
TRPC6 - Wikipedia
Transient receptor potential cation channel, subfamily C, member 6 or Transient receptor potential canonical 6, also known as TRPC6, is a protein encoded in the human by the TRPC6 gene.
Structure of the receptor-activated human TRPC6 and TRPC3 …
Apr 26, 2018 · Here we present the structure of human TRPC6 homotetramer in complex with a newly identified high-affinity inhibitor BTDM solved by single-particle cryo-electron microscopy …
TRPC6: physiological function and pathophysiological relevance
TRPC6 is a non-selective cation channel 6 times more permeable to Ca (2+) than to Na (+). Channel homotetramers heterologously expressed have a characteristic doubly rectifying …
TRPC6 transient receptor potential cation channel subfamily C …
TRPC6 N338S is a gain-of-function mutant identified in patient with doxorubicin-induced cardiotoxicity. Protein detection and localization of the non-selective cation channel TRPC6 in …
Transient Receptor Potential Canonical (TRPC) Channels: Then …
TRPCs are involved in the continually growing number of cell functions. Furthermore, mutations in the TRPC6 gene are associated with hereditary diseases, such as focal segmental …
TRPC6 in glomerular health and disease: what we know and what …
Mutations in TRPC6, a member of the transient repeptor potential (TRP) superfamily of non-selective cation channels, have been identified as causing a familial form of focal segmental …
TRPC6 Gene - GeneCards | TRPC6 Protein | TRPC6 Antibody
Mar 30, 2025 · TRPC6 (Transient Receptor Potential Cation Channel Subfamily C Member 6) is a Protein Coding gene. Diseases associated with TRPC6 include Focal Segmental …
TRPC channels: Structure, function, regulation and recent ... - PubMed
Recent advances in cryogenic electron microscopy have provided several high-resolution structures of TRPC channels. Growing evidence demonstrates the involvement of TRPC …
Transient receptor potential canonical type 6 (TRPC6) O …
Mar 17, 2023 · Transient receptor potential canonical type 6 (TRPC6) is a non-voltage-gated channel that principally conducts calcium. Elevated channel activation contributes to fibrosis, …
Structural basis for pharmacological modulation of the TRPC6 …
Here we report cryo-EM structures of TRPC6 in both antagonist-bound and agonist-bound states. The structures reveal two novel recognition sites for the small-molecule modulators …