RaSP is a method for making rapid and accurate predictions of changes in protein stability that enabled us to calculate ~300 million stability changes for nearly all possible single amino acid changes in the human proteome.

Some of the mutations that occur during influenza evolution can only be tolerated in conjunction with other mutations that increase the stability of a viral protein.

Protein stability in the cage formed by the chaperonin GroEL and its cofactor GroES is reduced by more than 5 kcal mol^-1 relative to that in bulk solution.

A unique form of regulation has been observed in the unfolded protein response of S. pombe, along with a novel mechanism of post-transcriptional mRNA processing.

A biochemical approach shows that SOX4 guaranteed the PGR protein stability through repressing the ubiquitin E3 ligase HERC4, to make the stroma cell conducive for response to progesterone and decidualization.

A cell-sized fully confined space significantly controls the emergence and stability of a protein wave, resulting in intracellular spatiotemporal regulation driven by a reaction-diffusion mechanism.

Cyclin D1 protein stability is regulated by ubiquitin-proteasome mechanism mediated by multiple E3 ligases, including newly identified Keap1, DDB2, and WSB2.

The ribosomal protein, Rps27l, plays an oncogenic role by promoting p53 degradation via stabilizing the Mdm2-Mdm4 complex, but a tumor suppressor role by preventing the aneuploidy and loss of p53 heterozygosity.

The transcription and splicing factor T-box3 is present in primary cilia, regulates multiple aspects of limb development, and interacts with members of the protein complex required for the stability and processing of the Gli3 transcription factor.

14-3-3 protein augments the protein stability of phosphorylated spastin and promotes the recovery of spinal cord injury in mice.