18 results on '"Sorensen, Brenda R."'
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2. Calcium-induced conformational switching of Paramecium calmodulin provides evidence for domain coupling
3. An interdomain linker increases the thermostability and decreases the calcium affinity of the calmodulin N-domain
4. Paramecium calmodulin mutants defective in ion channel regulation associate with melittin in the absence of calcium but require it for tertiary collapse
5. The 32- and 14-kilodalton subunits of replication protein A are responsible for species-specific interactions with single-stranded DNA
6. Interactions between domains of APO calmodulin alter calcium binding and stability
7. Proteolytic footprinting titrations for estimating ligand-binding constants and detecting pathways of conformational switching of calmodulin
8. The neuronal voltage-dependent sodium channel type II IQ motif lowers the calcium affinity of the C-domain of calmodulin
9. Calcium binding to calmodulin mutants having domain-specific effects on the regulation of ion channels
10. Interdomain cooperativity of calmodulin bound to melittin preferentially increases calcium affinity of sites I and II
11. The Neuronal Voltage-Dependent Sodium Channel Type II IQ Motif Lowers the Calcium Affinity of the C-Domain of Calmodulin
12. The NMDA Receptor NR1 C1 Region Bound to Calmodulin: Structural Insights into Functional Differences between Homologous Domains
13. PU.1 Binding to ets Motifs within the Equine Infectious Anemia Virus Long Terminal Repeat (LTR) Enhancer: Regulation of LTR Activity and Virus Replication in Macrophages
14. Basic interdomain boundary residues in calmodulin decrease calcium affinity of sites I and II by stabilizing helix–helix interactions
15. Calcium Binding to Calmodulin Mutants Monitored by Domain-Specific Intrinsic Phenylalanine and Tyrosine Fluorescence
16. An Interdomain Linker Increases the Thermostability and Decreases the Calcium Affinity of the Calmodulin N-Domain
17. The 32- and 14-Kilodalton Subunits of Replication Protein A Are Responsible for Species-Specific Interactions with Single-Stranded DNA
18. Basic interdomain boundary residues in calmodulin decrease calcium affinity of sites I and II by stabilizing helixhelix interactions
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