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Probability of survival before 12 months of age by birth status, Nigeria 2003.

Lung: Tracheobronchial amyloidosis

Effects of the kLa on CHO-IgG cell cultures. The kLa was measured in 1-L OSR with working volumes from 200 to 600 mL (a). The CHO-IgG cells were cultivated in 1-L OSR in 200 (⃝), 300 (⃞), 400 (∆), 500 (●) and 600 mL (■). The DO (b), pH (c) and viable cell density (d) were measured at the times indicated. The shaking diameter was 5 cm.

Effects of the kLa on CHO-IgG cell cultures. The kLa was measured in 1-L OSR with working volumes from 200 to 600 mL (a). The CHO-IgG cells were cultivated in 1-L OSR in 200 (⃝), 300 (⃞), 400 (∆), 500 (●) and 600 mL (■). The DO (b), pH (c) and viable cell density (d) were measured at the times indicated. The shaking diameter was 5 cm.

Evolution of the amount of microbial cells (a), the extracellular lipase activity (b), and the LIP2 expression (c) in function of the reactor configuration

Specific rate for the extracellular lipase production by Y. lipolytica cultivated in a classical 20-L bioreactor (reference reactor) and in a P-SDR under different recirculation flow rates (corresponding each to a mean residence time in the non-mixed part of the reactor)

Specific rate for the extracellular lipase production by Y. lipolytica cultivated in a classical 20-L bioreactor (reference reactor) and in a P-SDR under different recirculation flow rates (corresponding each to a mean residence time in the non-mixed part of the reactor)

On/off cycle scheme for C-SDR (a stochastic scheme and b constant cycles scheme)

Evolution of the amount of microbial cells (a), the extracellular lipase activity (b), and the LIP2 expression (c) in function of the reactor configuration

Specific rate for the extracellular lipase production by Y. lipolytica cultivated in different reactor configuration (see Fig. for more details about these configurations)

Evolution of the amount of microbial cells (a), the extracellular lipase activity (b), and the LIP2 expression (c) in function of the reactor configuration

Specific rate for the extracellular lipase production by Y. lipolytica cultivated in different reactor configuration (see Fig. for more details about these configurations)

Comparison of a culture conducted in a P-SDR with classical pH regulation (a) where the normal yeast cell shape is observed and in a P-SDR conducted with the pH regulation performed at the level of non-mixed part (b) where filamentation is observed

Comparison of a culture conducted in a P-SDR with classical pH regulation (a) where the normal yeast cell shape is observed and in a P-SDR conducted with the pH regulation performed at the level of non-mixed part (b) where filamentation is observed

Intracellular growth ofL. pneumophilastrains in Jurkat cells and CD4+T cells. Jurkat cells were infected with L. pneumophila strains AA100jm and dotO mutant (MOI of 100) (A) or Corby and flaA mutant (MOI of 100) (B). (C) CD4+ T cells were also infected with Corby (MOI of 50). At the indicated time points after infection, the CFU was enumerated. Data are mean ± SD of triplicate cell cultures. (D and E) Direct fluorescent antibody staining of L. pneumophila strains. Jurkat cells were infected with AA100jm and dotO mutant (MOI of 100) (D) or Corby and flaA mutant (MOI of 100) (E) for 24 h. Jurkat cells were stained with fluorescein-conjugated anti-L. pneumophila antibody. Original magnification, ×600.

Intracellular growth ofL. pneumophilastrains in Jurkat cells and CD4+T cells. Jurkat cells were infected with L. pneumophila strains AA100jm and dotO mutant (MOI of 100) (A) or Corby and flaA mutant (MOI of 100) (B). (C) CD4+ T cells were also infected with Corby (MOI of 50). At the indicated time points after infection, the CFU was enumerated. Data are mean ± SD of triplicate cell cultures. (D and E) Direct fluorescent antibody staining of L. pneumophila strains. Jurkat cells were infected with AA100jm and dotO mutant (MOI of 100) (D) or Corby and flaA mutant (MOI of 100) (E) for 24 h. Jurkat cells were stained with fluorescein-conjugated anti-L. pneumophila antibody. Original magnification, ×600.

