@article{BeckerK.2007,
  added-at = {2008-10-14T16:07:18.000+0200},
  author = {Becker, Katja},
  biburl = {http://www.bibsonomy.org/bibtex/2652326609f5ca067f5f6782a7f884d25/nutribiochem},
  interhash = {214bc79e30254fa30d880330cd99356a},
  intrahash = {652326609f5ca067f5f6782a7f884d25},
  journal = {Spiegel der Forschung},
  keywords = {IFZ imported},
  number = 1,
  pages = {42-47},
  timestamp = {2008-10-14T16:07:18.000+0200},
  title = {Molekulare Maschinen und Alterung � der humane Redoxstoffwechsel},
  volume = 24,
  year = 2007
}

@article{BeckerKSchirmerRH.2007,
  added-at = {2008-10-14T16:07:18.000+0200},
  author = {Becker, K. and Schirmer, H. R.},
  biburl = {http://www.bibsonomy.org/bibtex/2ac10738f97d6701e59384add4eee6266/nutribiochem},
  interhash = {77957e387787473165bad2943fb772b2},
  intrahash = {ac10738f97d6701e59384add4eee6266},
  journal = {Biospektrum},
  keywords = {IFZ imported},
  number = 07,
  pages = {138-141},
  timestamp = {2008-10-14T16:07:18.000+0200},
  title = {Antioxidative Enzyme des Malariaerregers als Targets von Bonaria-Medikamenten},
  volume = 02,
  year = 2007
}

@article{Buchholz.2008,
  abstract = {Proliferation of the pathogenic Plasmodium asexual blood stages in host erythrocytes requires an exquisite capacity to protect the malaria parasite against oxidative stress. This function is achieved by a complex antioxidant defence system composed of redox-active proteins and low MW antioxidants. Here, we disrupted the P. berghei plasmoredoxin gene that encodes a parasite-specific 22 kDa member of the thioredoxin superfamily. The successful generation of plasmoredoxin knockout mutants in the rodent model malaria parasite and phenotypic analysis during life cycle progression revealed a non-vital role in vivo. Our findings suggest that plasmoredoxin fulfils a specialized and dispensable role for Plasmodium and highlights the need for target validation to inform drug development strategies.},
  added-at = {2008-10-14T16:07:18.000+0200},
  author = {Buchholz, Kathrin and Rahlfs, Stefan and Schirmer, Heiner R. and Becker, Katja and Matuschewski, Kai},
  biburl = {http://www.bibsonomy.org/bibtex/288be58900ce4b5c3072293d9fbc91bf8/nutribiochem},
  interhash = {872707ee175822f4914a1a0af2d30325},
  intrahash = {88be58900ce4b5c3072293d9fbc91bf8},
  issn = {1932-6203},
  journal = {PLoS ONE},
  keywords = {Animals Base_Sequence Blotting DNA_Primers IFZ Life_Cycle_Stages Messenger Peroxidases Plasmodium_berghei RNA Rats Reverse_Transcriptase_Polymerase_Chain_Reaction Western},
  number = 6,
  pages = {e2474-e2474},
  timestamp = {2008-10-14T16:07:18.000+0200},
  title = {Depletion of Plasmodium berghei plasmoredoxin reveals a non-essential role for life cycle progression of the malaria parasite},
  volume = 3,
  year = 2008
}

@article{Friebolin.20080313,
  abstract = {Plasmodium parasites are exposed to higher fluxes of reactive oxygen species and need high activities of intracellular antioxidant systems providing a steady glutathione flux. As a future generation of dual drugs, 18 naphthoquinones and phenols (or their reduced forms) containing three different linkers between the 4-aminoquinoline core and the redox active component were synthesized. Their antimalarial effects have been characterized in parasite assays using chloroquine-sensitive and -resistant strains of Plasmodium, alone or in drug combination, and in the Plasmodium berghei rodent model. In particular, two tertiary amides 34 and 36 showed potent antimalarial activity in the low nanomolar range against CQ-resistant parasites. The ability to compete both for (Fe (III))protoporphyrin and for chloroquine transporter was determined. The data are consistent with the presence of a carrier for uptake of the short chloroquine analogue 2 but not for the potent antimalarial amide 34, suggestin},
  added-at = {2008-10-14T16:07:18.000+0200},
  author = {Friebolin, Wolfgang and Jannack, Beate and Wenzel, Nicole and Furrer, Julien and Oeser, Thomas and Sanchez, P. Cecilia and Lanzer, Michael and Yardley, Vanessa and Becker, Katja and Davioud-Charvet, Elisabeth},
  biburl = {http://www.bibsonomy.org/bibtex/2b5fd6712f1a844b98b42a4084bc69b44/nutribiochem},
  interhash = {74c6a4dca43d995c6afa6d380908118c},
  intrahash = {b5fd6712f1a844b98b42a4084bc69b44},
  issn = {0022-2623},
  journal = {J Med Chem},
  keywords = {Animals Antimalarials Biological_Transport Cell_Line Combination Drug_Resistance Drug_Therapy Glutathione_Reductase Humans IFZ Inbred_BALB_C Malaria Mice Naphthalenes Parasitic_Sensitivity_Tests Plasmodium_berghei Plasmodium_falciparum Structure-Activity_Relationship Tumor chloroquine},
  number = 5,
  pages = {1260-1277},
  timestamp = {2008-10-14T16:07:18.000+0200},
  title = {Antimalarial dual drugs based on potent inhibitors of glutathione reductase from Plasmodium falciparum},
  volume = 51,
  year = {2008/03/13/}
}

