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Resort stage in rehabilitation of patients with chronic nonspecific salpingoophoritis

, : Resort stage in rehabilitation of patients with chronic nonspecific salpingoophoritis. Uspekhi Fiziologicheskikh Nauk 25(3): 33

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Michailov, Galin, V.; Sereda, Michael, W.; Brinkmann, Bastian, G.; Fischer, Tobias, M.; Haug, Bernhard; Birchmeier, Carmen; Role, Lorna; Lai, Cary; Schwab, Markus, H.; Nave, Klaus-Armin, 2004: Axonal neuregulin-1 regulates myelin sheath thickness. In the nervous system of vertebrates, myelination is essential for rapid and accurate impulse conduction. Myelin thickness depends on axon fiber size. We use mutant and transgenic mouse lines to show that axonal Neuregulin-1 (Nrg1) signals informa...

LiYanQin; YanHong; BaiBin, 2008: Change in iron transporter expression in human term placenta with different maternal iron status. Objectives: To better understand the molecular mechanism of human placental iron transfer, the protein and mRNA expression of iron transporters, transferrin receptor 1 (TfR1), ferritin and ferroportin 1 (FP1) were examined simultaneously. Study de...

Kudryashova, N. I.; Novikova, N. A., 1984: Drugs in the series of beta phenylisopropylamine derivatives 8. correlation between the pharmacological effect and structure in the series of beta phenylisopropylamine derivatives. The correlation between the chemical structure and neurotropic activity was studied in the series of N-substituted .beta.-phenylisopropylamine derivatives with the general formula C6H5CH2CH(CH3)NHX. Their toxicity, effect on the soporific action o...

Terawaki, Shin-Ichi; Maesaki, Ryoko; Okada, Kengo; Hakoshima, Toshio, 2003: Crystallographic characterization of the radixin FERM domain bound to the C-terminal region of the human Na+/H+-exchanger regulatory factor (NHERF). Radixin is a member of the ERM proteins, which cross-link plasma membranes and actin filaments. The N-terminal FERM domains of ERM proteins interact with Na+/H+-exchanger regulatory factors (NHERFs), which are PDZ-containing adaptor proteins, to m...

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