2021
An epilepsy-causing mutation leads to co-translational misfolding of the Kv7.2 channel
Urrutia J, Aguado A, Gomis-Perez C, Muguruza-Montero A, Ballesteros OR, Zhang J, Nuñez E, Malo C, Chung HJ, Leonardo A, Bergara A, Villarroel A. An epilepsy-causing mutation leads to co-translational misfolding of the Kv7.2 channel. BMC Biology 2021, 19: 109. PMID: 34020651, PMCID: PMC8138981, DOI: 10.1186/s12915-021-01040-1.Peer-Reviewed Original ResearchConceptsKv7.2 channelsChannel functionSequences of proteinsNon-native configurationsNascent chainsProper foldingEpilepsy-causing mutationsIQ motifResponsive domainHuman diseasesHelix ANative conformationFolding routeIon channelsKCNQ2 geneMutationsNeuronal compartmentsFoldingMisfoldingProteinKey pathogenic mechanismsPathogenic variantsSilico studiesPathogenic mechanismsSide chains
2014
The Ever Changing Moods of Calmodulin: How Structural Plasticity Entails Transductional Adaptability
Villarroel A, Taglialatela M, Bernardo-Seisdedos G, Alaimo A, Agirre J, Alberdi A, Gomis-Perez C, Soldovieri MV, Ambrosino P, Malo C, Areso P. The Ever Changing Moods of Calmodulin: How Structural Plasticity Entails Transductional Adaptability. Journal Of Molecular Biology 2014, 426: 2717-2735. PMID: 24857860, DOI: 10.1016/j.jmb.2014.05.016.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsConceptsC-lobeProtein Data Bank databaseStructure-function studiesDomain organizationProtein complexesCaM bindingHuman diseasesRole of CaMStructural plasticityGreat diversityCaM mutationsNew exciting avenuesThree-dimensional arrangementHuman pathophysiologyDiversity of targetsRemarkable varietyIndependent signalsCalmodulinDiversityExciting avenuesBindingRecent advancesTargetExceptional versatilityHelix