 1b sequences. Importantly, I719, the most relevant natural polymorphism, did not significantly alter the susceptibility of HCV to the triazine compounds. The preclinical properties of these triazine compounds support further investigation of entry inhibitors as a potential novel therapy for HCV infection.
MeSH term(s)	Antiviral Agents/chemistry ; Antiviral Agents/pharmacology ; Antiviral Agents/therapeutic use ; Cell Line ; Drug Resistance, Viral ; Genotype ; Hepacivirus/drug effects ; Hepacivirus/genetics ; Hepatitis C/drug therapy ; Hepatitis C/genetics ; Humans ; Small Molecule Libraries/chemistry ; Small Molecule Libraries/pharmacology ; Small Molecule Libraries/therapeutic use ; Triazines/chemistry ; Triazines/pharmacology ; Triazines/therapeutic use ; Viral Envelope Proteins/genetics ; Virus Internalization/drug effects
Chemical Substances	Antiviral Agents ; Small Molecule Libraries ; Triazines ; Viral Envelope Proteins
Language	English
Publishing date	2012-04-24
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.0035351
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Article: The crystal structure and mutational analysis of a novel RNA-binding domain found in the human Tap nuclear mRNA export factor.

Ho, Dona N / Coburn, Glen A / Kang, Yibin / Cullen, Bryan R / Georgiadis, Millie M

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

2002 Volume 99, Issue 4, Page(s) 1888–1893

Abstract: The Tap protein mediates the sequence nonspecific nuclear export of cellular mRNAs as well as the sequence-specific export of retroviral mRNAs bearing the constitutive transport element (CTE). Previously, the structures of individual Tap subdomains, ... ...

Abstract	The Tap protein mediates the sequence nonspecific nuclear export of cellular mRNAs as well as the sequence-specific export of retroviral mRNAs bearing the constitutive transport element (CTE). Previously, the structures of individual Tap subdomains, including ribonucleoprotein and leucine-rich repeat domains, have been described. Here, we report the crystal structure of a functional CTE RNA-binding domain of human Tap, including the N-terminal arm of the ribonucleoprotein domain and interdomain linking polypeptide. To identify residues that interact with the CTE, we have introduced 38 alanine substitutions for surface residues in the Tap CTE-binding domain and tested these mutants for their ability to support CTE-dependent nuclear RNA export and CTE binding. Four residues that cluster on a concave surface in the leucine-rich repeat domain were found to be critical for CTE binding and define a CTE-interacting surface on this domain. The second critical CTE-interacting surface on Tap is defined by three previously identified residues on the surface of the ribonucleoprotein domain. The structural and mutational data define a novel RNA-binding site on the Tap protein.
MeSH term(s)	Amino Acid Motifs ; Animals ; Binding Sites ; Cell Line ; Crystallography, X-Ray ; DNA Mutational Analysis ; Escherichia coli/metabolism ; Humans ; Models, Molecular ; Nuclear Proteins/chemistry ; Nuclear Proteins/genetics ; Nucleocytoplasmic Transport Proteins ; Protein Structure, Tertiary ; Quail ; RNA/metabolism ; RNA, Messenger/metabolism ; RNA-Binding Proteins/chemistry ; RNA-Binding Proteins/genetics ; Retroviridae/genetics ; Transfection
Chemical Substances	NXF1 protein, human ; Nuclear Proteins ; Nucleocytoplasmic Transport Proteins ; RNA, Messenger ; RNA-Binding Proteins ; RNA (63231-63-0)
Language	English
Publishing date	2002-02-19
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.042698599
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Article: Formation of Tap/NXT1 heterodimers activates Tap-dependent nuclear mRNA export by enhancing recruitment to nuclear pore complexes.

Wiegand, Heather L / Coburn, Glen A / Zeng, Yan / Kang, Yibin / Bogerd, Hal P / Cullen, Bryan R

Molecular and cellular biology

2001 Volume 22, Issue 1, Page(s) 245–256

Abstract: The Tap protein has been shown to activate the nuclear export of mRNA species bearing retroviral constitutive transport elements and is also believed to play an essential role in the sequence nonspecific export of cellular mRNAs. However, it has remained ...

