As a result, lactate accumulation induced a drop in mean and minimum ruminal pH, compared with C wethers (−0.70 and −0.33 pH units on average; P < 0.05). Vorinostat clinical trial Among probiotic treatments, pH was lowest for Lr + P, intermediate for P and highest for Lp + P (P < 0.05). P and Lr + P decreased propionate and butyrate proportions, whereas minor VFAs were reduced by all three probiotics (P < 0.05). The concentration of NH3-N was reduced for P and Lr + P fed wethers (P < 0.05), whereas it was numerically lower for those fed Lp + P. This decrease in NH3-N may be due to a decrease in deamination Androgen Receptor Antagonist screening library activity, as the proportion of Prevotella spp., a dominant bacterial genus that plays a central role in amino acid deamination in the rumen [33], was numerically lower in wethers fed with Lp + P and Lr + P (P = 0.1 and 0.06; respectively). In addition, probiotic supplementation increased ethanol concentration,

a minor fermentation product that does not accumulate

in the rumen except during lactic acidosis [34, 35] because of the heterofermentative metabolism of glucose by lactobacilli, which leads to lactate and ethanol production [36]. Table 3 Effects of bacterial probiotic supplementation on rumen fermentation AG-881 mw characteristics during acidosis induced by feed challenges   Treatments1    P value (Prob vs. C)2   C (n = 4)  P (n = 4)  Lp + P (n = 4)  Lr + P (n = 4) SEM  P   Lp + P   Lr + P  Wheat-induced lactic acidosis Ruminal pH                 Mean 5.25 4.55 4.76 4.33 BCKDHA 0.15 0.001 0.02 0.0001 Minimum 4.87 4.28 4.45 4.17 0.19 0.03 0.12 0.01 Total VFAs, mM 93.6 33.9 76.7 33.5 14.4 0.01 0.32 0.001 Acetate3, mol % 72.6 87.0 78.1 92.5 4.10 0.01 0.34 0.001 Propionate, mol % 12.2 6.63 10.6 3.82 2.49 0.10 0.63 0.02 Butyrate, mol % 12.8 5.79 10.2 3.52 1.94 0.01 0.33 0.001 Minor VFAs4, mol % 2.33 0.56 1.11 0.14 0.40 0.001 0.02 0.0001 Lactate, mM 33.8 71.1 64.9 79.6 9.28 0.005 0.02 0.001 NH3-N, mM 6.53 3.58 4.25 2.44 1.16 0.03 0.09 0.003 Ethanol, mM 6.57 12.4 17.2 14.4 1.85 0.02 0.0001 0.003 Corn-induced butyric subacute acidosis Ruminal pH                 Mean 5.49 5.61 5.74 5.65 0.08 0.30 0.03 0.18 Minimum 5.17 5.28 5.63 5.46 0.12 0.50 0.01 0.09 Total VFAs, mM 107 85.7 81.6 94.4 7.79 0.03 0.01 0.19 Acetate, mol % 63.2 67.4 68.7 66.9 1.75 0.08 0.03 0.13 Propionate, mol % 17.0 14.2 14.5 15.5 1.09 0.07 0.19 0.31 Butyrate, mol % 16.9 14.7 12.1 13.5 1.41 0.26 0.02 0.09 Minor VFAs, mol % 2.88 3.68 4.29 4.

Results and discussion To develop a specific aptamer for MMP2 protein, we performed a modified DNA PI3K Inhibitor Library cell line SELEX technique as described in the ‘Methods’ section. To select a high-affinity aptamer, we used nucleotides chemically

modified by benzylaminocarbonyl-dU (Benzyl-dU) at the 5′ 4EGI-1 positions, which mimic amino acid side chains. After eight rounds of SELEX, the enriched DNA pool was cloned and sequenced according to standard procedures. After each round of SELEX, binding assays were performed to measure the dissociation constant (K d) value of the aptamer pool using [α-32P] ATP. The sequence and secondary structure of the best aptamer selected in this study were presented in Figure 1. The mean B max and K d values of the aptamer were 35% ± 0.8% and 5.59 ± 0.52 nM, respectively (Figure 2). Figure 1 Sequence and check details secondary structure of the MMP2 aptamer. (a) Sequence of the 40-nucleotide random region (N40, shaded) and of the two constant regions flanking the random region. (b) The hairpin-like secondary structure of the aptamer is presented in the lower panel. Figure

