New Twitter policy:

At both the Tweet level and the account level, we will remove any free promotion of prohibited 3rd-party social media platforms, such as linking out (i.e. using URLs) to any of the below platforms on Twitter, or providing your handle without a URL.

Prohibited platforms:

• Facebook, Instagram, Mastodon, Truth Social, Tribel, Post and Nostr
• 3rd-party social media link aggregators such as linktr.ee, lnk.bio

Examples:

• “follow me @username on Instagram”
• “username@mastodon.social”
• “check out my profile on Facebook - facebook.com/username”

OK, Musk wins. Anyone who thinks this policy is even vaguely acceptable (or enforceable — good luck banning human cleverness at eluding regex patterns) can have Twitter. Enjoy it. What a goof.

“All oil-field workers are radiation workers.”

How is it possible that the rules about radiation exposure are so thourougly circumvented by the oil industry, like it’s no big deal?

by Dan Moren

Slate has a nice piece on the changing future of board games, from things that you play endlessly to a more finite experience, and the designer who started the trend:

Designers like Rob Daviau are at the center of this change. In 2008, Daviau was working at the toy behemoth Hasbro, cranking out variations on classic games—a Harry Potter edition of Clue, Star Wars Trivial Pursuit, and countless version of Risk. One day, at a brainstorming session for Clue, he cracked a joke. “I don’t know why they keep inviting these people over,” he said. “They’re all murderers.”

I’ve been playing Daviau’s Pandemic Legacy with a few friends since earlier this year, and it’s just as good as the buzz says. Last night, during our latest session, we ended up FaceTiming one of our players who couldn’t make it, because we had to share with her the utter craziness that had just gone down.

Seafall, Daviau’s next title, might be among the most hotly anticipated games of all time. When I was at Gen Con earlier this month, one of my friends made a beeline to the booth for publisher Z-Man as soon as the doors to the exhibit hall opened, but they were already sold out of all their copies. (It doesn’t ship for real until later this fall.)

The current Pandemic Legacy is billed as “Season 1”, so I’m intrigued to see what happens when a Season 2—which they’re reportedly working on—comes down the pike.

[Read on Six Colors.]

by William M. Jacobs, Tuomas P. J. Knowles, Daan Frenkel

Most proteins must remain soluble in the cytosol in order to perform their biological functions. To protect against undesired protein aggregation, living cells maintain a population of molecular chaperones that ensure the solubility of the proteome. Here we report simulations of a lattice model of interacting proteins to understand how low concentrations of passive molecular chaperones, such as small heat-shock proteins, suppress thermodynamic instabilities in protein solutions. Given fixed concentrations of chaperones and client proteins, the solubility of the proteome can be increased by tuning the chaperone–client binding strength. Surprisingly, we find that the binding strength that optimizes solubility while preventing irreversible chaperone binding also promotes the formation of weakly bound chaperone oligomers, although the presence of these oligomers does not significantly affect the thermodynamic stability of the solution. Such oligomers are commonly observed in experiments on small heat-shock proteins, but their connection to the biological function of these chaperones has remained unclear. Our simulations suggest that this clustering may not have any essential biological function, but rather emerges as a natural side-effect of optimizing the thermodynamic stability of the proteome.

"Trump found the flaw in the American Death Star"  

by Jeffrey R. Johnson, Silvia D. Santos, Tasha Johnson, Ursula Pieper, Marta Strumillo, Omar Wagih, Andrej Sali, Nevan J. Krogan, Pedro Beltrao

The African clawed frog Xenopus laevis is an important model organism for studies in developmental and cell biology, including cell-signaling. However, our knowledge of X. laevis protein post-translational modifications remains scarce. Here, we used a mass spectrometry-based approach to survey the phosphoproteome of this species, compiling a list of 2636 phosphosites. We used structural information and phosphoproteomic data for 13 other species in order to predict functionally important phospho-regulatory events. We found that the degree of conservation of phosphosites across species is predictive of sites with known molecular function. In addition, we predicted kinase-protein interactions for a set of cell-cycle kinases across all species. The degree of conservation of kinase-protein interactions was found to be predictive of functionally relevant regulatory interactions. Finally, using comparative protein structure models, we find that phosphosites within structured domains tend to be located at positions with high conformational flexibility. Our analysis suggests that a small class of phosphosites occurs in positions that have the potential to regulate protein conformation.