Cryptogam Algol 2003, 24:13–32. 37. Allen MB: Studies with Cyanidium caldarium , an click here anomalously pigmented chlorophyte. Arch Mikrobiol 1959, 32:270–277.PubMedCrossRef 38. Murasugi A, Wada C, Hayashi Y: Occurrence of acid-labile

sulfide in cadmium-binding peptide 1 from fission yeast. J Biochem 1983, 93:661–664.PubMed 39. Gupta A, Whitton BA, Morby AP, Huckle JW, Robinson NJ: Amplification and rearrangement of a prokaryotic metallothionein locus smt in Synechococcus PCC 6301 selected for tolerance to cadmium. P Roy Soc B-Biol Sci 1992, 248:273–281.CrossRef 40. Scarano G, Morelli E: Characterization of cadmium- and lead-phytochelatin complexes formed in a marine microalga in response to metal exposure. Biometals 2002, 15:145–151.PubMedCrossRef 41. Holmes JD, Smith PR, Evans-Gowing R, Richardson DJ, Russell DA, Sodeau JR: Energy-dispersive X-ray analysis of the extracellular cadmium sulfide crystallites of Klebsiella aerogenes . Arch Microbiol 1995, 163:143–147.PubMedCrossRef 42. Reese RN, White CA, Winge DR: Cadmium-sulfide crystallites in Cd-(γEC)nG peptide

complexes from tomato. Plant Physiol 1992, 98:225–229.PubMedCrossRef 43. Speiser DM, Abrahamson Fedratinib SL, Banuelos G, Ow DW: Brassica juncea produces a phytochelatin-cadmium-sulfide complex. Plant Physiol 1992, 99:817–821.PubMedCrossRef 44. Melis A, Chen H: Chloroplast selleck chemicals sulfate transport in green algae – genes, proteins and effects. Photosynth Res 2005, 86:299–307.PubMedCrossRef 45. Merchant SS, Prochnik SE, Vallon O, Harris EH, Karpowicz SJ, Witman GB, Terry A, Salamov A, Fritz-Laylin LK, Marechal-Drouard L, Marshall WF, Qu L, Nelson DR, Sanderfoot AA, Spalding MH, Kapitonov VV, Ren Q, Ferris P, Lindquist E, Shapiro H, Lucas SM, Grimwood J, Schmutz J, Cardol P, Cerutti H, Chanfreau G, Chen C, selleckchem Cognat V, Croft MT, Dent R, et al.: The Chlamydomonas genome reveals the evolution of key animal and plant functions RID A-3530–2008 RID A-1214–2009 RID A-1755–2010 RID C-1537–2010. Science 2007, 318:245–251.PubMedCrossRef

46. Pollock SV, Pootakham W, Shibagaki N, Moseley JL, Grossman AR: Insights into the acclimation of Chlamydomonas reinhardtii to sulfur deprivation. Photosynth Res 2005, 86:475–489.PubMedCrossRef 47. Kertesz MA: Bacterial transporters for sulfate and organosulfur compounds. Res Microbiol 2001, 152:279–290.PubMedCrossRef 48. Smith FW, Hawkesford MJ, Prosser IM, Clarkson DT: Isolation of a cDNA from Saccharomyces cerevisiae that encodes a high affinity sulphate transporter at the plasma membrane. Mol Gen Genet 1995, 247:709–715.PubMedCrossRef 49. Hawkesford MJ, De Kok LJ: Managing sulphur metabolism in plants. Plant Cell Environ 2006, 29:382–395.PubMedCrossRef 50.

Moreover, a recent study has shown that AMD3100, a small synthetic inhibitor of CXCR4, not binds only to CXCR4, but also to CXCR7 [31]. We propose that more attention should be paid to CXCL12/CXCR4 axis and CXCL12/CXCR7 axis.

