• Publications
  • Influence
MT1-MMP-Deficient Mice Develop Dwarfism, Osteopenia, Arthritis, and Connective Tissue Disease due to Inadequate Collagen Turnover
MT1-MMP is a membrane-bound matrix metalloproteinase (MT-MMP) capable of mediating pericellular proteolysis of extracellular matrix components. MT1-MMP is therefore thought to be an importantExpand
  • 1,210
  • 42
Analysis of fibronectin receptor function with monoclonal antibodies: roles in cell adhesion, migration, matrix assembly, and cytoskeletal organization
We have developed two rat mAbs that recognize different subunits of the human fibroblast fibronectin receptor complex and have used them to probe the function of this cell surface heterodimer. mAb 13Expand
  • 613
  • 15
  • PDF
Electron microscopy and structural model of human fibronectin receptor.
Highly‐purified human fibronectin receptor (a heterodimer of two distinct subunits, alpha and beta) was studied using electron microscopy and a variety of preparative procedures. It was found thatExpand
  • 244
  • 9
Membrane-type MMPs enable extracellular matrix permissiveness and mesenchymal cell proliferation during embryogenesis.
Peri-cellular remodeling of mesenchymal extracellular matrices is considered a prerequisite for cell proliferation, motility and development. Here we demonstrate that membrane-type 3 MMP, MT3-MMP, isExpand
  • 87
  • 8
  • PDF
Membrane‐type 1 matrix metalloproteinase is required for normal alveolar development
Matrix metalloproteinases (MMPs) are expressed during lung development, but their role may be limited, as mice deficient in MMP‐3, 7, 9, or 12 develop a normal adult lung. Because membrane‐type 1Expand
  • 81
  • 8
MT1‐MMP: A tethered collagenase
Gene ablation in mice offers a powerful tool to assay in vivo the role of selected molecules. Numerous new mouse models of matrix metalloproteinases (MMP) deficiency have been developed in the past 5Expand
  • 164
  • 7
The minimal essential sequence for a major cell type-specific adhesion site (CS1) within the alternatively spliced type III connecting segment domain of fibronectin is leucine-aspartic acid-valine.
Fibronectin contains at least two major domains that support cell adhesion. One is the central cell-binding domain that is recognized by a variety of cell types via the integrin alpha 5 beta 1. TheExpand
  • 339
  • 6
Characterization of a 140-kD avian cell surface antigen as a fibronectin-binding molecule
A 140,000-D protein cell surface antigen (140k) complex has been implicated in fibronectin-mediated cell-substratum attachment. We have used three different experimental systems to evaluate theExpand
  • 160
  • 6
  • PDF
Single subunit chimeric integrins as mimics and inhibitors of endogenous integrin functions in receptor localization, cell spreading and migration, and matrix assembly
The ability of single subunit chimeric receptors containing various integrin beta intracellular domains to mimic and/or inhibit endogenous integrin function was examined. Chimeric receptorsExpand
  • 239
  • 6
  • PDF
Transmembrane signal transduction by integrin cytoplasmic domains expressed in single-subunit chimeras.
Integrins are heterodimeric, transmembrane cell adhesion receptors that have recently been shown to function in transmembrane signal transduction. To examine the specific role of integrinExpand
  • 181
  • 5