, UK, 100 Z-Scheme posters, and 100 books entitled Music of Sunlight by Dr. Wilbert Veit, USA. We are grateful to Mahendra Rathore for the photographs provided for this Report. We also refer the readers to a web site (http://​www.​schooloflifescie​ncesdauniv.​org) for further information on this conference. References Blankenship RE (2007) 2007 Awards of the International Society Selleckchem VX-689 of Photosynthesis Research (ISPR). Photosynth Res 94:179–181CrossRef Eaton-Rye JJ (2007a) Celebrating

Govindjee’s 50 years in Photosynthesis Research and his 75th birthday. Photosynth Res 93(1–3):1–5PubMedCrossRef Eaton-Rye JJ (2007b) Snapshots of the Govindjee lab from the late 1960s to the late 1990s, and beyond. Photosynth Res 94(2–3):153–178CrossRef Govindjee (2004) Robert Emerson and Eugene Rabinowitch: understanding photosynthesis. In: Hoddeson L (ed) No boundaries. University of Illinois Press, Urbana, pp 181–194 Rebeiz CA, Benning C, Bohnert J, Hoober JK, Portis AR (2007) Govindjee was honored with the first lifetime achievement award, and Britta Forster and coworkers, with the first annual paper prize of Rebeiz foundation AMN-107 cell line for basic research. Photosynth Res 94(1):147–151CrossRef Strasser RJ, Srivastava A, Govindjee

(1995) Polyphasic chlorophyll a fluorescence transient in plants and cyanobacteria. Photochem Photobiol 61:32–42CrossRef”
“Professor emeritus Dr. rer. nat. habil. Paul Hoffmann (see Fig. 1) passed away after a serious illness on July 10, 2008, at the age of 77. The scientific community, in the field of photosynthesis research and at the Humboldt-Universität zu Berlin (Humboldt University Berlin), has lost a dedicated researcher, teacher, and colleague. Fig. 1 Professor Paul Hoffmann in his office in 1988. Courtesy of E. Helmer Paul Hoffmann was born in Sattel, a small

Silesian village near Grünberg (now Zielona Góra, Poland), in 1931, as the only son mafosfamide (he had four younger sisters) of a farmer and forestry worker. As a result of World War II, the family had to leave this region and migrated to Western Pomerania in 1945. Here, Paul Hoffmann attended a secondary school in Franzburg and passed the “Abitur” in 1951. In the same year he began to study see more biology at the University of Greifswald, one of the oldest universities in Germany, earlier focussing on botany, in particular, plant physiology. In 1956, he started his scientific career as an “Assistent” (scientific assistant) at the Botanical Institute, headed by the well-known plant physiologist Heinrich Borriss (1909–1985). At this time, he switched the field of his research activities from earlier electrophysiological studies on leaves of Elodea, the topic of his diploma thesis (completed in 1956), to problems related to photosynthesis.

PubMed 16. Drummond SE, Crombie NE, Cursiter MC, Kirk TR: Evidence that eating frequency is inversely related to body weight status in male, but not female, non-obese adults reporting valid dietary intakes. Int J Obes Relat Metab Disord 1998, 22 (2) : 105–12.PubMedCrossRef 17. Ruidavets JB, Bongard V, Bataille V, Gourdy P, Ferrieres

J: Eating frequency and body fatness in middle-aged men. Int J Obes Relat Metab Disord 2002, 26 (11) : 1476–83.PubMedCrossRef 18. Ma Y, Bertone ER, Stanek EJ, Reed GW, Herbert JR, Cohen NL, Merriam PA, Ockene IS: Association between eating patterns and obesity in a free-living US adult population. Am J Epidemiol 2003, 158 (1) : 85–92.PubMedCrossRef 19. Franko DL, Striegel-Moore RH, Thompson D, BMS202 chemical structure Affenito SG, Schreiber GB, Daniels SR, Crawford PB: The relationship between meal frequency and body mass index in black and white adolescent girls: more is less. Int J Obes (Lond) 2008, 32 (1) : 23–9.CrossRef 20. Dreon DM, Frey-Hewitt B, Ellsworth N, Williams PT, Terry RB, Wood PD: Dietary fat:carbohydrate ratio and obesity in middle-aged men. Am J Clin Nutr 1988, 47 (6) : 995–1000.PubMed 21. Kant AK, Schatzkin A, Graubard BI, Ballard-Barbach R: Frequency of eating occasions and weight change in the NHANES I Epidemiologic Follow-up Study. Int J Obes Relat Metab Disord 1995, 19 (7) : 468–74.PubMed 22. Summerbell CD, Moody RC,