Thus, further studies elucidating the role of CXCL12/CXCR7 axis in cancer development is needed. Conclusions In summary, CXCR7 was highly expressed in hepatocellular carcinoma tissues. We presented the first evidence that suppression of CXCR7 expression by RNA interference impairs in vitro cellular invasion, adhesion, VEGF secretion and angiogenesis. We also observed that knockdown of CXCR7 significantly inhibited tumor Selleck Compound Library growth but

not metastasis in vivo. Moreover, we found that VEGF stimulation up-regulated the expression of CXCR7 in SMMC-7721 cells and HUVECs. Taken together, this study provides novel evidence that inhibition of CXCR7 expression may be an effective Inhibitor Library solubility dmso approach to suppressing tumor growth of HCC. Acknowledgements We are extremely grateful to professor Weixue Tang (Chongqing Key Laboratory of Neurology, Chongqing, China) for her technical support, and Tingxiu Xiang (Chongqing Key Laboratory of Neurology, Chongqing, China)for her helpful discussion. We also thank other staffs working in the Department of Endorine Surgery and Breast Cancer Centre, the First Affiliated Hospital of Chongqing Medical University for they supported our work. References 1. Mann CD, Neal CP, Garcea G, Manson MM, Dennison AR, Berry DP: Prognostic molecular markers in hepatocellular carcinoma: a systematic review. Eur J Cancer 2007,43(6):979–92.PubMedCrossRef 2. Tung-Ping Poon R, Fan ST, Wong J: Risk factors, prevention, and management of postoperative selleck recurrence after resection of hepatocellular

carcinoma. Ann Surg 2000,232(1):10–24.PubMedCrossRef 3. Müller A, Homey B, Soto L-gulonolactone oxidase H, Ge N, Catron D, Buchanan ME, McClanahan T, Murphy E, Yuan W, Wagner SN, Barrera JL, Mohar A, Verástegui E, Zlotnik A: Involvement of chemokine receptors in breast cancer metastasis. Nature 2001,410(6824):50–6.PubMedCrossRef 4. Miao Z, Luker KE, Summers BC, Berahovich R, Bhojani MS, Rehemtulla A, Kleer CG, Essner JJ, Nasevicius A, Luker GD, Howard MC, Schall TJ: CXCR7 (RDC1) promotes breast and lung tumor growth in vivo and is expressed on tumor-associated vasculature. Proc Natl Acad Sci USA 2007,104(40):15735–40.PubMedCrossRef 5. Pablos JL, Amara A, Bouloc A, Santiago B, Caruz A, Galindo M, Delaunay T, Virelizier JL, Arenzana-Seisdedos F: Stromal-Cell Derived Factor Is Expressed by Dendritic Cells and Endothelium in Human Skin. Am J Pathol 1999,155(5):1577–86.PubMedCrossRef 6.

nov. , a novel species designation for Cronobacter sp. genomospecies 1, recovered from a leg infection, water and food ingredients. Intl J System Evol Microbiol 2011, in press. ecopy available 4. Food and Agriculture Organization-World Health Organization: Joint FAO/WHO workshop on Enterobacter sakazakii and other microorganisms in powdered infant formula, Geneva, 2–5 February, 2004. 2004. 5. Food and Agriculture Organization-World Health Organization: Enterobacter sakazakii and

Salmonella in powdered infant formula. Second Risk Assessment Workshop 16–20th January WHO Rome, Italy; 2006. 6. Forsythe S: Enterobacter sakazakii and other bacteria in powdered infant milk formula. Maternal Child Nutr 2005, 1:51–58.CrossRef 7. Iversen C, Forsythe SJ: Risk profile of Enterobacter sakazakii , an emergent pathogen associated with infant milk formula. Trends in Food Sci Technol 2003, 11:443–454.CrossRef 8. Friedemann VRT752271 in vivo M: Enterobacter sakazakii in food and beverages (other than infant formula and milk powder). Intl J Food Microbiol 2007,

