Building Regular Registers with Rational Malicious Servers and Anonymous Clients

The paper addresses the problem of emulating a regular register in a synchronous distributed system where clients invoking $$\mathsf{read}()$$ and $$\mathsf{write}()$$ operations are anonymous while server processes maintaining the state of the register may be compromised by rational adversaries (i.e., a server might behave as rational malicious Byzantine process). We first model our problem as a Bayesian game between a client and a rational malicious server where the equilibrium depends on the decisions of the malicious server (behave correctly and not be detected by clients vs returning a wrong register value to clients with the risk of being detected and then excluded by the computation). We prove such equilibrium exists and finally we design a protocol implementing the regular register that forces the rational malicious server to behave correctly

Randomized Two-Process Wait-Free Test-and-Set

We present the first explicit, and currently simplest, randomized algorithm for 2-process wait-free test-and-set. It is implemented with two 4-valued single writer single reader atomic variables. A test-and-set takes at most 11 expected elementary steps, while a reset takes exactly 1 elementary step. Based on a finite-state analysis, the proofs of correctness and expected length are compressed into one table.Comment: 9 pages, 4 figures, LaTeX source; Submitte

Cryo-EM of full-length α-synuclein reveals fibril polymorphs with a common structural kernel.

α-Synuclein (aSyn) fibrillar polymorphs have distinct in vitro and in vivo seeding activities, contributing differently to synucleinopathies. Despite numerous prior attempts, how polymorphic aSyn fibrils differ in atomic structure remains elusive. Here, we present fibril polymorphs from the full-length recombinant human aSyn and their seeding capacity and cytotoxicity in vitro. By cryo-electron microscopy helical reconstruction, we determine the structures of the two predominant species, a rod and a twister, both at 3.7 Å resolution. Our atomic models reveal that both polymorphs share a kernel structure of a bent β-arch, but differ in their inter-protofilament interfaces. Thus, different packing of the same kernel structure gives rise to distinct fibril polymorphs. Analyses of disease-related familial mutations suggest their potential contribution to the pathogenesis of synucleinopathies by altering population distribution of the fibril polymorphs. Drug design targeting amyloid fibrils in neurodegenerative diseases should consider the formation and distribution of concurrent fibril polymorphs

Atomic structures of fibrillar segments of hIAPP suggest tightly mated β-sheets are important for cytotoxicity.

hIAPP fibrils are associated with Type-II Diabetes, but the link of hIAPP structure to islet cell death remains elusive. Here we observe that hIAPP fibrils are cytotoxic to cultured pancreatic β-cells, leading us to determine the structure and cytotoxicity of protein segments composing the amyloid spine of hIAPP. Using the cryoEM method MicroED, we discover that one segment, 19-29 S20G, forms pairs of β-sheets mated by a dry interface that share structural features with and are similarly cytotoxic to full-length hIAPP fibrils. In contrast, a second segment, 15-25 WT, forms non-toxic labile β-sheets. These segments possess different structures and cytotoxic effects, however, both can seed full-length hIAPP, and cause hIAPP to take on the cytotoxic and structural features of that segment. These results suggest that protein segment structures represent polymorphs of their parent protein and that segment 19-29 S20G may serve as a model for the toxic spine of hIAPP