2001
Calpain proteolysis of αII-spectrin in the normal adult human brain
Huh G, Glantz S, Je S, Morrow J, Kim J. Calpain proteolysis of αII-spectrin in the normal adult human brain. Neuroscience Letters 2001, 316: 41-44. PMID: 11720774, DOI: 10.1016/s0304-3940(01)02371-0.Peer-Reviewed Original ResearchConceptsAdult human brainCalpain activationEvident neurological diseaseHuman brainCortical gray matterLong-term potentiationNormal adult human brainDendrites of neuronsCerebellar Purkinje cellsCalpain processingReactive astrocytesCerebral cortexPyramidal neuronsSynaptic remodelingClinical conditionsNeuronal apoptosisAdult brainPositive cellsNeurological diseasesGray matterPurkinje cellsTopographic distributionAlphaII-spectrinBrainCalpain proteolysis
1988
Proteolytic processing of human brain alpha spectrin (fodrin): identification of a hypersensitive site
Harris A, Morrow J. Proteolytic processing of human brain alpha spectrin (fodrin): identification of a hypersensitive site. Journal Of Neuroscience 1988, 8: 2640-2651. PMID: 3074159, PMCID: PMC6569499, DOI: 10.1523/jneurosci.08-07-02640.1988.Peer-Reviewed Original ResearchConceptsLong-term potentiationBrain spectrinCalcium-dependent mechanismCalcium-dependent neutral proteaseCalcium-dependent proteaseCentral molecular mechanismsSite of actionReceptor functionPostsynaptic membraneCalcium-dependent mannerFurther investigationMolecular mechanismsGel overlay techniqueAlpha subunitNeutral proteaseNonerythroid spectrinImportant moleculesProteolytic processingCleavage fragmentsPotentiationProtease
1980
Identification of proteolytically resistant domains of human erythrocyte spectrin.
Speicher D, Morrow J, Knowles W, Marchesi V. Identification of proteolytically resistant domains of human erythrocyte spectrin. Proceedings Of The National Academy Of Sciences Of The United States Of America 1980, 77: 5673-5677. PMID: 7003593, PMCID: PMC350131, DOI: 10.1073/pnas.77.10.5673.Peer-Reviewed Original Research