116:1–10.CrossRef 9. Codex Alimentarius Commission: Code of hygienic practice for powdered formulae for infants and young children. ALINORM 08/31/13 10. Kucerova E, Joseph S, Forsythe SJ: The Cronobacter genus: ubiquity and diversity. Quality Assurance and Safety of Crops & Foods 2011, 3:104–122.CrossRef 11. Iversen C, Lancashire L, Waddington M, Forsythe S, Ball YH25448 order G: Identification of Enterobacter sakazakii from closely related species: The use of selleckchem Artificial Neural Networks in the analysis of biochemical and 16S rDNA data. BMC Microbiology 2006.,6(28): 12. Baldwin A, Loughlin M, Caubilla-Barron J, Kucerova E, Manning G, Dowson C, Forsythe S: Multilocus until sequence typing of Cronobacter sakazakii and Cronobacter malonaticus reveals stable clonal structures with clinical significance which do not correlate with biotypes. BMC Microbiology 2009,9(1):223.PubMedCrossRef 13.

Cronobacter Multi Locus Sequence Typing Database [http://​pubmlst.​org/​cronobacter] 14. Joseph S, Forsythe SJ: Predominance of Cronobacter sakazakii ST4 in neonatal infections. Emerg Infect Dis 2011, 17:1713–1715.PubMedCrossRef 15. Kucerova E, Clifton SW, Xia XQ, Long F, Porwollik S, Fulton L, Fronick C, Minx P, Kyung K, Warren W, Fulton R, Feng D, Wollam A, Shah N, Bhonagiri V, Nash WE, Hallsworth-Pepin K, Wilson RK, McClelland M, Forsythe SJ: Genome sequence of Cronobacter sakazakii BAA-894 and Comparative Genomic Hybridization Analysis with other Cronobacter species. PLOS One 2010,5(3):e9556.PubMedCrossRef 16. Kanehisa M, Goto S, Kawashima S, Nakaya A: The KEGG databases at GenomeNet. Nucleic Acids Res 2002,30(1):42.PubMedCrossRef 17. Kothary MH, McCardell BA, Frazar CD, Deer D, Tall BD: Characterization of the zinc- containing metalloprotease encoded by zpx and development of a species-specific detection method for Enterobacter sakazakii . Appl and Env Microbiol 2007,73(13):4142–4151.CrossRef 18.

APMIS 2011,119(8):522–528.PubMedCrossRef 4. Cole AM, Tahk S, Oren A, Yoshioka PND-1186 in vitro D, Kim YH, Park A, Ganz T: Determinants of Staphylococcus aureus nasal carriage. Clin Diagn Lab Immunol 2001,8(6):1064–1069.PubMedCentralPubMed 5. Choi CS, Yin CS, Bakar AA, Sakewi Z, Naing NN, Jamal F, Othman N: Nasal carriage of Staphylococcus aureus

among healthy adults. J Microbiol Immunol Infect 2006,39(6):458–464.PubMed 6. Mahmutovic Vranic S, Puskar M: Staphylococcus aureus carriage among medical students. Med Glas Ljek komore Zenicko-doboj kantona 2012,9(2):325–329. 7. Foster TJ: Immune MK-8931 evasion by staphylococci. Nat Rev Microbiol 2005,3(12):948–958.PubMedCrossRef 8. Foster TJ, McDevitt D: Surface-associated proteins of Staphylococcus aureus: their possible roles in virulence. FEMS Microbiol Lett 1994,118(3):199–205.PubMedCrossRef 9. Guss B, Uhlen M, Nilsson B, Lindberg M, Sjoquist J, Sjodahl J: Region X, the cell-wall-attachment

part of staphylococcal protein A. Eur J Biochem 1984,138(2):413–420.PubMedCrossRef 10. Uhlen M, Lindberg M, Philipson L: The gene for staphylococcal protein A. Immunol Today 1984,5(8):244–248.CrossRef 11. Uhlen M, Guss B, Nilsson B, Gatenbeck S, Philipson L, Lindberg M: Complete sequence of the staphylococcal gene encoding protein A. A gene evolved through multiple duplications. J Biol Chem 1984,259(3):1695–1702.PubMed 12. Fournier B, Philpott DJ: Recognition of Staphylococcus Selleckchem MLN2238 aureus by the innate immune system. Clin Microbiol Rev 2005,18(3):521–540.PubMedCentralPubMedCrossRef 13. Strommenger B, Braulke C, Heuck very D, Schmidt C, Pasemann B, Nubel U, Witte W: spa Typing of Staphylococcus aureus as a Frontline Tool in Epidemiological Typing. J Clin Microbiol 2008,46(2):574–581.PubMedCentralPubMedCrossRef 14. Baum C, Haslinger-Loffler B, Westh H, Boye K, Peters G, Neumann C, Kahl BC: Non-spa-typeable clinical Staphylococcus aureus strains are naturally occurring protein A mutants. J Clin Microbiol 2009,47(11):3624–3629.PubMedCentralPubMedCrossRef 15. Palmqvist

