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

Mutational and structural analyses of the hinge region of membrane type 1-matrix metalloproteinase and enzyme processing.

The Journal of biological chemistry - 15 Jul 2005

Osenkowski Pamela, Meroueh Samy O, Pavel Dumitru, Mobashery Shahriar, Fridman Rafael

Abstract excerpt

Membrane type 1 (MT1)-matrix metalloproteinase (MMP) is a major mediator of collagen degradation in the pericellular space in both physiological and pathological conditions. Previous evidence has shown that on the cell surface, active MT1-MMP undergoes autocatalytic processing to a major membrane...

Read the complete abstract on PubMed

Topics

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

Share to Biotinylation
Share to Glycine
Share to Haplorhini

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Immunoprecipitation

Share to Matrix Metalloproteinase 2

Share to Metalloendopeptidases

Share to Proline

Share to Vaccinia virus

Source

Identifiers

PMID: 15901740
DOI: 10.1074/jbc.M414379200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-15901740-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutational and structural analyses of the hinge region of membrane type 1-matrix metalloproteinase and enzyme processing.PMID 15901740Read ↗

Collagenase unwinds triple-helical collagen prior to peptide bond hydrolysis.Semantic proximity Read ↗

Bilayer Membrane Modulation of Membrane Type 1 Matrix Metalloproteinase (MT1-MMP) Structure and Proteolytic Activity.Semantic proximity Read ↗

Structure of Human Pro-Matrix Metalloproteinase-2: Activation Mechanism RevealedSemantic proximity Read ↗

Molecular basis of proteolytic cleavage regulation by the extracellular matrix receptor dystroglycanSemantic proximity Read ↗

The canonical methionine 392 of matrix metalloproteinase 2 (gelatinase A) is not required for catalytic efficiency or structural integrity: probing the role of the methionine-turn in the metzincin metalloprotease superfamily.Semantic proximity Read ↗

Structural biochemistry and activation of matrix metalloproteasesSemantic proximity Read ↗

Structural Basis of Matrix Metalloproteinases and Tissue Inhibitors of MetalloproteinasesSemantic proximity Read ↗

Bioinformatic Comparison of Structures and Homology-Models of Matrix MetalloproteinasesSemantic proximity Read ↗

Unexpected crucial role of residue 272 in substrate specificity of fibroblast collagenase.Semantic proximity Read ↗

Identification of an Electrostatic Ruler Motif for Sequence-Specific Binding of Collagenase to Collagen.Semantic proximity Read ↗

Molecular basis of proteolytic cleavage regulation by the extracellular matrix receptor dystroglycan.Semantic proximity Read ↗

Identification of a functional missense variant in the matrix metallopeptidase 10 (MMP10) gene in two families with premature myocardial infarction.Semantic proximity Read ↗

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