Univariate GLM with <i>Bd</i> infection as the dependent variable to assess the effect of the 6 variables collected on the <i>Bd</i> infection status.

<p>Temp. (3 mo) and Rain (3 mo) denote temperature and precipitation for three months prior to sampling.</p

Contingency table for occurrences of <i>Dryophytes suweonensis</i> and <i>Lithobates catesbeianus</i> throughout the range of <i>D</i>. <i>suweonensis</i>.

<p>The expected counts are the value expected if there were no relationship between the occurrence of <i>D</i>. <i>suweonensis</i> and <i>L</i>. <i>catesbeianus</i>.</p

Summary map of sites sampled for both parts of this study.

<p>Description of the range of <i>Dryophytes suweonensis</i>, sites where the species was detected, sites where <i>Lithobates catesbeianus</i> was detected and sites where sampling for <i>Bd</i> sampling was conducted. This map was generated with ArcMap 9.3 (Environmental Systems Resource Institute, Redlands, California, USA; <a href="http://www.esri.com/" target="_blank">http://www.esri.com/</a>).</p

Sampling sites and occurrences of frogs for the <i>Bd</i> surveys.

<p>Sampling for <i>Bd</i> infection was conducted at 37 sites throughout the range of <i>Dryophytes suweonensis</i> in Republic of Korea. The unit used for “Bullfrog” is the binary encoded prevalence, and the number of individuals for “<i>Ds</i>” and “<i>Dj</i>”.</p

Treatment with the root extracts reduces expression of pro-inflammatory factors and raises PGDlevels

<p><b>Copyright information:</b></p><p>Taken from "Reduction of urate crystal-induced inflammation by root extracts from traditional oriental medicinal plants: elevation of prostaglandin Dlevels"</p><p>http://arthritis-research.com/content/9/4/R64</p><p>Arthritis Research & Therapy 2007;9(4):R64-R64.</p><p>Published online 5 Jul 2007</p><p>PMCID:PMC2206389.</p><p></p> and represent the averages of two experiments with four mice in each group, show the results from a separate experiment with seven mice per group, and shows the results from an experiment with five mice per group. The effect of the root extracts on the leukocyte density in the exudate was nearly identical in both experiments. (a) Pouch membrane IL-6 mRNA. Real-time RT-PCR, normalized to GAPDH, as outlined in the Methods and Materials section. The control group was assigned the relative expression level of 1. The numerical values (± standard error of the mean) were as follows: MSU, 55.47 ± 2.68; and MSU + extracts, 0.56 ± 0.12. (b) Pouch membrane TNF-α mRNA. Analysis was identical to (a): Ctrl, 1; MSU, 20.43 ± 2.91; and MSU + extracts, 0.81 ± 0.09. (c) IL-6 protein levels in the pouch exudate (ELISA, pg/ml): Ctrl, 44.75 ± 1.34; MSU, 391.54 ± 16.77; and MSU + extracts, 217.99 ± 7.26. (d) PGElevels in the pouch exudate (ELISA, pg/ml): Ctrl, 150.06 ± 20.84; MSU, 1530.49 ± 205.93; and MSU + extracts, 572.93 ± 72.88. (e) PGDlevels in the pouch exudate (ELISA, pg/ml): Ctrl, 5.98 ± 0.48; MSU, 11.02 ± 2.49; and MSU + extracts, 37.34 ± 5.77. PGD:PGEratios were as follows: Ctrl, 0.040; MSU, 0.007; and MSU + extracts, 0.065. Pouch membrane h-PGDS mRNA. Analysis was identical to (a). The numerical values were as follows: Ctrl, 1; MSU, 1.1 ± 0.28; and MSU + extracts, 3.72 ± 0.68. *, < 0.05 compared with MSU. Ctrl, control; ELISA, enzyme-linked immunosorbent assay; GAPDH, glyceraldehyde 3-phosphate dehydrogenase; h-PGDS, hematopoietic prostaglandin D synthase; IL, interleukin; MSU, monosodium urate; PGD, prostaglandin D; PGE, prostaglandin E; RT-PCR, reverse transcriptase polymerase chain reaction; TNF, tumor necrosis factor

Input Data for Sea Turtles in Jeju Island of the Korean Peninsula

This file includes input files for molecular analyses used in Jang et al., 2024 in Frontiers in marine science.Details for related methods were described in Jang et al., 2024 in Frontiers in marine science.</p

Folding-Degradation Relationship of a Membrane Protein Mediated by the Universally Conserved ATP-Dependent Protease FtsH

ATP-dependent protein degradation mediated by AAA+ proteases is one of the major cellular pathways for protein quality control and regulation of functional networks. While a majority of studies of protein degradation have focused on water-soluble proteins, it is not well understood how membrane proteins with abnormal conformation are selectively degraded. The knowledge gap stems from the lack of an in vitro system in which detailed molecular mechanisms can be studied as well as difficulties in studying membrane protein folding in lipid bilayers. To quantitatively define the folding-degradation relationship of membrane proteins, we reconstituted the degradation using the conserved membrane-integrated AAA+ protease FtsH as a model degradation machine and the stable helical-bundle membrane protein GlpG as a model substrate in the lipid bilayer environment. We demonstrate that FtsH possesses a substantial ability to actively unfold GlpG, and the degradation significantly depends on the stability and hydrophobicity near the degradation marker. We find that FtsH hydrolyzes 380–550 ATP molecules to degrade one copy of GlpG. Remarkably, FtsH overcomes the dual-energetic burden of substrate unfolding and membrane dislocation with the ATP cost comparable to that for water-soluble substrates by robust ClpAP/XP proteases. The physical principles elucidated in this study provide general insights into membrane protein degradation mediated by ATP-dependent proteolytic systems