Identification and characterization of a histone binding site of the non-structural protein 3 of hepatitis C virus (Q28139634)

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R Kühl

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R Laufs

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J Schulze zur Wiesch

Journal of Clinical Virology

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language of work or name

English

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publication date

June 1999

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published in

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volume

13

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issue

1-2

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page(s)

61-9

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cites work

Non-structural protein 3 of hepatitis C virus inhibits phosphorylation mediated by cAMP-dependent protein kinase

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Nonstructural protein 3 of hepatitis C virus blocks the distribution of the free catalytic subunit of cyclic AMP-dependent protein kinase

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7 January 2021

Characterisation of non-structural protein 3 of hepatitis C virus as modulator of protein phosphorylation mediated by PKA and PKC: evidences for action on the level of substrate and enzyme

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Protein kinase C recognizes the protein kinase A-binding motif of nonstructural protein 3 of hepatitis C virus

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Isolation of a cDNA clone derived from a blood-borne non-A, non-B viral hepatitis genome

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7 January 2021

Hepatitis C virus: the major causative agent of viral non-A, non-B hepatitis

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A simple graphical method for determining the inhibition constants of mixed, uncompetitive and non-competitive inhibitors

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The determination of enzyme inhibitor constants

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Characterization of RNA binding activity and RNA helicase activity of the hepatitis C virus NS3 protein

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A linear equation that describes the steady-state kinetics of enzymes and subcellular particles interacting with tightly bound inhibitors

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C-terminal domain of the hepatitis C virus NS3 protein contains an RNA helicase activity

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Hepatitis C virus shares amino acid sequence similarity with pestiviruses and flaviviruses as well as members of two plant virus supergroups

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7 January 2021

Structure of the histone octamer core of the nucleosome and its potential interactions with DNA

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Nuclear localization of the NS3 protein of hepatitis C virus and factors affecting the localization

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DNA sequencing with chain-terminating inhibitors

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Structure and organization of the hepatitis C virus genome isolated from human carriers

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Hepatitis C virus polyprotein processing: kinetics and mutagenic analysis of serine proteinase-dependent cleavage

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Review: molecular biology of the hepatitis C virus

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Transcription: in tune with the histones

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Structure of the hepatitis C virus RNA helicase domain

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A common topology of proteins catalyzing ATP-triggered reactions

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10.1016/S1386-6532(99)00007-4

Identifiers

DOI

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Fatcat ID

release_srjo4sixpfcavmiptd5ufty4yy

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/srjo4sixpfcavmiptd5ufty4yy

24 November 2022