@article{Buchholz.200801,
  abstract = {Methylene blue (MB) has experienced a renaissance mainly as a component of drug combinations against Plasmodium falciparum malaria. Here, we report biochemically relevant pharmacological data on MB such as rate constants for the uncatalyzed reaction of MB at pH 7.4 with cellular reductants like NAD(P)H (k = 4 M(-1) s(-1)), thioredoxins (k = 8.5 to 26 M(-1) s(-1)), dihydrolipoamide (k = 53 M(-1) s(-1)), and slowly reacting glutathione. As the disulfide reductases are prominent targets of MB, optical tests for enzymes reducing MB at the expense of NAD(P)H under aerobic conditions were developed. The product leucomethylene blue (leucoMB) is auto-oxidized back to MB at pH 7 but can be stabilized by enzymes at pH 5.0, which makes this colorless compound an interesting drug candidate. MB was found to be an inhibitor and/or a redox-cycling substrate of mammalian and P. falciparum disulfide reductases, with the kcat values ranging from 0.03 s(-1) to 10 s(-1) at 25 degrees C. Kinetic spectrosco},
  added-at = {2008-10-14T16:07:18.000+0200},
  author = {Buchholz, Kathrin and Schirmer, Heiner R. and Eubel, K. Jana and Akoachere, B. Monique and Dandekar, Thomas and Becker, Katja and Gromer, Stephan},
  biburl = {http://www.bibsonomy.org/bibtex/26df645811ef0bb6960d1c47ce69d8409/nutribiochem},
  interhash = {87286afedf7c4a5ce32c7f9abbc27d55},
  intrahash = {6df645811ef0bb6960d1c47ce69d8409},
  journal = {Antimicrob Agents Chemother},
  keywords = {Aerobiosis Animals Binding_Sites Disulfides Humans Hydrogen-Ion_Concentration IFZ Kinetics Methylene_Blue Oxidation-Reduction Oxidoreductases Plasmodium_falciparum Protozoan_Proteins Substrate_Specificity},
  number = 1,
  pages = {183-191},
  timestamp = {2008-10-14T16:07:18.000+0200},
  title = {Interactions of methylene blue with human disulfide reductases and their orthologues from Plasmodium falciparum},
  volume = 52,
  year = {2008/01//}
}

@article{ISI:000245158500007,
  abstract = {The resistance of the malarial parasite Plasmodium falciparum to
chloroquine represents an emerging problem since neither mode of drug
action nor mechanisms of resistance are fully elucidated. We describe a
protein expression profiling approach by SELDI-TOF-MS as a useful tool
for studying the proteome of malarial parasites. Reproducible and
complex protein profiles of the P. falciparum strains K1, Dd2, HB3 and
3D7 were measured on four array types. Hierarchical clustering led to a
clear separation of the two major subgroups ��resistant" and
��sensitive" as well as of the four parasite strains. Our study
delivers sets of regulated proteins derived from extensive comparative
analyses of 64 P.falciparum protein profiles. A group of 12 peaks
reflecting proteome changes under chloroquine treatment and a set of 10
potential chloroquine resistance markers were defined. Three of these
regulated peaks were preparatively enriched, purified and identified.
They were shown to represent the plasmo},
  added-at = {2008-10-14T16:07:18.000+0200},
  author = {Koncarevic, Sasa and Bogumil, Ralf and Becker, Katja},
  biburl = {http://www.bibsonomy.org/bibtex/26bdd6d5206a79a250d7157bcfc34a724/nutribiochem},
  interhash = {285356bd00223cc163b60a25060e8074},
  intrahash = {6bdd6d5206a79a250d7157bcfc34a724},
  issn = {1615-9853},
  journal = {PROTEOMICS},
  keywords = {IFZ Plasmodium_falciparum SELDI chloroquine mechanism_of_drug_action},
  number = 5,
  pages = {711-721},
  timestamp = {2008-10-14T16:07:18.000+0200},
  title = {SELDI-TOF-MS analysis of chloroquine resistant and sensitive Plasmodium falciparum strains},
  volume = 7,
  year = 2007
}

