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Article

Selective inhibition of ADAM12 catalytic activity through engineering of tissue inhibitor of metalloproteinase 2 (TIMP-2).

The Biochemical journal - 15 Aug 2010

Kveiborg Marie, Jacobsen Jonas, Lee Meng-Huee, Nagase Hideaki, Wewer Ulla M, Murphy Gillian

Abstract excerpt

The disintegrin and metalloprotease ADAM12 has important functions in normal physiology as well as in diseases, such as cancer. Little is known about how ADAM12 confers its pro-tumorigenic effect; however, its proteolytic capacity is probably a key component. Thus selective inhibition of ADAM12 activity may be of great value therapeutically and as an investigative tool to elucidate its mechanisms of action. We...

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Source

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Identifiers

PMID: 20533908
DOI: 10.1042/BJ20100649
PMCID: PMC3025530

Genes

ADAM12
ADAM17

Provenance

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Related research

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Research trail→

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Selective inhibition of ADAM12 catalytic activity through engineering of tissue inhibitor of metalloproteinase 2 (TIMP-2).PMID 20533908Read ↗

Delineating the molecular basis of the inactivity of tissue inhibitor of metalloproteinase-2 against tumor necrosis factor-alpha-converting enzyme.Semantic proximity Read ↗

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Unravelling the distinct biological functions and potential therapeutic applications of TIMP2 in cancerSemantic proximity Read ↗

Engineering N-terminal domain of tissue inhibitor of metalloproteinase (TIMP)-3 to be a better inhibitor against tumour necrosis factor-alpha-converting enzyme.Semantic proximity Read ↗

The C-terminal domains of TACE weaken the inhibitory action of N-TIMP-3.Semantic proximity Read ↗

The Specificity of TIMP-2 for Matrix Metalloproteinases Can Be Modified by Single Amino Acid MutationsSemantic proximity Read ↗

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