| scholarly article | Q13442814 |
| P2093 | author name string | Yuh-Hwa Wang | |
| Smita S Patel | |||
| Mikhail K Levin | |||
| P2860 | cites work | The hepatitis C viral NS3 protein is a processive DNA helicase with cofactor enhanced RNA unwinding | Q27472668 |
| A novel recombinant single-chain hepatitis C virus ns3-ns4a protein with improved helicase activity | Q27484233 | ||
| Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism | Q27617870 | ||
| Molecular views of viral polyprotein processing revealed by the crystal structure of the hepatitis C virus bifunctional protease-helicase | Q27620480 | ||
| Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding | Q27748908 | ||
| Modulation of hepatitis C virus NS3 protease and helicase activities through the interaction with NS4A | Q28374365 | ||
| C-terminal domain of the hepatitis C virus NS3 protein contains an RNA helicase activity | Q29620775 | ||
| Structure of helical RecA-DNA complexes. Complexes formed in the presence of ATP-gamma-S or ATP. | Q30403249 | ||
| Structure and function of hexameric helicases. | Q34019405 | ||
| General Methods for Analysis of Sequential “n-step” Kinetic Mechanisms: Application to Single Turnover Kinetics of Helicase-Catalyzed DNA Unwinding | Q34183054 | ||
| Pre-steady-state DNA unwinding by bacteriophage T4 Dda helicase reveals a monomeric molecular motor | Q34379148 | ||
| Bacteriophage T7 helicase/primase proteins form rings around single-stranded DNA that suggest a general structure for hexameric helicases | Q34387475 | ||
| Escherichia coli single-strand binding protein organizes single-stranded DNA in nucleosome-like units | Q36313556 | ||
| The nonstructural protein 3 protease/helicase requires an intact protease domain to unwind duplex RNA efficiently | Q36607807 | ||
| Unwinding of nucleic acids by HCV NS3 helicase is sensitive to the structure of the duplex | Q38305257 | ||
| An oligomeric form of E. coli UvrD is required for optimal helicase activity | Q38318982 | ||
| DNA helicases displace streptavidin from biotin-labeled oligonucleotides | Q38325603 | ||
| Transcription through the roadblocks: the role of RNA polymerase cooperation | Q39958725 | ||
| DNA helicases: enzymes with essential roles in all aspects of DNA metabolism | Q40732300 | ||
| Mechanisms of helicase-catalyzed DNA unwinding | Q41114786 | ||
| Hepatitis C virus NS3 RNA helicase activity is modulated by the two domains of NS3 and NS4A. | Q42045177 | ||
| Identification of the protease domain in NS3 of hepatitis C virus | Q42981605 | ||
| Product release is the major contributor to kcat for the hepatitis C virus helicase-catalyzed strand separation of short duplex DNA. | Q42989097 | ||
| The helicase from hepatitis C virus is active as an oligomer | Q42995731 | ||
| Helicase from hepatitis C virus, energetics of DNA binding | Q43038035 | ||
| E. coli Rep oligomers are required to initiate DNA unwinding in vitro | Q43655291 | ||
| DNA unwinding step-size of E. coli RecBCD helicase determined from single turnover chemical quenched-flow kinetic studies | Q44225424 | ||
| A Dimer of Escherichia coli UvrD is the active form of the helicase in vitro | Q44277846 | ||
| Cooperation between RNA polymerase molecules in transcription elongation | Q44429561 | ||
| A steady-state and pre-steady-state kinetic analysis of the NTPase activity associated with the hepatitis C virus NS3 helicase domain | Q45768399 | ||
| Characterization of RNA binding activity and RNA helicase activity of the hepatitis C virus NS3 protein | Q45769053 | ||
| Kinetic measurement of the step size of DNA unwinding by Escherichia coli UvrD helicase | Q47315601 | ||
| The Escherichia coli RecQ helicase functions as a monomer | Q47834685 | ||
| A Complex of the Bacteriophage T7 Primase-Helicase and DNA Polymerase Directs Primer Utilization | Q56904697 | ||
| The DExH protein NPH-II is a processive and directional motor for unwinding RNA | Q57259026 | ||
| P433 | issue | 25 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | hepatitis C | Q154869 |
| Hepatitis C virus | Q708693 | ||
| P304 | page(s) | 26005-26012 | |
| P577 | publication date | 2004-04-14 | |
| P1433 | published in | Journal of Biological Chemistry | Q867727 |
| P1476 | title | The functional interaction of the hepatitis C virus helicase molecules is responsible for unwinding processivity | |
| P478 | volume | 279 |
