IndraLab

Statements

HCN4 binds cGMP. 7 / 7
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"A recent crystal structure of the cytosolic C-terminal fragment of HCN4 bound to cGMP allowed the discovery of a new interaction site [XREF_BIBR], located at the interface between the CNBD and the C-linker."
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"We found that cAMP and cGMP bind to both the wild-type and mutant tetrameric HCN4 C-terminal regions with negative cooperativity, as we found previously for cAMP binding to the wild-type HCN4 as well [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"The nature of how gating is modified by the mutation, and the role of the wild-type residue in gating, remains to be determined.The K d values for cGMP binding in the wild-type HCN4 channel are approx[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"For cGMP binding to wild-type HCN4, a two-phase pattern in the binding isotherm was again best fitted with a two-independent binding site model ( Fig. 3 A ); this yielded high- and low-affinity bindin[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"These K d values for cGMP binding in the wild-type HCN4 channel suggest that this molecule may be an important facilitator of HCN4 opening in vivo."
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"These data suggest that a reduction of cGMP binding to the HCN4 channel may also contribute to the resting bradycardia in patients carrying the S672R HCN4 mutation.The thermodynamics of the interactio[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"A comparison of cAMP and cGMP binding to the wild-type HCN4 C-terminal tetramer shows differences."
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