2001
Dynamic molecular modeling of pathogenic mutations in the spectrin self-association domain
Zhang Z, Weed S, Gallagher P, Morrow J. Dynamic molecular modeling of pathogenic mutations in the spectrin self-association domain. Blood 2001, 98: 1645-1653. PMID: 11535493, DOI: 10.1182/blood.v98.6.1645.Peer-Reviewed Original ResearchConceptsSelf-association domainPoint mutationsHuman sequenceDrosophila alpha-spectrinDynamic molecular modelingHuman erythrocyte spectrinCytoskeletal functionSpecific point mutationsConservative substitutionsPrimary sequenceConformational rearrangementsAlpha-spectrinHelical regionHydrophilic residuesAmino acidsMutationsSpectrinSalt bridgeErythrocyte spectrinStructural consequencesPathogenic mutationsRepeat unitsMolecular modelingSequenceStructural disruption
1994
Ankyrin binds to two distinct cytoplasmic domains of Na,K-ATPase alpha subunit.
Devarajan P, Scaramuzzino D, Morrow J. Ankyrin binds to two distinct cytoplasmic domains of Na,K-ATPase alpha subunit. Proceedings Of The National Academy Of Sciences Of The United States Of America 1994, 91: 2965-2969. PMID: 8159688, PMCID: PMC43495, DOI: 10.1073/pnas.91.8.2965.Peer-Reviewed Original ResearchConceptsK-ATPase alpha subunitMembrane transport proteinsCytoplasmic domainAlpha subunitK-ATPaseTransport proteinsIntegral membrane transport proteinsDomain IIPutative cytoplasmic domainInteraction of ankyrinDistinct cytoplasmic domainsATPase domainHuman erythrocyte spectrinSignificant homologyUbiquitous proteinSpectrin cytoskeletonRecombinant fusion proteinPrimary sequenceAnkyrinFusion proteinChannel proteinsClear functionSubunitsProteinSpectrin binds