Ex-ante assessment of demand for improved forage seed and planting materials among Ethiopian smallholder farmers: A contingent valuation analysis

United States Agency for International Developmen

Ex-ante assessment of demand for improved forage seed and planting materials among smallholder farmers in Ethiopia: A contingent valuation analysis

United States Agency for International Developmen

Ex-ante assessment of potential market demands and commercial viabilities for private forage seeds production in Ethiopia

United States Agency for International Developmen

Value chains, markets and economics: Africa RISING Science, Innovations and Technologies with Scaling Potential from the Ethiopian Highlands

United States Agency for International Developmen

Uniform cross phase modulation for nonclassical radiation pulses

We propose a scheme to achieve a uniform cross phase modulation (XPM) for two nonclassical light pulses and study its application for quantum non-demolition measurements of the photon number in a pulse and for controlled phase gates in quantum information. We analyze the scheme by quantizing a common phenomenological model for classical XPM. Our analysis first treats the ideal case of equal cross-phase modulation and pure unitary dynamics. This establishes the groundwork for more complicated studies of non-unitary dynamics and difference in phase shifts between the two pulses where decohering effects severely affect the performance of the scheme.Comment: 11 pages, 4 figures. To appear in J. Opt. Soc. Am.

Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facilitates folding of kinase and non-kinase clients

The tumor suppressors Tsc1 and Tsc2 form the tuberous sclerosis complex (TSC), a regulator of mTOR activity. Tsc1 stabilizes Tsc2; however, the precise mechanism involved remains elusive. The molecular chaperone heat-shock protein 90 (Hsp90) is an essen- tial component of the cellular homeostatic machinery in eukary- otes. Here, we show that Tsc1 is a new co-chaperone for Hsp90 that inhibits its ATPase activity. The C-terminal domain of Tsc1 (998–1,164 aa) forms a homodimer and binds to both protomers of the Hsp90 middle domain. This ensures inhibition of both subunits of the Hsp90 dimer and prevents the activating co- chaperone Aha1 from binding the middle domain of Hsp90. Conversely, phosphorylation of Aha1-Y223 increases its affinity for Hsp90 and displaces Tsc1, thereby providing a mechanism for equilibrium between binding of these two co-chaperones to Hsp90. Our findings establish an active role for Tsc1 as a facilita- tor of Hsp90-mediated folding of kinase and non-kinase clients— including Tsc2—thereby preventing their ubiquitination and proteasomal degradation