Recruitment of Matrix Metalloproteinase-9 (MMP-9) to the Fibroblast Cell Surface by Lysyl Hydroxylase 3 (LH3) Triggers Transforming Growth Factor-β (TGF-β) Activation and Fibroblast Differentiation

Cancer-associated-fibroblasts and tumour cells: a diabolic liaison driving cancer progression

(2011) Paolo Cirri et al.   CANCER AND METASTASIS REVIEWS

Small-Molecule Anticancer Compounds Selectively Target the Hemopexin Domain of Matrix Metalloproteinase-9

(2011) A. Dufour et al.   CANCER RESEARCH

Hallmarks of cancer: Interactions with the tumor stroma

(2010) Kristian Pietras et al.   EXPERIMENTAL CELL RESEARCH

Role of Matrix Metalloproteinase-9 Dimers in Cell Migration

(2010) Antoine Dufour et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

 4 1 integrin and 190-kDa CD44v constitute a cell surface docking complex for gelatinase B/MMP-9 in chronic leukemic but not in normal B cells

(2008) J. Redondo-Munoz et al.   BLOOD

Biological and Pathobiological Functions of Gelatinase Dimers and Complexes

(2008) Nabin Malla et al.   CONNECTIVE TISSUE RESEARCH

Selective Modulation of Matrix Metalloproteinase 9 (MMP-9) Functions via Exosite Inhibition

(2008) Janelle L. Lauer-Fields et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

The glycosyltransferase activities of lysyl hydroxylase 3 (LH3) in the extracellular space are important for cell growth and viability

(2008) Chunguang Wang et al.   JOURNAL OF CELLULAR AND MOLECULAR MEDICINE