Entropy Increases from Different Sources Support the High-affinity Binding of the N-terminal Inhibitory Domains of Tissue Inhibitors of Metalloproteinases to the Catalytic Domains of Matrix Metalloproteinases-1 and -3

Reactive-site mutants of N-TIMP-3 that selectively inhibit ADAMTS-4 and ADAMTS-5: biological and structural implications

(2010) Ngee H. Lim et al.   BIOCHEMICAL JOURNAL

Assessing Energetic Contributions to Binding from a Disordered Region in a Protein−Protein Interaction,

(2010) Sangwoo Cho et al.   BIOCHEMISTRY

The tissue inhibitors of metalloproteinases (TIMPs): An ancient family with structural and functional diversity

(2010) Keith Brew et al.   BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR 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

ProtorP: a protein-protein interaction analysis server

(2008) C. Reynolds et al.   BIOINFORMATICS

Inactivation of N-TIMP-1 by N-terminal acetylation when expressed in bacteria

(2008) Steven R. Van Doren et al.   BIOPOLYMERS

Progress in matrix metalloproteinase research

(2008) G MURPHY et al.   MOLECULAR ASPECTS OF MEDICINE