📣 Help Shape the Future of UKRI's Gateway to Research (GtR)

We're improving UKRI's Gateway to Research and are seeking your input! If you would be interested in being interviewed about the improvements we're making and to have your say about how we can make GtR more user-friendly, impactful, and effective for the Research and Innovation community, please email gateway@ukri.org.

Conserved residues of the C-terminal p16 domain of primase are involved in modulating the activity of the bacterial primosome. (2008)

First Author: Chintakayala K

Attributed to: The molecular details of the bacterial helicase-primase complex funded by BBSRC

Abstract

No abstract provided

Bibliographic Information

Digital Object Identifier: http://dx.doi.org/10.1111/j.1365-2958.2008.06155.x

PubMed Identifier: 18366438

Publication URI: http://europepmc.org/abstract/MED/18366438

Type: Journal Article/Review

Volume: 68

Parent Publication: Molecular microbiology

Issue: 2

ISSN: 0950-382X