L. pneumophila-induced IL-8 mRNA expression in T cells. (A) Total RNA was extracted from Jurkat cells infected with AA100jm, dotO mutant, Corby, or flaA mutant (MOI of 100) for the indicated time intervals and used for RT-PCR. (B) Jurkat cells were infected with the indicated concentrations of L. pneumophila for 4 h. Total RNA was extracted and used for RT-PCR. (C) Total RNA was extracted from CD4+ T cells infected with Corby (MOI of 50) for 3 h and used for RT-PCR. (D) Jurkat cells were infected with live L. pneumophila Corby or flaA mutant (MOI of 100) for 4 h or incubated with L. pneumophila under the indicated treatment for 4 h. PFA, paraformaldehyde. Total RNA was extracted and used for RT-PCR. Representative examples of three experiments with similar results.

L. pneumophila-induced IL-8 mRNA expression in T cells. (A) Total RNA was extracted from Jurkat cells infected with AA100jm, dotO mutant, Corby, or flaA mutant (MOI of 100) for the indicated time intervals and used for RT-PCR. (B) Jurkat cells were infected with the indicated concentrations of L. pneumophila for 4 h. Total RNA was extracted and used for RT-PCR. (C) Total RNA was extracted from CD4+ T cells infected with Corby (MOI of 50) for 3 h and used for RT-PCR. (D) Jurkat cells were infected with live L. pneumophila Corby or flaA mutant (MOI of 100) for 4 h or incubated with L. pneumophila under the indicated treatment for 4 h. PFA, paraformaldehyde. Total RNA was extracted and used for RT-PCR. Representative examples of three experiments with similar results.

TLR mRNA expression in T cells. (A) Expression of TLR mRNA in Jurkat cells. Total RNA was extracted from Jurkat cells and used for RT-PCR. (B) CD4+ T cells were infected without or with Corby (MOI of 50) for 3 h. Total RNA was extracted from CD4+ T cells and used for RT-PCR. Representative examples of three experiments with similar results.

TLR mRNA expression in T cells. (A) Expression of TLR mRNA in Jurkat cells. Total RNA was extracted from Jurkat cells and used for RT-PCR. (B) CD4+ T cells were infected without or with Corby (MOI of 50) for 3 h. Total RNA was extracted from CD4+ T cells and used for RT-PCR. Representative examples of three experiments with similar results.

IL-8 production from Jurkat cells during infection withL. pneumophilastrains. (A) Jurkat cells were infected with the indicated L. pneumophila strains at an MOI of 100 for the indicated time periods. (B) Jurkat cells were infected with the varying concentrations of the indicated L. pneumophila strains for 24 h. (C) CD4+ T cells were infected without or with Corby for 3 h. IL-8 concentrations in the supernatants were determined by ELISA. Data are mean ± SD values collected in three experiments.

IL-8 production from Jurkat cells during infection withL. pneumophilastrains. (A) Jurkat cells were infected with the indicated L. pneumophila strains at an MOI of 100 for the indicated time periods. (B) Jurkat cells were infected with the varying concentrations of the indicated L. pneumophila strains for 24 h. (C) CD4+ T cells were infected without or with Corby for 3 h. IL-8 concentrations in the supernatants were determined by ELISA. Data are mean ± SD values collected in three experiments.

L. pneumophilainfection activates IL-8 promoter in Jurkat cells. (A) Jurkat cells transfected with -1481-luc were infected with L. pneumophila Corby at the indicated MOI values for 6 h. The luciferase activities were expressed relative to cells transfected with -1481-luc followed by mock-infection. *, P < 0.01, as determined by the Student t test. (B) Reporter assay using plasmid DNA containing serial deletions in 5'-flanking region of the IL-8 gene. (Left) Schematic representation of the IL-8 reporter constructs, demonstrating locations of several known binding sites for transcription factors. (Right) The indicated luciferase reporter constructs were transfected into Jurkat cells, and the cells were subsequently infected with Corby strain (MOI of 100) for 6 h. The activities are expressed relative to that of cells transfected with -50-luc followed by mock-infection, which was defined as 1. The numbers on the bars depict fold induction relative to the basal level measured in uninfected cells. (C) Relative importance of AP-1, NF-IL-6, and NF-κB binding sites in IL-8 promoter. Wild-type and mutated plasmids were transfected into Jurkat cells. The transfected cells were infected without or with Corby. The activities are expressed relative to that of cells transfected with -133-luc followed by mock-infection, which was defined as 1. Luciferase activities were normalized based on the Renilla luciferase activity from phRL-TK. The numbers on the bars depict fold induction relative to the basal level measured in uninfected cells. LUC, luciferase. Graph data are mean ± SD values of three experiments.