Abstract	The Tap protein has been shown to activate the nuclear export of mRNA species bearing retroviral constitutive transport elements and is also believed to play an essential role in the sequence nonspecific export of cellular mRNAs. However, it has remained unclear how Tap activity is regulated in vivo. Here, we report that the small NXT1/p15-1 protein functions as a critical cofactor for Tap-mediated mRNA export in both human and invertebrate cells. In the absence of NXT1 binding, the Tap protein is unable to effectively interact with components of the nuclear pore complex and both Tap nucleocytoplasmic shuttling and the nuclear export of mRNA molecules tethered to Tap are therefore severely attenuated. Formation of a Tap/NXT1 heterodimer enhances nucleoporin binding both in vitro and in vivo and induces the formation of a Tap/NXT1/nucleoporin ternary complex that is likely to be a key intermediate in the process of nuclear mRNA export. The critical importance of NXT1 for the nuclear export of poly(A)(+) RNA is emphasized by the finding that specific inhibition of the expression of the Drosophila homolog of human NXT1, by using RNA interference, results in the nuclear accumulation of poly(A)(+) RNA in cultured insect cells. These data suggest that NXT1 may act as a molecular switch that regulates the ability of Tap to mediate nuclear mRNA export by controlling the interaction of Tap with components of the nuclear pore.
MeSH term(s)	Active Transport, Cell Nucleus/physiology ; Animals ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Cell Line ; Cell Nucleus/metabolism ; Cytoplasm/metabolism ; Dimerization ; Drosophila ; Drosophila Proteins ; Fluorescent Dyes/metabolism ; Genes, Reporter ; Humans ; Karyopherins/genetics ; Karyopherins/metabolism ; Microscopy, Fluorescence ; Nuclear Pore/metabolism ; Nuclear Pore Complex Proteins/genetics ; Nuclear Pore Complex Proteins/metabolism ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Nucleocytoplasmic Transport Proteins ; Protein Binding ; RNA, Messenger/metabolism ; RNA-Binding Proteins/genetics ; RNA-Binding Proteins/metabolism ; Receptors, CCR5/genetics ; Receptors, CCR5/metabolism ; Receptors, Cytoplasmic and Nuclear ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism ; Two-Hybrid System Techniques ; Exportin 1 Protein
Chemical Substances	Carrier Proteins ; Drosophila Proteins ; Fluorescent Dyes ; Karyopherins ; NXF1 protein, human ; NXT1 protein, human ; Nuclear Pore Complex Proteins ; Nuclear Proteins ; Nucleocytoplasmic Transport Proteins ; Nxt1 protein, Drosophila ; RNA, Messenger ; RNA-Binding Proteins ; Receptors, CCR5 ; Receptors, Cytoplasmic and Nuclear ; Recombinant Fusion Proteins
Language	English
Publishing date	2001-12-10
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	779397-2
ISSN	1098-5549 ; 0270-7306
ISSN (online)	1098-5549
ISSN	0270-7306
DOI	10.1128/MCB.22.1.245-256.2002
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Article: Inhibition of human immunodeficiency virus type 1 replication in primary macrophages by using Tat- or CCR5-specific small interfering RNAs expressed from a lentivirus vector.

Lee, Ming-Ta M / Coburn, Glen A / McClure, Myra O / Cullen, Bryan R

Journal of virology

2000 Volume 77, Issue 22, Page(s) 11964–11972

Abstract: Although several groups have demonstrated that RNA interference, induced by transfection of small interfering RNA (siRNA) duplexes, can protect cells against a viral challenge in culture, this protection is transient. Here, we describe lentivirus ... ...

Abstract	Although several groups have demonstrated that RNA interference, induced by transfection of small interfering RNA (siRNA) duplexes, can protect cells against a viral challenge in culture, this protection is transient. Here, we describe lentivirus expression vectors that can stably express siRNAs at levels sufficient to block virus replication. We have used these vectors to stably express siRNAs specific for the essential human immunodeficiency virus type 1 (HIV-1) Tat transcription factor or specific for a cellular coreceptor, CCR5, that is required for infection by the majority of primary HIV-1 isolates. These lentivirus vectors are shown to protect cells, including primary macrophages, against HIV-1 infection in culture by inducing selective degradation of their target mRNA species. These data suggest that it should be possible to block the expression of specific viral or cellular genes in vivo by using viral vectors to stably express the appropriate siRNAs.
MeSH term(s)	Antiviral Agents/physiology ; CCR5 Receptor Antagonists ; Cells, Cultured ; Genes, tat ; Genetic Therapy ; Genetic Vectors ; HIV-1/physiology ; Humans ; Lentivirus/genetics ; Macrophages/virology ; RNA, Small Interfering/genetics ; RNA, Small Interfering/physiology ; Receptors, CCR5/genetics ; Virus Replication
Chemical Substances	Antiviral Agents ; CCR5 Receptor Antagonists ; RNA, Small Interfering ; Receptors, CCR5
Language	English
Publishing date	2000-12-20
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/jvi.77.22.11964-11972.2003
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Article ; Online: Novel small-molecule inhibitors of hepatitis C virus entry block viral spread and promote viral clearance in cell culture.

