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dc.contributor.editorÅgren, Magnus S.
dc.contributor.editorKeller, Ulrich
dc.date.accessioned2021-05-01T15:34:59Z
dc.date.available2021-05-01T15:34:59Z
dc.date.issued2020
dc.identifierONIX_20210501_9783039366484_740
dc.identifier.urihttps://directory.doabooks.org/handle/20.500.12854/68994
dc.description.abstractZinc-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.
dc.languageEnglish
dc.subject.classificationthema EDItEUR::G Reference, Information and Interdisciplinary subjects::GP Research and information: generalen_US
dc.subject.classificationthema EDItEUR::P Mathematics and Science::PS Biology, life sciencesen_US
dc.subject.otherhemagglutinin-B
dc.subject.othertranswell co-cultures
dc.subject.othermatrix metalloproteinases
dc.subject.otherTNF-α
dc.subject.othermatrix metalloproteinase
dc.subject.otherperitoneal mesothelial cell
dc.subject.othergastric cancer
dc.subject.othermetastatic dissemination
dc.subject.otherMT4-MMP
dc.subject.othercancer
dc.subject.otherdiseases
dc.subject.otheraggrecan
dc.subject.otheraggrecanase
dc.subject.otherADAMTS
dc.subject.othercartilage
dc.subject.otherarthritis
dc.subject.otherMMP-2
dc.subject.otherMMP-9
dc.subject.otherinhibitor
dc.subject.otherallodynia
dc.subject.othercaspase-3
dc.subject.otherneuropathic
dc.subject.otherpain
dc.subject.otherdorsal root ganglion
dc.subject.otherspinal nerve ligation
dc.subject.othertuberculosis
dc.subject.othertuberculous meningitis
dc.subject.otherHIV-TB-associated IRIS
dc.subject.otherextracellular matrix breakdown
dc.subject.otheradult
dc.subject.otherpediatric
dc.subject.otherlung
dc.subject.othercentral nervous system
dc.subject.othermatrix-metalloproteinase
dc.subject.othermonocytes
dc.subject.otherinflammation
dc.subject.otherphagocytosis
dc.subject.otherapoptosis
dc.subject.otherblood sampling
dc.subject.otheranticoagulants
dc.subject.otherhigh-molecular-weight heparin
dc.subject.otherIL-16
dc.subject.othersICAM-1
dc.subject.otherIL-8
dc.subject.otherT cells
dc.subject.othera disintegrin and metalloproteinase
dc.subject.otherEMMPRIN
dc.subject.otherCD147
dc.subject.otherectodomain shedding
dc.subject.otherMMPs
dc.subject.otherPTMs
dc.subject.otherglycosylation
dc.subject.otherphosphorylation
dc.subject.otherglycosaminoglycans
dc.subject.otherinterleukin
dc.subject.otherIL-6
dc.subject.otherIL-11
dc.subject.othertrans-signaling
dc.subject.othermetalloproteases
dc.subject.otherADAM
dc.subject.otherMMP
dc.subject.othermeprin
dc.subject.othermatrix metalloproteinases (MMPs)
dc.subject.otherprotease
dc.subject.othersignaling
dc.subject.otherinvasion
dc.subject.otherchemokine
dc.subject.othercytokine
dc.subject.otherproteomics
dc.subject.otherinterferon
dc.subject.otherAgkistrodon venom
dc.subject.othermetalloproteinase
dc.subject.otherfibrinogen
dc.subject.otherantithrombotic
dc.subject.othermetabolomics
dc.subject.otherextracellular matrix
dc.subject.othercytokines
dc.subject.otherproteinases
dc.subject.otherinterstitial collagens
dc.subject.otherwound healing
dc.titleMatrix Metalloproteinase
dc.typebook
oapen.identifier.doi10.3390/books978-3-03936-649-1
oapen.relation.isPublishedBy46cabcaa-dd94-4bfe-87b4-55023c1b36d0
oapen.relation.isbn9783039366484
oapen.relation.isbn9783039366491
oapen.pages262
oapen.place.publicationBasel, Switzerland


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