Matrix metalloproteinases: they're not just for matrix anymore!

By L. Mccawley, L. Matrisian. Current Opinion in Cell Biology, 2001

1,336 citations recorded by the source corpus.

Subfields: Cancer Research, Molecular Biology, Oncology

View Paper: https://www.semanticscholar.org/paper/3e126c0bb0ca79d19981ef76c728d2123ab5abef

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cancer Research

1. S. Gill
2. W. Parks
3. I. Stamenkovic
4. C. Brinckerhoff
5. T. Klein
6. Rainer Bischoff
7. L. Sorokin
8. L. Matrisian

In Molecular Biology

1. S. Gill
2. W. Parks
3. I. Stamenkovic
4. C. Brinckerhoff
5. L. Sorokin
6. L. Matrisian
7. B. Engelhardt

In Oncology

1. S. Gill
2. W. Parks
3. I. Stamenkovic
4. C. Brinckerhoff
5. L. Matrisian
6. C. Libert
7. Zena Werb
8. Hao-Hsiu Huang

Citations in the corpus

• Extracellular matrix remodelling: the role of matrix metalloproteinases (2003, background): “Tumour necrosis factor α (TNFα) is released from the cell surface by ADAM-17 and MMP-1, -3, and -7 [8,61], while Fas ligand (FasL) is shed as a result of MMP-7-mediated proteolysis [62,63].”
• Extracellular matrix structure. (2016, background): “degrading ability, MMPs, along with ADAMs and ADAMTSs dispose growth factors and cytokines to the ECM, whereas their actions on matrix molecules, including collagen, elastin, various PGs, cell membrane molecules such as integrins and receptors, generate bioactive molecules the so called matrikines [”
• Matrix metalloproteinases: Contribution to pathogenesis, diagnosis and treatment of periodontal inflammation (2006, background): “The exocite processings and cleavages have been found to result usually in small-size molecules or peptides (59,64,80), the effects of which may in fact be clearly more potent than the full-size parent or native molecule (3,5,59).”
• Matrix metalloproteinases as modulators of inflammation and innate immunity (2004, background): “Recently, we have found evidence that MMPs can act on as many non-matrix substrates as ECM substrate”
• Chemokine and cytokine processing by matrix metalloproteinases and its effect on leukocyte migration and inflammation (2007, background): “The story has been made even more complex by the increasing number of studies revealing many nonmatrix substrates for MMPs, such as chemokines, growth factors, and receptors, indicating that MMPs influence an even wider array of physiological and pathological processes [4].”
• The blood–brain and the blood–cerebrospinal fluid barriers: function and dysfunction (2009, background): “There is increasing evidence that the general digestion of ECM molecules originally attributed to MMPs does not hold true for the in vivo situation [103, 104].”
• Physiology and pathophysiology of matrix metalloproteases (2010, background): “MMP-1 has a wide substrate specificity and is capable of degrading aggrecan, versican, perlecan, nidogen, serpins and tenascin-C (McCawley and Matrisian 2001).”
• Matrix metalloproteinases: a tail of a frog that became a prince (2002, background): “As our knowledge of this family continues to grow, we are learning that their activities are not limited to matrix degradatio”
• Metalloproteinases and their inhibitors: regulators of wound healing. (2008, background): “…bioactive molecules such as growth factors, cytokines and chemokines, as well as their respective receptors, the ability to degrade ECM proteins has been demonstrated for some members of the MMP family using gain- or loss-of-function approaches (McCawley & Matrisian, 2001; Parks et al., 2004).”
• The role of TIMPs in regulation of extracellular matrix proteolysis. (2015, background): “In fact, studies using mice genetically deficient for different metalloproteinases or TIMPs have demonstrated that metalloproteinases process many biologically active proteins, including cytokines, chemokines, and cell surface proteins [7,21].”