ADAM-10 Regulates MMP-12 during Lipopolysaccharide-Induced Inflammatory Response in Macrophages
Journal of Immunology Research, 2022 A disintegrin and metalloprotease 10 (ADAM-10), a member of the ADAM protease family, has biological activities related to TNF-α activation, cell adhesion, and migration, among other functions.
Yan Jiang +9 more
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The ADAMs family of metalloproteases: multidomain proteins with multiple functions [PDF]
Genes & Development, 2003 The ADAMs family of transmembrane proteins belongs to the zinc protease superfamily. Members of the family have a modular design, characterized by the presence of metalloprotease and integrin receptor-binding activities, and a cytoplasmic domain that in many family members specifies binding sites for various signal transducing proteins.
Darren F. Seals, Sara A. Courtneidge
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Frontiers in Cell and Developmental Biology, 2020 A disintegrin and metalloproteinase (ADAM) family of proteins play versatile roles in cancer development and progression. In the present study, we investigated the role of ADAM proteins in colorectal cancer (CRC) cell migration and invasion focusing on ...
Lina Sun +9 more
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ADAMDEC1 accelerates GBM progression via activation of the MMP2-related pathway
Frontiers in Oncology, 2022 The ADAM (a disintegrin and metalloprotease) gene-related family including ADAM, ADAMTS, and ADAM-like decysin-1 has been reported to play an important role in the pathogenesis of multiple diseases, including cancers (lung cancer, gliomas, colorectal ...
Huimin Qi +11 more
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Role of ADAMs in the Ectodomain Shedding and Conformational Conversion of the Prion Protein [PDF]
Journal of Biological Chemistry, 2009 The cellular prion protein (PrP(C)) is essential for the pathogenesis and transmission of prion diseases. PrP(C) is bound to the plasma membrane via a glycosylphosphatidylinositol anchor, although a secreted, soluble form has also been identified.
Taylor, David R +6 more
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Preferred SH3 domain partners of ADAM metalloproteases include shared and ADAM-specific SH3 interactions. [PDF]
PLoS ONE, 2015 A disintegrin and metalloproteinases (ADAMs) constitute a protein family essential for extracellular signaling and regulation of cell adhesion. Catalytic activity of ADAMs and their predicted potential for Src-homology 3 (SH3) domain binding show a ...
Iivari Kleino +4 more
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Snake venom disintegrins update: insights about new findings [PDF]
Journal of Venomous Animals and Toxins including Tropical Diseases, 2023 Snake venom disintegrins are low molecular weight, non-enzymatic proteins rich in cysteine, present in the venom of snakes from the families Viperidae, Crotalidae, Atractaspididae, Elapidae, and Colubridae.
Gabriela de Oliveira Almeida +3 more
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Evolutionary divergence and functions of the
Human Genomics, 2009 The 'A-disintegrin and metalloproteinase' (ADAM) and 'A-disintegrin and metalloproteinase with thrombospondin motifs' (ADAMTS) genes make up two similar, yet distinct, gene families.
Brocker Chad N +2 more
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Proteomic analysis of Biomphalaria glabrata plasma proteins with binding affinity to those expressed by early developing larval Schistosoma mansoni. [PDF]
PLoS Pathogens, 2017 Interactions between early developing Schistosoma mansoni larval stages and the hemolymph of its snail intermediate host represent the first molecular encounter with the snail's immune system.
Xiao-Jun Wu +7 more
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ADAM-15 Disintegrin-Like Domain Structure and Function
Toxins, 2010 The ADAM (a disintegrin-like and metalloproteinase) proteins are a family of transmembrane cell-surface proteins with important functions in adhesion and proteolytic processing in all animals.
Dong Lu +3 more
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