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Their findings reveal a previously unknown dinucleotide binding pocket within the DnaA oligomer, where two bases of a repeating DnaA-trio sequence tightly bind, enabling the capture of a single DNA strand.

The direction of light-induced changes is also unusual, since for other Cry proteins only the reverse process has been described, i.e., from monomer arrangements in the dark to dimer or higher oligomer arrangements in the light.

Since then, annual NIH support for studies labeled “amyloid, oligomer, and Alzheimer’s” has risen from near zero to $287 million in 2021.

An exception was Harvard University’s Dennis Selkoe, a leading advocate of the amyloid and toxic oligomer hypotheses, who has cited the Nature paper at least 13 times.

Such oligomers are notoriously unstable, converting to other oligomer types spontaneously.