[Objective]To discuss the clinical experiences and unique views of Professor XIA Guicheng, a master of Chinese medicine in treating adenomyosis dysmenorrhea. [Method] To analyze the understanding of professor XIA Guicheng about the pathogenesis of adenomyosis dysmenorrhea. To sum up the clinical experiences in treating adenomyosis dysmenorrhea according to the kidney to adjust the cycle. [Result]For adenomyosis dysmenorrhea, XIA believes that the pathogenesis of this disease is the key virtual reality. The virtual refers to the deficiency of kidney-yang which is the root of its occurrence.The subject refers to the blood stasis which is its pathological basis. The deficiency of kidney-yang losses of warm effect, leading to stagnation of Qi and blood stasis for dysmenorrhea. According to the principle ofJi ze zhi biao,huan ze zhi ben, when the dysmenorrhea attacks severely, we should control the pain from the standard treatment, mainly including relieving spasm and pain ,warming Yang wet and tranquilizing mind. We ought to value the root cause in normal time, that is the kidney to adjust the cycle. In particular, we pay attention to the inter ovulation period of warming kidney to help Yang, and the patient's daily life, emotional diet. [Conclusion] Professor XIA Guicheng 's experience in treating adenomyosis dysmenorrhea is worth to spread.

Objectives To explore the route of ESBL producing bacteria in neonatal faeces, and to investigate the gene and drug resistance of ESBL producing bacteria in intestinal tract of neonates. Methods Fecal samples of healthy newborns and their mothers were collected, and bacterial cultures were carried out using selective ESBL medium. The positive strains were identified by Time-of-flight mass spectrometry. ESBL genotyping and resistance gene detection were performed by whole genome sequencing technique. Results In 146 neonatal fecal specimens, the positive rate of ESBL producing bacteria was 8.90％,and the positive rate in the first time stool was 3.23％. Seventy-two hours after birth, the positive rate of fecal ESBL producing bacteria was 13.10％. Among the 13 ESBL producing strains, there were 9 strains of CTX type, 3 strains of TEM type and 1 strain of SHV type. Nine strains of CTX include five types such as CTX-M-24, CTX-M-18, CTX-M-27, CTX-M-42 and CTX-M-15. The positive rate of ESBL producing bacteria was 21.6％ in 167 mothers' fecal specimens. The ESBL genotype included 24 strains of CTX type, 6 strains of TEM type, 4 strains of SHV type and 2 strains of QnrS type. Twenty-four strains of CTX include CTX-M-24, CTX-M-14, CTX-M-18, CTX-M-27, CTX-M-42 and CTX-M-15. There were 2 or 3 ESBL genotypes in 12 maternal and neonatal specimens. It was detected to have 6 types of resistance gene such as aadA5, strA, strB, sul1, sul2 and dfrA17 in 49 strains of ESBL producing bacteria in maternal and neonatal strains. Resistance genes were exactly the same in the neonates as in mothers who were detected to have ESBL producing bacteria. A variety of resistance genes were detected in feces in 7 neonates and 23 mothers. Conclusions The neonates in hospital may be detected to have ESBL produing bacteria in the intestinal tract at the same time as their mothers or separately. However, there are many ways for neonates to have ESBL producing bacteria in intestinal tract. There are many genotypes and resistance genes of ESBL producing bacteria.

GPCR proteins represent the largest family of signaling membrane proteins in eukaryotic cells. Their importance to basic cell biology, human diseases, and pharmaceutical interventions is well established. Many crystal structures of GPCR proteins have been reported in both active and inactive conformations. These data indicate that agonist binding alone is not sufficient to trigger the conformational change of GPCRs necessary for binding of downstream G-proteins, yet other essential factors remain elusive. Based on analysis of available GPCR crystal structures, we identified a potential conformational switch around the conserved Asp2.50, which consistently shows distinct conformations between inactive and active states. Combining the structural information with the current literature, we propose an energy-coupling mechanism, in which the interaction between a charge change of the GPCR protein and the membrane potential of the living cell plays a key role for GPCR activation.
Binding Sites ; GTP-Binding Proteins ; chemistry ; genetics ; metabolism ; Humans ; Hydrogen Bonding ; Membrane Potentials ; Models, Molecular ; Protein Conformation ; Receptors, G-Protein-Coupled ; chemistry ; genetics ; metabolism ; Signal Transduction