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

Single-molecule analysis reveals the kinetics and physiological relevance of MutL-ssDNA binding.

PloS one - 12 Nov 2010

Park Jonghyun, Jeon Yongmoon, In Daekil, Fishel Richard, Ban Changill, Lee Jong-Bong

Abstract excerpt

DNA binding by MutL homologs (MLH/PMS) during mismatch repair (MMR) has been considered based on biochemical and genetic studies. Bulk studies with MutL and its yeast homologs Mlh1-Pms1 have suggested an integral role for a single-stranded DNA (ssDNA) binding activity during MMR. We have developed single-molecule Förster resonance energy transfer (smFRET) and a single-molecule DNA flow-extension assays to examine...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphatases
Share to Adenosine Triphosphate

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Base Pair Mismatch

Share to DNA, Single-Stranded

Share to Escherichia coli Proteins

Share to Fluorescence Resonance Energy Transfer

Share to MutL Proteins

Share to Osmolar Concentration

Source

Open in PubMed Open full text

Identifiers

PMID: 21103398
DOI: 10.1371/journal.pone.0015496
PMCID: PMC2980497

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Single-molecule analysis reveals the kinetics and physiological relevance of MutL-ssDNA binding.PMID 21103398Read ↗

Intrinsically disordered regions regulate both catalytic and non-catalytic activities of the MutLα mismatch repair complex.Semantic proximity Read ↗

Dynamics of MutS-mismatched DNA complexes are predictive of their repair phenotypes.Semantic proximity Read ↗

Dynamic human MutSα–MutLα complexes compact mismatched DNASemantic proximity Read ↗

Mispair-bound human MutS–MutL complex triggers DNA incisions and activates mismatch repairSemantic proximity Read ↗

MutL: conducting the cell's response to mismatched and misaligned DNASemantic proximity Read ↗

Mechanism of MutS searching for DNA mismatches and signaling repair.Semantic proximity Read ↗

MutL-catalyzed ATP hydrolysis is required at a post-UvrD loading step in methyl-directed mismatch repair.Semantic proximity Read ↗

Dynamic control of strand excision during human DNA mismatch repairSemantic proximity Read ↗

Characterization of the defects in the ATP lid of E. coli MutL that cause transient hypermutability.Semantic proximity Read ↗

Direct observation of three conformations of MutS protein regulated by adenine nucleotides.Semantic proximity Read ↗

The molecular mechanism of DNA damage recognition by MutS homologs and its consequences for cell death response.Semantic proximity Read ↗

Nuclease activity of the MutS homologue MutS2 from Thermus thermophilus is confined to the Smr domain.Semantic proximity Read ↗

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