N, Foster T, Tarkowski A, Josefsson E: Protein A is a virulence factor in Staphylococcus aureus arthritis and septic death. Microb Pathog 2002,33(5):239–249.PubMedCrossRef 16. Patel AH, Kornblum J, Kreiswirth B, Novick R, Foster TJ: Regulation of the protein A-encoding gene in Staphylococcus aureus. Gene 1992,114(1):25–34.PubMedCrossRef 17. Patel AH, Nowlan P, Weavers ED, Foster T: Virulence of protein A-deficient and alpha-toxin-deficient mutants of Staphylococcus aureus isolated by allele replacement. Infect Immun 1987,55(12):3103–3110.PubMedCentralPubMed 18. Poston SM, Glancey GR, Wyatt JE, Hogan T, Foster TJ: Co-elimination of mec and spa genes in Staphylococcus aureus and the effect of agr and protein A production on bacterial adherence to cell monolayers. J Med Microbiol 1993,39(6):422–428.PubMedCrossRef 19.

Genetics 2007,176(3):1567–1577.PubMedCrossRef

43. Giglio MP, Hunter T, Bannister JV, Bannister WH, Hunter GJ: The manganese superoxide dismutase gene of Caenorhabditis elegans. Biochem Mol Biol Int 1994,33(1):37–40.PubMed 44. Petriv OI, Rachubinski RA: Lack of peroxisomal catalase causes a progeric phenotype in Caenorhabditis elegans. J Biol Chem 2004,279(19):19996–20001.PubMedCrossRef 45. Gilbert HF: Molecular Quisinostat order and cellular aspects of thiol-disulfide exchange. Adv Enzymol Relat Areas Mol Biol 1990, 63:69–172.PubMed 46. Powis G, Montfort WR: Properties and biological activities of thioredoxins. Annu Rev Biophys Biomol Struct 2001, 30:421–455.PubMedCrossRef 47. Jee C, Vanoaica L, Lee J, Park BJ, Ahnn J: Thioredoxin is related to life span GS-1101 nmr regulation and oxidative stress response in Caenorhabditis elegans. Genes Cells 2005,10(12):1203–1210.PubMedCrossRef 48. Miranda-Vizuete A, Gonzalez

JC, Gahmon G, Burghoorn J, Navas P, Swoboda P: Lifespan decrease in a Caenorhabditis elegans mutant lacking TRX-1, a thioredoxin expressed in ASJ sensory neurons. FEBS Lett 2006,580(2):484–490.PubMedCrossRef 49. Felix MA, Ashe A, Piffaretti J, Wu G, Nuez I, Belicard T, Jiang Y, Zhao G, Franz CJ, Goldstein LD, et al.: Natural and experimental infection of Caenorhabditis nematodes by novel viruses related NSC 683864 nmr to nodaviruses. PLoS Biol 2011,9(1):e1000586.PubMedCrossRef 50. Hahm JH, Kim S, Paik YK: GPA-9 is a novel regulator of innate immunity against Escherichia coli foods in adult Caenorhabditis elegans. Aging Cell 2011,10(2):208–219.PubMedCrossRef 51. Kawli T, He F, Tan MW: It takes nerves to fight infections: insights on neuro-immune interactions from C. elegans. Dis Model Mech 2010,3(11–12):721–731.PubMedCrossRef 52. Kawli T, Tan MW: Levetiracetam Neuroendocrine signals modulate the innate immunity of Caenorhabditis elegans through insulin signaling. Nat Immunol 2008,9(12):1415–1424.PubMedCrossRef 53. Kawli T, Wu C, Tan MW: Systemic and cell intrinsic roles of Gqalpha signaling in the regulation of innate immunity, oxidative stress, and longevity

