Choose an application

• Reference Manager
• EndNote
• RefWorks (Direct export to RefWorks)

Almost 25 years ago, the first mammalian transient receptor potential (TRP) channel was cloned and published. TRP channels now represent an extended family of 28 members fulfilling multiple roles in the living organism. Identified functions include control of body temperature, transmitter release, mineral homeostasis, chemical sensing, and survival mechanisms in a challenging environment. The TRP channel superfamily covers six families: TRPC with C for “canonical”, TRPA with A for “ankyrin”, TRPM with M for “melastatin”, TRPML with ML for “mucolipidin”, TRPP with P for “polycystin”, and TRPV with V for “vanilloid”. Over the last few years, new findings on TRP channels have confirmed their exceptional function as cellular sensors and effectors. This Special Book features a collection of 8 reviews and 7 original articles published in “Cells” summarizing the current state-of-the-art on TRP channel research, with a main focus on TRP channel activation, their physiological and pathophysiological function, and their roles as pharmacological targets for future therapeutic options.

n/a --- transient receptor potential channels --- photochromic ligands --- elementary immunology --- Purkinje cell --- EPSC --- substance P --- chemicals --- organ toxicity --- lymphocytes --- HSP70 --- physiology --- bioavailable --- inflammatory bowel disease --- platelets --- pollutants --- yeast --- regulatory T cells --- kinase --- Saccharomyces cerevisiae --- manganese --- cerebellum --- TRP channel --- NHERF --- inflammation --- nanoHPLC-ESI MS/MS --- TRPM7 --- chemical probes --- TRPM8 --- dorsal column nuclei --- TRPV2 --- TRPV3 --- calcitonin gene-related peptide --- TRPV1 --- ion channels --- transient receptor potential --- 2D gel electrophoresis --- MALDI-TOF MS(/MS) --- TRPV4 --- overproduction --- sulfur mustard --- oxidative stress --- graft versus host disease --- menthol --- topical --- chemosensor --- AP18 --- calcium signalling --- mucosal epithelium --- cuneate nucleus --- production platform --- TRPC channels --- ulcerative colitis --- channel structure --- xerostomia --- neutrophils --- cardiovascular system --- TRPC5 --- TRPC6 --- TRPC3 --- TRPC4 --- calcium signaling --- protein purification --- adipose tissue --- transient receptor potential (TRP) channels --- sodium --- TH17 --- diacylglycerol --- hypersensitivity --- TRPY1 --- GABAB --- HEK293 --- thrombosis --- ion channel --- TRPC --- pathophysiology --- SMAD --- toxicology --- endothelium --- calcium --- proteomics --- TRPA1 --- salivary glands --- TRP channels --- lipid mediators --- sensors --- radiation --- TRPM4 channel --- human medulla oblongata --- mGluR1 --- small molecules --- TRPC3 pharmacology

Choose an application

• Reference Manager
• EndNote
• RefWorks (Direct export to RefWorks)

Gap Junction Structure and Chemical Regulation: Direct Calmodulin Role in Cell-to-Cell Channel Gating describes and discusses the findings of major studies conducted during the past century on the structure and chemical regulation of direct cell-to-cell communication via gap junction channels. Chapters bring together important findings on direct cell communication, from its history, to its structure and regulation. These channels are essential for normal organ function, and mutations in their protein (connexin) cause various diseases. The book is useful for established investigators who need a review on the field and young investigators who need a thorough resource for study and comprehension.

Christian shrines --- Christian saints --- Spain --- Cult --- Catholic Church --- Customs and practices. --- Nansa River Valley (Spain) --- Religious life and customs. --- Gap junctions (Cell biology) --- Connexins. --- Calmodulin. --- Gap Junctions --- Cell Communication. --- chemistry. --- Cell Interaction --- Cell-to-Cell Interaction --- Cell Communications --- Cell Interactions --- Cell to Cell Interaction --- Cell-to-Cell Interactions --- Communication, Cell --- Communications, Cell --- Interaction, Cell --- Interaction, Cell-to-Cell --- Interactions, Cell --- Interactions, Cell-to-Cell --- Bovine Activator Protein --- Cyclic AMP-Phosphodiesterase Activator --- Phosphodiesterase Activating Factor --- Phosphodiesterase Activator Protein --- Phosphodiesterase Protein Activator --- Regulator, Calcium-Dependent --- Calcium-Dependent Activator Protein --- Calcium-Dependent Regulator --- AMP-Phosphodiesterase Activator, Cyclic --- Activating Factor, Phosphodiesterase --- Activator Protein, Bovine --- Activator Protein, Calcium-Dependent --- Activator Protein, Phosphodiesterase --- Activator, Cyclic AMP-Phosphodiesterase --- Activator, Phosphodiesterase Protein --- Calcium Dependent Activator Protein --- Calcium Dependent Regulator --- Cyclic AMP Phosphodiesterase Activator --- Factor, Phosphodiesterase Activating --- Protein Activator, Phosphodiesterase --- Protein, Bovine Activator --- Protein, Calcium-Dependent Activator --- Protein, Phosphodiesterase Activator --- Regulator, Calcium Dependent --- Calcium Signaling --- Calcium-dependent activator protein --- Calcium-dependent regulator --- Calcium-binding proteins --- Membrane proteins --- Junctions, Gap (Cell biology) --- Nexus (Cell biology) --- Cell junctions --- Connexins --- Church of Rome --- Roman Catholic Church --- Katholische Kirche --- Katolyt︠s︡ʹka t︠s︡erkva --- Römisch-Katholische Kirche --- Römische Kirche --- Ecclesia Catholica --- Eglise catholique --- Eglise catholique-romaine --- Katolicheskai︠a︡ t︠s︡erkovʹ --- Chiesa cattolica --- Iglesia Católica --- Kościół Katolicki --- Katolicki Kościół --- Kościół Rzymskokatolicki --- Nihon Katorikku Kyōkai --- Katholikē Ekklēsia --- Gereja Katolik --- Kenesiyah ha-Ḳatolit --- Kanisa Katoliki --- כנסיה הקתולית --- כנסייה הקתולית --- 가톨릭교 --- 천주교 --- Nansa Valley (Spain)