• Publications
  • Influence
Matrix metalloproteinases and their inhibitors in connective tissue remodeling
  • J. Woessner
  • Biology, Medicine
  • FASEB journal : official publication of the…
  • 1 May 1991
Matrix metalloproteinases are an important group of zinc enzymes responsible for degradation of the extracellular matrix components such as collagen and proteoglycans in normal embryogenesis andExpand
  • 3,152
  • 92
Handbook of proteolytic enzymes
(Abbreviated Contents Including Section Headings:) Serine Peptidases. Serine Peptidases and Their Clans. Family S1 of Trypsin (Clan SA). Tissue Kallikrein and Its Relatives. Other Families of ClanExpand
  • 2,004
  • 69
  • PDF
Matrix metalloproteinases and TIMPs
ABBREVIATIONS INTRODUCTION MMP SEQUENCES TIMP SEQUENCES THREE DIMENSIONAL STRUCTURES OF THE MMPS AND TIMPS ACTIVATION OF THE ZYMOGEN FORMS OF MMPS PROTEIN SUBSTRATES OF THE MMPS SPECIFICITYExpand
  • 411
  • 31
CD44 anchors the assembly of matrilysin/MMP-7 with heparin-binding epidermal growth factor precursor and ErbB4 and regulates female reproductive organ remodeling.
CD44 is a facultative proteoglycan implicated in cell adhesion and trafficking, as well as in tumor survival and progression. We demonstrate here that CD44 heparan sulfate proteoglycan (CD44HSPG)Expand
  • 453
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TIMP-3 Binds to Sulfated Glycosaminoglycans of the Extracellular Matrix*
  • Wei-Hsuan Yu, Shuan-su C. Yu, Q. Meng, K. Brew, J. Woessner
  • Biology, Medicine
  • The Journal of Biological Chemistry
  • 6 October 2000
Of the four known tissue inhibitors of metalloproteinases (TIMPs), TIMP-3 is distinguished by its tighter binding to the extracellular matrix. The present results show that glycosaminoglycans such asExpand
  • 319
  • 21
Evidence for metalloproteinase and metalloproteinase inhibitor imbalance in human osteoarthritic cartilage.
Cartilage specimens from tibial plateaus, obtained from 13 osteoarthritic (OA) patients and seven controls, were selected from three regions: zone A, center of fibrillated area; zone B, area adjacentExpand
  • 593
  • 13
  • PDF
Heparan Sulfate Proteoglycans as Extracellular Docking Molecules for Matrilysin (Matrix Metalloproteinase 7)*
  • Wei-Hsuan Yu, J. Woessner
  • Chemistry, Medicine
  • The Journal of Biological Chemistry
  • 11 February 2000
Many matrix metalloproteinases (MMPs) are tightly bound to tissues; matrilysin (MMP-7), although the smallest of the MMPs, is one of the most tightly bound. The most likely docking molecules forExpand
  • 228
  • 13
The family of matrix metalloproteinases.
  • J. Woessner
  • Medicine
  • Annals of the New York Academy of Sciences
  • 1994
  • 183
  • 13
The Family of Matrix Metalloproteinasesa
  • 418
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Matrix Metalloproteinase Inhibition: From The Jurassic To The Third Millennium
  • J. Woessner
  • Chemistry, Medicine
  • Annals of the New York Academy of Sciences
  • 1 June 1999
ABSTRACT: A brief historical introduction to the matrix metalloproteinase (MMP) field, which began in 1962, is followed by an overview of the inhibition of these proteases by natural inhibitors suchExpand
  • 145
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