in Caenorhabditis elegans. Proc Natl Acad Sci USA 2010,107(31):13788–13793.PubMedCrossRef 54. Avery L: The genetics of feeding in Caenorhabditis elegans. Genetics 1993,133(4):897–917.PubMed 55. Millet AC, Ewbank JJ: Immunity in Caenorhabditis elegans. Curr Opin Immunol 2004,16(1):4–9.PubMedCrossRef 56. Ewbank JJ, Barnes TM, Lakowski B, Lussier M, Bussey H, Hekimi S: Structural and functional conservation of the Caenorhabditis elegans timing gene clk-1. Science 1997,275(5302):980–983.PubMedCrossRef 57. Kayser EB, Sedensky MM, Morgan PG: The effects of complex I function and oxidative damage on lifespan and anesthetic sensitivity in Caenorhabditis elegans. Mech Ageing Dev 2004,125(6):455–464.PubMedCrossRef 58.

In all of these environments, the most ubiquitous species are Rhodotorula laryngis and Cr. victoriae.

On the other hand, C. sake, D. fristingensis, G. antarctica and Sp. salmonicolor have been APO866 clinical trial isolated only in the Southern Cone (South American glaciers and Antarctica). This work reports DAPT mouse for the first time the isolation of Cryptococcus gastricus, Cryptococcus gilvescens, D. fristingensis and Leucosporidiella creatinivora from an Antarctic region. Also isolated was W. anomalus, which is not generally found in cold regions. During molecular analysis of the yeasts, most isolates assigned to the same species possessed identical D1/D2 and ITS sequences. Thus, combining these rDNA regions is a useful technique for rapid identification and typing of yeasts, as others have suggested [14, 20, 21]. However, the isolates identified as Leuconeurospora sp. were 0.7% and 0.9% different in their D1/D2 (578 bp) and ITS (534 bp) sequences, respectively.

Similarly, the isolates identified as D. fristingensis exhibited identical D1/D2 (456 bp) sequences, but their ITS (479 bp) sequences were markedly different (4.4%), and their overlap was punctuated with several gaps. Furthermore, given the physiological differences between isolates that are identical or similar at molecular level, strongly support that the definitions of yeast species must be supplemented by classical characterizations. Most yeast isolates showed lipase activity, consistent with a previous report in which all of the filamentous fungi from BCKDHA Antarctica displayed this activity [22]. Among the find more “cold loving” yeasts, lipase activity

has been described in Pseudozyma antarctica[23], Leucosporidium antarcticum[24] and in species of Cryptococcus and Rhodotorula[25]. Unlike this last-mentioned study, we detected lipase activity in R. laryngis also. Lipase activity has also been described in W. anomalus from tropical environments [26]. The least common extracellular activity was xylanase, observed only in the D. fristingensis isolate. Although this activity has been previously described in Cryptococcus species [27, 28], no xylanase activity was observed in the Cryptococcus isolates identified here. Consistent with our results, protease, amylase and esterase extracellular activities have been reported in several yeast species isolated from cold and tropical environments [24–26, 29–33]. However, we present the first report of extracellular amylase activity in Le. creatinivora, H. watticus, Leuconeurospora sp. and D. fristingensis. In addition to Mrakia and Rhodotorula species, for which extracellular pectinase activity has been described [33], we detected pectinase activity in species of Wickerhamomyces, Metschnikowia, Dioszegia, Leucosporidiella and Candida.

