Synaptic contacts of association fibres in the brain of the bee

̈rmann, Freidrich-Wilhelm Schu

doi:10.1016/0006-8993(71)90552-x

Cited by 67 publications

(46 citation statements)

References 9 publications

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“…Recombinant thioredoxins f and m were purified as described in the literature (19) and kept frozen at Ϫ80°C in small aliquots. The concentration was determined spectrophotometrically using an extinction coefficient at 278 nm of 16,830 and 20,500 M Ϫ1 cm Ϫ1 for thioredoxins f and m, respectively (19).…”

Section: Thioredoxin Purificationmentioning

confidence: 99%

Activation of the Potato Tuber ADP-glucose Pyrophosphorylase by Thioredoxin

Ballícora¹,

Frueauf²,

Fu³

et al. 2000

Journal of Biological Chemistry

164

106

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The potato tuber (Solanum tuberosum L.) ADP-glucose pyrophosphorylase (ADP-GlcPPase) catalyzes the first committed step in starch biosynthesis. The main type of regulation of this enzyme is allosteric, and its activity is controlled by the ratio of activator, 3-phosphoglycerate to inhibitor, P i . It was reported (Fu, Y., Ballicora, M. A., Leykam, J. F., and Preiss, J. (1998) J. Biol. Chem. 273, 25045-25052) that the enzyme was activated by reduction of the Cys 12 disulfide linkage present in the catalytic subunits. In this study, both reduced thioredoxin f and m from spinach (Spinacia oleracea) leaves reduced and activated the enzyme at low concentrations (10 M) of activator (3-phosphoglycerate). Fifty percent activation was at 4.5 and 8.7 M for reduced thioredoxin f and m, respectively, and 2 orders of magnitude lower than for dithiothreitol. The activation was reversed by oxidized thioredoxin. Cys 12 is conserved in the ADP-GlcPPases from plant leaves and other tissues except for the monocot endosperm enzymes. We postulate that in photosynthetic tissues, reduction could play a role in the fine regulation of the ADP-GlcPPase mediated by the ferredoxin-thioredoxin system. This is the first time that a covalent mechanism of regulation is postulated in the synthesis of starch.

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Section: Thioredoxin Purificationmentioning

confidence: 99%

Activation of the Potato Tuber ADP-glucose Pyrophosphorylase by Thioredoxin

Ballícora¹,

Frueauf²,

Fu³

et al. 2000

Journal of Biological Chemistry

164

106

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show abstract

“…Trx regulates the activity of various enzymes through formation or reduction of a disulfide bridge in the enzyme molecule (25)(26)(27). In the last couple of years a number of studies have been attempted to elucidate the variety of target proteins of Trxs in plant cells, in chloroplasts, and in bacteria using two-dimensional gel electrophoresis analysis (28) or Trx-affinity chromatography with immobilized mutant Trx (6, 29 -31).…”

mentioning

confidence: 99%

Anti-oxidative Stress System in Cyanobacteria

Hosoya-Matsuda

Motohashi

Yoshimura

et al. 2005

Journal of Biological Chemistry

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“…Interestingly, Arhgef7 and Cdc42 interact to p21-activated kinase (Pak), which regulates cellular processes including rearrangement of the actinmyosin cytoskeleton, mitogen-activated protein kinase signaling pathway, and antiapoptotic pathway. 6,7 The Arhgef7, known as Pak-interacting exchange factor beta, binds tightly to the conserved prolinerich Pak sequence. Thereafter, the interaction Cdc42 to Pak at the regulatory N-terminal induces a conformational change.…”

mentioning

confidence: 99%

“…It opens the Pak kinase domain and leads to autophosphorylation, and then exogenous substrate such as proapoptotic protein Bad is activated by phosphorylated Pak. 7 Pak-mediated phosphorylation of Bad blocks cell death. 7 Datta et al 8 demonstrated that activated Akt (a serine-threonine kinase) phosphorylates Bad and promotes cell survival.…”

mentioning

confidence: 99%