Shanks J, Stock MJ, Geissler C: Relationship between feeding pattern and body mass index in 220 free-living people in four age groups. Eur J Clin Nutr 1996, 50 Rabusertib research buy (8) : 513–9.PubMed 23. Andersson I, Rossner S: Meal patterns in obese and normal weight Lck men: the ‘Gustaf’ study. Eur J Clin Nutr 1996, 50 (10) : 639–46.PubMed 24. Crawley H, Summerbell C: Feeding frequency and BMI among teenagers aged 16–17 years. Int J Obes Relat Metab Disord 1997, 21 (2) : 159–61.PubMedCrossRef 25. Titan SM, Welch A, Luben R, Oakes S, Day N, Khaw KT: Frequency of eating and concentrations of serum cholesterol in the Norfolk

population of the European prospective investigation into cancer (EPIC-Norfolk): cross https://www.selleckchem.com/products/gw3965.html sectional study. Bmj 2001, 323 (7324) : 1286–8.PubMedCrossRef 26. Berteus Forslund H, Lindroos AK, Sjöström L, Lissner L: Meal patterns and obesity in Swedish women-a simple instrument describing usual meal types, frequency and temporal distribution. Eur J Clin Nutr 2002, 56 (8) : 740–7.PubMedCrossRef 27. Pearcey SM, de Castro JM: Food intake and meal patterns of weight-stable and weight-gaining persons. Am J Clin Nutr 2002, 76 (1) : 107–12.PubMed 28. Yannakoulia M, Melistas L, Solomou E, Yiannakouris N: Association of eating frequency with body fatness in pre- and postmenopausal women. Obesity (Silver Spring) 2007, 15 (1) : 100–6.CrossRef 29. Duval K, Strychar I, Cyr MJ, Prudhomme D, Rabasa-Lhoret R, Doucet E: Physical activity is a confounding factor of the relation between eating frequency and body composition. Am J Clin Nutr 2008, 88 (5) : 1200–5.PubMed 30.

These results raise the question of whether metformin also has a beneficial effect on the endometrium in women with PCOS and EC. A recent study from our laboratory has shown that a combination of metformin and oral contraceptives is capable of reverting early-stage EC into normal endometria in addition to improving insulin resistance in women with PCOS [49]. Although this is a MK5108 solubility dmso promising result, we note that our preliminary report must be taken with caution and that further research is certainly needed before co-treatment with metformin and oral contraceptives can be recommended in clinical practice. Having said that, the promising results with metformin raise the questions

of whether metformin alone affects endometrial function in women with PCOS, how a positive effect of metformin combined with oral contraceptives could inhibit the development of atypical endometrial selleck chemical selleck screening library hyperplasia and EC at the molecular level, how our findings

affect treatment guidelines for PCOS women with and without insulin resistance, whether metformin as a general anti-cancer drug inhibits EC development in women regardless of whether they also have PCOS, and whether metformin can prevent EC development in women without endometrial pathology but only with risk factors or in women with pre-malignant endometrial disease. Promising evidence for the use of metformin in women with EC It is still far too early to say whether there is any future for metformin as a means of preventing or treating EC in women, and there are no clinical trials assessing single metformin treatment of recurrent or metastatic

EC. However, metformin, in combination with mammalian target of rapamycin (mTOR) inhibitors, seems to be effective in inhibiting EC progression in women with recurrent or metastatic EC [67] and it is also associated with improved recurrence-free survival and overall survival in postmenopausal Bortezomib nmr women with diabetes mellitus and EC [34]. Possible mechanisms of metformin in the endometrium Expression and localization of OCTs and MATEs Metformin is highly hydrophilic and readily crosses the plasma membrane [68]. However, there is convincing evidence that organic cation transporters (OCTs) are actively involved in the cellular uptake of metformin and that multidrug and toxin extrusion proteins (MATEs) contribute to the excretion of metformin [69]. Although OCT1–3 and MATE1 and 2 have been identified in humans and rodents [69] – and although OCTs and MATEs are often co-localized in vivo [70] – the actual distributions of OCT1–3 and MATE1 and 2 have been shown to be species and tissue specific [69, 70]. The human endometrium, the specialized lining of the uterus, is composed mainly of luminal and glandular epithelial cells along with fibroblastic cells that make up the stroma [71].

