Query author contributions in Reactome
Reactome depends on collaboration between our curation team and outside experts to assemble and peer-review its pathway modules. The integration of ORCID within Reactome enables us to meet a key challenge with authoring, curating and reviewing biological information by incentivizing and crediting the external experts that contribute their expertise and time to the Reactome curation process. More information is available at ORCID and Reactome.
If you have an ORCID ID that is not listed on this page, please forward this information to us and we will update your Reactome pathway records.
Details on Person Calcium-activated chloride channels (CaCCs) are ubiquitously...
| Class:Id | Summation:2684912 |
|---|---|
| _displayName | Calcium-activated chloride channels (CaCCs) are ubiquitously... |
| _timestamp | 2013-01-28 10:21:13 |
| created | [InstanceEdit:2684910] Jassal, Bijay, 2012-12-03 |
| literatureReference | [LiteratureReference:2684929] International Union of Basic and Clinical Pharmacology. LXXXV: calcium-activated chloride channels [LiteratureReference:2684895] The TMEM16 protein family: a new class of chloride channels? |
| modified | [InstanceEdit:2684964] Jassal, Bijay, 2012-12-03 [InstanceEdit:3000513] Jassal, Bijay, 2013-01-28 [InstanceEdit:9733355] Wu, Guanming, 2021-06-04 |
| text | Calcium-activated chloride channels (CaCCs) are ubiquitously expressed and implicated in physiological processes such as sensory transduction, fertilization, epithelial secretion, and smooth muscle contraction. The anoctamin family of transmembrane proteins (ANO, TMEM16) belong to CaCCs and have been shown to transport Cl- ions when activated by intracellular Ca2+ (Galietta 2009, Huang et al. 2012). There are currently 10 members, ANO1-10, all having a similar structure, with eight putative transmembrane domains and cytosolic amino- and carboxy-termini. ANO1 and 2 possess Ca2+ activated Cl- transport activity (Yang et al. 2008, Scudieri et al. 2012) while the remaining members also show some demonstrable activity (Tian et al. 2012). All CLCAs contain a consensus cleavage motif which is recognised by an internal zincin metalloprotease domain within the N terminus. Self-proteolysis within the secretory pathway yields N- and C-terminal fragments, a step critical for CLCA activation of calcium-activated chloride channels (CaCCs) mediated through the N-terminal fragment (Yurtsever et al. 2012). |
| (summation) | [Reaction:2684901] ANOs transport cytosolic Cl- to extracellular region [Homo sapiens] |
| [Change default viewing format] | |
No pathways have been reviewed or authored by Calcium-activated chloride channels (CaCCs) are ubiquitously... (2684912)
