The isolated N-terminal domains of TIMP-1 and TIMP-3 are insufficient for ADAM10 inhibition.

By M. Rapti, S. Atkinson, Meng H Lee, Andrew Trim, M. Moss, Gillian Murphy. 2008

45 citations recorded by the source corpus.

Subfields: Molecular Biology, Oncology

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

1. Hideaki Nagase
2. K. Brew
3. M. Handsley
4. D. Edwards
5. C. Pennington
6. Gillian Murphy

In Oncology

1. M. Handsley
2. Hideaki Nagase
3. D. Edwards
4. C. Pennington

Citations in the corpus

• The C-terminal domains of ADAMTS-4 and ADAMTS-5 promote association with N-TIMP-3 (2009, background): “The isolated N-terminal domains of TIMP-1 and TIMP-3 are insufficient for ADAM10 inhibition.”
• The tissue inhibitors of metalloproteinases (TIMPs): An ancient family with structural and functional diversity (2010, background): “Other TIMPs have limited inhibitory activities for ADAMs: TIMP-1 and TIMP-2 inhibit ADAM10 [24] and ADAM12 [27], respectively.”
• The ADAM metalloproteinases (2008, background): “However, the TIMPs show much greater specificity towards the ADAM proteinases (see Table 1).”