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

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

Mutation research - 15 May 1996

Crone T M, Goodtzova K, Pegg A E

Abstract excerpt

Amino acid residues in the human O6-alkylguanine-DNA alkyltransferase (AGT) were mutated and seventeen of the mutant proteins expressed in the ada- ogt-E. coli strain GWR 109 which is very sensitive to killing by methylating agents because of the absence of endogenous alkyltransferases. Thirteen of the mutations tested (delta-10, delta 1-19, R128A, N137A, H146A, R147A, delta N157, Y158A, E172Q, delta 92-97,...

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 Base Sequence
Share to DNA Repair

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

Share to Escherichia coli

Share to Molecular Sequence Data

Share to Mutation

Share to Recombinant Proteins

Share to Structure-Activity Relationship

Source

Identifiers

PMID: 8632775
DOI: 10.1016/0921-8777(95)00058-5

Genes

AGT

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

Amino acid residues affecting the activity and stability of human O6-alkylguanine-DNA alkyltransferase.PMID 8632775Read ↗

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

Mutations in the Ada O6-alkylguanine-DNA alkyltransferase conferring sensitivity to inactivation by O6-benzylguanine and 2,4-diamino-6-benzyloxy-5-nitrosopyrimidine.Semantic proximity Read ↗

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

Interaction of mammalian O(6)-alkylguanine-DNA alkyltransferases with O(6)-benzylguanine.Semantic proximity Read ↗

The role of human O(6)-alkylguanine-DNA alkyltransferase in promoting 1,2-dibromoethane-induced genotoxicity in Escherichia coli.Semantic proximity Read ↗

Altering Residue 134 Confers an Increased Substrate Range of Alkylated Nucleosides to the E. coli OGT Protein.Semantic proximity Read ↗

Inhibition of O6-methylguanine-DNA methyltransferase by an alkyltransferase-like protein from Escherichia coli.Semantic proximity Read ↗

Tumor-associated mutations in O⁶ -methylguanine DNA-methyltransferase (MGMT) reduce DNA repair functionality.Semantic proximity Read ↗

Substrate binding pocket residues of human alkyladenine-DNA glycosylase critical for methylating agent survival.Semantic proximity Read ↗

Degradation of the alkylated form of the DNA repair protein, O(6)-alkylguanine-DNA alkyltransferase.Semantic proximity Read ↗

Substrate-Specific Inactivation of Human AAG by Tumor-Associated Single Nucleotide Polymorphic Variants.Semantic proximity Read ↗

Effect of O6-alkylguanine-DNA alkyltransferase on the frequency and spectrum of mutations induced by N-methyl-N'-nitro-N-nitrosoguanidine in the HPRT gene of diploid human fibroblasts.Semantic proximity Read ↗

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