L. pneumophilainfection activates IL-8 promoter in Jurkat cells. (A) Jurkat cells transfected with -1481-luc were infected with L. pneumophila Corby at the indicated MOI values for 6 h. The luciferase activities were expressed relative to cells transfected with -1481-luc followed by mock-infection. *, P < 0.01, as determined by the Student t test. (B) Reporter assay using plasmid DNA containing serial deletions in 5'-flanking region of the IL-8 gene. (Left) Schematic representation of the IL-8 reporter constructs, demonstrating locations of several known binding sites for transcription factors. (Right) The indicated luciferase reporter constructs were transfected into Jurkat cells, and the cells were subsequently infected with Corby strain (MOI of 100) for 6 h. The activities are expressed relative to that of cells transfected with -50-luc followed by mock-infection, which was defined as 1. The numbers on the bars depict fold induction relative to the basal level measured in uninfected cells. (C) Relative importance of AP-1, NF-IL-6, and NF-κB binding sites in IL-8 promoter. Wild-type and mutated plasmids were transfected into Jurkat cells. The transfected cells were infected without or with Corby. The activities are expressed relative to that of cells transfected with -133-luc followed by mock-infection, which was defined as 1. Luciferase activities were normalized based on the Renilla luciferase activity from phRL-TK. The numbers on the bars depict fold induction relative to the basal level measured in uninfected cells. LUC, luciferase. Graph data are mean ± SD values of three experiments.

NF-κB signal is essential for flagellin-dependent activation of the IL-8 promoter byL. pneumophila. (A) Flagellin is required for induction of NF-κB binding activity. Nuclear extracts from Jurkat cells infected with Corby or flaA mutant were mixed with IL-8 NF-κB probe (MOI, 100:1). (B) Sequence specificity of NF-κB binding activity and characterization of proteins that bound to the NF-κB binding site. Competition assays were performed with nuclear extracts from cells infected with Corby for 2 h. 100-fold excess amounts of competitor were added (lanes 3 to 5). A supershift assay in the same nuclear extracts also was performed. Antibodies (Ab) were added (lanes 6 to 10). Arrows indicate specific complexes, while arrowheads indicate the DNA binding complexes supershifted. (C) Flagellin-induced p65 translocation. Cells were infected with Corby or flaA mutant. Nuclear extracts were subjected to immunoblotting. (D) Flagellin activates NF-κB through the classical and alternative pathways. Cells were infected with Corby or flaA mutant. Lysates were subjected to immunoblotting. (E) Overexpression of dominant negative mutants inhibits L. pneumophila-induced activation of the IL-8 promoter. Cells were transfected with -133-luc and the mutant plasmids and then infected with Corby for 6 h. The solid bar indicates luciferase activity of -133-luc and empty vector without infection. Activity is expressed relative to that of cells transfected with -133-luc with further Corby infection, which was defined as 100. Data are means ± SD values of three experiments. dn, dominant negative. *, P < 0.05; **, P < 0.001 (by Student t test).

NF-κB signal is essential for flagellin-dependent activation of the IL-8 promoter byL. pneumophila. (A) Flagellin is required for induction of NF-κB binding activity. Nuclear extracts from Jurkat cells infected with Corby or flaA mutant were mixed with IL-8 NF-κB probe (MOI, 100:1). (B) Sequence specificity of NF-κB binding activity and characterization of proteins that bound to the NF-κB binding site. Competition assays were performed with nuclear extracts from cells infected with Corby for 2 h. 100-fold excess amounts of competitor were added (lanes 3 to 5). A supershift assay in the same nuclear extracts also was performed. Antibodies (Ab) were added (lanes 6 to 10). Arrows indicate specific complexes, while arrowheads indicate the DNA binding complexes supershifted. (C) Flagellin-induced p65 translocation. Cells were infected with Corby or flaA mutant. Nuclear extracts were subjected to immunoblotting. (D) Flagellin activates NF-κB through the classical and alternative pathways. Cells were infected with Corby or flaA mutant. Lysates were subjected to immunoblotting. (E) Overexpression of dominant negative mutants inhibits L. pneumophila-induced activation of the IL-8 promoter. Cells were transfected with -133-luc and the mutant plasmids and then infected with Corby for 6 h. The solid bar indicates luciferase activity of -133-luc and empty vector without infection. Activity is expressed relative to that of cells transfected with -133-luc with further Corby infection, which was defined as 100. Data are means ± SD values of three experiments. dn, dominant negative. *, P < 0.05; **, P < 0.001 (by Student t test).