2 Affinity of the MMP2 aptamer. (a) 32P-labeled aptamers and different MMP2 protein concentrations were used to examine the binding affinity of the MMP2 aptamer. (b) Images of radiolabeled aptamer that interacted with proteins in the binding assay. To determine whether the MMP2 aptamer could be used to precipitate the target protein, we performed precipitation and then western blotting using anti-MMP2 antibody. To do this, we biotinylated the aptamer and used streptavidin beads for the precipitation. MMP2 in buffer containing 10% serum was incubated with the biotinylated MMP2 aptamer, and the protein-aptamer complex was then precipitated and detected by immunoblotting. The aptamer successfully precipitated MMP2 protein (Figure 3), whereas the biotinylated control 4��8C aptamer did not (data not shown). Figure 3 Precipitation of MMP2 protein by MMP2 aptamer. MMP2 protein in buffer containing 10% serum was incubated with the aptamer (0.2 μg/ml) overnight

at 4°C. The protein was detected by immunoblotting with anti-MMP2 antibody. Next, we examined whether the MMP2 aptamer could be applied for immunohistochemical purposes in pathological tissues, that is, atherosclerotic plaques and gastric cancer tissues. In both tissue types, the MMP2 aptamer successfully detected MMP2 (Figure 4), whereas the control aptamer did not (data not shown). To further confirm the specificity of the aptamer for immunohistochemistry, we performed peptide blocking. Immunohistochemistry was performed after incubating the aptamer for 2 h with the bare protein, and the intensities of positive signals were significantly reduced (Figure 5). Figure 4 Comparison of the tissue staining abilities of anti-MMP2 antibody and MMP2 aptamer. Normal aorta, atherosclerotic plaques, and gastric cancer tissues were stained with anti-MMP2 antibody and MMP2 aptamer. Similar staining patterns were observed.

Bull Math Biol 2004, 66:523–537.CrossRefPubMed 37. Hybiske K, Stephens RS: Mechanisms AZD4547 clinical trial of host cell exit

by the intracellular bacterium Chlamydia. Proc Natl Acad Sci USA 2007, 104:11430–11435.CrossRefPubMed 38. Raulston JE: Response of Chlamydia trachomatis serovar E to iron restriction in vitro and evidence for iron-regulated chlamydial proteins. Infect Immun 1997, 65:4539–4547.PubMed 39. Bailey L, Gylfe A, Sundin C, Muschiol S, Elofsson M, Nordstrom P, Henriques-Normark B, Lugert R, Waldenstrom A, Wolf-Watz H, Bergstrom S: Small molecule inhibitors of type III secretion in Yersinia block the Chlamydia pneumoniae infection cycle. FEBS Lett 2007, 581:587–595.CrossRefPubMed 40. Shivshankar P, Lei

L, Wang J, Zhong G: Rottlerin inhibits chlamydial intracellular growth and blocks chlamydial acquisition of sphingolipids from host cells. Appl Environ Microbiol 2008, 74:1243–1249.CrossRefPubMed 41. Wolf Caspase-independent apoptosis K, Betts HJ, Chellas-Gery B, Hower S, selleck chemicals llc Linton CN, Fields KA: Treatment of Chlamydia trachomatis with a small molecule inhibitor of the Yersinia type III secretion system disrupts progression of the chlamydial developmental cycle. Mol Microbiol 2006, 61:1543–1555.CrossRefPubMed 42. Yan Y, Silvennoinen-Kassinen S, Tormakangas L, Leinonen M, Saikku P: Selective cyclooxygenase inhibitors prevent the growth of Chlamydia pneumoniae in HL cells. Int J Antimicrob Agents 2008, 32:78–83.CrossRefPubMed 43. Coombes BK, Mahony JB: Identification of MEK- and phosphoinositide 3-kinase-dependent signalling as essential events during Chlamydia pneumoniae invasion of HEp2 cells. Cell Microbiol 2002, 4:447–460.CrossRefPubMed 44. Muschiol S, Bailey L, Gylfe A, Sundin C, Hultenby K, Bergstrom S, Elofsson M, Wolf-Watz H, Normark S, Henriques-Normark B: A small-molecule inhibitor of type III secretion inhibits different stages of the infectious cycle of Chlamydia trachomatis. Proc Natl Acad Sci USA 2006, 103:14566–14571.CrossRefPubMed 45. Johnson DL, Mahony JB:Chlamydophila pneumoniae PknD exhibits dual amino acid