Function Symbol Name S Score Chemokine LY3039478 CCL20 Chemokine (C-C Motif) Ligand 20 13.542   CXCL3 Chemokine (C-X-C Motif) Ligand 3 11.866   CXCL2 Chemokine (C-X-C Motif) Ligand

2 11.742   IL8 Interleukin 8 11.393   CXCL1 Chemokine (C-X-C Motif) Ligand 1 11.096   CXCL6 Chemokine (C-X-C Motif) Ligand 6 10.79   CCL2 Chemokine (C-C Motif) Ligand 2 5.294 TNF/NFkB superfamily TNFAIP3 Tumor Necrosis Factor, Alpha-Induced Protein 3 11.678   IKBA Nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor, alpha 10.956   TNIP1 TNFAIP3 Interacting Protein 1 9.344   TNFAIP2 Tumor Necrosis Factor, Alpha-Induced Protein 2 8.293   OPTN Optineurin 6.487   IL32 Interleukin 32 6.12   NFKB1 Nuclear Factor Kappa B (P105) 5.355 Apoptosis/Cell death UBD Ubiquitin D 11.647   BIRC3 Baculoviral IAP Repeat-Containing 3 11.063   CFLAR CASP8 And FADD-Like Apoptosis Regulator 6.224   SGK Serum/Glucocorticoid Regulated Kinase 5.705   ISG20 www.selleckchem.com/products/blasticidin-s-hcl.html Interferon Stimulated Exonuclease Gene 20 kda 5.575 Extracellular Matrix MMP7 Matrix Metallopeptidase 7 (Matrilysin, Uterine) 9.812   SDC4 Syndecan 4 (Amphiglycan, Ryudocan) 8.923

  LAMA3 Laminin, Alpha 3 5.824   LAMC2 Laminin, Gamma 2 5.32 Folate receptor FOLR1 Folate Receptor 1 (Adult) 8.963 Redox state SOD2 Superoxide Dismutase 2, Mitochondrial 8.879   TXNRD1 Thioredoxin Reductase 1 6.378 Cell Epoxomicin purchase adhesion ICAM1 Intercellular Adhesion Molecule 1 8.879   FNDC3B Fibronectin Type III Domain Containing 3B 5.851 Cytokines/Receptors IFNGR1 Interferon Gamma Receptor 1 8.403   CSF2 Colony Stimulating Factor

2 5.101   PLAT Plasminogen Activator, Tissue 7.464   SERPINB2 Serpin Peptidase Inhibitor 2 6.319 Energy metabolism ATP1B1 Atpase, Na+/K+ Transporting, Beta 1 Peptide 7.184 Nuclear transcription CEBPD CCAAT/Enhancer Binding Protein Delta 6.708   RARRES1 Retinoic Acid Receptor Responder 6.179 Antibacterial LCN2 Lipocalin 2 6.6   PI3 Peptidase Inhibitor 3 (Elafin) 5.057 Cell signalling CDC42 Cell Division Cycle 42 7.28   DUSP5 Dual Specificity Phosphatase 5 6.541   SGPL1 Sphingosine-1-Phosphate Alectinib Lyase 1 6.242 Cytoskeleton/cytokinesis TPM1 Tropomyosin 1 5.689   PDLIM5 PDZ And LIM Domain 5 5.169 Transcription, protein synthesis and export SF3B1 Splicing Factor 3b, Subunit 1, 5.146   UGCG UDP-Glucose Ceramide Glucosyltransferase 5.388 Cell cycle PLK2 Polo-Like Kinase 2 5.55 Structural SYNGR3 Synaptogyrin 3 5.133 Antigen presentation TAP1 Transporter 1, ATP-Binding Cassette 5.207 Chemokine and cytokine analyses Cultured cells were prepared and induced as described above. After 6 h. incubation, the media was removed and stored at -20°C until examined using a Coulter-Alter Flow Cytometer in conjunction with a BD cytometric bead array human inflammation kit according to manufacturer’s instructions (BD Biosciences, Oxford, UK).

