Inhibition of ADAMTS4 (aggrecanase‐1) by tissue inhibitors of metalloproteinases (TIMP‐1, 2, 3 and 4)

By G. Hashimoto, T. Aoki, Hiroyuki Nakamura, K. Tanzawa, Y. Okada. 2001

176 citations recorded by the source corpus.

Subfields: Cancer Research, Molecular Biology, Oncology

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. R. Khalil
2. Hideaki Nagase
3. K. Brew
4. S. Zhong
5. D. Edwards
6. S. Gill
7. Gillian Murphy

In Molecular Biology

1. R. Khalil
2. Hideaki Nagase
3. K. Brew
4. D. Edwards
5. S. Zhong
6. S. Gill
7. Gillian Murphy

In Oncology

1. R. Khalil
2. S. Zhong
3. Hideaki Nagase
4. D. Edwards
5. S. Gill

Citations in the corpus

• A Disintegrin and Metalloproteinase (ADAM) and ADAM with Thrombospondin Motifs (ADAMTS) Family in Vascular Biology and Disease (2019, background): “Ren P, Hughes M, Krishnamoorthy S, Zou S, Zhang L, Wu D, et al. Critical Role of ADAMTS-4 in the Development of Sporadic Aortic Aneurysm and Dissection in Mice.”
• The role of TIMPs in regulation of extracellular matrix proteolysis. (2015, background): “The proteolytic activity of ADAM10 can be inhibited by TIMP1 and -3, whereas, TIMP3 alone is an efficient inhibitor of ADAMTS4 and -TS5, which are postulated to cleave aggrecan, a component of cartilage matrix [8–10].”
• The tissue inhibitors of metalloproteinases (TIMPs): An ancient family with structural and functional diversity (2010, background): “TIMP-3 is unique among the mammalian TIMPs in inhibiting a broader array of metalloproteinases including several members of the ADAM and ADAMTS families [21,22,24–27].”
• The C-terminal domains of ADAMTS-4 and ADAMTS-5 promote association with N-TIMP-3 (2009, background): “(2001), although higher values of 4-8 nM have been reported in other studies (Hashimoto et al., 2001;Wayne et al., 2007).”
• Calcium pentosan polysulfate directly inhibits enzymatic activity of ADAMTS4 (aggrecanase‐1) in osteoarthritic chondrocytes (2008, methodology): “TIMP-3 is considered to be the physiological inhibitor of ADAMTS4 [15,18], and it is predictable that TIMP-3 inhibits”
• The ADAMTS (A Disintegrin and Metalloproteinase with Thrombospondin motifs) family (2015, background): “Where multiple TIMPs have been tested, as is the case for ADAMTS2 [34] and ADAMTS4 [35], TIMP-3 emerges as the most effective inhibitor.”