2,158 research outputs found
Designation of a Neotype for Kamimuria tibialis (Pictet, 1841), and K. uenoi Kohno, 1947, spec. propr., stat. n. (Plecoptera, Perlidae)
No full textKamimuria tibialis (Pictet, 1841) in the current sense includes two species, which agree with two forms distinguished by Kohno (1947). A neotype of Kamimuria tibialis is designated for stability of nomenclature and the other one of Kohno's forms is elevated to the rank of a species, K. uenoi Kohno, 1947, stat. n [K. t. uenoi]. The penes of the two species are described and the males, females, nymphs and eggs are redescribed
Alteration of Transcriptional Activity of the mouse Estrogen Receptor by N-terminal deletions and C-terminal point mutations
No full textHigh second-order optical nonlinearities in thermally poled sol-gel silica
No full textSilica glass samples prepared by a sol-gel process, the mixture of silica sol for gelation and colloidal silica particles, have been thermally poled in vacuum by continuous high voltage (8-12 kV) at elevated temperature (280°C). High second-order nonlinearities (>1pm/V), located under the anodic surface, have been measured and the values are higher than those obtained in fixed silica glass, poled under the same conditions. A model for thermal poling is suggested which explains the experimental results in sol-gel silica and the difference between thermal poling of sol-gel and fused silica. The granular structure and the boundaries of sol-gel silica seem to play a major role in establishing the electrical properties of the depletion layer during and after poling
p73 independent of c-Myc represses transcription of platelet-derived growth factor beta-receptor through interaction with NF-Y
No full textWe recently reported that c-Myc represses the transcription of platelet-derived growth factor (PDGF) beta-receptor (Izumi, H., Molander, C., Penn, L. Z., Ishisaki, A., Kohno, K., and Funa, K. (2001) J. Cell Sci. 114, 1533-1544). We demonstrate here that the p53 family protein p73alpha represses PDGF beta-receptor transcription essentially by the same mechanism. p73alpha but not p73beta or p53 represses the transcription in concordance with its ability to bind NF-YC and NF-YB. None of other p73 isoforms (i.e. p73beta, p73gamma, p73epsilon), C-terminal deletion mutants of p73alpha, and p53 is able to bind NF-Y with the exception of p63alpha. This finding suggests that the sterile alpha-motif domain present only in p73alpha and p63alpha is the interaction site. For the repression, the N-terminal transactivation domain of p73alpha is also indispensable, arguing for the importance of the activity of p73alpha in the mechanism. p73alpha binds the C-terminal HAP domain of NF-YC previously found to be the interaction site with c-Myc and TBP. Because c-Myc induces and activates p73alpha (Zaika, A., Irwin, M., Sansome, C., and Moll, U. M. (2001) J. Biol. Chem. 276, 11310-11316) and they bind each other (Uramoto, H., Izumi, H., Ise, T., Tada, M., Uchiumi, T., Kuwano, M., Yasumoto, K., Funa, K., and Kohno, K. (2002) J. Biol. Chem. 277, in press), we examined whether the repression by p73 is dependent on c-Myc. However, Myc-null rat fibroblasts are also susceptible to p73alpha-induced repression. Serum stimulation of NIH3T3 cells gradually decreased the amount of endogenous NF-Y binding to the PDGF beta-receptor promoter, whereas NF-YA expression in the nuclear extracts remains unchanged. Our results indicate that serum stimulation induces c-Myc and p73alpha, leading to the down-regulation of PDGF beta-receptor expression by repressing its transcription
Recommended from our members
Comment on “Theory of Current-Driven Domain Wall Motion: Spin Transfer versus Momentum Transfer”
No full textA Comment on the Letter by Gen Tatara and Hiroshi Kohno, Phys. Rev. Lett. 92 086601 (2004). The authors of the Letter offer a Reply.</p
Design of the Grand Roof at Tokyo Station
No full textp. 1242-1253This paper describes the design method of long and unique shape membrane structure in
capital Tokyo. The membrane structure, designed to create an impression of Japan's
traditional Washi paper, forms gentle curves of varying size and inclination, to become the
new face of the Yaesu side of the Tokyo Station. To achieve such a light membrane
