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

A conserved motif in the disordered linker of human MLH1 is vital for DNA mismatch repair and its function is diminished by a cancer family mutation.

Nucleic acids research - 7 Jul 2023

Wolf Karla, Kosinski Jan, Gibson Toby J, Wesch Nicole, Dötsch Volker, Genuardi Maurizio, Cordisco Emanuela Lucci, Zeuzem Stefan, Brieger Angela, Plotz Guido

Abstract excerpt

DNA mismatch repair (MMR) is essential for correction of DNA replication errors. Germline mutations of the human MMR gene MLH1 are the major cause of Lynch syndrome, a heritable cancer predisposition. In the MLH1 protein, a non-conserved, intrinsically disordered region connects two conserved, catalytically active structured domains of MLH1. This region has as yet been regarded as a flexible spacer, and missense...

Read the complete abstract on PubMed

Topics

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

Share to Colorectal Neoplasms, Hereditary Nonpolyposis
Share to DNA Mismatch Repair

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Genetic Predisposition to Disease

Share to Germ-Line Mutation

Share to Mutation

Share to MutL Protein Homolog 1

Share to MutS Homolog 2 Protein

Share to Nuclear Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 37224528
DOI: 10.1093/nar/gkad418
PMCID: PMC10325900

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A conserved motif in the disordered linker of human MLH1 is vital for DNA mismatch repair and its function is diminished by a cancer family mutation.PMID 37224528Read ↗

Disruption of protein-protein interaction hotspots in the C-terminal domain of MLH1 confers mismatch repair deficiency.Semantic proximity Read ↗

Characterization of a highly conserved binding site of Mlh1 required for exonuclease I-dependent mismatch repair.Semantic proximity Read ↗

Structure of the human MLH1 N-terminus: implications for predisposition to Lynch syndrome.Semantic proximity Read ↗

Mutations in the MutSalpha interaction interface of MLH1 can abolish DNA mismatch repair.Semantic proximity Read ↗

TheMLH1variants p.Arg265Cys and p.Lys618Ala affect protein stability while p.Leu749Gln affects heterodimer formationSemantic proximity Read ↗

Disentangling the mutational effects on protein stability and interaction of human MLH1Semantic proximity Read ↗

Disentangling the mutational effects on protein stability and interaction of human MLH1Semantic proximity Read ↗

Functional analysis of human MLH1 variants using yeast and in vitro mismatch repair assays.Semantic proximity Read ↗

A structural hinge in eukaryotic MutY homologues mediates catalytic activity and Rad9-Rad1-Hus1 checkpoint complex interactions.Semantic proximity Read ↗

Identification of Lynch syndrome mutations in the MLH1-PMS2 interface that disturb dimerization and mismatch repair.Semantic proximity Read ↗

Mismatch repair MLH complexes make distinct contributions to post-replicative mismatch repair versus trinucleotide repeat expansionsSemantic proximity Read ↗

Identification of non-synonymous SNPs affecting structure and function of MLH1 and NBN proteins: a computational approach.Semantic proximity Read ↗

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