| Q42991620 | A Brownian motor mechanism of translocation and strand separation by hepatitis C virus helicase |
| Q27487128 | A Genetic Interaction between Hepatitis C Virus NS4B and NS3 Is Important for RNA Replication |
| Q90245981 | A high ATP concentration enhances the cooperative translocation of the SARS coronavirus helicase nsP13 in the unwinding of duplex RNA |
| Q33900524 | Autoinhibition of Escherichia coli Rep monomer helicase activity by its 2B subdomain |
| Q41841562 | Binding by the hepatitis C virus NS3 helicase partially melts duplex DNA. |
| Q34368072 | Cooperative translocation enhances the unwinding of duplex DNA by SARS coronavirus helicase nsP13. |
| Q38756284 | DNA mechanics as a tool to probe helicase and translocase activity. |
| Q34652749 | DNA unwinding and protein displacement by superfamily 1 and superfamily 2 helicases |
| Q54455405 | DNA unwinding by Escherichia coli DNA helicase I (TraI) provides evidence for a processive monomeric molecular motor. |
| Q30420796 | Development of chemical inhibitors of the SARS coronavirus: viral helicase as a potential target |
| Q34658134 | Displacement of a DNA binding protein by Dda helicase |
| Q47104636 | Dissociation of Rad51 Presynaptic Complexes and Heteroduplex DNA Joints by Tandem Assemblies of Srs2. |
| Q27676962 | Domain-level rocking motion within a polymerase that translocates on single-stranded nucleic acid |
| Q38066334 | Duplex RNA activated ATPases (DRAs): platforms for RNA sensing, signaling and processing |
| Q40545307 | Effect of D168V mutation in NS3/4A HCV protease on susceptibilities of faldaprevir and danoprevir |
| Q37346577 | Enhanced nucleic acid binding to ATP-bound hepatitis C virus NS3 helicase at low pH activates RNA unwinding |
| Q27478372 | Enzymatic Defects of the nsP2 Proteins of Semliki Forest Virus Temperature-Sensitive Mutants |
| Q41963658 | Escherichia coli RNase R has dual activities, helicase and RNase |
| Q27487760 | Establishing a Mechanistic Basis for the Large Kinetic Steps of the NS3 Helicase |
| Q36593736 | Evidence for a functional dimeric form of the PcrA helicase in DNA unwinding |
| Q36394319 | Fine tuning of a DNA fork by the RecQ helicase |
| Q24701782 | Functional cross-talk between distant domains of chikungunya virus non-structural protein 2 is decisive for its RNA-modulating activity |
| Q27488958 | Helicase inhibitors as specifically targeted antiviral therapy for hepatitis C |
| Q27486377 | Hepatitis C virus NS3 helicase forms oligomeric structures that exhibit optimal DNA unwinding activity in vitro |
| Q37547774 | Hepatitis C virus RNA replication and virus particle assembly require specific dimerization of the NS4A protein transmembrane domain. |
| Q34003758 | Hepatitis C virus non-structural protein 3 (HCV NS3): a multifunctional antiviral target |
| Q35545841 | Inhibition of BACH1 (FANCJ) helicase by backbone discontinuity is overcome by increased motor ATPase or length of loading strand. |
| Q42978132 | Insights into the oligomerization state-helicase activity relationship of West Nile virus NS3 NTPase/helicase |
| Q64388590 | Intermediates revealed in the kinetic mechanism for DNA unwinding by a monomeric helicase |
| Q27491347 | Investigation of Translocation, DNA Unwinding, and Protein Displacement by NS3h, the Helicase Domain from the Hepatitis C Virus Helicase |
| Q37560680 | Isothermal DNA amplification in vitro: the helicase-dependent amplification system |
| Q33876054 | Kinetic mechanism for DNA unwinding by multiple molecules of Dda helicase aligned on DNA. |
| Q38345204 | Kinetics of DNA unwinding by the RecD2 helicase from Deinococcus radiodurans |
| Q34277309 | Mechanism of nucleic acid unwinding by SARS-CoV helicase. |
| Q34521150 | Mechanisms of helicases |
| Q40507545 | Modulation of the nucleoside triphosphatase/RNA helicase and 5'-RNA triphosphatase activities of Dengue virus type 2 nonstructural protein 3 (NS3) by interaction with NS5, the RNA-dependent RNA polymerase. |
| Q27487294 | Monitoring helicase activity with molecular beacons |
| Q34638456 | Monomeric PcrA helicase processively unwinds plasmid lengths of DNA in the presence of the initiator protein RepD. |
| Q34312992 | Monomeric nature of dengue virus NS3 helicase and thermodynamic analysis of the interaction with single-stranded RNA. |
