ADP-ribose gating of the calcium-permeable LTRPC2 channel revealed by Nudix motif homology

By A. Perraud, A. Fleig, Christopher A. Dunn, Leigh Ann Bagley, P. Launay, C. Schmitz, Alexander J Stokes, Qiqin Zhu, M. Bessman, R. Penner and 2 more. Nature, 2001

916 citations recorded by the source corpus.

Subfields: Molecular Biology, Physiology

View Paper: https://www.semanticscholar.org/paper/8d4201258c5cedc1e7689eeadde9ddaaf18c4f40

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

1. D. Clapham
2. D. Julius
3. B. Nilius
4. G. Owsianik
5. C. Montell
6. W. Neuhausser
7. D. McKemy
8. Ardem Patapoutian

In Physiology

1. G. Owsianik
2. B. Nilius
3. D. Julius
4. Arne May

Citations in the corpus

• The transient receptor potential family of ion channels (2011, background): “For example, a Nudix hydrolase domain of TRPM2 functions as an ADP­ribose pyrophosphatase [21].”
• TRPM2-mediated Ca2+ influx induces chemokine production in monocytes that aggravates inflammatory neutrophil infiltration (2008, background): “TRPM2, a member of the TRPM subfamily, is a Ca 2+ -permeable channel activated by intracellular messengers such as ADP-ribose (ADPR), nicotinamide adenine dinucleotide (NAD + ) and cyclic ADPR (cADPR”
• Hypomagnesemia with secondary hypocalcemia is caused by mutations in TRPM6, a new member of the TRPM gene family (2002, positive): “These findings emphasize the growing functional diversity of TRPM family members, which have previously been shown to be important in cellular processes such as cell survival, progression of tumors and intracellular signalin”
• An introduction to TRP channels. (2006, background): “Inhibitors of poly (ADP-ribose) polymerase, a potential enzymatic source of ADPR, prevent TRPM2 activation but do not block the channel directly (121).”
• Reactive Oxygen Species in Inflammation and Tissue Injury (2014, neutral): “Intracellular application of ADPR, the substrate of the NUDT9 enzyme, specifically induced TRPM2 gating (343).”
• TRP Channels (2012, neutral): “significant expression in human gastrointestinal tract (GI), Functional properties”
• Identification of a cold receptor reveals a general role for TRP channels in thermosensation (2002, background): “Among members of this subfamily, TRPM2 and TRPM7 have been electrophysiologically characterized and shown to behave as bifunctional proteins in which enzymatic activities associated with their long C-terminal domains are believed to regulate channel openin”
• Evolution and function of the ADP ribosyl cyclase/CD38 gene family in physiology and pathology. (2008, neutral): “naling molecule in vertebrate systems (279).”
• The TRP Superfamily of Cation Channels (2005, background): “TRPM2 is composed of a C-terminal ADP-ribose pyrophosphatase (NUDT9) domain (172, 173).”