Bay 11-7082 blocksL. pneumophila-induced NF-κB activation and IL-8 secretion. Jurkat cells were pretreated with or without Bay 11-7082 (20 μM) for 1 h prior to L. pneumophila Corby infection and subsequently were infected with Corby (MOI, 100:1) for the indicated times. Cell lysates were prepared and subjected to immunoblotting with the indicated antibodies (A) and nuclear extracts from the harvested cells were analyzed for NF-κB and Oct-1 (B). Jurkat cells were pretreated with the indicated concentrations of Bay 11-7082 for 1 h prior to Corby infection and subsequently infected with Corby (MOI, 100:1) for 4 h (C) and 24 h (D). IL-8 mRNA expression on the harvested cells was analyzed by RT-PCR (C) and the supernatants were subjected to ELISA to determine IL-8 secretion (D). Data in (A)-(C) are representative examples of three independent experiments with similar results. Data are mean ± SD from three experiments.

Bay 11-7082 blocksL. pneumophila-induced NF-κB activation and IL-8 secretion. Jurkat cells were pretreated with or without Bay 11-7082 (20 μM) for 1 h prior to L. pneumophila Corby infection and subsequently were infected with Corby (MOI, 100:1) for the indicated times. Cell lysates were prepared and subjected to immunoblotting with the indicated antibodies (A) and nuclear extracts from the harvested cells were analyzed for NF-κB and Oct-1 (B). Jurkat cells were pretreated with the indicated concentrations of Bay 11-7082 for 1 h prior to Corby infection and subsequently infected with Corby (MOI, 100:1) for 4 h (C) and 24 h (D). IL-8 mRNA expression on the harvested cells was analyzed by RT-PCR (C) and the supernatants were subjected to ELISA to determine IL-8 secretion (D). Data in (A)-(C) are representative examples of three independent experiments with similar results. Data are mean ± SD from three experiments.

L. pneumophilaactivates AP-1 signal through flagellin. (A) Time course of AP-1 activation in Jurkat cells infected with L. pneumophila, evaluated by EMSA. Nuclear extracts from Jurkat cells, infected with Corby or flaA mutant (MOI, 100:1), for the indicated time periods, were mixed with IL-8 AP-1 32P-labeled probe. (B) Sequence specificity of AP-1 binding activity and characterization of AP-1/CREB/ATF proteins that bound to the AP-1 binding site of the IL-8 gene. Competition assays were performed with nuclear extracts from Jurkat cells infected with Corby for 2 h. Where indicated, 100-fold excess amounts of each specific competitor oligonucleotide were added to the reaction mixture with labeled probe AP-1 (lanes 2 to 4). A supershift assay of AP-1 DNA binding complexes in the same nuclear extracts also was performed. Where indicated, appropriate antibodies (Ab) were added to the reaction mixture before the addition of the 32P-labeled probe (lanes 6 to 17 and 19). Arrows indicate specific complexes, while arrowheads indicate the DNA binding complexes supershifted by antibodies. (C) Jurkat cells were infected with Corby or flaA mutant for the indicated time periods. Cell lysates were prepared and subjected to immunoblotting with the indicated antibodies. Data are representative examples of three independent experiments with similar results.