| Q39761738 | Multiple Escherichia coli RecQ helicase monomers cooperate to unwind long DNA substrates: a fluorescence cross-correlation spectroscopy study. |
| Q38332393 | Multiple full-length NS3 molecules are required for optimal unwinding of oligonucleotide DNA in vitro |
| Q33855134 | Mutual inhibition of RecQ molecules in DNA unwinding |
| Q27487940 | NS3 Helicase from the Hepatitis C Virus Can Function as a Monomer or Oligomer Depending on Enzyme and Substrate Concentrations |
| Q27485332 | NS3 Peptide, a Novel Potent Hepatitis C Virus NS3 Helicase Inhibitor: Its Mechanism of Action and Antiviral Activity in the Replicon System |
| Q43047125 | NS3 from Hepatitis C Virus Strain JFH-1 Is an Unusually Robust Helicase That Is Primed To Bind and Unwind Viral RNA. |
| Q34770065 | Non-hexameric DNA helicases and translocases: mechanisms and regulation |
| Q114704016 | Novel insights into the function of an N-terminal region of DENV2 NS4B for the optimal helicase activity of NS3 |
| Q43037770 | Nucleic acid unwinding by hepatitis C virus and bacteriophage t7 helicases is sensitive to base pair stability |
| Q34144302 | PcrA helicase dismantles RecA filaments by reeling in DNA in uniform steps |
| Q37420255 | PcrA helicase tightly couples ATP hydrolysis to unwinding double-stranded DNA, modulated by the initiator protein for plasmid replication, RepD. |
| Q42986507 | Periodic cycles of RNA unwinding and pausing by hepatitis C virus NS3 helicase |
| Q57752886 | Pif1 helicase unfolding of G-quadruplex DNA is highly dependent on sequence and reaction conditions |
| Q38341109 | Protein displacement by an assembly of helicase molecules aligned along single-stranded DNA. |
| Q27477448 | RNA translocation and unwinding mechanism of HCV NS3 helicase and its coordination by ATP |
| Q31095266 | RPA alleviates the inhibitory effect of vinylphosphonate internucleotide linkages on DNA unwinding by BLM and WRN helicases |
| Q27478187 | Role of Divalent Metal Cations in ATP Hydrolysis Catalyzed by the Hepatitis C Virus NS3 Helicase: Magnesium Provides a Bridge for ATP to Fuel Unwinding |
| Q36889452 | Sequence-dependent base pair stepping dynamics in XPD helicase unwinding. |
| Q34316979 | Severe acute respiratory syndrome coronavirus replication inhibitor that interferes with the nucleic acid unwinding of the viral helicase |
| Q34313069 | Simultaneous binding to the tracking strand, displaced strand and the duplex of a DNA fork enhances unwinding by Dda helicase |
| Q27485422 | Single Strand Binding Proteins Increase the Processivity of DNA Unwinding by the Hepatitis C Virus Helicase |
| Q27318290 | Single-molecule visualization of RecQ helicase reveals DNA melting, nucleation, and assembly are required for processive DNA unwinding |
| Q36016901 | Specific domains in yeast translation initiation factor eIF4G strongly bias RNA unwinding activity of the eIF4F complex toward duplexes with 5'-overhangs |
| Q36490245 | Step-by-step progress toward understanding the hepatitis C virus RNA helicase |
| Q41960449 | Stimulation of UvrD helicase by UvrAB. |
| Q38318511 | Structural and biological identification of residues on the surface of NS3 helicase required for optimal replication of the hepatitis C virus |
| Q47814527 | Structure and function of Pif1 helicase |
| Q27473280 | Structure-Based Mutational Analysis of the NS3 Helicase from Dengue Virus |
| Q27481034 | Studying Hepatitis C Virus: Making the Best of a Bad Virus |
| Q43216345 | The Q Motif Is Involved in DNA Binding but Not ATP Binding in ChlR1 Helicase |
| Q34607601 | The hepatitis C virus NS3 protein: a model RNA helicase and potential drug target |
| Q33885300 | The protease domain increases the translocation stepping efficiency of the hepatitis C virus NS3-4A helicase |
| Q42980155 | Two-state model for helicase translocation and unwinding of nucleic acids |
| Q36447325 | Understanding helicases as a means of virus control. |
| Q42017301 | Unmasking the active helicase conformation of nonstructural protein 3 from hepatitis C virus |
| Q39174963 | Unwinding activity of cold shock proteins and RNA metabolism |
| Q38286510 | What we know but do not understand about nidovirus helicases |
| Q27932247 | Yeast Pif1 helicase exhibits a one-base-pair stepping mechanism for unwinding duplex DNA |
| Q92287295 | Zika virus NS3 is a canonical RNA helicase stimulated by NS5 RNA polymerase |
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