The comparative

soil metaproteomics revealed that learn more Sugarcane ratooning induced changes in the expression levels of soil proteins originated from the plants, microbes and fauna. A majority of up-regulated plant proteins were found to be related to carbohydrate and amino acid metabolism and stress response, while most of up-regulated microbial proteins were involved in membrane transport and signal transduction. In conclusion, sugarcane ratooning practice induced great changes in the soil enzyme activities, the catabolic diversity of microbial community and the expression level of soil proteins. These changes were found to influence the biochemical processes in the rhizosphere ecosystem and mediated the interactions between plants and soil microbes. The soil proteins identified in our study are almost certainly a small part of the diversity of proteins that were expressed by the plants SAR302503 and soil microbial Natural Product Library research buy communities. Yet, environmental metaproteomics is a powerful tool to study plant-microbe interactions in soil. Methods Site

description and soil sampling The sugarcane cultivar ‘Gan-nang’ was used in this study. The study plots were completely randomized and located at the experimental farm (26°09′N, 119°23′E) of Ministry of Agriculture Key Laboratory for Sugarcane Genetic Improvement, Fujian Agriculture and Forestry University, Fuzhou, P. R. China. The first site (defined as ‘RS’) was a field used for ratoon sugarcane cultivation, in which sugarcane was newly planted on February 15, 2009 and then ratooned in 2010. The second site (defined as ‘NS’) was a field kept fallow in 2009 and then used for newly planted sugarcane cultivation on February 15, 2010. The field with no sugarcane crop (bare fallow) during the entire experimental period of 2 years was used as a control (defined as ‘CK’). These three different treatments (‘CK’, ‘NS’ and ‘RS’) were organized within a single field site and under the same field management conditions during the entire experimental period. Three replicates were taken for each treatment.

Approximately, 150 grams of soil samples from 3 cultivation patterns were obtained from 5 random locations on each plot second in September 15, 2010. Soil sampling of all three treatments was carried out at the same time in order to minimize the effect of year-to-year environmental variability. The plot samples were mixed to make composite samples. The intact roots were carefully uprooted with a forked spade and shaken to remove loosely attached soil. The rhizospheric soil tightly attached to the roots was collected and then sieved through 2 mm mesh to remove plant roots, leaf remains, insects, etc. The fresh soil samples were immediately used for soil enzyme and BIOLOG analysis. For protein extraction, the soil samples were dried at 70°C for 2 h, pulverized in a mortar, and sieved through a 0.45 mm mesh to extract soil proteins.

In the renal circulation the vessels are end arteries and so it is usually sufficient to block the branch feeding the see more bleeding site. In the liver a rich collateral circulation

means that this approach may not be ideal and embolising the vessels on both sides of the bleeding, so called ‘closing the front and back door!’ might be better. This can Fedratinib sometimes be achieved by passing beyond the bleeding point with the microcatheter and deploying a coil, then withdrawing proximal to the haemorrhage and deploying a second coil. Table 1 Embolic materials TEMPORARY PERMANENT GELFOAM SLURRY COILS OR MICROCOILS (OFTEN FIBRED TO SPEED THE THROMBOTIC EFFECT) AUTOLOGOUS CLOT PARTICLES   OCCLUSION DEVICES   GLUE   ONYX If it proves impossible to obtain a superselective position close to the bleeding site then the choice is between proximal vessel embolisation with an occlusion device or larger coil to decrease haemostatic pressure at the bleeding site (good for splenic bleeding but prevents a second embolisation attempt if bleeding recurs) EPZ015938 in vivo or the use of particles or

gel foam to pass into the distal circulation, blocking smaller vessels. Use of particles runs a higher risk of ischaemic damage than superselective coil embolisation and therefore a temporary agent is often preferable. If using particles then larger sizes (500 μm diameter) are preferred as this leaves the capillary bed the potential to revascularise later from collaterals. Onyx (ev3, Irvine, California,

