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Remarkably, human CXCR4 is a more efficient receptor for FIV than either feline CXCR4 or rat CXCR4 [11].

Interestingly, human CXCR4 is a more efficient receptor for FIV than either feline CXCR4 or rat CXCR4 and was in fact employed in the original study that showed CXCR4 was the entry receptor for FIV [11].

While the overall results are mixed, it appears that there are differences between the 4-repeat allele and 7-repeat allele with the 4-repeat allele being a more efficient receptor than the 7-repeat allele [7], [57], [58].

This conversion has been proposed to lead to a more efficient receptor clustering (particularly important for DR5-induced apoptosis), which provides a more potent death signal resulting in enhanced apoptosis compared to its soluble counterpart [ 31].

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Viruses capable of replicating to higher titers could result from a unique access to cell types that facilitate high-titer replication through more efficient receptor-envelope interactions, viral replicase differences that increase replication efficiency within host cells, decreased sensitivity to host innate immunologic responses, or by altering the physiological host responses such as fever.

Higher order TRAIL aggregates have been associated with increased activity due to more efficient death receptor clustering.

It is suggested that the reason for the experimental observations which show that blunt conductors are more efficient lightning receptors than sharp ones is the presence of glow corona at the tip of the sharp ones during the time of lightning strikes.

Hapten clustering has been extensively investigated in the field of carbohydrate vaccines, where this approach is thought to enhance the immune response by mimicking the natural spatial arrangement of carbohydrates on cancer cells, while also promoting more efficient B cell receptor cross-linking.

From an evolutionary point of view, it is interesting that CXCL9 seems to have evolved towards a robust antibacterial chemokine with relatively weak receptor interaction, while CXCL10 and CXCL11 both have more efficient interaction with the receptor but are less antibacterial and more protease sensitive than CXCL9.

PPARG has been shown to potentiate the effects of a variety of chemotherapeutic regimens on the assumption that the addition of a specific ligand would render the receptor more efficient in transactivating target genes [29].

Possibly, the glycosylation occurring close to the antigen-binding site results in more efficient blocking of toxin receptor sites as compared to glycosylation occurring more distant from the antigen-binding site.

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