Ali H. Shaib

Hello world, meet 1,000× Expansion Microscopy.
1,000,000,000× expansion by volume! A gel that starts at a few centimeters will then expand to the volume of an Olympic swimming pool. biorxiv.org/content/10.648…
In our new bioRxiv preprint, work carried out between MIT and UMG, led by Helena Hu in collaboration with scientists from the labs of @eboyden3 Ed Boyden, Silvio Rizzoli, and myself, we present Thousandfold Expansion Microscopy.
By enlarging biological specimens across multiple rounds of expansion, molecular-scale features, as small as the distances between adjacent amino acids, can be visualized with conventional optical microscopes.
Democratizing super-resolution microscopy.

Insane work. Recommended read

Lol even AI hates Reviewer 2 🫣😅

there probably isn’t a historically honest three-person solution.

before ChR2, genetically targeted optical control of neurons had already been demonstrated, notably by Gero Miesenböck and colleagues.

Peter Hegemann and his group traced the algal light response to the proteins that became known as channelrhodopsins.

Georg Nagel then provided the decisive electrophysiological proof that ChR1 and ChR2 are directly light-gated ion channels, showed that ChR2 could depolarize mammalian cells, and later provided the construct used for the neuronal work.

Karl Deisseroth helped make the transition into neurons and drove the development of optogenetics into a broadly usable neuroscience technology.

Ed Boyden played a key intellectual role in recognizing microbial opsins as a route to precise neural control, then carried out the now-famous 1 a.m. experiments demonstrating millisecond control of neuronal firing with ChR2, work that became central to the landmark 2005 paper.

the 2026 Nobel is defensible, but still unjust if the aim is to capture the essence of how optogenetics was actually invented. the problem is not simply the choice of one name over another. the three-person limit has aged poorly against the history of the field.

synapsin disappears. actin remembers.
biorxiv.org/content/10.648… (preprint)
in latest work led by Daniel Mansour and Rajdeep Chowdhury, from our group and those of Rangamani and Rizzoli, we show that synapsin-1 and actin form ordered nanoscale assemblies.

combining ONE microscopy, reconstitution experiments and computational modelling, we reveal a regular actin scaffold within synapsin condensates. When the condensates dissolve, the actin architecture largely persists, suggesting a structural memory that could guide their reassembly.

this offers a possible mechanism for how synapses maintain their organization through cycles of activity. Synapsin helps build the actin scaffold, which could then provide a lasting template for rebuilding synaptic vesicle clusters.