structure in Japan where many natural disasters such as earthquakes and typhoons occur frequently, we adopted some ideas in order to solve technical problems.Sadamoto, M.; Yoshie, K.; Kohno, T.; Muraoka, T.; Takanashi, M. (2010). Design of the Grand Roof at Tokyo Station. Editorial Universitat Politècnica de València. https://riunet.upv.es/handle/10251/706
On rational K[pi,1] spaces and Koszul algebras
No full textthis paper were first studied in the arrangement setting in [2, 20, 21, 22, 14, 13]. Falk [13] studied conditions for X to be a rational K[ß; 1]. He proved that X is a rational K[ß; 1] for every arrangement of so called fiber-type. This is a topologically defined class that coincides with the combinatorially defined class of supersolvable arrangements (see [25] for definitions). Falk [13] and Kohno [22] proved Corollary 5.3 for complements of hyperplane arrangements. It is still unknown if X can be a rational K[ß; 1] for a not supersolvable arrangement or if the LCS formula can hold without X being a rationa
Inhibition of the mitochondria-shaping protein Opa1 restores sensitivity to Gefitinib in a lung adenocarcinomaresistant cell line
No full textDrug resistance limits the efficacy of chemotherapy and targeted cancer treatments, calling for the identification of druggable targets to overcome it. Here we show that the mitochondria-shaping protein Opa1 participates in resistance against the tyrosine kinase inhibitor gefitinib in a lung adenocarcinoma cell line. Respiratory profiling revealed that oxidative metabolism was increased in this gefitinib-resistant lung cancer cell line. Accordingly, resistant cells depended on mitochondrial ATP generation, and their mitochondria were elongated with narrower cristae. In the resistant cells, levels of Opa1 were increased and its genetic or pharmacological inhibition reverted the mitochondrial morphology changes and sensitized them to gefitinib-induced cytochrome c release and apoptosis. In vivo, the size of gefitinib-resistant lung orthotopic tumors was reduced when gefitinib was combined with the specific Opa1 inhibitor MYLS22. The combo gefitinib-MYLS22 treatment increased tumor apoptosis and reduced its proliferation. Thus, the mitochondrial protein Opa1 participates in gefitinib resistance and can be targeted to overcome it
Mutational analysis of the estrogen receptor ligand-binding domain: Influence of ligand structure and stereochemistry on transactivation
No full textThe mouse estrogen receptor (mER) exhibits ligand stereochemical specificity for indenestrol A (IA), a stilbestrol estrogen. IA has a chiral C3 methyl group, and the mER preferentially binds the S-enantiomer (IA-S). resulting in elevated biological activity when compared with the IA-R enantiomer. To elucidate the mechanisms for this stereochemical recognition, we have constructed a series of mERs with individual amino acid substitutions at Met521, His528, Met532, and Val537. The abilities of yeast-expressed wild-type and mutant mERs to transactivate an estrogen-responsive reporter gene construct were measured in the presence of diethylstilbestrol (DES) and IA enantiomers. The concentration of IA-S required to induce half-maximal transactivation by wild-type mER was 10-fold lower than IA-R, which is attributed to the 15-fold greater binding affinity for IA-S. Wild-type mER displayed similar dose-response curves for IA-R and demethyl IA, which lacks a C3 methyl group, demonstrating that the presence and correct orientation of the C3 methyl group on the IA compound is required for high-affinity ligand binding and transcriptional activity. Each mutant exhibited a reduced preference for IA-S enantiomer with respect to transactivation, suggesting that this region of the mER functions in ligand stereochemical recognition and activation. A mutation at Met532 diminished DES- and IA-S-induced transactivation by 7.5-fold and 40-fold respectively, with minimal change on their binding affinity. These data suggest that Met532 is required for transactivation induced by the potent agonist, IA-S, and the M532G mutation effectively uncouples IA-S ligand binding from transactivation. Use of these stereochemically different ligands in combination with mutagenesis of the mER demonstrates that ligand structure could influence transactivation by specifically altering the conformation of the mER AF-2 region
- …
