TY  - GEN
AU  - Ågren,Magnus S.
AU  - Keller,Ulrich
AU  - Ågren,Magnus S.
AU  - Keller,Ulrich
TI  - Matrix Metalloproteinase
SN  - books978-3-03936-649-1
PY  - 2020///
CY  - Basel, Switzerland
PB  - MDPI - Multidisciplinary Digital Publishing Institute
KW  - Research & information: general
KW  - bicssc
KW  - Biology, life sciences
KW  - hemagglutinin-B
KW  - transwell co-cultures
KW  - matrix metalloproteinases
KW  - TNF-α
KW  - matrix metalloproteinase
KW  - peritoneal mesothelial cell
KW  - gastric cancer
KW  - metastatic dissemination
KW  - MT4-MMP
KW  - cancer
KW  - diseases
KW  - aggrecan
KW  - aggrecanase
KW  - ADAMTS
KW  - cartilage
KW  - arthritis
KW  - MMP-2
KW  - MMP-9
KW  - inhibitor
KW  - allodynia
KW  - caspase-3
KW  - neuropathic
KW  - pain
KW  - dorsal root ganglion
KW  - spinal nerve ligation
KW  - tuberculosis
KW  - tuberculous meningitis
KW  - HIV-TB-associated IRIS
KW  - extracellular matrix breakdown
KW  - adult
KW  - pediatric
KW  - lung
KW  - central nervous system
KW  - matrix-metalloproteinase
KW  - monocytes
KW  - inflammation
KW  - phagocytosis
KW  - apoptosis
KW  - blood sampling
KW  - anticoagulants
KW  - high-molecular-weight heparin
KW  - IL-16
KW  - sICAM-1
KW  - IL-8
KW  - T cells
KW  - a disintegrin and metalloproteinase
KW  - EMMPRIN
KW  - CD147
KW  - ectodomain shedding
KW  - MMPs
KW  - PTMs
KW  - glycosylation
KW  - phosphorylation
KW  - glycosaminoglycans
KW  - interleukin
KW  - IL-6
KW  - IL-11
KW  - trans-signaling
KW  - metalloproteases
KW  - ADAM
KW  - MMP
KW  - meprin
KW  - matrix metalloproteinases (MMPs)
KW  - protease
KW  - signaling
KW  - invasion
KW  - chemokine
KW  - cytokine
KW  - proteomics
KW  - interferon
KW  - Agkistrodon venom
KW  - metalloproteinase
KW  - fibrinogen
KW  - antithrombotic
KW  - metabolomics
KW  - extracellular matrix
KW  - cytokines
KW  - proteinases
KW  - interstitial collagens
KW  - wound healing
N1  - Open Access
N2  - 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
UR  - https://mdpi.com/books/pdfview/book/2762
UR  - https://directory.doabooks.org/handle/20.500.12854/68994
ER  -