scholarly article | Q13442814 |
P356 | DOI | 10.1002/PROT.25102 |
P698 | PubMed publication ID | 27410462 |
P2093 | author name string | Ping Xie | |
P2860 | cites work | Active and passive mechanisms of helicases | Q24610541 |
Single-molecule studies reveal dynamics of DNA unwinding by the ring-shaped T7 helicase | Q24642351 | ||
Real-time observation of bacteriophage T4 gp41 helicase reveals an unwinding mechanism | Q24669910 | ||
RNA translocation and unwinding mechanism of HCV NS3 helicase and its coordination by ATP | Q27477448 | ||
NS3 helicase actively separates RNA strands and senses sequence barriers ahead of the opening fork | Q27481047 | ||
Three conformational snapshots of the hepatitis C virus NS3 helicase reveal a ratchet translocation mechanism | Q27490905 | ||
Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism | Q27617870 | ||
Crystal structure of the N-terminal domain of the DnaB hexameric helicase | Q27619052 | ||
Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides | Q27625337 | ||
UvrD helicase unwinds DNA one base pair at a time by a two-part power stroke | Q27640956 | ||
High-resolution structure of the E.coli RecQ helicase catalytic core | Q27642248 | ||
Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP | Q27742867 | ||
Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding | Q27748908 | ||
Protein structure. Engineering of a superhelicase through conformational control | Q30373810 | ||
Protein structure. Direct observation of structure-function relationship in a nucleic acid-processing enzyme | Q30373812 | ||
Direct imaging of single UvrD helicase dynamics on long single-stranded DNA | Q30540348 | ||
DNA helicases: 'inching forward'. | Q33840733 | ||
Autoinhibition of Escherichia coli Rep monomer helicase activity by its 2B subdomain | Q33900524 | ||
The 2B domain of the Escherichia coli Rep protein is not required for DNA helicase activity | Q34415176 | ||
Opening of nucleic-acid double strands by helicases: active versus passive opening. | Q34554888 | ||
Monomeric PcrA helicase processively unwinds plasmid lengths of DNA in the presence of the initiator protein RepD. | Q34638456 | ||
Uncoupling DNA translocation and helicase activity in PcrA: direct evidence for an active mechanism. | Q35116428 | ||
Dda helicase tightly couples translocation on single-stranded DNA to unwinding of duplex DNA: Dda is an optimally active helicase | Q36024282 | ||
Helicase processivity and not the unwinding velocity exhibits universal increase with force | Q36209445 | ||
Dwell-Time Distribution, Long Pausing and Arrest of Single-Ribosome Translation through the mRNA Duplex | Q36247332 | ||
Mechanisms of a ring shaped helicase | Q36578943 | ||
Overstretching B-DNA: the elastic response of individual double-stranded and single-stranded DNA molecules | Q36798786 | ||
Sequence-dependent base pair stepping dynamics in XPD helicase unwinding. | Q36889452 | ||
PcrA helicase tightly couples ATP hydrolysis to unwinding double-stranded DNA, modulated by the initiator protein for plasmid replication, RepD. | Q37420255 | ||
Single-molecule fluorescence reveals the unwinding stepping mechanism of replicative helicase. | Q37706259 | ||
Interactions of bacteriophage T7 DNA primase/helicase protein with single-stranded and double-stranded DNAs | Q38314172 | ||
Escherichia coli DNA helicase II is active as a monomer | Q38325692 | ||
Kinetic mechanism for formation of the active, dimeric UvrD helicase-DNA complex | Q38353902 | ||
Model of ribosome translation and mRNA unwinding | Q39498168 | ||
Dynamics of monomeric and hexameric helicases | Q39963769 | ||
A unified model of nucleic acid unwinding by the ribosome and the hexameric and monomeric DNA helicases | Q40818710 | ||
Single-molecule imaging of the oligomer formation of the nonhexameric Escherichia coli UvrD helicase | Q41761243 | ||
Single-base pair unwinding and asynchronous RNA release by the hepatitis C virus NS3 helicase | Q41820638 | ||
ATP binding modulates the nucleic acid affinity of hepatitis C virus helicase | Q43049108 | ||
E. coli Rep oligomers are required to initiate DNA unwinding in vitro | Q43655291 | ||
T7 DNA helicase: a molecular motor that processively and unidirectionally translocates along single-stranded DNA. | Q44121888 | ||
Initiation and re-initiation of DNA unwinding by the Escherichia coli Rep helicase | Q44175920 | ||
A Dimer of Escherichia coli UvrD is the active form of the helicase in vitro | Q44277846 | ||
A motor that makes its own track: helicase unwinding of DNA. | Q53848563 | ||
Bacillus stearothermophilus PcrA monomer is a single-stranded DNA translocase but not a processive helicase in vitro. | Q54437963 | ||
P433 | issue | 11 | |
P407 | language of work or name | English | Q1860 |
P304 | page(s) | 1590-1605 | |
P577 | publication date | 2016-07-13 | |
P1433 | published in | Proteins | Q7251514 |
P1476 | title | Processivity of nucleic acid unwinding and translocation by helicases | |
P478 | volume | 84 |