USA) is a polymer dissolved in dimethyl sulphoxide (DMS0) which is ZD1839 purchase delivered as a liquid but becomes solid when in contact with blood. It takes time to prepare and deliver and is therefore less useful in the acute situation, but in the context of prevention of delayed haemorrhage it can be extremely useful as it can be deployed from a microcatheter proximal to a target. From the point of injection it will follow even tiny vessels distally to fill a pseudo aneurysm and continue on beyond, shutting both front and back doors without necessitating manipulation through the lesion with a microcatheter and wire. Figure 2 demonstrates embolisation of multiple hepatic artery aneurysms with onyx. Figure 2 a) A patient with vasculitic hepatic artery aneurysms presented following minor trauma. Axial contrast enhanced CT demonstrates haematoma around a pseudoaneurysm (arrow) indicating that this is the likely cause of recent haemodynamic instability. b) 3D volume rendered reconstruction demonstrates 3 aneurysms arising from a branch of the left hepatic artery (arrows). The right hepatic artery arose from the SMA. c) Selective arteriogram of the coeliac axis with standard catheter after 2 aneurysms had been embolised with onyx (ev3, Irvine, CA, USA). The cast of the onyx is demonstrated, and some distal embolisation (arrow) of onyx. d) A microcatheter is demonstrated within the final bleeding aneurysm (arrow).

CrossRef 8. Volfkovich YM, Sosenkin VE, Bagotzky VS: Structural and wetting properties of fuel cell components. J Power Sources 2010, 195:5429.CrossRef 9. Volfkovich YM, Sakars AV, Volinsky AA: Application of the standard porosimetry method for nanomaterials. Int J Nanotechnol

2005, 2:292.CrossRef 10. Volfkovich YM, Bagotzky VS: The method of standard porosimetry: 1. Principles and possibilities. J Power Sources 1994, 48:327.CrossRef 11. Volfkovich YM, Bagotzky VS, Sosenkin VE, Blinov IA: The standard contact porosimetry. Colloids Surf A: Physicochem Eng Aspect 2001, 187–188:349.CrossRef Belinostat 12. Szczygieł J: Optimising the porous structure of heterogeneous reforming catalysts with a globular model of the grain. Comp Chem Eng 2011, 35:2334.CrossRef 13. Gierak A, Leboda R, Tracz E: Topography and morphology of the carbon deposit obtained by pyrolysis of methylene chloride on a silica gel surface. J Analyt Appl Pyrolysis 1988, 13:89.CrossRef

14. Leboda R, Mendyk E, Gierak A, Tertykh VA: Hydrothermal modification of silica gels (xerogels) 2. Effect of the duration of treatment on their porous structure. Colloids and Surfaces A: Physicochem. Eng Aspect 1995, 105:191.CrossRef 15. Jones FE, Schoonover RM: Handbook of Mass Measurements. London: CRC Press; 2002.CrossRef 16. Helfferich F: Ion Exchange. New York: Dover; 1995. 17. Berezina NP, Kononenko NA, Dyomina OA, Gnusin NP: Characterization of ion-exchange membrane materials: properties vs structure. Adv Colloid

Epigenetics Compound Library interface Sci 2008, 139:3.CrossRef 18. Brinker CJ, Scherer GW: Sol–Gel Science: The Physics and Chemistry Poziotinib chemical structure of Sol–Gel Process. Amsterdam: Elsevier; 1990. 19. Alves-Rosa MA, Martins L, Pulcinelli SH, Santilli CV: Design of microstructure of zirconia foams from the emulsion template properties. Soft Matter 2013, 9:550.CrossRef 20. Guinier A, Fournet G: Small-Angle Scattering of X-Rays. New York: Wiley; 1955. L-NAME HCl 21. Fagherazzi G, Ploizzi S, Bettinelli M, Speghini A: Yttria-based nano-sized powders: a new class of fractal materials obtained by combustion synthesis. J Mater Res 2000, 15:586.CrossRef 22. Sastry PU, Sen D, Mazumder S, Chandrasekaran S: Fractal behavior of nanocrystalline ceria–yttria solid solution. J Solid State Chem 2003, 176:57.CrossRef 23. Volfkovich YM: Influence of the electric double layer on the internal interface in an ion exchanger on its electrochemical and sorption properties. Soviet Electrochemistry 1984, 20:621. 24. Robinson RA, Stokes RH: Electrolyte Solutions. Mineola NY: Dover; 2002. 25. Walsh F: A First Course in Electrochemical Engineering. London: Alresford Press; 1993. 26. Parsons R: Handbook of Electrochemical Constants. London: Butterworth Scientific Publications; 1959. Competing interests The authors declare that they have no competing interests.