They also claimed that the mechanism of AgNP toxicity may involve a combination of both physical and chemical interactions. There was a direct correlation between the toxicity of AgNPs and their surface charge. The more negative the zeta value, the less toxic are the AgNPs to bacillus

species. The zeta potential of AgNPs/citrate was −38 mV, whereas the zeta potential of AgNPs/PVP and AgNPs/BPEI were −10 and +40 mV, respectively [20]. Therefore, the various stabilizers for AgNPs affect not only on the stability but also on the antibacterial activity of AgNP colloid [1, 14, 20, 21]. In this study, we prepared four colloidal AgNP solutions at a concentration of 1-mM Ag in different stabilizers, namely PVP, PVA, alginate, and sericin with EGFR targets the same concentration of 0.5% (w/v). Subsequently, GSK2126458 molecular weight the antibacterial activity of these colloidal AgNP solutions was investigated. To further demonstrate the effect of AgNPs on antibacterial activity and apply the development in practice,

the AgNPs were added into a handwash solution, and the antibacterial activity was also tested. Methods Material Pure-grade AgNO3 was purchased from Shanghai Chemical Reagent Co., Shanghai, China The pharmaceutical grade PVP K90 was a product from Merck, Darmstadt, Germany. PVA 217 was a product of Kuraray, Tokyo, Japan. Alginate was a product of Hayashi Pure Chemical Industries, Osaka, Japan, and sericin was purchased from Sigma, St. Louis, MO, USA. Distilled water was used throughout the preparation of colloidal AgNP solutions. The strain of Escherichia coli ATCC 6538 was provided by the University of Medical Pharmacy, Ho Chi Minh City. The INK 128 research buy Luria-Bertani (LB) medium purchased form Himedia, Mumbai, India contains 10 g triptone, 5 g yeast extract, 10 g sodium chloride, and 1 L distilled water. Synthesis of AgNPs Four colloidal solution samples of 1-mM AgNPs stabilized in 0.5% (w/v) stabilizers of PVP, PVA, alginate, and sericin were prepared by gamma Co-60 irradiation method as described in our previous papers [9, 13]. Briefly,

the stabilizers were dissolved in water to reach a concentration of 0.5%. AgNO3 was then dissolved in the above prepared solution to obtain a final concentration from of 1-mM Ag+. The mixture was poured into glass bottles with plastic caps. The irradiation of these solutions at dose of 6 kGy for the synthesis of AgNPs was carried out on a Co-60 irradiator with a dose rate of approximately 1.2 kGy/h at VINAGAMMA Center, Ho Chi Minh City. Absorption spectra of the irradiated AgNP solutions with dilution by water to 0.1-mM AgNPs were taken on an UV-vis spectrophotometer, Jasco V-630 (Easton, MD, USA). The AgNP sizes were measured using a transmission electron microscope (TEM; JEM 1010, JEOL, Tokyo, Japan).

Careful investigation of structure-activity relationships may eventually allow design of optimised antimicrobial compounds with high activity and CP-690550 concentration minimal side effects [9–15]. Many AMPs fold into an amphipathic structure, and it is believed that this topology enables

pore formation or disintegration of bacterial cell membranes leading to bacterial cell death. The amphipathic properties usually include cationic patches that promote interaction with the anionic bacterial membrane as well as hydrophobic patches that favor integration into the membrane. Since this is the most common mode of action for AMPs there has been an intense focus on their ability to adapt an amphipathic conformation [16, 17]. In particular, design of peptides with

a high propensity to fold into a helical amphipathic conformation click here has attracted considerable interest [13, 18–20]. We have previously described a synthetic approach for design of α-peptide/β-peptoid chimeras possessing a design with alternating N-alkylated β-alanine (β-peptoid) and α-amino acid units (Figure 1). In addition, preliminary investigations showed that such peptidomimetics constitute a novel subclass of proteolytically stable antimicrobial compounds [21–23]. This design displays chiral unnatural β-peptoid residues that appear to contribute with structure-promoting effects and lipophilicity, while Selleckchem LY2835219 strongly cationic properties and intramolecular hydrogen bonding capacity are introduced via the α-amino acids lysine and/or homoarginine [24]. The precise secondary structure

