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Matrix Metalloproteinase

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 ma...

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Bibliographic Details
Main Author: Ågren, Magnus S.
Other Authors: Keller, Ulrich
Format: eBook
Language:English
Published: Basel, Switzerland MDPI - Multidisciplinary Digital Publishing Institute 2020
Subjects:
Matrix Metalloproteinases (mmps)
Matrix Metalloproteinase
Interferon
Meprin
Mt4-mmp
Mmps
Caspase-3
Inflammation
Aggrecanase
Cartilage
Il-16
Allodynia
Spinal Nerve Ligation
Phosphorylation
Monocytes
Cd147
Il-8
Protease
Glycosaminoglycans
High-molecular-weight Heparin
Metalloproteases
Sicam-1
Hiv-tb-associated Iris
Diseases
Cytokines
Peritoneal Mesothelial Cell
Adamts
Inhibitor
Metalloproteinase
Wound Healing
Chemokine
Ectodomain Shedding
Arthritis
Extracellular Matrix Breakdown
Adam
Gastric Cancer
Matrix-metalloproteinase
Mmp-2
Cytokine
Adult
Glycosylation
Apoptosis
Phagocytosis
Mmp
Signaling
Transwell Co-cultures
Tuberculous Meningitis
Research & Information: General / Bicssc
Pediatric
Proteinases
Biology, Life Sciences / Bicssc
Central Nervous System
Cancer
Lung
Proteomics
Interstitial Collagens
Interleukin
Metastatic Dissemination
Il-11
Extracellular Matrix
Fibrinogen
Mmp-9
Tuberculosis
Antithrombotic
Pain
Il-6
Dorsal Root Ganglion
Matrix Metalloproteinases
T Cells
Invasion
Ptms
Aggrecan
Blood Sampling
Emmprin
A Disintegrin And Metalloproteinase
Agkistrodon Venom
Anticoagulants
Tnf-α
Neuropathic
Metabolomics
Trans-signaling
Hemagglutinin-b
Online Access:
Collection: Directory of Open Access Books - Collection details see MPG.ReNa
Description
Summary: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.
Item Description:Creative Commons (cc), https://creativecommons.org/licenses/by/4.0/
Physical Description:1 electronic resource (262 p.)
ISBN:9783039366491
books978-3-03936-649-1
9783039366484

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