Metalloproteinase inhibitors: biological actions and therapeutic opportunities

By A. Baker, D. Edwards, Gillian Murphy. Journal of Cell Science, 2002

1,206 citations recorded by the source corpus.

Subfields: Cancer Research, Genetics, Hematology

View Paper: https://www.semanticscholar.org/paper/e29ef373958f388765a002906b0b694c12c47b45

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. Gillian Murphy
2. R. Khalil
3. Hideaki Nagase
4. Xi Wang
5. P. E. Van den Steen
6. J. Vandooren
7. G. Opdenakker
8. S. Gill

In Genetics

1. Gillian Murphy
2. Xi Wang
3. R. Khalil

In Hematology

1. Gillian Murphy
2. Hideaki Nagase
3. A. Newby
4. R. Khalil
5. S. Gill
6. James P. Quigley
7. D. Edwards
8. Xi Wang

Citations in the corpus

• Matrix metalloproteinases and tumor metastasis (2006, background): “However, soluble MMPs are found mainly in the proenzyme form [32] or in a complex with natural MMP inhibitors such as TIMPs or α2-macroglobulin [34], thus the precise functional contributions of plasma MMPs to malignant progression are unclear.”
• Matrix Metalloproteinases, Vascular Remodeling, and Vascular Disease. (2018, background): “MMP-19 may exhibit anti-angiogenic effects on endothelial cells by processing human plasminogen in a characteristic cleavage pattern to generate three angiostatin-like fragments, with a molecular weight of 35, 38, and 42 kDa, that decrease the phosphorylation of c-met, inhibit the proliferation of h”
• Matrix metalloproteinases. (2010, background): “Another interesting alternative to synthetic MMPs inhibitors is the use of gene therapy approaches aimed at delivering TIMPs at tumour sites [217,218].”
• Matrix metalloproteinases: role in arthritis. (2006, background): “Cleaving this region causes a structural change in the inhibitor, trapping the proteinase in the alpha2M molecule (75) thereby neutralizing the enzymatic activity of the proteinase.”
• The ADAM metalloproteinases (2008, background): “Moreover, a Thr2Gly replacement at position 2, which reduces the affinity of TIMP-1 for MMPs by three orders of magnitude, retained potency against ADAM-17.”
• Structure and function of matrix metalloproteinases and TIMPs. (2006, neutral): “Based on those studies a large number of MMP inhibitors have been designed and synthesized and some were clinically tested for the treatment of patients with cancer or arthritis, but they showed little efficacy so far [104].”
• Metalloproteinases and their inhibitors: regulators of wound healing. (2008, background): “This role is illustrated by decreased Clara cell proliferation in mice lacking MMP14, ultimately resulting in impaired wound healing (Atkinson et al., 2007).”
• Metalloproteinases and Wound Healing (2015, background): “The endogenous regulators of the MMP activity are the TIMPs; they are 20–39 kDa secreted proteins and are able to inhibit a range of MMPs.”
• Progress in matrix metalloproteinase research. (2008, background): “MMPs such as MMP-2, MMP-3, MMP-9, MMP-10 and MMP-19 are also elevated in arthritis and, along with MMP-13 these enzymes degrade non-collagen matrix components of the joints (Cawston and Wilson, 2006).”
• The role of TIMPs in regulation of extracellular matrix proteolysis. (2015, background): “As well, both TIMP1 and -3 associate with latent or pro-MMP9 while TIMP2, -3 and -4 are capable of interaction with pro-MMP2 [1].”