L. pneumophilaactivates AP-1 signal through flagellin. (A) Time course of AP-1 activation in Jurkat cells infected with L. pneumophila, evaluated by EMSA. Nuclear extracts from Jurkat cells, infected with Corby or flaA mutant (MOI, 100:1), for the indicated time periods, were mixed with IL-8 AP-1 32P-labeled probe. (B) Sequence specificity of AP-1 binding activity and characterization of AP-1/CREB/ATF proteins that bound to the AP-1 binding site of the IL-8 gene. Competition assays were performed with nuclear extracts from Jurkat cells infected with Corby for 2 h. Where indicated, 100-fold excess amounts of each specific competitor oligonucleotide were added to the reaction mixture with labeled probe AP-1 (lanes 2 to 4). A supershift assay of AP-1 DNA binding complexes in the same nuclear extracts also was performed. Where indicated, appropriate antibodies (Ab) were added to the reaction mixture before the addition of the 32P-labeled probe (lanes 6 to 17 and 19). Arrows indicate specific complexes, while arrowheads indicate the DNA binding complexes supershifted by antibodies. (C) Jurkat cells were infected with Corby or flaA mutant for the indicated time periods. Cell lysates were prepared and subjected to immunoblotting with the indicated antibodies. Data are representative examples of three independent experiments with similar results.

MAPKs activation byL. pneumophilathrough flagellin and inhibition ofL. pneumophila-induced CREB and ATF1 activation and IL-8 transcription by p38 inhibitor. (A) Jurkat cells were infected with Corby or flaA mutant (MOI, 100:1), and lysates were subjected to immunoblotting. Cells were pretreated with the indicated concentrations of SB203580 for 1 h prior to infection and subsequently infected with Corby (MOI, 100:1) for 4 h (B) and for 6, 8, 12, or 24 h (C). IL-8 mRNA expression on the harvested cells was analyzed by RT-PCR (B) and the supernatants were subjected to ELISA to determine IL-8 secretion (C). (D) Cells were transfected with -133-luc and then pretreated with the indicated concentrations of SB203580 for 1 h prior to infection. They were infected subsequently with Corby for 6 h. Luciferase (LUC) activity was assayed. The solid bar indicates LUC activity of -133-luc without infection. (E) Cells were transfected with -133-luc and dominant negative mutants and then infected with Corby for 6 h. The solid bar indicates LUC activity of -133-luc without infection. All values were calculated as the change (n-fold) in induction values relative to the basal level measured in uninfected cells. Data are mean ± SD of three experiments. (F) Cells were pretreated with or without SB203580 (50 μM) for 1 h prior to infection and subsequently were infected with Corby (MOI, 100:1). Lysates were subjected to immunoblotting. dn, dominant negative.

MAPKs activation byL. pneumophilathrough flagellin and inhibition ofL. pneumophila-induced CREB and ATF1 activation and IL-8 transcription by p38 inhibitor. (A) Jurkat cells were infected with Corby or flaA mutant (MOI, 100:1), and lysates were subjected to immunoblotting. Cells were pretreated with the indicated concentrations of SB203580 for 1 h prior to infection and subsequently infected with Corby (MOI, 100:1) for 4 h (B) and for 6, 8, 12, or 24 h (C). IL-8 mRNA expression on the harvested cells was analyzed by RT-PCR (B) and the supernatants were subjected to ELISA to determine IL-8 secretion (C). (D) Cells were transfected with -133-luc and then pretreated with the indicated concentrations of SB203580 for 1 h prior to infection. They were infected subsequently with Corby for 6 h. Luciferase (LUC) activity was assayed. The solid bar indicates LUC activity of -133-luc without infection. (E) Cells were transfected with -133-luc and dominant negative mutants and then infected with Corby for 6 h. The solid bar indicates LUC activity of -133-luc without infection. All values were calculated as the change (n-fold) in induction values relative to the basal level measured in uninfected cells. Data are mean ± SD of three experiments. (F) Cells were pretreated with or without SB203580 (50 μM) for 1 h prior to infection and subsequently were infected with Corby (MOI, 100:1). Lysates were subjected to immunoblotting. dn, dominant negative.

SP600125 inhibitsL. pneumophila-induced IL-8 expression and secretion. Jurkat cells were pretreated with the indicated concentrations of SP600125 for 1 h prior to L. pneumophila Corby infection and subsequently infected with Corby (MOI, 100:1) for 4 h (A) and 24 h (B). IL-8 mRNA expression on harvested cells was analyzed by RT-PCR (A) and the supernatants were subjected to ELISA to determine IL-8 secretion (B). Data are mean ± SD of three experiments. (C) Jurkat cells were pretreated with or without SP600125 (20 μM) for 1 h prior to L. pneumophila Corby infection and subsequently infected with Corby (MOI, 100:1) for the indicated times. Cell lysates were prepared and subjected to immunoblotting with the indicated antibodies. Data in (A) and (C) are representative examples of three independent experiments with similar results.