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Total RNA was isolated from theses samples and used to prepare cRNA probes for hybridization with Affymetrix GeneChip Rat 230 2.0 arrays (Figure 3). The hybridized microarrays were then scanned and the signals acquired (Figure 4). At the 12th week, liver cirrhosis occurred in 10 of 10 rats, so we took the HM781-36B clinical trial pooled cirrhotic tissues from the 10 rats for the microarrays. At the 14th week, dysplastic nodules occurred only in the livers of 2/10 rats, so we took the pooled dysplastic nodules from the two rats for the microarrays. At the 16th week, early tumor nodules occurred

in the liver of 8/10 rats, so we took the pooled tumor nodules from the eight rats for the microarrays. At the 20th week, tumor nodules occurred in all of the ten HMPL-504 supplier rats(10/10), but lung metastasis only occurred in the two of them, so we took the pooled

tumor nodules in the liver from the two rats with lung metastasis for the microarrays. We used the pooled liver tissues from the control rats killed at the 12th, 14th, 16th and the 20th week for the microarrays. The decision to pool the mRNA from the rat livers was made in order to obtain a representative analysis of gene expression changes across more than one animal. Figure 3 Total RNA isolated from the liver tissues of the rats was identified by agar electrophoresis. (A) from normal rats; (B-E) from DEN-treated rats: cirrhosis tissue at 12th week (B), dysplastic nodules at the 14th week (C), early cancerous nodules at the 16th week (D), cancerous nodules with lung metastasis selleck at the 20th week (E). Figure 4 Scatter plot of gene expression comparisons between the normal rats and DEN-exposured rats. Each point represents a single gene or EST. x-axis:

control (from liver tissue of normal rat); y-axis: liver tissue from DEN- treated rat at 12th week (A); at 14th week (B); at 16th week (C); at 20th week (D). The red points represent Progesterone ‘present’ states both in control and DEN exposed; blue points represent ‘no present’ in either of control and DEN-exposed; yellow points represent ‘absent’ states both in control and DEN-exposed. Analysis of the differential expression genes The differential expression genes of cirrhotic tissue, dysplastic nodules, early tumors nodules and tumor nodules from rats with lung metastasis compared with the tissue from normal rats were screened and to determine the upregulated and downregulated DEGs. The results are shown in Table 1. Table 1 Number of differential expression genes (DEGs) of liver tissues from DEN-treated rats compared with control. DEGs 12th week 14th week 16th week 20th week Up-regulated DEGs 681 857 1223 999 Down-regulated DEGs 687 732 1016 906 Total 1368 1589 2239 1905 NOTE: The words ’12th week, 14th week, 16th week, 20th week’ in the table indicate the cirrhosis tissue, dysplastic nodules, early cancerous nodules and cancerous nodules with metastasis, respectively.

​pasteur.​fr/​TubercuList/​[11] using Align two sequences (bl2seq) of BLAST http://​blast.​ncbi.​nlm.​nih.​gov/​Blast.​cgi[32]. The SNPs obtained by the sequence analysis were used to screen other 100 clinical isolates through Sequenom MassARRAY system. All the SNPs were analysed further for the change in amino acids in the corresponding protein sequences through Gene Runner software version 3.05 (Hastings Software, Inc.) available at http://​www.​generunner.​net. Computational methods Structure homology-based method (PolyPhen) to predict functional

and structural changes in proteins In order selleck chemicals to analyze the learn more impact of nonsynonymous SNPs on the structure and function of proteins of mce operons, Polyphen server http://​genetics.​bwh.​harvard.​edu/​pph/​[33] was used. Protein sequences in FASTA format with the position of amino acid variants indicated were submitted as the query. Polyphen server calculates position- specific independent counts (PSIC) scores for each of the two variants

based on the parameters such as sequence-based characterization of the substitution site, profile analysis of homologous sequences, and mapping of the substitution site to a known protein’s three dimensional structure and then the difference between the PSIC scores of the two variants are computed. find more The higher the PSIC score (> 1.5) difference, the higher the functional impact a particular amino acid substitution

is likely to have. Neural network-based sequence information method (PMut) to predict pathological character of nonsynonymous SNPs PMut server http://​mmb2.​pcb.​ub.​es:​8080/​PMut/​[34] was used to predict pathological relevance of nonsynonymous SNPs in the mce operon proteins. The software uses different kinds of sequence information to label mutations from the databases of disease-associated mutations (DAMU), and neural networks (NNs) to process the databases of DAMUs and neutral mutations (NEMUs). The resulting vector of properties is then utilized to decide whether the mutation is pathological or not. Dichloromethane dehalogenase Although, PMut is designed to analyze pathological character associated with mutations in the human proteins. A number of workers [35, 36] have qualitatively interpreted the functionality of mutated non-human proteins especially that of microbes. We submitted the protein sequences as the query, the location of the mutation and the amino acid residues were also furnished. Small NN (20 nodes, 1 hidden layer) with using 2/3 input parameters (pam40 matrix index, pssm index, variability index) was used to train the database as it is recommended for predictions of non-human proteins [34]. NN output greater than 0.5 is predicted as pathological otherwise neutral.

