162,995 research outputs found
Nori: Japanese seaweed culture [5]
No full textPhoto shows a woman in Western dress (Yofuku) wearing cold mask in winter, handling Nori (dried edible seaweed) in a market in Shimogamo, Kyoto, Japanwoman in Western dress (Yofuku) wearing cold mask in winter Nori (dried seaweed) etc. in Market in Shimogamo Kyoto, Japan
Nori: Japanese seaweed culture [7]
No full textPhoto shows some Japanese people gathering nori (seaweed) on the beach at Chiba, JapanSeaweed Gatherers Chiba Japa
The tame Nori fundamental group
No full textWe introduce three notion of tameness of the Nori fundamental group scheme
for a normal quasiprojective variety over an algebraically closed field. It
is proved that these three notions agree if admits a smooth completion with
strict normal crossing divisor as the complement. We also prove a Lefschetz
type restriction theorem for the tame Nori fundamental group scheme for such an
.Comment: 12 page
[Report to Chief J. E. Curry, by an unknown author #1]
No full textReport to Chief J. E. Curry, by an unknown author. The report contains a list of officers who gave depositions to the United States Attorney
[Report to Chief J. E. Curry, by an unknown author #2]
No full textReport to Chief J. E. Curry, by an unknown author. The report contains a list of officers who gave depositions to the United States Attorney
Nori motives of curves with modulus and Laumon 1-motives
No full text30 pages. The main result is now valid over any number fieldInternational audienceLet be a number field. We describe the category of Laumon 1-isomotives over as the universal category in the sense of Nori associated with a quiver representation built out of smooth proper -curves with two disjoint effective divisors and a notion of H^1_\dR for such "curves with modulus". This result extends and relies on the theorem of J. Ayoub and L. Barbieri-Viale that describes Deligne's category of 1-isomotives in terms of Nori's Abelian category of motives
Fatty acyl-CoA-acyl-CoA-binding protein complexes activate the Ca2+ release channel of skeletal muscle sarcoplasmic reticulum
No full textWe previously reported that fatty acyl-CoA esters activate ryanodine receptor/Ca2+ release channels in a terminal cisternae fraction from rabbit skeletal muscle [Fulceri, Nori, Gamberucci, Volpe, Giunti and Benedetti (1994) Cell Calcium 15, 109-116]. Skeletal muscle cytosol contains a high-affinity fatty acyl-CoA-binding protein (ACBP) [Knudsen, Hojrup, Hansen, H.O., Hansen, H. F. and Roepstorff(1989) Biochem. J. 262, 513-519]. We show here that palmitoyl-CoA (PCoA) in a complex with a molar excess of bovine ACBP causes a discrete Ca2+ efflux or allows Ca2+ release from the Ca2+-preloaded terminal cisternae fraction by sub-optimal caffeine concentrations. Both effects were abolished by elevating the free [Mg2+] in the system, which inhibits the Ca2+ release channel activity. Sensitization towards caffeine was a function of both the concentration of the complex and the [PCoA]-to-[ACBP] ratio. In all experimental conditions the calculated free [PCoA] was no more than 50 nM, and such concentrations by themselves were inactive on Ca2+ release channels. The K-D for PCoA binding was approx. 2 nM for bovine and yeast ACBP, and slightly higher (8 nM) for rat ACBP. The PCoA-rat ACBP complex behaved in the same manner as the PCoA-bovine ACBP complex, whereas the ester complexed with yeast ACBP was more active in activating/sensitizing Ca2+ efflux. A non-hydrolysable analogue of PCoA bound to (bovine) ACBP also sensitized the Ca2+ release channel towards caffeine. These findings indicate that fatty acyl-CoA-ACBP complexes either interact directly with one or more components in the terminal cisternae membranes or, through interaction with the component(s), donate the fatty acyl-CoA esters to high-affinity binding sites of the membrane, thus affecting (and possibly regulating) Ca2+ release channel activity
ALGEBRAIC AND NORI FUNDAMENTAL GERBES