Glen A Coburn / Danielle N Fisch / Sameer M Moorji / Jean-Marc de Muys / Jose D Murga / Dorothy Paul / Kathleen P Provoncha / Yakov Rotshteyn / Amy Q Han / Dapeng Qian / Paul J Maddon / William C Olson

PLoS ONE, Vol 7, Iss 4, p e

2012 Volume 35351

Abstract	Combinations of direct-acting anti-virals offer the potential to improve the efficacy, tolerability and duration of the current treatment regimen for hepatitis C virus (HCV) infection. Viral entry represents a distinct therapeutic target that has been validated clinically for a number of pathogenic viruses. To discover novel inhibitors of HCV entry, we conducted a high throughput screen of a proprietary small-molecule compound library using HCV pseudoviral particle (HCVpp) technology. We independently discovered and optimized a series of 1,3,5-triazine compounds that are potent, selective and non-cytotoxic inhibitors of HCV entry. Representative compounds fully suppress both cell-free virus and cell-to-cell spread of HCV in vitro. We demonstrate, for the first time, that long term treatment of an HCV cell culture with a potent entry inhibitor promotes sustained viral clearance in vitro. We have confirmed that a single amino acid variant, V719G, in the transmembrane domain of E2 is sufficient to confer resistance to multiple compounds from the triazine series. Resistance studies were extended by evaluating both the fusogenic properties and growth kinetics of drug-induced and natural amino acid variants in the HCVpp and HCV cell culture assays. Our results indicate that amino acid variations at position 719 incur a significant fitness penalty. Introduction of I719 into a genotype 1b envelope sequence did not affect HCV entry; however, the overall level of HCV replication was reduced compared to the parental genotype 1b/2a HCV strain. Consistent with these findings, I719 represents a significant fraction of the naturally occurring genotype 1b sequences. Importantly, I719, the most relevant natural polymorphism, did not significantly alter the susceptibility of HCV to the triazine compounds. The preclinical properties of these triazine compounds support further investigation of entry inhibitors as a potential novel therapy for HCV infection.
Keywords	Medicine ; R ; Science ; Q
Subject code	570
Language	English
Publishing date	2012-01-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
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Article ; Online: Effects of a carbohydrate-, protein-, and ribose-containing repletion drink during 8 weeks of endurance training on aerobic capacity, endurance performance, and body composition.

Cramer, Joel T / Housh, Terry J / Johnson, Glen O / Coburn, Jared W / Stout, Jeffrey R

Journal of strength and conditioning research

2012 Volume 26, Issue 8, Page(s) 2234–2242

Abstract: This study compared a carbohydrate-, protein-, and ribose-containing repletion drink vs. carbohydrates alone during 8 weeks of aerobic training. Thirty-two men (age, mean ± SD = 23 ± 3 years) performed tests for aerobic capacity (V(O2)peak), time to ... ...