SP600125 inhibitsL. pneumophila-induced IL-8 expression and secretion. Jurkat cells were pretreated with the indicated concentrations of SP600125 for 1 h prior to L. pneumophila Corby infection and subsequently infected with Corby (MOI, 100:1) for 4 h (A) and 24 h (B). IL-8 mRNA expression on harvested cells was analyzed by RT-PCR (A) and the supernatants were subjected to ELISA to determine IL-8 secretion (B). Data are mean ± SD of three experiments. (C) Jurkat cells were pretreated with or without SP600125 (20 μM) for 1 h prior to L. pneumophila Corby infection and subsequently infected with Corby (MOI, 100:1) for the indicated times. Cell lysates were prepared and subjected to immunoblotting with the indicated antibodies. Data in (A) and (C) are representative examples of three independent experiments with similar results.

Diagnosis and BAL

BAL pattern, most important diagnoses, remarks

Survival free of myocardial infarction

Demographics

Coronary angiography/intervention

Stenting/results after stenting

In-hospital outcome

Follow-up

Amino acid sequence alignment of representative members of the mammalian and the plant metallothionein (MT) families. The plant MTs are additionally divided into four subfamilies comprising the MT1, MT2, MT3, and Ec proteins. Cys residues are highlighted with a black background, aromatic amino acids with a grey background. His residues are accentuated with a black frame. Sequences denoted with an asterisk represent exceptions to the otherwise highly conserved Cys distribution pattern within a plant MT subfamily. In Arabidopsis thaliana MT1A, the linker region is additionally reduced to just seven amino acids

Amino acid sequence alignment of representative members of the mammalian and the plant metallothionein (MT) families. The plant MTs are additionally divided into four subfamilies comprising the MT1, MT2, MT3, and Ec proteins. Cys residues are highlighted with a black background, aromatic amino acids with a grey background. His residues are accentuated with a black frame. Sequences denoted with an asterisk represent exceptions to the otherwise highly conserved Cys distribution pattern within a plant MT subfamily. In Arabidopsis thaliana MT1A, the linker region is additionally reduced to just seven amino acids

The two metal–thiolate cluster structures formed with divalent metal ions in, e.g., the vertebrate MTs: a M 4 II Cys11 cluster of the α-domain and b M 3 II Cys9 cluster of the β-domain. Only the coordinating sulfur atoms of the Cys residues are shown

The two metal–thiolate cluster structures formed with divalent metal ions in, e.g., the vertebrate MTs: a M 4 II Cys11 cluster of the α-domain and b M 3 II Cys9 cluster of the β-domain. Only the coordinating sulfur atoms of the Cys residues are shown

Probable β-sheet arrangements within the linker regions of plant MTs. a The entire linker sequence forms a single long antiparallel β-sheet structure (cyan) and hence a rather rigid scaffold to bring the Cys-rich regions (long, grey terminal tubes) into proximity for joint cluster formation (metal ions are depicted as blue spheres). The amino acids of the linker region form a more flexible structure with four shorter β-sheets, which allow a single cluster arrangement (b) or a dumbbell-shaped arrangement with two clusters (c)

Probable β-sheet arrangements within the linker regions of plant MTs. a The entire linker sequence forms a single long antiparallel β-sheet structure (cyan) and hence a rather rigid scaffold to bring the Cys-rich regions (long, grey terminal tubes) into proximity for joint cluster formation (metal ions are depicted as blue spheres). The amino acids of the linker region form a more flexible structure with four shorter β-sheets, which allow a single cluster arrangement (b) or a dumbbell-shaped arrangement with two clusters (c)

a The dumbbell-shaped arrangement similar to the arrangement in Fig. a can be transformed in a jackknife-like movement into a single domain cluster form upon binding of an additional metal ion (red sphere). b This transformation can be reversed upon removal of the additional metal ion. The grey arrows show the direction of movement of the Cys-rich regions and the red arrow shows the release of the additional metal ion

a The dumbbell-shaped arrangement similar to the arrangement in Fig. a can be transformed in a jackknife-like movement into a single domain cluster form upon binding of an additional metal ion (red sphere). b This transformation can be reversed upon removal of the additional metal ion. The grey arrows show the direction of movement of the Cys-rich regions and the red arrow shows the release of the additional metal ion

