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

Targeting ADAM12 in Human Disease: Head, Body or Tail?

(2009) J. Jacobsen et al.   CURRENT PHARMACEUTICAL DESIGN

ADAM12 localizes with c-Src to actin-rich structures at the cell periphery and regulates Src kinase activity

(2009) Dorte Stautz et al.   EXPERIMENTAL CELL RESEARCH

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

(2008) Magdalini Rapti et al.   BIOCHEMICAL JOURNAL

Cellular roles of ADAM12 in health and disease

(2008) Marie Kveiborg et al.   INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY

Structural Determinants of the ADAM Inhibition by TIMP-3: Crystal Structure of the TACE-N-TIMP-3 Complex

(2008) Magdalena Wisniewska et al.   JOURNAL OF MOLECULAR BIOLOGY

Catalytic Properties of ADAM12 and Its Domain Deletion Mutants†

(2007) Jonas Jacobsen et al.   BIOCHEMISTRY

Mapping and characterization of the functional epitopes of tissue inhibitor of metalloproteinases (TIMP)-3 using TIMP-1 as the scaffold: A new frontier in TIMP engineering

(2002) Meng-Huee Lee et al.   PROTEIN SCIENCE