PMC

We show three different learning strategies in the Class-IL scenario. Random storage and acquisition stores instances into, and acquires them from, the buffer randomly. Random acquisition stores instances into the buffer using our importance-based strategy and acquires them from the buffer randomly. Random storage stores instances into the buffer randomly and acquires them from the buffer using our uncertainty-based strategy. The results are shown as a function of the storage fraction, b, and acquisition fraction, a, and are an average across five seeds. Improvement in performance of the random acquisition and random storage learning strategies relative to the random storage and acquisition strategy points to the benefit of our storage and acquisition mechanisms, respectively.

(A) Macroscopic hydrogel formed by FUS (240μM). Bar, 1mm.
(B) EM of FUS hydrogel treated with buffer reveals a fibrillary network that is disrupted by Kapβ2. Molar ratio of Kapβ2:FUS=0.675. Bar, 0.1μm.
(C, D) Storage modulus (C) and loss modulus (D) of FUS hydrogels treated with buffer or Kapβ2. Molar ratio of Kapβ2:FUS=0.675. Values are means±SEM.
(E, F) Storage modulus (E) and loss modulus (F) of FUS hydrogels treated with buffer or Kapβ2^W460A:W730A. Molar ratio of Kapβ^W460A:W730A:FUS=0.415. Values are means±SEM.
(G) FUS hydrogels were treated with buffer, Kapβ2 or Kapβ2^W460A:W730A. Molar ratio of Kapβ/Kapβ^W460A:W730A:FUS=0.563.
(H) FUS^1-214 hydrogels were treated with Kapβ2. Molar ratio of Kapβ2:FUS^1-214=0.15.
(I) Macroscopic hydrogel formed by hnRNPA1 (3.1mM). Bar, 1mm.
(J) EM of solid-like hnRNPA1 gels treated with buffer reveals fibrillar network (left) that is disrupted by Kapβ2 (right). Molar ratio of Kapβ:hnRNPA1=0.13. Bar, 0.5μm.
(K, L) Storage modulus (K) and loss modulus (L) of hnRNPA1 gels treated with buffer, Kapβ2 or Kapβ2^W460A:W730A. Molar ratio of Kapβ2:hnRNPA1=0.13. Values are means±SEM.
(M) Solid-like hnRNPA1 gels were treated with Kapβ2. Note partial disassembly of hnRNPA1 hydrogel by Kapβ2 over time (indicated by the bracket). Molar ratio of Kapβ2:hnRNPA1=0.13.
(N, O) Storage modulus (N) and loss modulus (O) of hnRNPA1 gels treated with buffer or GFP. Molar ratio of GFP:hnRNPA1=0.27. Values are means±SEM.
(P, Q) Storage modulus (P) and loss modulus (Q) of hnRNPA1^D262V gels treated with buffer or Kapβ2. Molar ratio of Kapβ:hnRNPA1^D262V=0.76. Values are means±SEM.
(R, S) Storage modulus (R) and loss modulus (S) of hnRNPA1^{G274A:P288A:Y289A} gels treated with buffer or Kapβ2. Molar ratio of Kapβ:hnRNPA1^{G274A:P288A:Y289A}=0.13. Values are means±SEM.
See also .

Ricin challenge study. Mice immunized with lyophilized or liquid vaccine not exposed to high temperature storage had the highest survival rate during a ricin challenge. Vaccine formulations: No immunization (), liquid vaccine with no high temperature storage (), liquid vaccine with 3.5 weeks of high temperature storage at 40°C (), RiVax vaccine lyophilized with slow cooling in histidine buffer with high temperature storage for 4 weeks at 40°C (), RiVax vaccine lyophilized with slow cooling in ammonium acetate buffer with high temperature storage for 4 weeks at 40°C (), RiVax vaccine lyophilized with rapid cooling in histidine buffer with high temperature storage for 4 weeks at 40°C () and RiVax vaccine lyophilized with rapid cooling in ammonium acetate buffer with high temperature storage for 4 weeks at 40°C ().

The Φ cleavage mutant disrupts membranes less efficiently than wild-type virus. (A) ISVP-induced pore formation. T1L/T3D M2 or T1L/T3D M2 Y581A ISVPs at 2 × 10¹² particles/ml were incubated in virus storage buffer supplemented with CF-loaded EE liposomes for 20 min at the indicated temperatures. After 20 min, the reactions were diluted 1:50 into virus storage buffer. The samples were equilibrated to room temperature for 15 min prior to measurement of fluorescence. Levels of 0 and 100% CF leakage were determined by incubating an equivalent number of CF-loaded liposomes in virus storage buffer alone or virus storage buffer supplemented with 0.5% Triton X-100, respectively. Data are presented as means ± SDs. *, P ≤ 0.05 (n = 3 independent replicates). (B and C) Osmotic protection of ISVP-induced hemolysis. T1L/T3D M2 (B) or T1L/T3D M2 Y581A (C) ISVPs at 2 × 10¹² particles/ml were incubated in virus storage buffer supplemented with RBCs and the indicated PEG molecules for 1 h at 37°C. After 1 h, hemolysis was quantified by measuring the absorbance of the supernatant at 405 nm. Levels of 0 and 100% hemolysis were determined by incubating an equivalent number of RBCs in virus storage buffer alone or virus storage buffer supplemented with 0.8% Triton X-100, respectively. For each virus, relative hemolysis was normalized to the no-PEG control. Data are presented as means ± SDs (n = 3 independent replicates).