helicase

Various methods are used to measure helicase activity in vitro.

Precisely what goes wrong with helicase in Werner's syndrome is not known.

The helicase activity is located in the N terminal domain.

Below is a short description of the helicase discovery history:

Other helicase domains are also present in c4orf21 orthologs.

Mcm 2-7 form a six-subunit complex and is thought to have helicase activity.

In eukaryotes, helicase function is provided by the T antigen.

The Pif1 helicase is also involved in this pathway as it aids creation of long flaps.

In 1982-1983, the first direct biochemical assay was developed for measuring helicase activity.

The inhibited helicase activity leads to the inhibition of transcription.

These protein products have homology in seven conserved helicase motifs.

There is no helicase encoded by the virus.

The most studied SF4 helicase is gp4 from bacteriophage T7.

Without the Pif1 helicase, the flaps would not become long enough to need cleavage by Dna2.

A majority of these proteins are in the RNA helicase family.

The Ter-Tus complex is able to stop helicase activity, terminating replication.

This could cause the helicase to cut DNA segments meant for transcription.

Loading of the DnaB helicase is the key step in replication initiation.

Helicase motifs are conserved in many proteins.

This sequence has helicase and replicase activity.

It is a homolog of the bacterial RecQ helicase.

The variable portion of the amino acid sequence is related to the specific features of each helicase.

Among actinomycetales, it is common to find that the traA gene codes for both relaxase and helicase.

Relaxase also unwinds the plasmid being conjugated with its helicase properties.

However, local strand separation occurs by a process wherein the helicase enzyme is loaded at any place along the duplex.