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

Specific amino acid sequences required for O6-methylguanine-DNA methyltransferase activity: analyses of three residues at or near the methyl acceptor site.

Carcinogenesis - 1 May 1992

Chueh L L, Nakamura T, Nakatsu Y, Sakumi K, Hayakawa H, Sekiguchi M

Abstract excerpt

O6-Methylguanine-DNA methyltransferase plays an important role in preventing tumor induction. To elucidate the significance of a highly conserved amino acid sequence of methyltransferase protein, amino acid substitutions were introduced by site-directed mutagenesis of cloned cDNA for human methyltransferase and the activity and stability of mutant forms of enzyme were examined. When cysteine-145, to which the...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Cysteine

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

Share to Drug Resistance

Share to Escherichia coli

Share to Histidine

Share to Molecular Sequence Data

Share to Mutation

Share to Phenotype

Source

Identifiers

PMID: 1586996
DOI: 10.1093/carcin/13.5.837

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

Specific amino acid sequences required for O6-methylguanine-DNA methyltransferase activity: analyses of three residues at or near the methyl acceptor site.PMID 1586996Read ↗

Mutations in human O6-alkylguanine-DNA alkyltransferase imparting resistance to O6-benzylguanine.Semantic proximity Read ↗

Amino acid residues affecting the activity and stability of human O6-alkylguanine-DNA alkyltransferase.Semantic proximity Read ↗

DNA methylation and cancer.Semantic proximity Read ↗

cDNA cloning and chromosomal assignment of the human O6-methylguanine-DNA methyltransferase. cDNA expression in Escherichia coli and gene expression in human cells.Semantic proximity Read ↗

Selective excision of 5-carboxylcytosine by a thymine DNA glycosylase mutant.Semantic proximity Read ↗

Regulation of O6-methylguanine-DNA methyltransferase by methionine in human tumour cellsSemantic proximity Read ↗

The role of tyrosine-158 in O6-alkylguanine-DNA alkyltransferase activity.Semantic proximity Read ↗

Dominant sensitization variants of human O(6)-methylguanine-DNA-methyltransferase obtained by a mutational screen of surface residues.Semantic proximity Read ↗

Creation of human alkyltransferases resistant to O6-benzylguanine.Semantic proximity Read ↗

A comparative study of the biochemical properties of human and mouse recombinant O6-methylguanine-DNA methyltransferases.Semantic proximity Read ↗

Identification of amino acids important for target recognition by the DNA:m5C methyltransferase M.NgoPII by alanine-scanning mutagenesis of residues at the protein-DNA interface.Semantic proximity Read ↗

The role of two conserved amino acids, glutamine 90 and asparagine 137, in O6-methylguanine-DNA methyltransferase stability, activity and substrate specificity.Semantic proximity Read ↗

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