Amino acid sequence alignment of representative members of the plant Ec subfamily with Cys and His residues highlighted as in Fig. . The residues comprising the N-terminal γ-domain and the C-terminal βE-domain are indicated with an orange ellipsoid and a green ellipsoid, respectively. Below this, the NMR solution structures of the two domains of wheat Ec-1 are shown; no information about the relative orientation of these two domains to each other is available. ZnII ions are depicted as blue spheres and parts of the coordinating Cys and His side chains are shown in stick mode

Amino acid sequence alignment of representative members of the plant Ec subfamily with Cys and His residues highlighted as in Fig. . The residues comprising the N-terminal γ-domain and the C-terminal βE-domain are indicated with an orange ellipsoid and a green ellipsoid, respectively. Below this, the NMR solution structures of the two domains of wheat Ec-1 are shown; no information about the relative orientation of these two domains to each other is available. ZnII ions are depicted as blue spheres and parts of the coordinating Cys and His side chains are shown in stick mode

β-sheet and α-helix contents of selected plant MTs as predicted for the linker regions or determined with IR, Raman, or NMR spectroscopy for the entire proteins

Two examples of Philips SSL devices. In each of the examples left-side picture is the device and right-side picture is the exploded view of the same device. (a) SSL retrofit lamp and (b) SSL lamp for halogen lamp sockets

Two examples of Philips SSL devices. In each of the examples left-side picture is the device and right-side picture is the exploded view of the same device. (a) SSL retrofit lamp and (b) SSL lamp for halogen lamp sockets

(a) An SSL module general block diagram. The three major parts of an SSL module are represented: optical part, SSL driver, and interconnection. (b) An example of an SSL device [32, 33]

SSL driver and LED board of a commercial retrofit lamp without its external casing. The driver part supports just the basic function to drive the LED part. (a) Top part of the boards; the optical part is one high brightness LED. (b) Bottom part of the boards

SSL driver and LED board of a commercial retrofit lamp without its external casing. The driver part supports just the basic function to drive the LED part. (a) Top part of the boards; the optical part is one high brightness LED. (b) Bottom part of the boards

The block diagram of an SSL driver with its basic functions. Regardless of the input block, the rest of SSL driver building blocks are the same. (a) When the input power is alternative current (AC) the input block is an AC to DC converter. (b) When the input power is direct current (DC) the input block is an inverse polarity protection circuit

The block diagram of an SSL driver with its basic functions. Regardless of the input block, the rest of SSL driver building blocks are the same. (a) When the input power is alternative current (AC) the input block is an AC to DC converter. (b) When the input power is direct current (DC) the input block is an inverse polarity protection circuit

The block of an SSL driver with basic functions and additional functions

An example of an SSL device with additional functions such as microcontroller, sensors, and wireless communication capability. (a) Complete device with optical part and SSL driver and (b) just the SSL driver

An example of an SSL device with additional functions such as microcontroller, sensors, and wireless communication capability. (a) Complete device with optical part and SSL driver and (b) just the SSL driver

Three examples for different application fields of SSL devices. (a) Indoor lighting, (b) outdoor street lighting, (c) automotive lighting, which in this figure is the headlamp of the car

Two important aspects of an SSL driver: the technology parameters and application-induced criteria. In this figure the details related to “application-induced criteria” are shown. In Fig. the details of “technology parameters” are explained

Two important aspects of an SSL driver: the technology parameters and application-induced criteria. In this figure the details related to “application-induced criteria” are shown. In Fig. the details of “technology parameters” are explained

Two important aspects of an SSL driver: the technology parameters and application-induced criteria. In this figure the details related to “technology parameters” are shown. In Fig. the details of “application-induced criteria” are explained

Two important aspects of an SSL driver: the technology parameters and application-induced criteria. In this figure the details related to “technology parameters” are shown. In Fig. the details of “application-induced criteria” are explained