Only proteins with q-value below 0.05 or those present in only one of two compared analytical groups were taken into consideration during further analysis. The protein concentration was measured by Bradford’s method [35]. Results and discussion Batch fermentation Microbiological synthesis of 1,3-PD by C. butyricum DSP1 was carried out at an increasing capacity of bioreactors. The efficiency of 1,3-PD production from crude glycerol during the scale-up process

was investigated. For this purpose batch fermentations were performed in 6.6 L, 42 L and 150 L bioreactors. The results obtained were used to calculate the basic kinetic parameters of the fermentation processes (Table 2). It was found that the scale-up process did not have any effect BMN 673 ic50 on the growth of microorganisms or 1,3-PD synthesis. Table 2 Kinetic parameter values from C. butyricum DSP1 in 6.6 L, 42 L and 150 L bioreactors Parameter/fermentation scale 6.6 L 42 L 150 L Time of fermentation (h) 33 32 28 Max biomass, Xmax (g/L) 1.2 1.2 1.3 Time taken to reach max biomass, t (h) 15 16 14 Max specific growth rate, μ (1/h) 0.067 0.062 0.071 Max 1,3-PD concentration, selleck screening library 1,3-PDmax (g/L) 37.63 ± 1.2 36.40 ± 1.6 37.20 ± 1.4 1,3-PD productivity P1,3-PD (g/L/h) 1.12 1.13 1.33 1,3-PD yield, Y1,3-PD (g1,3- PD/gGly) 0.53 0.52 0.53 Max butyric acid

concentration, Butmax (g/L) 4.26 ± 0.09 3.57 ± 0.08 GPX6 4.22 ± 0.07 Butyric acid productivity PBut (g/L/h) 0.13 0.11 0.15 Butyric acid yield, YBut (gBut/gGly) 0.06 0.05 0.06 Max acetic acid concentration, Acemax (g/L) 2.0 ± 0.03 1.9 ± 0.03 2.2 ± 0.02 Acetic acid productivity PAce (g/L/h) 0.06 0.06 0.08

Acetic acid yield, YAce (gLac/gGly) 0.03 0.03 0.03 Max buy Lazertinib Lactic acid concentration, Lacmax (g/L) 3.14 ± 0.02 2.84 ± 0.03 3.63 ± 0.04 Lactic acid productivity PLac (g/L/h) 0.09 0.09 0.12 Lactic acid yield, YLac (gLac/gGly) 0.04 0.04 0.05 Each point is the mean value of two independent measurements. The concentration of the diol in the 150 L bioreactor was close to concentrations achieved in the 6.6 L and 42 L bioreactors and averaged 37 g/L. In all batch fermentations the glycerol was completely utilized. However, some differences were observed in the productivity of the bioreactors as their capacity increased, with the 150 L bioreactor giving 1.33 g/L/h, which probably depended on the quantity of biomass (Table 2). The plateau of microorganism growth was achieved in the14th hour of cultivation and was followed by the stationary phase. The profiles of by-products formed in the respective bioreactors were comparable. The first scale-up experiments on 1,3-PD synthesis from glycerol (by C. butyricum DSM 5431) were described by Günzel et al. [24] and involved fermentation starting in a 1.4 L bioreactor and proceeding to a 2000 L bioreactor.