of these chimeras still remains to be elucidated, nevertheless, circular dichroism (CD) spectroscopy clearly indicates about the presence of some degree of secondary structure [22, 23]. Interestingly, a higher degree of secondary structure was found for analogues containing chiral side chains in the β-peptoid units (i.e. compounds 2 and 3 in Figure 1) as compared to chimeras with achiral β-peptoid residues (i.e. compound 1 in Figure 1) [22], but the effect of this on antibacterial activity remains largely unresolved [23]. Figure 1 Chemical structure of the six α-peptide/β-peptoid chimeras The membrane-destabilizing effects of the chimeras have only been investigated in model liposomes prepared from phosphatidylcholine, a phospholipid found predominantly in eukaryotic cells, and several of the chimeras permeabilized such liposomal membranes [24]. Most studies on membrane activity of antimicrobial peptides have in fact been performed on model membranes [25–28] while the effects on cell membranes of viable bacteria have often not been tested. Also, the effect of membrane permeabilization on killing of bacteria has not been tested [27].

The intensity of GFP expression was quantitated using Image J. Chemotaxis assay Aggregation competent cells were prepared and stimulated with a glass capillary micropipette (Femtotip, Eppendorf, Hamburg, Germany) filled with 0.1 mM cAMP [56]. Time-lapse image series were captured and stored on a computer hard drive at 30 seconds intervals with a CCD camera. The DIAS this website software (Soltech, Oakdale, IA, USA) was used to trace individual cells along image series and determine cell motility parameters [57]. Subcellular fractionation Cells ALK inhibitor were collected by centrifugation and resuspended at a density of 2 × 108 cells/ml in MES buffer (20 mM 2-[N-morpholino]ethane sulfonic acid, 1 mM

EDTA, 250 mM sucrose, pH 6.5) supplemented with a protease inhibitor mixture (Roche Diagnostics, Mannheim, Germany). Cells were lysed

on ice by sonication and light microscopy was performed to ensure that at least 95% of the cells were broken. Cytosolic and particulate fractions were separated by ultracentrifugation (100,000 × g for 30 minutes). Alternatively the cell lysate was centrifuged to equilibrium on a discontinuous sucrose gradient atop an 84% (w/v) cushion. After centrifugation fractions were collected from the top and analyzed in Western blots or used for measurement of acid and alkaline phosphatase activities as described [52]. F-actin determination Chemoattractant BIBW2992 mouse induced F-actin formation in aggregation competent cells was quantitated as described [58]. Briefly, cells were resuspended at 2 × 107 cells/ml in Soerensen buffer and starved for 6 to 8 hours. Cells were stimulated with 1 μM cAMP and 50 μl samples were taken at various time points. The reaction was terminated by addition of 450 μl stop solution (3.7% formaldehyde, 0.1% Triton X-100, 0.25 μM TRITC-phalloidin in 20 mM potassium phosphate, 10 mM PIPES, 5 mM EGTA, 2 mM MgCl2 pH 6.8). After staining for 1 hour, samples were centrifuged for 5 minutes at 15,000 × g. Pellets were extracted with 1 ml methanol for 16 hours and fluorescence (540/565 nm) was read in a PTI fluorimeter

(Photon Technology Intl., Seefeld, Germany). Essentially the same procedure was used to determine the F-actin content of vegetative cells except that fluorescence values were Aprepitant normalized to the total protein content of the samples as determined with the method of Lowry. Rac1 activation assay The Rac1 activation assay was performed as described [31]. Cells were starved for 6 to 8 hours in Soerensen buffer at a cell density of 1 × 107/ml, concentrated to 4 × 107/ml and stimulated with 1 μM cAMP. Aliquots were immediately removed and lysed in 5 × lysis buffer (50 mM HEPES pH 7.5, 2.5% Triton X-100, 500 mM NaCl, 100 mM MgCl2, 1 mM DTT) containing protease inhibitors at 4°C. The cell lysate was then mixed with glutathione-Sepharose beads previously loaded with bacterially expressed CRIB of Dictyostelium WASP fused to GST.