Generic process of estimating the reliability of an electronic system based on stress and damage model

NA60 data in 158 AGeV In+In collisions. Left panel: invariant mass spectra of unlike sign dimuons (upper histogram), combinatorial background (dashed line), fake signal (dashed-dotted line) and the resulting signal (lower histogram) [20]. Right panel: excess dimuons after subtracting the hadronic cocktail, excluding the ρ, compared to cocktail ρ (thin solid line), π + π − annihilation with an unmodified ρ (dash-dotted line), dropping ρ mass (dashed line) and in-medium ρ broadening (thick solid line) [80].

NA60 data in 158 AGeV In+In collisions. Left panel: invariant mass spectra of unlike sign dimuons (upper histogram), combinatorial background (dashed line), fake signal (dashed-dotted line) and the resulting signal (lower histogram) [20]. Right panel: excess dimuons after subtracting the hadronic cocktail, excluding the ρ, compared to cocktail ρ (thin solid line), π + π − annihilation with an unmodified ρ (dash-dotted line), dropping ρ mass (dashed line) and in-medium ρ broadening (thick solid line) [80].

The NA60 dimuon excess in semi-central In+In collisions at 158 AGeV, integrated over all p T compared to calculations of [83]. The curves represent partial contributions and their sum as indicated in the figure.

The NA60 dimuon excess in semi-central In+In collisions at 158 AGeV, integrated over all p T compared to calculations of [83]. The curves represent partial contributions and their sum as indicated in the figure.

Absolutely normalized excess dimuon mass spectrum corrected for acceptance and reconstruction efficiency, measured by NA60 in In+In collisions at 158 AGeV and compared to theoretical calculations of Renk/Ruppert [83], Hees/Rapp [81, 82] and Dusling/Zahed [84]. Both the data and the calculations are subject to a p T cut of 200 MeV/c on the single muon tracks [6, 85].

Absolutely normalized excess dimuon mass spectrum corrected for acceptance and reconstruction efficiency, measured by NA60 in In+In collisions at 158 AGeV and compared to theoretical calculations of Renk/Ruppert [83], Hees/Rapp [81, 82] and Dusling/Zahed [84]. Both the data and the calculations are subject to a p T cut of 200 MeV/c on the single muon tracks [6, 85].

Invariant mass e + e − spectrum measured by PHENIX in $$\sqrt{{s}_{{}_{NN }}}$$ = 200 GeV minimum bias Au+Au collisions at mid-rapidity. The data are compared to the cocktail of expected yields from light mesons and semi-leptonic open charm decays. Statistical (bars) and systematic (boxes) errors are plotted separately. The bottom panel shows the data to cocktail ratio with the band around 1 representing the systematic uncertainty in the cocktail [49].

Invariant mass e + e − spectrum measured by PHENIX in $$\sqrt{{s}_{{}_{NN }}}$$ = 200 GeV minimum bias Au+Au collisions at mid-rapidity. The data are compared to the cocktail of expected yields from light mesons and semi-leptonic open charm decays. Statistical (bars) and systematic (boxes) errors are plotted separately. The bottom panel shows the data to cocktail ratio with the band around 1 representing the systematic uncertainty in the cocktail [49].

Invariant m T spectrum of the e + e − pair excess (after subtracting the cocktail and the charm contribution) measured in the mass range 0.3 < m ee < 0. 75 GeV/c 2 by PHENIX in $$\sqrt{{s}_{{}_{NN }}}$$ = 200 GeV minimum bias Au+Au collisions at mid-rapidity. The solid line represents the fit to the sum of two exponential functions shown separately by the dashed and dotted lines. Statistical (bars) and systematic (boxes) errors are plotted separately [49].

Invariant m T spectrum of the e + e − pair excess (after subtracting the cocktail and the charm contribution) measured in the mass range 0.3 < m ee < 0. 75 GeV/c 2 by PHENIX in $$\sqrt{{s}_{{}_{NN }}}$$ = 200 GeV minimum bias Au+Au collisions at mid-rapidity. The solid line represents the fit to the sum of two exponential functions shown separately by the dashed and dotted lines. Statistical (bars) and systematic (boxes) errors are plotted separately [49].