Molecular cloning of a cDNA encoding mouse DNA helicase B, which has homology to Escherichia coli RecD protein, and identification of a mutation in the DNA helicase B from tsFT848 temperature-sensitive DNA replication mutant cells

Author： Omori A.   Ishimi Y.   Tada S.   Kobayashi T.   Kusa Y.   Okumura N.   Kodaira H.   Seki M.   Enomoto T.  

Publisher： Oxford University Press

ISSN： 1362-4962

Source： Nucleic Acids Research, Vol.29, Iss.18, 2001-09, pp. : 3835-3840

Disclaimer: Any content in publications that violate the sovereignty, the constitution or regulations of the PRC is not accepted or approved by CNPIEC.

Previous Menu Next

Abstract

Related content

DNA Binding and Helicase Domains of the Escherichia Coli Recombination Protein RecG

By Mahdi Akeel A.   McGlynn Peter   Levett Stuart D.   Lloyd Robert G.  

Nucleic Acids Research, Vol. 25, Iss. 19, 1997-10 ,pp. : 3875-3880

Oxford University Press

Access to resources Recommend Favorite

Bacteriophage P1 Ban protein is a hexameric DNA helicase that interacts with and substitutes for Escherichia coli DnaB

By Lemonnier Marc  

Nucleic Acids Research, Vol. 31, Iss. 14, 2003-07 ,pp. : 3918-3928

Oxford University Press

Access to resources Recommend Favorite

Cloning of a cDNA Encoding a Novel Importin-alpha Homologue, Qip1: Discrimination of Qip1 and Rch1 from hSrp1 by Their Ability to Interact with DNA Helicase Q1/RecQL

By Seki T.   Tada S.   Katada T.   Enomoto T.  

Biochemical and Biophysical Research Communications, Vol. 234, Iss. 1, 1997-05 ,pp. : 48-53

Elsevier

Access to resources Recommend Favorite

A DNA Helicase Purified by Replication Protein a (RPA) Affinity Chromatography from Mouse FM3A Cells

By Hughes Patrick   Baldacci Giuseppe  

Nucleic Acids Research, Vol. 25, Iss. 19, 1997-10 ,pp. : 3881-3888

Oxford University Press

Access to resources Recommend Favorite

An Arabidopsis cDNA encoding a DNA-binding protein that is highly similar to the DEAH family of RNA/DNA helicase genes

By Isono Kyoichi   Yamamoto Hiroshi  

Nucleic Acids Research, Vol. 27, Iss. 18, 1999-09 ,pp. : 3728-3735

Oxford University Press

Access to resources Recommend Favorite