In addition to increased national demand for land due to increased MK-8931 purchase population and consumption patterns, cross-border large-scale land acquisitions have recently taken place in capital-rich but food-poor countries (often oil-rich and water poor countries), such as

Mozambique, Demographic Republic of Congo or Zambia. These transactions, sometimes referred to as ‘the rush for Africa’s land’ or a ‘land grab’, are receiving increased attention from researchers, institutions and the media (Lambin and Meyfroidt 2011; World Bank 2011). Our results further show that implementation of a narrowly focussed REDD + mechanism could result in unintended MLN2238 perverse land-cover change and carbon leakage. Similarly, potentially harmful side effects for some biodiversity areas have been reported (Miles and Kapos 2008; Strassburg et al. 2010). Our REDD scenarios illustrate a critical argument for the ongoing discussion within the UNFCCC: if REDD + does not include, or is not complemented by, initiatives to reduce the need for conversion of additional natural ecosystems, the effectiveness of REDD + on climate change mitigation will be significantly compromised. Our results show that 96 % of forested land in developing

countries is characterised by a medium, BI 2536 solubility dmso high or very high likelihood of conversion, and many biodiversity hotspots in Latin America, Africa and Southeast Asia present likelihood

Thalidomide of further conversion. Our BAU scenario also suggests that forests will have three times higher conversion rates than other ecosystems, therefore suggesting that forests are indeed the first priority for policies addressing land-use and land-cover change. However, our results also show that if no measures to reduce demand for land are implemented, the net mitigation impact of REDD (whether 100 or 50 % effective) can be reduced significantly by emissions arising from land-use and land-cover change “forced” into non-forested land, or “cross-biome leakage”. This might be a conservative estimate, as it ignores the likely greater land requirements given the lower agricultural yield potential of some of these alternative ecosystems. Similarly, Galford et al. (2010) investigated greenhouse gas emissions from alternative futures of deforestation and agricultural management in the southern Amazon and concluded a need for taking into account post-clearing emissions and a need for of an integrated assessment of land-cover changes. In agreement with others (e.g. Galford et al. 2010) we also highlight, however, that avoided deforestation remains an important strategy for minimising future greenhouse emissions and that REDD + mitigation impacts are substantial, particularly where land-cover change is avoided on tropical forest peatlands.

Simona Kamenšek is a recipient of a Ph.D grant from ARRS. References 1. Selleck S63845 Dubnau D, Losick R: Bistability in bacteria. Mol Microbiol 2006, 61:564–572.PubMedCrossRef 2. Veening JW, Smits WK, Kuipers OP: Bistability, epigenetics, and bet-hedging in bacteria. Annu Rev Microbiol 2008, 62:193–210.PubMedCrossRef 3. Mrak P, Podlesek Z, van Putten JPM, Žgur-Bertok D: Heterogeneity in expression of the Escherichia coli colicin K activity gene cka is controlled by the SOS system and stochastic factors. Mol Gen Genet

2007, 277:391–401. 4. Keren I, Kaldalu N, Spoering A, Wang Y, Lewis K: Persister cells and tolerance to antimicrobials. FEMS Microbiol Lett 2004, 230:13–18.PubMedCrossRef 5. Friedberg EC, Walker GC, Siede W, Wood RD, Schultz RS, Ellenberger T: DNA repair and mutagenesis. LY2606368 cost 2nd edition. ASM press, Washington, DC; 2006–957. 6. Radman M: Phenomenology of an inducible mutagenic DNA repair pathway in Escherichia coli : SOS repair hypothesis. In Molecular and environmental aspects of mutagenesis.

Edited by: Prakash L, Sherman F, Miller C, Lawrence C, Tabor HW. Springfield, Illinois: Charles C. Thomas Publisher; 1974:128–142. 7. Erill I, Escribano M, Campoy S, Barbé J: In silico analysis I-BET151 cell line reveals substantial variability in the gene contents of the gamma proteobacteria LexA-regulon. Bioinformatics 2003, 19:2225–2236.PubMedCrossRef 8. Cascales E, Buchanan SK, Duché D, Kleanthous C, Lloubès R, Postle K, Riley M, Slatin S, Cavard D: Colicin biology. Microbiol Mol

