Claudio Coddou
Catholic University of the North
47 Papers
366 Citations
Claudio Coddou is an academic researcher from Catholic University of the North. The author has contributed to research in topics: Receptor & Purinergic receptor. The author has an hindex of 18, co-authored 41 publications. Previous affiliations of Claudio Coddou include National Institutes of Health & University of Santiago, Chile.
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Papers
Activation and Regulation of Purinergic P2X Receptor Channels
TL;DR: Data obtained from numerous site-directed mutagenesis experiments accumulated during the last 15 years are discussed with reference to the crystal structure, allowing a structural interpretation of the molecular basis of orthosteric and allosteric ligand actions.
512
Prenatal to Early Postnatal Nicotine Exposure Impairs Central Chemoreception and Modifies Breathing Pattern in Mouse Neonates: A Probable Link to Sudden Infant Death Syndrome
Jaime Eugenín,Marcelo Otárola,Eduardo Bravo,Claudio Coddou,Verónica Cerpa,Miguel Reyes-Parada,Isabel Llona,Rommy von Bernhardi +7 more
TL;DR: Results indicate that nicotine exposure affects the respiratory rhythm pattern generator and causes a decline in central chemoreception during early postnatal life, Consequently, breathing would become highly vulnerable, failing to respond to chemosensory demands.
79
Small molecule positive allosteric modulation of TRPV1 activation by vanilloids and acidic pH
Krisztian Kaszas,Jason M. Keller,Claudio Coddou,Santosh K. Mishra,Mark A. Hoon,Stanko S. Stojilkovic,Kenneth A. Jacobson,Michael J. Iadarola +7 more
TL;DR: Positive modulation of TRPV1 sensitivity suggests that it may be possible to produce a selective analgesia through calcium overload restricted to highly active nociceptive nerve endings at sites of tissue damage and inflammation.
51
Characterization of the antagonist actions of 5-BDBD at the rat P2X4 receptor.
TL;DR: The effects of 5-BDBD in long-term potentiation experiments performed in rat hippocampal slices are studied, finding this antagonist can partially decrease LTP, a response that is believed to be mediated in part by endogenous P2X4Rs.
43
Extracellular histidine residues identify common structural determinants in the copper/zinc P2X2 receptor modulation
Ramón A. Lorca,Claudio Coddou,M. Consuelo Gazitúa,Paulina Bull,Cristian Arredondo,J. Pablo Huidobro-Toro +5 more
TL;DR: It is proposed that His120, His192, His213 and His245 form part of a common allosteric metal‐binding site of the P2X2 receptor, which for the specific coordination of copper, but not zinc, additionally involves His319.
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