We determine the full 1/ $$ \sqrt{\uplambda} $$λ correction to the flat-space Wilson coefficients which enter the AdS Virasoro-Shapiro amplitude in $$ \mathcal{N} $$N = 4 SYM theory at strong coupling. The assumption that the Wilson coefficients are in the ring of single-valued multiple zeta values, as expected for closed string amplitudes, is surprisingly powerful and leads to a unique solution to the dispersive sum rules relating Wilson coefficients and OPE data obtained in [1]. The corresponding OPE data fully agrees with and extends the results from integrability. The Wilson coefficients to order 1/ $$ \sqrt{\uplambda} $$λ can be summed into an expression whose structure of poles and residues generalises that of the Virasoro-Shapiro amplitude in flat space.

We consider the four-point correlator of the stress-energy tensor in $$ \mathcal{N} $$N = 4 SYM, to leading order in inverse powers of the central charge, but including all order corrections in 1/λ. This corresponds to the AdS version of the Virasoro-Shapiro amplitude to all orders in the small α′/low energy expansion. Using dispersion relations in Mellin space, we derive an infinite set of sum rules. These sum rules strongly constrain the form of the amplitude, and determine all coefficients in the low energy expansion in terms of the CFT data for heavy string operators, in principle available from integrability. For the first set of corrections to the flat space amplitude we find a unique solution consistent with the results from integrability and localisation.

A bstract: We present a constructive method to compute the AdS Virasoro-Shapiro amplitude, order by order in AdS curvature corrections. At k ^th order the answer takes the form of a genus zero world-sheet integral involving weight 3 k single-valued multiple polylogarithms. The coefficients in our ansatz are fixed, order by order, by requiring: crossing symmetry; the correct supergravity limit; the correct structure of poles, determined by dispersive sum rules; and the dimensions of the first few Konishi-like operators, available from integrability. We explicitly construct the first two curvature corrections. Our final answer then reproduces all localisation results and all CFT data available from integrability, to this order, and produces a wealth of new CFT data for planar $$ \mathcal{N} $$ N = 4 SYM at strong coupling.

We study the stress tensor four-point function for $$ \mathcal{N} $$N = 4 SYM with gauge group G = SU(N), SO(2N + 1), SO(2N) or USp(2N) at large N . When G = SU(N), the theory is dual to type IIB string theory on AdS₅× S⁵ with complexified string coupling τ_s, while for the other cases it is dual to the orbifold theory on AdS₅× S⁵/ℤ₂. In all cases we use the analytic bootstrap and constraints from localization to compute 1-loop and higher derivative tree level corrections to the leading supergravity approximation of the correlator. We give perturbative evidence that the localization constraint in the large N and finite complexified coupling τ limit can be written for each G in terms of Eisenstein series that are modular invariant in terms of τ_s ∝ τ, which allows us to fix protected terms in the correlator in that limit. In all cases, we find that the flat space limit of the correlator precisely matches the type IIB S-matrix. We also find a closed form expression for the SU(N) 1-loop Mellin amplitude with supergravity vertices. Finally, we compare our analytic predictions at large N and finite τ to bounds from the numerical bootstrap in the large N regime, and find that they are not saturated for any G and any τ , which suggests that no physical theory saturates these bootstrap bounds.

The sirtuin enzymes are a family of lysine deacylases that regulate gene transcription and metabolism. Sirtuin 5 (SIRT5) hydrolyzes malonyl, succinyl, and glutaryl ϵ‐N‐carboxyacyllysine posttranslational modifications and has recently emerged as a vulnerability in certain cancers. However, chemical probes to illuminate its potential as a pharmacological target have been lacking. Here we report the harnessing of aryl fluorosulfate‐based electrophiles as an avenue to furnish covalent inhibitors that target SIRT5. Alkyne‐tagged affinity‐labeling agents recognize and capture overexpressed SIRT5 in cultured HEK293T cells and can label SIRT5 in the hearts of mice upon intravenous injection of the compound. This work demonstrates the utility of aryl fluorosulfate electrophiles for targeting of SIRT5 and suggests this as a means for the development of potential covalent drug candidates. It is our hope that these results will serve as inspiration for future studies investigating SIRT5 and general sirtuin biology in the mitochondria.