The Thought Remolding Campaign of the Chinese Communist Party-state

In its comprehensive analysis of a wide range of primary and secondary sources in both Chinese and Western languages, this authoritative work stands as the definitive study of the theory, implementation and legacy of the Chinese Communist Party's thought-remolding campaign. This decades-long campaign involved the extraction of confessions from millions of Chinese citizens suspected of heterodoxy or disobedience to party dictates, along with their subjection to various forms of "re-education" and indoctrination. Hu Ping's carefully structured overview provides a valuable insider's perspective, and supersedes the previous landmark study on this vastly interesting topic.Deze studie gaat in op de theorie, uitvoering en nalatenschap van de propagandacampagne van de Chinese Communistische Partij. Deze decennialange campagne bestond onder andere uit het ondervragen van miljoenen burgers die verdacht werden van andersdenkendheid of ongehoorzaamheid. Deze zorgvuldig gestructureerde verhandeling overstijgt de klassieke studie Thought Reform and the Psychology of Totalism (1969) van Robert jay Lifton. In tegenstelling tot het werk van Lifton, hanteert Hu Pings studie een eigentijds postcommunistisch perspectief en is het verrijkt met ervaringen van Chinezen die direct gevolgen hebben ondervonden van de maoïstische propagandacampagne

Antibacterial Activities and Mechanism of Action of Acetone Extracts from Rabdosia rubescens

The antibacterial activities and mechanism of action of acetone extracts from R. rubescens were reported in this paper. The results showed that 80% acetone extracts had both the highest contents of total phenolics and flavonoids. Acetone extracts showed better antibacterial activities against Gram-positive bacterial strains and there were no inhibitory effects found on tested Gram-negative bacteria. In addition, 80% acetone extracts from R. rubescens had relatively higher antibacterial activities with the lowest values of MIC and MBC at 2.5 mg/mL and 5 mg/mL against B. subtilis. The antibacterial mechanism of 80% acetone extracts against Bacillus subtilis might be described as disrupting cell wall, increasing cell membrane permeability, and finally leading to the leakage of cell constituent

Transmembrane Signaling and Conformational Regulation of Integrin

Integrins are heterodimeric cell adhesion molecules that play an essential role in hemostasis, thrombosis, cell migration, and can transmit bidirectional signals. The inside-out activating signal triggers integrin conformational change, leading to high affinity for extracellular ligands. Binding of extracellular matrix ligands to integrins results in outside-in signaling that leads to formation of focal adhesion (FA) complex at the integrin cytoplasmic tails and activation of downstream signal pathways. Transmembrane/cytoplasmic domains are hypothesized to associate in resting integrins, whereas ligand binding and intracellular activating signals induce transmembrane domain separation. However, how this conformational change affects integrin outside-in signaling and whether the á subunit cytoplasmic domain is important for this signaling remain elusive. Using Chinese Hamster Ovary (CHO) cells that stably expressed different integrin áIIbâ3 constructs, we discovered that an áIIb cytoplasmic domain truncation led to integrin activation but not defective outside-in signaling. In addition, preventing transmembrane domain separation abolished both inside-out and outside-in signaling. Our research revealed that transmembrane domain separation is a downstream conformational change after the cytoplasmic domain dissociation in inside-out activation and indispensable for ligand-induced outside-in signaling. It has been proposed that integrins adopt a bent, low affinity conformation under physiological conditions and can switch to an extended conformation through a “switchblade”-like conformational change. It is extremely important to verify if the model universally applies to all integrin families. Due to the highly divergent cytoplasmic domain, â8 integrin is unlikely to adopt a general mechanism for affinity regulation. Therefore the â8 integrin may uniquely assume an extended, high affinity conformation under physiological conditions. We discovered that â8 indeed showed high binding to vitronectin under physiological conditions. Further studies identified that the I-EGF domains on the â8 integrin extracellular lower leg are critical for this high affinity conformation. We also pinpointed a critical role of the â8 integrin EGF domain 1 and 2 in this high affinity conformation. Mutating either one of the cysteine pair at the â3 EGF1 domain C-terminus resulted in high affinity conformation, probably due to disruption of the EGF1-EGF2 interface. Our study also showed that the â8 ectodomain lower stalk does not negatively affect outside-in signaling