Background: DDR1 is a constitutively dimeric receptor tyrosine kinase that is activated by collagen. The mechanism of transmembrane signaling is unknown.Results: DDR1 activation is unaffected by disulfide cross-links, insertions, or deletions in the extracellular juxtamembrane region.Conclusion: The extracellular juxtamembrane region of DDR1 does not transmit a conformational change across the cell membrane.Significance: The activation mechanism of DDR1 appears to be unique among receptor tyrosine kinases.

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In this paper, we consider a stabilization problem of a two-qubit system under continuous measurement. Our objective is to stabilize two types of quantum entangled state which play an important role in quantum information technology. In this paper, we show that the global stabilization at a specific quantum entangled state by continuous inputs is possible. An effectiveness of the control input is verified by numerical simulation.

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