IndraLab

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ADAM10 binds DDR1. 13 / 14
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"We next examined the interaction between DDR1 and ADAM10 on the cell surface using in situ proximity ligation assay (PLA)."
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"The data indicate that both proform and active form of ADAM10 were coimmunoprecipitated with endogenous DDR1, suggesting that endogenous ADAM10 and DDR1 form a complex on the cell surface."
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"We next investigated whether endogenous ADAM10 can form a complex with endogenous DDR1 in A431 cells."
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"The data indicate that both proform and active form of ADAM10 were coimmunoprecipitated with endogenous DDR1, suggesting that endogenous ADAM10 and DDR1 form a complex on the cell surface."
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"We next examined interaction of endogenous DDR1 and ADAM10 in A431 cells, using PLA ( xref )."
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"In addition, some research found that ADAM10 also can interact with DDR1 to cleave it when collagen is bound to DDR1 [ xref , xref ] ( xref )."
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"DDR1 interacts with ADAM10 on the cell surface."
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"We postulated that a potential reason for weak sensitivity of ADAM10 dependent DDR1 shedding to TIMP-3 inhibition may be due to steric hindrance caused by complex formation between ADAM10 and DDR1."
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"Although it is not clear whether ADAM10 and DDR1 directly interact with each other, these data suggest that they are at least in the same molecular complex on the cell surface."
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"We next examined the interaction between DDR1 and ADAM10 on the cell surface using in situ proximity ligation assay (PLA)."
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"DDR1 interacts with ADAM10 on the cell surface."
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"This idea is supported by our observation that collagen stimulation of A431 cells resulted in loss of endogenous ADAM10 and DDR1 complex on the cell surface (XREF_FIG)."
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"It was shown that DDR1 and ADAM10 form a stable complex even before collagen stimulation without cleavage, and collagen binding to DS domain of DDR1 somehow renders DDR1 available for ADAM10 to cleave [ xref ]."
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