4058 ± 0.35 nmol of Rh-UTES/cm2 of etched area, which corresponds

at approximately 20% of the initial solution concentration (1.16 μM) [19]. By comparing the optical features of bare PSiMc with that obtained after device functionalization, it is clear that the emission spectra show important optical changes. The most remarkable is the well-defined emission curve in the 525 to 625-nm range attributed to the fluorescent Selleckchem LY2874455 emission of Rh-UTES derivative, which confirms the attachment of the derivative molecule on the PSi surface. Exposure of PSiMc/Rh-UTES sensor at a heavy metal solution produced two new changes: first, an increase in the integrated emission intensity of 0.13-fold and secondly, a 16-nm red shift (552 to 568 nm)

of the main peak position. As we mentioned before, some studies have demonstrated that the spirolactam-rhodamine derivatives can be used to develop liquid phase OFF-ON metal ion-fluorescent chemosensors, mainly because their chemical structure may change in the presence of metal ions. In agreement with those contributions, we believe that the enhanced emission observed when the PSiMc/Rh-UTES sensor captured the Hg2+ ions is produced by the formation of metal-ligand coordination bonds, which in turn induces the spirolactam ring opening [23]. Thus, based on this coordination mechanism, the red shift in the fluorescent emission may be attributed to the electronic interactions of PSiMc/Rh-UTES-Hg2+ www.selleckchem.com/products/GDC-0941.html complex (Figure 9c). A similar optical behavior was found in the liquid phase chemosensor; however, our solid device presents several advantages that are related with (i) the easy operation of the device, (ii) special solvents that are not needed, (iii) the higher stability of the fluorescent derivative when immobilized in the solid support, and (iv) the possibility of portability. Then, by comparing spectra (c) and (d) which correspond at the sensing of two different Hg2+ ion concentrations (3.45 and 6.95 μM, respectively), a 6-nm red shift (from 568 to 574 nm) and a fluorescent emission enhancement of 0.12-fold was observed. In this case, the

red shift may be attributed to PSi-derivative-Hg2+ Inositol oxygenase interaction processes produced in the reduced space of PSi pores. Our hypothesis is that after increasing the metal ion concentration, the derivative Rh-UTES receptor changed its chemical structure, provoking a molecular reorganization inside the pore. According to Tu and co-workers [24], the chemical change can reduce the distances between neighboring molecules limiting their free stretching movement and leading to their self-interaction, which may reduce their excited state energy and produce the red shift in the spectra. On other hand, the enhancement of the emission intensity observed when the PSiMc/Rh-UTES device coordinates higher amount of Hg2+ ions confirms that the fluorescent intensity of the PSiMc hybrid device is metal concentration 4SC-202 manufacturer dependent [25, 26].

Second, the sequence of MinC is less conserved than that of MinD in bacteria (data not shown). MinC could be too divergent to be recognized by sequence in higher plants. It is hard to understand why AtMinD is localized to static puncta in chloroplasts in previous study [20] instead of a dynamic oscillating pattern. Here we show that AtMinD is CRISPR/Cas9 activator localized to puncta

at the polar regions in E. coli cells (Figure 2D and 2E) and puncta in chloroplasts (Figure 2A). By interacting with either endogenous or transiently expressed AtMinD, EcMinC-GFP, EcMinC-YFPN and EcMinC-YFPC are localized to puncta in chloroplasts too. These data further suggest that the punctate localization pattern of AtMinD in chloroplasts shown before [20, 24] may be true. There are usually only one or two GFP-labeled puncta in one chloroplast. It is possible that chloroplasts constrict in-between puncta. However, this hasn’t been confirmed. So far, it seems that the working

mechanism of Min system in plastids is a lot different from that in E. coli. However, the study of Min system in plastids is limited and our understanding about it is not very clear. AtMinE seems to have an antagonistic role to AtMinD in plastid, because the chloroplast division phenotype caused by overexpression of AtMinE was similar to that caused by EPZ5676 ic50 antisense suppression of AtMinD in Arabidopsis [17, 19]. This kind of relationship is still similar to that of EcMinE and EcMinD [7]. Further study needs to be done to understand the working mechanism of AtMinE in plastids. Conclusion In this paper, we have shown that AtMinD was localized to puncta at the polar region PI3K inhibitor and is functional in E. coli. AtMinD may function through the interaction with EcMinC. It is not necessary for AtMinD to oscillate Glutathione peroxidase to keep the cell division site at the center of E. coli cells. In Bacillus subtilis, the MinCD proteins are localized to polar regions without oscillation [27]. There is no MinE in B. subtilis [27]. Instead, another protein DivIVA tethers MinCD to poles of the cell and prevents FtsZ polymerization and division apparatus assembly at the end of the cells [27]. AtMinD and EcMinC in E. coli HL1 mutant (ΔMinDE)