Biol Rev 2007, 71:158–229.PubMedCrossRef 9. Kirkup BC, Riley MA: Antibiotic mediated antagonism leads to a bacterial game of rock-paper-scissors in vivo. Nature 2004, 428:412–414.PubMedCrossRef 10. Walker D, Rolfe M, Thompson A, Moore GR, James R, Hinton CD, Kleanthous C: Transcriptional profiling of colicin-induced cell death of Escherichia coli MG1655 identifies potential mechanisms by which bacteriocins promote bacterial diversity. J Bacteriol 2004, 186:866–869.PubMedCrossRef 11. Braun V, Schaller K, Wabl MR: Isolation, characterization and action of colicin M. C59 in vivo Antimicrob Agents Chemother 1974, 5:520–533.PubMed 12. Harkness RE, Braun V: Inhibition of lipopolysaccharide O-antigen synthesis by colicin-M. J Biol Chem 1989, 264:14716–14722.PubMed 13. Harkness RE, Braun V: Colicin-M inhibits peptidoglycan biosynthesis by interfering with lipid carrier recycling. J Biol Chem 1989, 264:6177–6182.PubMed 14. Lu FM, Chak KF: Two overlapping SOS boxes in ColE operons are responsible for the viability of cells harboring the Col plasmid. Mol Gen Genet 1996, 251:407–411.PubMedCrossRef 15. Harkness RE, Ölschläger T: The biology of colicin-M. FEMS Microbiol Rev 1991, 8:27–41.PubMedCrossRef 16.

Photochem Photobiol 4:641–655CrossRef Krasnovsky AA (1972) The fragments of the photosynthetic electron transport chain in model systems. Biophys J 12:749–763PubMedCentralPubMedCrossRef Krasnovsky AA (1977) Photoproduction of hydrogen in photosynthetic systems. In: Belinostat mouse Castellani A (ed) Research in photobiology. Plenum Press, New York, p 361CrossRef Krasnovsky AA (1979) Photoproduction

of hydrogen in photosynthetic and artificial systems. In: Barber J (ed) Topics in photosynthesis, vol 3. Elsevier, Amsterdam, pp 281–298 Krasnovsky Semaxanib research buy AA (1985a) The model of photosynthetic electron transfer. Physiol Veg 23:611–618 Krasnovsky AA (1985b) Problems of formation and storage of sun energy in photosynthesis. Bull USSR Acad Sci (in Russ); see pp 3–16 Krasnovsky AA (1992) Excited chlorophyll and related problems. Photosynth Res 33:177–193PubMedCrossRef Krasnovsky AA (1997) (published posthumously) A lifetime journey with photosynthesis. Compr Biochem 40:205–252 [This article was

first written in Russian by Acad. A.A. Krasnovsky, and then translated in English, and published by his son A.A. Krasnovsky, Jr.] Krasnovsky AA, Bystrova MI (1986) Self-assembly of chlorophyll aggregated structures. Biosystems 12:181–194CrossRef Krasnovsky AA, Nikandrov VV, Brin GP, Gogotov IN, Oshchepkov VP (1975) Photoproduction of hydrogen in solutions of chlorophyll, NADH

and chloroplasts. Dokl Akad Nauk SSSR (in Russ) 225:231–233 Krasnovsky AA, Brin GP, Nikandrov VV (1976) Photoreduction Mizoribine cost of oxygen and photoproduction of hydrogen on inorganic photocatalysts. Dokl Akad Nauk SSSR (in Russ) 229:990–993 Krasnovsky AA, Semenova AN, Nikandrov VV (1982) Chlorophyll-containing liposomes: photoreduction of methyl viologen and photoproduction of hydrogen. Photobiochem Photobiophys 4:227–232 Litvin FF, Krasnovsky AA (1957) Investigation by fluorescence spectra of intermediate stages of chlorophyll biosynthesis in etiolated leaves. Dokl AN SSSR (Russ) 117:106–109 Nuijs AM, Shuvalov VA, van Gorkom HJ, Plijter JJ, Duysens LNM (1986) Picosecond absorbance difference spectroscopy on the primary reactions and the antenna-excited states in photosystem I particles. Edoxaban Biochim Biophys Acta 850:310–318CrossRef Porret D, Rabinowitch E (1937) Reversible bleaching of chlorophyll. Nature 140:321–322CrossRef Rabinowitch E (1945, 1951, 1956) Photosynthesis and related processes. Volume I (1945), Volume II. Part A (1951); and Volume II, Part B (1956). Interscience Publishers, New York [Eectronic files of these books are available free at http://​www.​life.​illinois.​edu/​govindjee/​g/​Books.​html and another web site. Source: «Biodiversity Heritage library» on the internet] Rabinowitch E, Weiss J (1936) Reversible oxidation and reduction of chlorophyll.