Tissue inhibitors of metalloproteinases: evolution, structure and function.

By K. Brew, D. Dinakarpandian, Hideaki Nagase. Biochimica et Biophysica Acta, 2000

1,990 citations recorded by the source corpus.

Subfields: Cancer Research, Hematology, Pulmonary and Respiratory Medicine

View Paper: https://www.semanticscholar.org/paper/d276c4f9b6d184e0a3a3f79c29f98933ba310db4

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In Cancer Research

In Hematology

In Pulmonary and Respiratory Medicine

Citations in the corpus

The role of TIMPs in regulation of extracellular matrix proteolysis. (2015, background): “There are four homologous members of the TIMP family [1–3].”
Axis of evil: molecular mechanisms of cancer metastasis (2003, neutral): “For nomenclature, classification, domain structure, and biological functions of MMPs, we refer to excellent recent reviews (Brew et al., 2000; Sternlicht and Werb, 2001; Egeblad and Werb, 2002).”
The matrix metalloproteinase system: changes, regulation, and impact throughout the ovarian and uterine reproductive cycle. (2003, background): “The preliminary information regarding the specificity of this inhibitor and mode of action suggests that TIMP-4 has traits similar to TIMP-2 (15, 16, 25).”
The C-terminal domains of ADAMTS-4 and ADAMTS-5 promote association with N-TIMP-3 (2009, background): “The inhibitory machinery of TIMPs is contained in their N-terminal domains, and in most cases, the C-terminal domains of both MMPs and TIMPs have a minimal effect on complex formation (Brew et al., 2000).”
Matrix metalloproteinases in neuroinflammation (2002, background): “Four endogenously produced TIMPs have been described; they inhibit both the MMPs and the ADAMs families (Brew et al., 2000).”
Tight junctions and the modulation of barrier function in disease (2008, background): “Tissue inhibitors of metalloproteinases (TIMPs) form complexes with either activated MMPs or with their pro-forms after their secretion, thus regulating MMP activity under physiological conditions (Brew et al. 2000; Yong et al. 2001).”
Expression of matrix-metalloproteinases and their inhibitors in the wounds of diabetic and non-diabetic patients (2002, background): “TIMPs are relatively small proteins (21 000 to 29 000 Mr) yet they have several biological functions, including inhibition of active MMPs, stimulation of cell division, binding to ECM, inhibition of angiogenesis and induction of apoptosis [30, 31].”
Matrix metalloproteinases: role in arthritis. (2006, background): “Currently, four family members have been identified (TIMP-1, -2, -3, -4) (77).”
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).”