may work in a manner similar to the BsMinD and BsMinC in Bacillus subtilis. Methods E. coli strains and bacterial expression vector construction The E. coli strains used in this study were DH5α, HL1 (ΔMinDE) [21] and RC1 (ΔMinCDE) [28]. The culture were grown to OD600 = 0.4 – 0.45 at 37°C in LB medium with 100 μg/ml ampicillin, 50 μg/ml kanamycin or 25 μg/ml chloramphenicol respectively as required. AtMinD lacking the coding region of the N-terminal 57 amino acid residues were amplified by using primers: AD1F1, CGGAATTCAACAAGGAATTTCTATGCCGGAACTCGCCGGAGAAACGC and AD1R1, GCAAGCTTTTAGCCGCCAAAGAAAGAGAAGA. EcMinD and EcMinDE were amplified from the genomic DNA of DH5α by primers: EcDF1, GCGGAATTCAAGGAATTTCTATGGCACG and EcDR1, GCGAAGCTTATCCTCCGAACAAGCG or EcER1, GCGAAGCTTA CAGCGGGCTTATTTCAG.

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“Fulvoincarniti “being invalid, it would also be illegitimate if it had been validly published. The type species indicated for subsect. “Fulvoincarnati” was H. pudorinus, and not the taxon to which the name H. pudorinus was applied (i.e., H. abieticola), subsect. “Fulvoincarnati “thus would have been a superfluous (therefore, illegitimate) name for subsect. Pudorini rather than being a legitimate name for the new subsect. Salmonicolores if it had been validly published. Kovalenko (1989, 1999) followed Singer’s classification, but included in subsect. “Fulvoincarnati” [invalid, illeg.] H. secretanii – a species that belongs in sect. Aurei. Hygrophorus selleck chemical [subgen. Colorati ] sect. Aurei (Bataille)

E. Larss., stat. nov. MycoBank MB804114. Type species Hygrophorus aureus Arrh., in Fr., Monogr. Hymenomyc. Suec. (Upsaliae) 2: 127 (1863) ≡ Hygrophorus hypothejus GF120918 nmr (Fr. : Fr.) Fr. var. aureus (Arrh.) Imler, Bull. trimest. Soc. mycol. Fr. 50: 304 (1935) [1934] = Hygrophorus hypothejus (Fr. : Fr.) Fr., Epicr. syst. mycol. (Upsaliae): 324 (1838), ≡ Agaricus hypothejus Fr., Observ. Mycol. (Havniae) 2: 10 (1818). Basionym Hygrophorus

[unranked] Aurei Bataille, Mém. Soc. émul. Doubs, sér. 8 4: 161 (1910) [1909]. Pileus glutinous or subviscid when moist, color cream buff, yellow, olive, brown, gold or orange; stipe glutinous with a partial veil sometimes forming an annulus or dry. Ectomycorrhizal, predominantly associated with conifers. Phylogenetic support Sect. Aurei appears as a monophyletic group in the analysis presented by Larsson (2010; unpublished data), including H. hypothejus (=H. aureus), H. hypothejus var. aureus, H. gliocyclus, H. flavodiscus and H. speciosus in subsect. Aurei and H. karstenii and

H. secretanii in subsect. Discolores, but MPBS support for the branch is lacking. Sect. Casein kinase 1 Aurei is polyphyletic in our ITS analysis (Online Resource 9). Subsections included Subsect. Aurei and subsect. Discolores, E. Larss., subsect. nov. Comments We added H. karstenii and H. secretanii to this distinctive group and raised the rank to section. Hygrophorus [subgen. Colorati sect. Aurei ] subsect. Aurei (Bataille) Candusso, Hygrophorus. Fungi europ. (Alassio) 6: 222 (1997). Type species Hygrophorus aureus Arrh., in Fr., Monogr. Hymenomyc. Suec. (Upsaliae) 2: 127 (1863) ≡ Hygrophorus hypothejus (Fr. : Fr.) Fr. var. aureus (Arrh.) Imler, Bull. trimest. Soc. mycol. Fr. 50: 304 (1935) [1934], = Hygrophorus hypothejus (Fr. : Fr.) Fr., Epicr. syst. mycol. (Upsaliae): 324 (1838), ≡ Agaricus hypothejus Fr., Observ. Mycol. (Havniae) 2: 10 (1818). Basionym Hygrophorus [unranked] Aurei Bataille, Mém. Soc. émul. Doubs, sér. 8 4: 161 (1910) [1909]. Pileus glutinous, colored citrine, gold, yellow, orange, olive or brown; lamellae subdecurrent, pale, yellowish to orange; stipe glutinous with a partial veil sometimes forming an annulus, pale or stained yellowish, Sirtuin activator inhibitor orange or brown.