Disease relevance of Rhus

• Only paraffin wax in cetyl alcohol statistically (p<0.01) reduced Rhus allergic contact dermatitis [1].
• Robustaflavone, a naturally occurring biflavanoid isolated from Rhus succedanea, was found to be a potent inhibitor of hepatitis B virus (HBV) replication in 2.2.15 cells, with an effective concentration (EC50) of 0.25 microM, and a selectivity index (SI, IC50/EC90) of 153 [2].

High impact information on Rhus

• The magnetic susceptibility of Rhus vernicifera laccase has been remeasured over the temperature range 5-260 K [3].
• Interaction of Rhus laccase with dioxygen and its reduction intermediates [4].
• With Rhus laccase, the new signal is shown to originate from one of the copper ions that are nondetectable in the resting enzyme, and evidence is presented for the signals in Polyporus laccase and cytochrome c oxidase also stemming from the metal pairs that are antiferromagnetically coupled in the oxidized enzymes [5].
• The type 1 site of a plant laccase (Rhus vernicifera) is reduced moderately slowly by both Fe(II) and a bulky organic substrate, 1,4-hydroquinone (with 6 equiv of substrate, k(obs) = 0.029 and 0.013 s(-)(1), respectively) [6].
• The effect of pH on Cu(I) and Cu(II) forms of the isolated soluble domain of the stellacyanin from Rhus vernicifera (SCu), the Japanese lacquer tree, has been studied by electronic and NMR spectroscopy and using direct electrochemical measurements [7].

Biological context of Rhus

• Kinetics of the reduction of Rhus vernicifera laccase by ferrocyanide ion [8].
• Current enzyme studies on the biosynthesis of gallotannins with cell-free extracts from leaves of staghorn sumac (Rhus typhina L.) revealed the existence of two new beta-glucogallin-dependent galloyltransferases (EC 2.3.1.-) that preferentially catalyzed the acylation of hexa- and heptagalloylglucoses [9].
• In this study, we prepared a flavonoid-containing fraction from a crude acetone extract of Rhus verniciflua Stokes (RVS), traditionally used as a food additive and as an herbal medicine, and named RVS chloroform-methanol fraction (RCMF) [10].
• 36 kDa glycoprotein isolated from Rhus verniciflua Stokes fruit has a protective activity to glucose/glucose oxidase-induced apoptosis in NIH/3T3 cells [11].
• 36 kDa glycoprotein isolated from Rhus verniciflua stokes inhibits G/GO-induced mitochondrial apoptotic signal pathways in BNL CL.2 cells [12].

Anatomical context of Rhus

• The present study was carried out to investigate the antioxidative and antiapoptotic activities of 36 kDa RVS glycoprotein isolated from Rhus verniciflua Stokes fruits (RVS) in NIH/3T3 cells in vitro [11].

Associations of Rhus with chemical compounds

• Spectroscopic and kinetic studies on the oxygen-centered radical formed during the four-electron reduction process of dioxygen by Rhus vernicifera laccase [13].
• Fluoride effects on the activity of Rhus laccase and the catalytic mechanism under steady-state conditions [14].
• Stability of Japanese-lacquer-tree (Rhus vernicifera) laccase to thermal and chemical denaturation: comparison with ascorbate oxidase [15].
• Anaerobic reactions of Rhus vernicifera laccase and its type-2 copper-depleted derivatives with hexacyanoferrate(II) [16].
• Stellacyanin from Rhus vernificera is a blue copper protein in which the metal is coordinated to a Cys, two His, and a Gln residue [17].

Gene context of Rhus

• Electron spin-echo decay envelopes for types I and II copper of Rhus vernicifera laccase and for type II copper of procine ceruloplasmin have been studied [18].
• Gallotannin biosynthesis: two new galloyltransferases from Rhus typhina leaves preferentially acylating hexa- and heptagalloylglucoses [9].
• Stereochemistry of anion complexes of type 2 Cu(II) in Rhus vernicifera laccase. Analogy with superoxide dismutase and Cu(II) carbonic anhydrase [19].
• Room temperature ESR spectra of Rhus vernicifera laccase and derivatives [20].
• Nitrite reactivity of the binuclear copper site in T2D Rhus laccase: preparation of half met-NO2- T2D laccase and its correlation to half met-NO2- hemocyanin and tyrosinase [21].

Analytical, diagnostic and therapeutic context of Rhus

• Titrations with ferrocyanide of japanese-lacquer-tree (Rhus vernicifera) laccase and of the type 2 copper-depleted enzyme. Interrelation of the copper sites [22].
• The thermal denaturation of laccase from the Japanese lacquer tree (Rhus vernicifera) was studied by differential scanning calorimetry [15].
• A circular dichroism study of the reactions of Rhus laccase with dioxygen [23].
• The oxygen biosensor consisted of the Rhus vernicifera laccase and ascorbate as substrate enclosed in pouches of low-density polyethylene under nitrogen gas [24].
• Glycoprotein of Rhus verniciflua Stokes (RVS glycoprotein) was isolated and identified using SDS-PAGE [25].

References