ADAM-17 Is Activated by the Mitogenic Protein Kinase ERK in a Model of Kidney Fibrosis [PDF]
The American Journal of the Medical Sciences, 2010 Chronic kidney disease affects 1 of 9 Americans. Recent studies showed increased activation of the metalloenzyme disintegrin ADAM-17 during the development of the disease and that threonine phosphorylation of ADAM-17 may be an important regulator of the enzyme activity.
L. Gabriel Navar +5 more
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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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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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Evidence for functional redundancy between C. elegans ADAM proteins SUP-17/Kuzbanian and ADM-4/TACE
Developmental Biology, 2005 Iva Greenwald, Sophie Jarriault
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Detection of the ADAM proteins in the ejaculated bovine sperm
International journal of health sciences, 2022 The current study aimed to detect specific types of ADAM proteins in the bovine sperm. Histology study of tissue of male reproduction was involved with testis, head, body, and the tail of the epididymis. Results showed that the testis composed of the parenchyma of testis contained the seminiferous tubules which are surrounded by two layers externally ...
Asseel Yassin +2 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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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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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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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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