Active metalloproteases of the A Disintegrin and Metalloprotease (ADAM) family: biological function and structure.
By T. Klein, Rainer Bischoff. 2011
187 citations recorded by the source corpus.
Subfields: Cancer Research, Immunology and Allergy, Oncology, Computational Biology & Bioinformatics
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In Cancer Research
In Immunology and Allergy
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Citations in the corpus
- Accurate prediction of protein structures and interactions using a 3-track neural network (2021, positive): “…thrombospondin motifs) families of metalloproteases are encoded by more than 40 human genes, mediate cell-cell and cell-matrix interactions ( 20 , 21 ), and are involved in a range of human diseases, including cancer metastasis, inflammatory disorders, neurological diseases, and asthma ( 21 , 22 ).”
- A Disintegrin and Metalloproteinase (ADAM) and ADAM with Thrombospondin Motifs (ADAMTS) Family in Vascular Biology and Disease (2019, background): “There are 22 ADAMs in human [62], 14 of these ADAMs including ADAM-1, 2, 3, 6, 7, 18, 20, 21, 22, 28, 29, 30, 32 and 33 are restricted to embryo development, and are mainly expressed and conduct their function in the reproductive system such as testis, epididymis and uterus.”
- Biochemistry and molecular biology of gelatinase B or matrix metalloproteinase-9 (MMP-9): The next decade (2013, background): “…e.g. serine proteinases and thiol proteases (Barrett et al., 2012), other subfamilies, including, A disintegrin and metalloproteinases (ADAMs) (Klein & Bischoff, 2011; Murphy, 2008) and a disintegrin and MMP with thrombospondin motifs (ADAMTSs) (Apte, 2009) and unique members such as t-PA.”