An evolutionarily conserved protein sequence present in diverse species like yeast, frogs, chickens, and humans binds a well-known template for microtubule nucleation, the gamma-tubulin ring complex, activating and enhancing its ability to nucleate microtubules, even under low tubulin concentrations.

Quantitative microscopy and theory show that the size of Xenopus laevis egg extract spindles is controlled by a spatially-regulated autocatalytic growth mechanism driven by microtubule-stimulated microtubule nucleation.

A massively parallel analysis of the effects of mutations on amyloid beta nucleation provide the first comprehensive atlas of how mutations alter the formation of amyloid fibrils.

The protein TPX2 and the protein complex augmin together recruit the microtubule nucleator γ-TuRC to a pre-existing microtubule where they initiate branching microtubule nucleation.

Switches in cell state downstream of pathogen exposure are driven by a deeply conserved disorder-to-order phase transition in an immunity signaling network.

CAMSAP2 co-condensates with αβ-tubulin to induce microtubule nucleation and growth, serving as a microtubule-organizing centre for non-centrosomal microtubules.

Four αβ-tubulin dimers associate laterally on γ-TuRC to define the rate-limiting transition state for microtubule nucleation.

Self-assembly of bacterial ice nucleation proteins is required for efficient activity and is mediated by electrostatic interactions, creating long and thin fibres.

Heterochromatin is established at nucleation sites associated with open chromatin and RNA transcripts and matures into stable domains if they are found near transposable elements targeted by maternally deposited piRNAs.

The high affinity α-synuclein-monomer binder AS69 converts into a strong sub-stoichiometric inhibitor of nucleation processes upon formation of the AS69-α-synuclein complex, achieving reduced aggregation in vitro and in vivo.