Papilin in development; a pericellular protein with a homology to the ADAMTS metalloproteinases.
By I. Kramerova, N. Kawaguchi, L. Fessler, R. Nelson, Yali Chen, A. Kramerov, M. Kusche‐Gullberg, J. Kramer, Brian D. Ackley, A. Sieron and 2 more. 2000
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Citations in the corpus
- A Disintegrin and Metalloproteinase (ADAM) and ADAM with Thrombospondin Motifs (ADAMTS) Family in Vascular Biology and Disease (2019, background): “Papilin inhibits ADAMTS-2 by binding both the enzyme and its substrate [60].”
- The procollagen N-proteinases ADAMTS2, 3 and 14 in pathophysiology. (2015, background): “Papilin has also been reported to be an inhibitor of ADAMTS2, by binding both the enzyme and the substrate [23].”
- ADAMTS proteins in human disorders (2018, background): “1 [105] Autosomal recessive Geleophysic dysplasia 1 231050 ADAMTSL2, 9q34.”
- Basement membranes: cell scaffoldings and signaling platforms. (2011, unknown): “It has an amino-terminal cassette of domains similar to the carboxyterminal ADAMTS subgroup of secreted, matrix-associated metalloproteinases (Kramerova et al. 2000).”