Matrix Metalloproteinase
Material type:
ArticleLanguage: English Publication details: Basel, Switzerland MDPI - Multidisciplinary Digital Publishing Institute 2020Description: 1 electronic resource (262 p.)ISBN: - books978-3-03936-649-1
- 9783039366484
- 9783039366491
- Research & information: general
- Biology, life sciences
- hemagglutinin-B
- transwell co-cultures
- matrix metalloproteinases
- TNF-α
- matrix metalloproteinase
- peritoneal mesothelial cell
- gastric cancer
- metastatic dissemination
- MT4-MMP
- cancer
- diseases
- aggrecan
- aggrecanase
- ADAMTS
- cartilage
- arthritis
- MMP-2
- MMP-9
- inhibitor
- allodynia
- caspase-3
- neuropathic
- pain
- dorsal root ganglion
- spinal nerve ligation
- tuberculosis
- tuberculous meningitis
- HIV-TB-associated IRIS
- extracellular matrix breakdown
- adult
- pediatric
- lung
- central nervous system
- matrix-metalloproteinase
- monocytes
- inflammation
- phagocytosis
- apoptosis
- blood sampling
- anticoagulants
- high-molecular-weight heparin
- IL-16
- sICAM-1
- IL-8
- T cells
- a disintegrin and metalloproteinase
- EMMPRIN
- CD147
- ectodomain shedding
- MMPs
- PTMs
- glycosylation
- phosphorylation
- glycosaminoglycans
- interleukin
- IL-6
- IL-11
- trans-signaling
- metalloproteases
- ADAM
- MMP
- meprin
- matrix metalloproteinases (MMPs)
- protease
- signaling
- invasion
- chemokine
- cytokine
- proteomics
- interferon
- Agkistrodon venom
- metalloproteinase
- fibrinogen
- antithrombotic
- metabolomics
- extracellular matrix
- cytokines
- proteinases
- interstitial collagens
- wound healing
| Item type | Home library | Collection | Call number | Materials specified | Status | Date due | Barcode | |
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Electronic-Books
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OPJGU Sonepat- Campus | E-Books Open Access | Available |
Open Access star Unrestricted online access
Zinc-dependent matrix metalloproteinases (MMPs) belong to metzincins that comprise not only 23 human MMPs but also other metalloproteinases, such as 21 human ADAMs (a disintegrin and metalloproteinase domain) and 19 secreted ADAMTSs (a disintegrin and metalloproteinase thrombospondin domain). The many setbacks from the clinical trials of broad-spectrum MMP inhibitors for cancer indications in the late 1990s emphasized the extreme complexity of the participation of these proteolytic enzymes in biology. This editorial mini-review summarizes the Special Issue, which includes four review articles and 10 original articles that highlight the versatile roles of MMPs, ADAMs, and ADAMTSs, in normal physiology as well as in neoplastic and destructive processes in tissue. In addition, we briefly discuss the unambiguous involvement of MMPs in wound healing.
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