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

Covalent modification of matrix metalloproteinases by a photoaffinity probe: influence of nucleophilicity and flexibility of the residue in position 241.

Bioconjugate chemistry - 1 Feb 2009

Dabert-Gay Anne-Sophie, Czarny B, Lajeunesse E, Thai R, Nagase H, Dive V

Abstract excerpt

A photoaffinity probe, developed for the specific labeling of matrix metalloproteinase (MMP) active sites, was recently shown to covalently modify a single residue in human MMP-12, namely, Lys(241), by reacting selectively with the side chain epsilon-amino group of that residue. The residue in position 241 of MMPs is not conserved; thus, variability in this position may be responsible for the dispersion in...

Read the complete abstract on PubMed

Topics

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

Share to Binding Sites
Share to Cross-Linking Reagents

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Histidine

Share to Hydrogen-Ion Concentration

Share to Matrix Metalloproteinases

Share to Mutation

Source

Identifiers

PMID: 19138112
DOI: 10.1021/bc800478b

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 8 closest

Covalent modification of matrix metalloproteinases by a photoaffinity probe: influence of nucleophilicity and flexibility of the residue in position 241.PMID 19138112Read ↗

Fluorescent peptomer substrates for differential degradation by metalloproteasesSemantic proximity Read ↗

Monitoring conformational changes in peroxisome proliferator-activated receptor α by a genetically encoded photoamino acid, cross-linking, and mass spectrometry.Semantic proximity Read ↗

Two structural states of complexes of peptide and class II major histocompatibility complex revealed by photoaffinity-labeled peptides.Semantic proximity Read ↗

DNA binding by an amino acid residue in the C-terminal half of the Rel homology region.Semantic proximity Read ↗

Identification of the dimerisation interface of human interleukin-8 by IL-8-variants containing the photoactivatable amino acid benzoyl-phenylalanine.Semantic proximity Read ↗

Molecular approximation between residue 10 of secretin and its receptor demonstrated by photoaffinity labeling.Semantic proximity Read ↗

Tyr219 of human matrix metalloproteinase 7 is not critical for catalytic activity, but is involved in the broad pH-dependence of the activity.Semantic proximity Read ↗

Identification of a hexapeptide binding region in the nociceptin (ORL1) receptor by photo-affinity labelling with Ac-Arg-Bpa-Tyr-Arg-Trp-Arg-NH2.Semantic proximity Read ↗

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