No full textIn this paper we extend the generalized algebraic fundamental group constructed in Esnault and Hogadi, (Trans. Amer. Math. Soc.364(5) (2012), 2429–2442) to general fibered categories using the language of gerbes. As an application we obtain a Tannakian interpretation for the Nori fundamental gerbe defined in Borne and Vistoli (J. Algebraic Geom.(2014), S1056–3911, 00638-X) for nonsmooth non-pseudo-proper algebraic stacks.</jats:p
Fatty acyl-CoA acyl-CoA-binding protein complexes activate the Ca2+ release channel of skeletal muscle sarcoplasmic reticulum
No full textWe previously reported that fatty acyl-CoA esters activate ryanodine receptor/Ca2+ release channels in a terminal cisternae fraction from rabbit skeletal muscle [Fulceri, Nori, Gamberucci, Volpe, Giunti and Benedetti (1994) Cell Calcium 15, 109-116]. Skeletal muscle cytosol contains a high-affinity fatty acyl-CoA-binding protein (ACBP) [Knudsen, Hojrup, Hansen, H.O., Hansen, H.F. and Roepstorff (1989) Biochem. J. 262, 513-519]. We show here that palmitoyl-CoA (PCoA) in a complex with a molar excess of bovine ACBP causes a discrete Ca2+ efflux or allows Ca2+ release from the Ca2+-preloaded terminal cisternae fraction by sub-optimal caffeine concentrations. Both effects were abolished by elevating the free [Mg2+] in the system, which inhibits the Ca2+ release channel activity. Sensitization towards caffeine was a function of both the concentration of the complex and the [PCoA]-to-[ACBP] ratio. In all experimental conditions the calculated free [PCoA] was no more than 50 nM, and such concentrations by themselves were inactive on Ca2+ release channels. The KD for PCoA binding was approx. 2 nM for bovine and yeast ACBP, and slightly higher (8 nM) for rat ACBP. The PCoA-rat ACBP complex behaved in the same manner as the PCoA-bovine ACBP complex, whereas the ester complexed with yeast ACBP was more active in activating/sensitizing Ca2+ efflux. A non-hydrolysable analogue of PCoA bound to (bovine) ACBP also sensitized the Ca2+ release channel towards caffeine. These findings indicate that fatty acyl-CoA-ACBP complexes either interact directly with one or more components in the terminal cisternae membranes or, through interaction with the component(s), donate the fatty acyl-CoA esters to high-affinity binding sites of the membrane, thus affecting (and possibly regulating) Ca2+ release channel activity
Targeting of calsequestrin to the sarcoplasmic reticulum of skeletal muscle following deletion of its carboxy-terminal acidic tail
No full textCalsequestrin (CS) is the Ca(2+) binding protein of the junctional sarcoplasmic reticulum (jSR) lumen. Recently, a chimeric CS-HA1, obtained by adding the nine-amino-acid viral epitope hemagglutinin (HA1) to the COOH terminus of CS, was shown to be correctly segregated to the sarcoplasmic reticulum [A. Nori, K. A. Nadalini, A. Martini, R. Rizzuto, A. Villa, and P. Volpe. Am. J. Physiol. 272 (Cell Physiol. 41): C1420-C1428, 1997]. A putative targeting mechanism of CS to jSR implies electrostatic interactions between negative charges on CS and positive charges on intraluminal domains of jSR integral proteins, such as triadin and junctin. To test this hypothesis, 2 deletion mutants of chimeric CS were engineered: CS-HA1DeltaGlu-Asp, in which the 14 acidic residues [-Glu-(Asp)(5)-Glu-(Asp)(7)-] of the COOH-terminal tail were removed, and CS-HA1Delta49(COOH), in which the last, mostly acidic, 49 residues of the COOH terminus were removed. Both mutant cDNAs were transiently transfected in HeLa cells, myoblasts of rat skeletal muscle primary cultures, or regenerating soleus muscle fibers of adult rats. The expression and intracellular localization of CS-HA1 mutants were studied by epifluorescence microscopy with use of antibodies against CS or HA1. CS-HA1 mutants were shown to be expressed, sorted, and correctly segregated to jSR. Thus short or long deletions of the COOH-terminal acidic tail do not influence the targeting mechanism of C
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