8 LSA1735 lsa1735 Putative cobalt ABC transporter, membrane-spanning subunit     -0.6 LSA1736 lsa1736 Putative cobalt

ABC transporter, ATP-binding subunit -0.6     LSA1737 lsa1737 Putative cobalt ABC transporter, ATP-binding subunit -0.7     LSA1838 lsa1838 Putative metal ion ABC transporter, membrane-spanning subunit     -0.5 LSA1839 lsa1839 Putative metal ion ABC transporter, substrate-binding lipoProtein Tyrosine Kinase inhibitor protein precursor     -0.6 Amino acid transport and metabolism Transport/binding of amino CP673451 chemical structure acids LSA0125 lsa0125 Putative amino acid/polyamine transport protein 0.6     LSA0189 lsa0189 Putative amino acid/polyamine transport protein     -0.7 LSA0311 lsa0311 Putative glutamate/aspartate:cation symporter -1.1   -1.0 LSA1037 lsa1037 Putative Apoptosis inhibitor amino acid/polyamine transport protein 1.0 0.8 0.5 LSA1219 lsa1219 Putative cationic amino acid transport protein 0.7     LSA1415 lsa1415 Putative amino acid/polyamine transport protein 1.1   0.7 LSA1424 lsa1424 Putative L-aspartate transport protein -1.4 -0.9 -1.2 LSA1435 lsa1435 Putative amino acid:H(+) symporter 1.0   0.8 LSA1496 lsa1496 Putative glutamine/glutamate ABC transporter, ATP-binding subunit   1.2   LSA1497 lsa1497

Putative glutamine/glutamate ABC transporter, membrane-spanning/substrate-binding subunit precursor   0.7   Transport/binding of proteins/peptides LSA0702 oppA Oligopeptide ABC transporter, substrate-binding lipoprotein precursor   1.3 1.0 LSA0703 oppB Oligopeptide ABC transporter, membrane-spanning subunit   0.8 0.8 LSA0704 oppC

Oligopeptide LY294002 ABC transporter, membrane-spanning subunit   1.8 1.0 LSA0705 oppD Oligopeptide ABC transporter, ATP-binding subunit   1.2 1.1 LSA0706 oppF Oligopeptide ABC transporter, ATP-binding subunit   1.2 1.2 Protein fate LSA0053 pepO Endopeptidase O 0.6     LSA0133 pepR Prolyl aminopeptidase 1.5     LSA0226 pepN Aminopeptidase N (lysyl-aminopeptidase-alanyl aminopeptidase)     -0.7 LSA0285 pepF1 Oligoendopeptidase F1     -0.7 LSA0320 pepD3 Dipeptidase D-type (U34 family)   -0.8 -0.5 LSA0424 pepV Xaa-His dipeptidase V (carnosinase) 1.6     LSA0643 pepX X-Prolyl dipeptidyl-aminopeptidase 0.6     LSA0888 pepT Tripeptide aminopeptidase T 0.6     LSA1522 pepS Aminopeptidase S 0.5     LSA1686 pepC1N Cysteine aminopeptidase C1 (bleomycin hydrolase) (N-terminal fragment), authentic frameshift   1.6   LSA1688 pepC2 Cysteine aminopeptidase C2 (bleomycin hydrolase)   0.7   LSA1689 lsa1689 Putative peptidase M20 family 1.0   1.1 Metabolism of amino acids and related molecules LSA0220_c dapE Succinyl-diaminopimelate desuccinylase -1.4   -1.5 LSA0316 sdhB L-serine dehydratase, beta subunit (L-serine deaminase) -0.7     LSA0370* arcA Arginine deiminase (arginine dihydrolase) 1.9     LSA0372* arcC Carbamate kinase 0.5     LSA0463 lsa0463 Putative 2-hydroxyacid dehydrogenase -0.7     LSA0509 kbl 2-amino-3-ketobutyrate coenzyme A ligase (glycine acetyltransferase) 1.