Polymeric ADAM Protein Mimics Interrogate Mammalian Sperm–Egg Binding [PDF]
ChemBioChem, 2009 AbstractROMPing with the ADAMs family: The sperm‐surface display of egg adhesion proteins was investigated using multivalent polymer sperm mimics. Ruthenium‐catalyzed ring opening metathesis polymerization (ROMP) was used to synthesize heterovalent polymers.magnified imageThe sperm proteins ADAM2 and ADAM3, members of the ADAM family of proteins, have ...
Younjoo Lee, Nicole S. Sampson
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Role of ADAM and ADAMTS proteases in pathological tissue remodeling
Cell Death Discovery, 2023 Pathological tissue remodeling is closely associated with the occurrence and aggravation of various diseases. A Disintegrin And Metalloproteinases (ADAM), as well as A Disintegrin And Metalloproteinase with ThromboSpondin motifs (ADAMTS), belong to zinc ...
Zhaoni Wang +3 more
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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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Nuclear translocation and signalling of L1-CAM in human carcinoma cells requires ADAM10 and presenilin/gamma-secretase activity [PDF]
, 2009 L1-CAM (L1 cell-adhesion molecule), or more simply L1, plays an important role in the progression of human carcinoma. Overexpression promotes tumour-cell invasion and motility, growth in nude mice and tumour metastasis.
Altevogt, Peter +6 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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Evidence for functional redundancy between C. elegans ADAM proteins SUP-17/Kuzbanian and ADM-4/TACE
Developmental Biology, 2005 Sophie Jarriault, Iva Susan Greenwald
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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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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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Secretion-Positive LGI1 Mutations Linked to Lateral Temporal Epilepsy Impair Binding to ADAM22 and ADAM23 Receptors [PDF]
, 2016 Autosomal dominant lateral temporal epilepsy (ADTLE) is a focal epilepsy syndrome caused by mutations in the LGI1 gene, which encodes a secreted protein.
Belluzzi, Elisa +7 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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