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Herein, we demonstrate that a flexible, air-permeable, thermoelectric (TE) power generator can be prepared by applying a TE polymer (e.g. poly(3,4-ethylenedioxythiophene):poly(4-styrenesulfonate)) coated commercial fabric and subsequently by linking the coated strips with a conductive connection (e.g. using fine metal wires). The poly(3,4-ethylenedioxythiophene):poly(4-styrenesulfonate) coated fabric shows very stable TE properties from 300 K to 390 K. The fabric device can generate a TE voltage output (V) of 4.3 mV at a temperature difference (ΔT) of 75.2 K. The potential for using fabric TE devices to harvest body temperature energy has been discussed. Fabric-based TE devices may be useful for the development of new power generating clothing and self-powered wearable electronics.

Bi2Te3 based alloy nanosheet (NS)/poly(3,4-ethylenedioxythiophene):poly(4-styrenesulfonate) (PEDOT:PSS) composite films were prepared separately by spin coating and drop casting techniques. The drop cast composite film containing 4.10 wt % Bi2Te3 based alloy NSs showed electrical conductivity as high as 1295.21 S/cm, which is higher than that (753.8 S/cm) of a dimethyl sulfoxide doped PEDOT:PSS film prepared under the same condition and that (850-1250 S/cm) of the Bi2Te3 based alloy bulk material. The composite film also showed a very high power factor value, ∼32.26 μWm(-1) K(-2). With the content of Bi2Te3 based alloy NSs increasing from 0 to 4.10 wt %, the electrical conductivity and Seebeck coefficient of the composite films increase simultaneously.

Ipomoeassin F is a potent natural cytotoxin that inhibits growth of many tumor cell lines with single-digit nanomolar potency. However, its biological and pharmacological properties have remained largely unexplored. Building upon our earlier achievements in total synthesis and medicinal chemistry, we used chemical proteomics to identify Sec61α (protein transport protein Sec61 subunit alpha isoform 1), the pore-forming subunit of the Sec61 protein translocon, as a direct binding partner of ipomoeassin F in living cells. The interaction is specific and strong enough to survive lysis conditions, enabling a biotin analogue of ipomoeassin F to pull down Sec61α from live cells, yet it is also reversible, as judged by several experiments including fluorescent streptavidin staining, delayed competition in affinity pulldown, and inhibition of TNF biogenesis after washout. Sec61α forms the central subunit of the ER protein translocation complex, and the binding of ipomoeassin F results in a substantial, yet selective, inhibition of protein translocation in vitro and a broad ranging inhibition of protein secretion in live cells. Lastly, the unique resistance profile demonstrated by specific amino acid single-point mutations in Sec61α provides compelling evidence that Sec61α is the primary molecular target of ipomoeassin F and strongly suggests that the binding of this natural product to Sec61α is distinctive. Therefore, ipomoeassin F represents the first plant-derived, carbohydrate-based member of a novel structural class that offers new opportunities to explore Sec61α function and to further investigate its potential as a therapeutic target for drug discovery.

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Increased amounts of reactive oxygen species (ROS) induce apoptosis in mammalian cells. PUMA (P53 up-regulated modulator of apoptosis), a mitochondrial proapoptotic BH3-only protein, induces rapid apoptosis through a Bax-and mitochondria-dependent pathway. However, the molecular basis of PUMA-induced apoptosis is largely not understood. Using a combination of biophysical and biochemical methods and PUMA-inducible colorectal cells, DLD-1.PUMA, we showed that (a) PUMA-induced apoptosis is dose and time dependent; (b) PUMA-induced apoptosis is directly associated with ROS generation; (c) diphenyleneiodonium chloride, a ROS blocker, or BAX-inhibiting peptide, a suppressor of BAX translocation, decreased ROS generation and apoptosis in DLD-1.PUMA cells; (d) overexpression of PUMA induced up-regulation (>1.34-fold) of peroxiredoxin 1 and down-regulation (by 25%) of stathmin through proteasome-mediated degradation; and (e) hydrogen peroxide down-regulated stathmin and disrupted the cellular microtubule network. Our findings indicate that PUMA induces apoptosis, in part, through the BAX-dependent generation of superoxide and hydrogen peroxide. ROS overproduction and oxidative stress induce proteome-wise alterations, such as stathmin degradation and disorganization of the cell microtubule network, in apoptotic cells. (Cancer Res 2005; 65(5): 1647-54)

A temperature-conditional, photosynthesis-deficient mutant of the green alga Chlamydomonas reinhardtii, previously recovered by genetic screening, results from a leucine 290 to phenylalanine (L290F) substitution in the chloroplast-encoded large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco, EC 4.1.1.39). Rubisco purified from mutant cells grown at 25°C has a reduction in CO 2 /O 2 specificity and is inactivated at lower temperatures than those that inactivate the wild-type enzyme. Second-site alanine 222 to threonine (A222T) or valine 262 to leucine (V262L) substitutions were previously isolated via genetic selection for photosynthetic ability at the 35°C restrictive temperature. These intragenic suppressors improve the CO 2 /O 2 specificity and thermal stability of L290F Rubisco in vivo and in vitro. In the present study, directed mutagenesis and chloroplast transformation were used to create the A222T and V262L substitutions in an otherwise wild-type enzyme. Although neither substitution improves the CO 2 /O 2 specificity above the wild-type value, both improve the thermal stability of wild-type Rubisco in vitro. Based on the x-ray crystal structure of spinach Rubisco, large subunit residues 222, 262, and 290 are far from the active site. They surround a loop of residues in the nuclear-encoded small subunit. Interactions at this subunit interface may substantially contribute to the thermal stability of the Rubisco holoenzyme.Genetic screening for conditional lethal mutants identifies only those relatively few amino acid substitutions that are critical for protein structure or function (reviewed in Refs. 1 and 2). One such mutant of the green alga Chlamydomonas reinhardtii results from an L290F substitution in the chloroplast-encoded large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco, 1 EC 4.1.1.39) (3, 4). This mutant contains enough Rubisco holoenzyme at 25°C to grow photoautotrophically but lacks holoenzyme and requires acetate for growth at the 35°C restrictive temperature (3). Because the mutant enzyme subunits are synthesized and assembled into holoenzyme at apparently normal rates (4), the reduced level of Rubisco must result from increased degradation of an unstable holoenzyme in vivo (4 -6). Rubisco purified from mutant cells grown at 25°C has decreases in catalytic efficiency, CO 2 /O 2 specificity, and holoenzyme thermal stability (4 -6) despite the fact that residue 290 resides at the bottom of the ␣/␤-barrel active-site domain, relatively far from the active-site residues (7). In an attempt to understand the nature of this distant effect, photosynthesis-competent revertants were selected from the L290F mutant strain at 35°C (5, 8). Either an A222T or V262L large subunit substitution was found to complement the original mutant substitution (8). Comparison of enzymes purified from cells grown at 25°C revealed that the A222T and V262L substitutions increased the CO 2 /O 2 specificity of the L290F enzyme back to the wild-type level (8). Residues 222 and 262 ...