Abstract	This study compared a carbohydrate-, protein-, and ribose-containing repletion drink vs. carbohydrates alone during 8 weeks of aerobic training. Thirty-two men (age, mean ± SD = 23 ± 3 years) performed tests for aerobic capacity (V(O2)peak), time to exhaustion (TTE) at 90% V(O2)peak, and percent body fat (%fat), and fat-free mass (FFM). Testing was conducted at pre-training (PRE), mid-training at 3 weeks (MID3), mid-training at 6 weeks (MID6), and post-training (POST). Cycle ergometry training was performed at 70% V(O2)peak for 1 hours per day, 5 days per week for 8 weeks. Participants were assigned to a test drink (TEST; 370 kcal, 76 g carbohydrate, 14 g protein, 2.2 g d-ribose; n = 15) or control drink (CON; 370 kcal, 93 g carbohydrate; n = 17) ingested immediately after training. Body weight (BW; 1.8% decrease CON; 1.3% decrease TEST from PRE to POST), %fat (5.5% decrease CON; 3.9% decrease TEST), and FFM (0.1% decrease CON; 0.6% decrease TEST) decreased (p ≤ 0.05), whereas V(O2)peak (19.1% increase CON; 15.8% increase TEST) and TTE (239.1% increase CON; 377.3% increase TEST) increased (p ≤ 0.05) throughout the 8 weeks of training. Percent decreases in %fat from PRE to MID3 and percent increases in FFM from PRE to MID3 and MID6 were greater (p ≤ 0.05) for TEST than CON. Overall, even though the TEST drink did not augment BW, V(O2)peak, or TTE beyond carbohydrates alone, it did improve body composition (%fat and FFM) within the first 3-6 weeks of supplementation, which may be helpful for practitioners to understand how carbohydrate-protein recovery drinks can and cannot improve performance in their athletes.
MeSH term(s)	Adult ; Beverages ; Body Composition/drug effects ; Body Composition/physiology ; Dietary Carbohydrates/administration & dosage ; Dietary Proteins/administration & dosage ; Dietary Supplements ; Exercise Test ; Exercise Tolerance/drug effects ; Exercise Tolerance/physiology ; Humans ; Male ; Oxygen Consumption/drug effects ; Oxygen Consumption/physiology ; Physical Endurance/drug effects ; Physical Endurance/physiology ; Ribose/administration & dosage ; Young Adult
Chemical Substances	Dietary Carbohydrates ; Dietary Proteins ; Ribose (681HV46001)
Language	English
Publishing date	2012-08
Publishing country	United States
Document type	Journal Article ; Randomized Controlled Trial ; Research Support, Non-U.S. Gov't
ZDB-ID	1156349-7
ISSN	1533-4287 ; 1064-8011
ISSN (online)	1533-4287
ISSN	1064-8011
DOI	10.1519/JSC.0b013e3182606cec
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Article ; Online: The discovery of pyrano[3,4-b]indole-based allosteric inhibitors of HCV NS5B polymerase with in vivo activity.

Laporte, Matthew G / Jackson, Randy W / Draper, Tandy L / Gaboury, Janet A / Galie, Kristin / Herbertz, Torsten / Hussey, Alison R / Rippin, Susan R / Benetatos, Christopher A / Chunduru, Srinivas K / Christensen, Joel S / Coburn, Glen A / Rizzo, Christopher J / Rhodes, Gerry / O'Connell, John / Howe, Anita Y M / Mansour, Tarek S / Collett, Marc S / Pevear, Daniel C /

Young, Dorothy C / Gao, Tiejun / Tyrrell, D Lorne J / Kneteman, Norman M / Burns, Christopher J / Condon, Stephen M

ChemMedChem

2008 Volume 3, Issue 10, Page(s) 1508–1515

MeSH term(s)	Allosteric Regulation ; Animals ; Antiviral Agents/chemical synthesis ; Antiviral Agents/chemistry ; Antiviral Agents/pharmacology ; Hepacivirus/drug effects ; Hepacivirus/genetics ; Hepacivirus/metabolism ; Indoles/chemical synthesis ; Indoles/chemistry ; Indoles/pharmacology ; Inhibitory Concentration 50 ; Mice ; Mice, SCID ; Mice, Transgenic ; Pyrans/chemical synthesis ; Pyrans/chemistry ; Pyrans/pharmacology ; RNA, Viral/blood ; RNA, Viral/isolation & purification ; RNA-Dependent RNA Polymerase/antagonists & inhibitors ; RNA-Dependent RNA Polymerase/metabolism ; Viral Nonstructural Proteins/antagonists & inhibitors ; Viral Nonstructural Proteins/metabolism
Chemical Substances	Antiviral Agents ; Indoles ; Pyrans ; RNA, Viral ; Viral Nonstructural Proteins ; NS-5 protein, hepatitis C virus (EC 2.7.7.48) ; RNA-Dependent RNA Polymerase (EC 2.7.7.48)
Language	English
Publishing date	2008-08-26
Publishing country	Germany
Document type	Journal Article
ZDB-ID	2218496-X
ISSN	1860-7187 ; 1860-7179
ISSN (online)	1860-7187
ISSN	1860-7179
DOI	10.1002/cmdc.200800168
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