Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Comparison of DNA polymerases alpha, delta, and epsilon of mouse cell line FM3A and its temperature-sensitive mutant tsFT20.

The Tohoku journal of experimental medicine - 1 Jan 1994

Ikehata H

Abstract excerpt

DNA polymerases (pol) alpha, delta and epsilon of a mouse cell line FM3A and its temperature-sensitive derivative tsFT20, which is defective in DNA replication at a non-permissive temperature, were purified by chromatographic procedures monitored by a set of relatively specific assays for the respective DNA polymerase activities. The pol epsilon activity was separated into two fractions with similar enzymatic...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to DNA-Directed DNA Polymerase
Share to DNA Replication
Share to Enzyme Stability

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Mice, Inbred C3H

Share to Mutation

Share to Temperature

Share to Tumor Cells, Cultured

Source

Identifiers

PMID: 8036623
DOI: 10.1620/tjem.172.65

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Comparison of DNA polymerases alpha, delta, and epsilon of mouse cell line FM3A and its temperature-sensitive mutant tsFT20.PMID 8036623Read ↗

Immunoaffinity-purified DNA polymerase alpha from a mouse temperature-sensitive mutant, tsFT20 strain, is heat-labile.Semantic proximity Read ↗

Isolation of temperature-sensitive cell cycle mutants from mouse FM3A cells. Characterization of mutants with special reference to DNA replication.Semantic proximity Read ↗

Characterization of DNA synthesis at a restrictive temperature in the temperature-sensitive mutants, tsFT5 cells, that belong to the complementation group of ts85 cells containing a thermolabile ubiquitin-activating enzyme E1. Involvement of the ubiquitin-conjugating system in DNA replication.Semantic proximity Read ↗

In vivo reconstitution of Saccharomyces cerevisiae DNA polymerase epsilon in insect cells. Purification and characterization.Semantic proximity Read ↗

Complementation by a cloned human ubiquitin-activating enzyme E1 of the S-phase-arrested mouse FM3A cell mutant with thermolabile E1.Semantic proximity Read ↗

Characterization of DNA synthesis and DNA-dependent ATPase activity at a restrictive temperature in temperature-sensitive tsFT848 cells with thermolabile DNA helicase B.Semantic proximity Read ↗

A backup role of DNA polymerase kappa in Ig gene hypermutation only takes place in the complete absence of DNA polymerase eta.Semantic proximity Read ↗

The essential DNA polymerases delta and epsilon are involved in repair of UV-damaged DNA in the yeast Saccharomyces cerevisiae.Semantic proximity Read ↗

Fidelity of DNA polymerase alpha partially purified from a mutator mutant and wild-type mouse FM3A cells.Semantic proximity Read ↗

Defective DNA replication and repair associated with decreases in deoxyribonucleotide pools in a mouse cell mutant with thermolabile ubiquitin-activating enzyme E1.Semantic proximity Read ↗

Temperature-sensitive mutation of DNA polymerase alpha induces growth-suppressive phenotypes involving retinoblastoma protein and cyclin D1.Semantic proximity Read ↗

Involvement of the essential yeast DNA polymerases in induced gene conversion.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.