<i>In Silico</i> Design of <i>phaCAB</i> Expression Constructs for Cellulolytic Hosts Toward Hemp Hurd Valorisation and Polyhydroxybutyrate Biosynthesis. [PDF]
Myeni ZR +4 more
europepmc +1 more source
Transient receptor potential canonical 3 is required for HPV-induced malignant transformation of cervical epithelial cells. [PDF]
Tan Y +9 more
europepmc +1 more source
Integrated genome mining and phytohormone profiling of six plant growth-promoting elite bacterial strains. [PDF]
Ercole TG +7 more
europepmc +1 more source
TRP channels in epileptogenesis: calcium dysregulation mechanisms and pharmacological targeting strategies. [PDF]
Deng G +9 more
europepmc +1 more source
Implant-derived titanium particles impair macrophage bacterial clearance via TRPC1 and lysosomal dysfunction. [PDF]
Girón Bastidas J +6 more
europepmc +1 more source
Functional and structural basis of a hypermorphic TRPC3 variant. [PDF]
Bell B +10 more
europepmc +1 more source
Pyrazole-derived TRPC3 antagonist ameliorates synaptic dysfunctions and memory deficits in Alzheimer's disease models. [PDF]
Wang J +18 more
europepmc +1 more source
The mammalian TRPC cation channels
Transient Receptor Potential-Canonical (TRPC) channels are mammalian homologs of Transient Receptor Potential (TRP), a Ca(2+)-permeable channel involved in the phospholipase C-regulated photoreceptor activation mechanism in Drosophila. The seven mammalian TRPCs constitute a family of channels which have been proposed to function as store-operated as ...
Mohamed Trebak +2 more
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This chapter reviews recent evidence indicating that canonical or classical transient receptor potential (TRPC) channels are directly or indirectly mechanosensitive (MS) and can therefore be designated as mechano-operated channels (MOCs). The MS functions of TRPCs may be mechanistically related to their better known functions as store-operated and ...
Owen P, Hamill, Rosario, Maroto
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Organization and function of TRPC channelosomes
Pflügers Archiv - European Journal of Physiology, 2007TRPC proteins constitute a family of conserved Ca2+-permeable cation channels which are activated in response to agonist-stimulated PIP2 hydrolysis. These channels were initially proposed to be components of the store-operated calcium entry channel (SOC).
Indu S, Ambudkar, Hwei Ling, Ong
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