| scholarly article | Q13442814 |
| P2093 | author name string | T M Lohman | |
| J A Ali | |||
| N K Maluf | |||
| P433 | issue | 4 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | Escherichia coli | Q25419 |
| P304 | page(s) | 815-834 | |
| P577 | publication date | 1999-11-01 | |
| P1433 | published in | Journal of Molecular Biology | Q925779 |
| P1476 | title | An oligomeric form of E. coli UvrD is required for optimal helicase activity | |
| P478 | volume | 293 |
| Q42991620 | A Brownian motor mechanism of translocation and strand separation by hepatitis C virus helicase |
| Q44277846 | A Dimer of Escherichia coli UvrD is the active form of the helicase in vitro |
| Q42030386 | A nonuniform stepping mechanism for E. coli UvrD monomer translocation along single-stranded DNA |
| Q35173001 | A parallel quadruplex DNA is bound tightly but unfolded slowly by pif1 helicase |
| Q49354812 | Advanced DNA-Based Point-of-Care Diagnostic Methods for Plant Diseases Detection |
| Q38000984 | Alternative molecular tests for virological diagnosis. |
| Q54437963 | Bacillus stearothermophilus PcrA monomer is a single-stranded DNA translocase but not a processive helicase in vitro. |
| Q38311085 | Characterisation of the catalytically active form of RecG helicase |
| Q24305956 | Characterization and mutational analysis of the RecQ core of the bloom syndrome protein |
| Q43198071 | Characterization of a thermostable UvrD helicase and its participation in helicase-dependent amplification |
| Q42925190 | DNA Binding Induces Dimerization of Saccharomyces cerevisiae Pif1 |
| Q40458920 | DNA Helicases. |
| Q44225424 | DNA unwinding step-size of E. coli RecBCD helicase determined from single turnover chemical quenched-flow kinetic studies |
| Q90110279 | DNA-Unwinding Dynamics of Escherichia coli UvrD Lacking the C-Terminal 40 Amino Acids |
| Q30420796 | Development of chemical inhibitors of the SARS coronavirus: viral helicase as a potential target |
| Q30540348 | Direct imaging of single UvrD helicase dynamics on long single-stranded DNA |
| Q44199583 | DnaB drives DNA branch migration and dislodges proteins while encircling two DNA strands. |
| Q38346362 | Ensemble and single-molecule fluorescence-based assays to monitor DNA binding, translocation, and unwinding by iron-sulfur cluster containing helicases. |
| Q28360438 | Escherichia coli DbpA is an RNA helicase that requires hairpin 92 of 23S rRNA. |
| Q38308417 | Escherichia coli MutL loads DNA helicase II onto DNA. |
| Q36593736 | Evidence for a functional dimeric form of the PcrA helicase in DNA unwinding |
| Q73693880 | Evidence for a functional monomeric form of the bacteriophage T4 DdA helicase. Dda does not form stable oligomeric structures |
| Q37745673 | Fluorometric assays for characterizing DNA helicases |
| Q34183054 | General Methods for Analysis of Sequential “n-step” Kinetic Mechanisms: Application to Single Turnover Kinetics of Helicase-Catalyzed DNA Unwinding |
| Q38240728 | Grip it and rip it: structural mechanisms of DNA helicase substrate binding and unwinding. |
| Q43038035 | Helicase from hepatitis C virus, energetics of DNA binding |
| Q24533521 | Helicase-dependent isothermal DNA amplification |
| Q44175920 | Initiation and re-initiation of DNA unwinding by the Escherichia coli Rep helicase |
| Q37777437 | Insight into helicase mechanism and function revealed through single-molecule approaches |
| Q38353902 | Kinetic mechanism for formation of the active, dimeric UvrD helicase-DNA complex |
| Q47583592 | Large domain movements upon UvrD dimerization and helicase activation |
| Q34521150 | Mechanisms of helicases |
| Q33967263 | Modulation of UvrD helicase activity by covalent DNA-protein cross-links |
| Q38332393 | Multiple full-length NS3 molecules are required for optimal unwinding of oligonucleotide DNA in vitro |
| Q27469761 | Mutations That Affect Dimer Formation and Helicase Activity of the Hepatitis C Virus Helicase |
| Q33855134 | Mutual inhibition of RecQ molecules in DNA unwinding |
| Q34770065 | Non-hexameric DNA helicases and translocases: mechanisms and regulation |
| 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 |
| Q57752886 | Pif1 helicase unfolding of G-quadruplex DNA is highly dependent on sequence and reaction conditions |
| Q34379148 | Pre-steady-state DNA unwinding by bacteriophage T4 Dda helicase reveals a monomeric molecular motor |
| Q38341109 | Protein displacement by an assembly of helicase molecules aligned along single-stranded DNA. |
| Q30373812 | Protein structure. Direct observation of structure-function relationship in a nucleic acid-processing enzyme |
| Q28910444 | RNA Remodeling Activity of DEAD Box Proteins Tuned by Protein Concentration, RNA Length, and ATP |
| Q24598928 | RecQ helicase translocates along single-stranded DNA with a moderate processivity and tight mechanochemical coupling |
| Q57752804 | Regulation of UvrD Helicase Activity by MutL |
| Q36761497 | Regulation of bacterial RecA protein function |
| Q35211193 | Self-assembly of Escherichia coli MutL and its complexes with DNA |
| Q38358750 | Self-association equilibria of Escherichia coli UvrD helicase studied by analytical ultracentrifugation |
| Q36889452 | Sequence-dependent base pair stepping dynamics in XPD helicase unwinding. |
| Q30579543 | Single-molecule assay reveals strand switching and enhanced processivity of UvrD |
| Q41761243 | Single-molecule imaging of the oligomer formation of the nonhexameric Escherichia coli UvrD helicase |
| Q42921287 | Structure and Mechanisms of SF1 DNA Helicases |
| Q43858136 | Studies on the mode of Ku interaction with DNA. |
| Q55054097 | Superfamily I helicases as modular components of DNA-processing machines. |
| Q34415176 | The 2B domain of the Escherichia coli Rep protein is not required for DNA helicase activity |
| Q33761309 | The UvrD303 hyper-helicase exhibits increased processivity |
| Q45651468 | The functional interaction of the hepatitis C virus helicase molecules is responsible for unwinding processivity |
| Q33885300 | The protease domain increases the translocation stepping efficiency of the hepatitis C virus NS3-4A helicase |
| Q38350448 | The unstructured C-terminal extension of UvrD interacts with UvrB, but is dispensable for nucleotide excision repair |
| Q36783587 | Translocation of Saccharomyces cerevisiae Pif1 helicase monomers on single-stranded DNA. |
| Q92295767 | UvrD helicase activation by MutL involves rotation of its 2B subdomain |
| Q38286510 | What we know but do not understand about nidovirus helicases |
Search more.