1) The screenshot is my reaching out to Levent to coordinate our releases. I hope it’s clear from the message that we came in with the best possible intentions.

2) I never ever asked for Levent to be removed from authorship of his own work (as indicated by my text). I was surprised to learn during the call with Tristan that they had only solved Euler and not Navier-Stokes; after learning this we brainstormed possible paths forward. One option we discussed was that Tristan could be the lead author on a rewrite of OpenAI’s Navier-Stokes proof. It is in that context that I said “it would be simpler if Levent was not an Anthropic employee” because I felt it would be inappropriate for an Anthropic employee to author OpenAI’s work. Importantly it was admitted that internal Anthropic models had been used in their proof of Euler blowup; I therefore felt I could not consider Levent to be an independent academic. Another option I wanted to propose (but got cut short) is to offer access to our internal model so that they could try to finish their proof and bridge the gap between Euler and NS. Again I did not know how to navigate giving access to internal OpenAI IP to an Anthropic employee.

3) To reiterate it plainly: as my text clearly indicates, and as I said during our call, OpenAI's intention was to do everything possible to celebrate their mathematical achievements and the heroic efforts that they made on Euler. In the call I was immediately met with a litany of slander, including direct threats that if we were to announce Navier-Stokes he would immediately go to the press with a barrage of unfounded accusations. I refuted all these accusations but he replied “there is nothing you can do, I simply do not trust you”. I was confused why one would turn an incredible source for celebration (of their achievements!) into such bickering, which is when I said that I did not understand why one would risk their career [over unfounded accusations]. Genuinely, at that moment, I was trying to care for him and do a last ditch attempt to get a chance to give them all the credits that they deserve. I deeply apologize for this extremely poor choice of words, it is the opposite of what I was trying to convey. (I should say that I retracted them on the spot by the way.)

4) Overall, on a personal level, it was incredibly difficult to have these conversations. Levent refused to attend any of the meetings despite my repeated asking. As Sholto Douglas said, there will need to be coordination between Anthropic and OpenAI in the future; I felt I was doing a proxy negotiation with Anthropic while the Anthropic employee refused to directly participate.

Finally, recalcitrant peptides are depleted in cytoplasmic and mitochondrial domains and strongly enrichedby up to 16-foldin calcium-dependent phospholipid-binding C2 domains. C2 domains mediate Ca2+-regulated binding of proteins to anionic phospholipids on membrane surfaces, (58) and their enrichment indicates that peptide persistence is disproportionately associated with proteins stabilized at membranes, rather than within freely soluble intracellular compartments. Loss of ionic homeostasis and rising intracellular Ca2+ during post-mortem decay (6) would be expected to further promote sustained membrane association of such proteins. Membrane-adjacent microenvironments are structurally constrained, concentrating redox-active substrates and catalysts (such as lipids and metals) while restricting diffusion and oxygen availability relative to the cytosol. In this context, radical oxidation is less likely to proceed via chain propagation, which requires continuous access to molecular oxygen, (59) and more likely to locally terminate via cross-linking. Such cross-linking would be expected to reduce molecular mobility and solubility, sterically hinder enzymatic and hydrolytic attack, and promote the formation of insoluble aggregates resistant to degradation. (60)

A further factor likely reinforcing this taphonomic trajectory is the brain’s unusually large and heterogeneous reservoir of redox-active iron. (61) Nervous tissue contains high iron concentrations relative to most other soft tissues, distributed across multiple pools such as heme proteins, ferritin-bound stores, and iron-rich compartments associated with mitochondria, myelin, and oligodendrocytes. (62) In life, these pools are tightly regulated to support oxidative metabolism while limiting collateral damage. (63) After death, however, progressive membrane failure and loss of regulatory control are expected to alter iron speciation and availability, increasing the likelihood of local metal-catalyzed radical generation. Importantly, such chemistry need not produce uniform oxidative destruction: when redox reactions involving iron occur within membrane-adjacent or diffusion-limited microenvironments, they may favor the formation of short-lived aromatic radicals that terminate by covalent cross-linking rather than by chain-propagating oxidation (Table S22). The enrichment of peroxidaseswhich often involve heme iron or metal cofactors (64)among recalcitrant peptides is compatible with localized, metal-associated redox chemistry, in which iron-containing cofactors may contribute to peroxide-driven radical formation without sustaining chain-propagating oxidation.

The brain is particularly predisposed to follow this trajectory. In life, it is among the most oxidatively stressed organs: it consumes a disproportionate share of oxygen, is rich in redox-active metals, and relies heavily on antioxidant and repair systems to maintain protein integrity. (65) Additionally, the brain combines extreme membrane density, (66) an abundance of structurally stable, long-lived proteins that accumulate heterogeneous oxidative modifications during life, (67) and anatomical sequestration within the cranial vault. Together, these features establish a post-mortem environment characterized by pre-existing chemical and structural heterogeneity, limited molecular mobility, and restricted oxygen exchange: conditions that favor local, diffusion-limited radical reactions and termination by cross-linking rather than runaway, chain-propagating oxidation. Notably, the molecular features that define this post-mortem pathway closely parallel those that stabilize aggregation-prone protein assemblies in neurodegenerative disease: enrichment of -sheet and structurally ordered fragments, (68) redox-active residue modifications, (69) and oxidative cross-links (70) are hallmarks of pathological protein aggregation in vivo. While the biological contexts differ fundamentally, these parallels indicate that common chemical processes govern protein persistence across clinical and geological time scales.

I know that 28 was wrong.

However, you seem to be totally ignorant with regards to algorithmic complexity. That means you do not even have the very basics needed to be in this exchange.