@article{MailuBMBeckerK.2007,
  added-at = {2008-10-14T16:07:18.000+0200},
  author = {?},
  biburl = {http://www.bibsonomy.org/bibtex/26be732b9e6fd4a0342d646b1d4548c57/nutribiochem},
  interhash = {69f3894f3e4d8e21ac2a1fd3e7d69344},
  intrahash = {6be732b9e6fd4a0342d646b1d4548c57},
  journal = {e.velop" 52 (Internetmagazin der Bundesregierung zur Entwicklungspolitik)},
  keywords = {IFZ imported},
  timestamp = {2008-10-14T16:07:18.000+0200},
  title = {Warum haben Kinder in Afrika so oft Fieber?},
  volume = 52,
  year = 2007
}

@article{ISI:000243161500006,
  abstract = {Thioredoxin reductase (TrxR)-as part of a major thiol regulating
system-allows redox metabolism to adjust to cellular requirements.
Therefore, changes at the redox level reflect as a pars pro toto
changes concerning the entire cell. Three different TrxR isoenzymes,
TrxR1 as cytosolic, TrxR2 as mitochondrial, and TrxR3 as
testis-specific thiol regulator are known. All three enzymes contain a
reactive and solvent accessible selenocysteine residue which is located
on a flexible C-terminal arm of the protein. This selenocysteine is
essentially involved in the catalytic cycle of TrxR and thus represents
an attractive binding site for inhibitors. Many tumor cells have
elevated TrxR levels and TrxR has been shown to play a major role in
drug resistance. Inhibition of TrxR and its related redox reactions may
thus contribute to a successful single, combinatory or adjuvant cancer
therapy. A great number of effective natural and synthetic TrxR
inhibitors are now available possessing antitumor pot},
  added-at = {2008-10-14T16:07:18.000+0200},
  author = {Urig, Sabine and Becker, Katja},
  biburl = {http://www.bibsonomy.org/bibtex/298fc799baaf6683cce2261568661c055/nutribiochem},
  interhash = {e448675e60688327246d8e3676110edd},
  intrahash = {98fc799baaf6683cce2261568661c055},
  issn = {1044-579X},
  journal = {SEMINARS IN CANCER BIOLOGY},
  keywords = {IFZ cancer chemotherapy inhibitor redox_sensitivity reductase thioredoxin},
  number = 6,
  pages = {452-465},
  timestamp = {2008-10-14T16:07:18.000+0200},
  title = {On the potential of thioredoxin reductase inhibitors for cancer therapy},
  volume = 16,
  year = 2006
}

@article{ISI:000253127600068,
  added-at = {2008-10-14T16:07:18.000+0200},
  author = {Buchholz, Kathrin and Matuschewski, Kai and Schirmer, Heiner R. and Becker, Katja},
  biburl = {http://www.bibsonomy.org/bibtex/2950f50c2f369b21dbf7e9fcc5af989bd/nutribiochem},
  interhash = {42cdc52b9e0d82dd1663d3034be763ef},
  intrahash = {950f50c2f369b21dbf7e9fcc5af989bd},
  issn = {0020-7519},
  journal = {INTERNATIONAL JOURNAL FOR PARASITOLOGY},
  keywords = {IFZ imported},
  number = {Suppl. 1},
  pages = {S37},
  timestamp = {2008-10-14T16:07:18.000+0200},
  title = {Functional characterization of Plasmodium redoxrelated enzymes},
  volume = 38,
  year = 2008
}

@article{BuchholzKMailuBSchirmerRHBeckerK.2007,
  added-at = {2008-10-14T16:07:18.000+0200},
  author = {Buchholz, Kathrin and Mailu, Boniface and Schirmer, Heiner R. and Becker, Katja},
  biburl = {http://www.bibsonomy.org/bibtex/2c072e353590f0dd3fcaa54cff28c17a0/nutribiochem},
  interhash = {ba31e033cd0d1123b259047d48dafd82},
  intrahash = {c072e353590f0dd3fcaa54cff28c17a0},
  journal = {Frontiers in Drug Design and Discovery},
  keywords = {IFZ imported},
  pages = {225-255},
  timestamp = {2008-10-14T16:07:18.000+0200},
  title = {Structure-based drug development against malaria},
  volume = 3,
  year = 2007
}

@article{ISI:000253127600044,
  added-at = {2008-10-14T16:07:18.000+0200},
  author = {?},
  biburl = {http://www.bibsonomy.org/bibtex/215e69ea67a17d90be5bc2317eb09aff3/nutribiochem},
  interhash = {b8a9d1b6f9510788eccbbbd27c36aebb},
  intrahash = {15e69ea67a17d90be5bc2317eb09aff3},
  issn = {0020-7519},
  journal = {INTERNATIONAL JOURNAL FOR PARASITOLOGY},
  keywords = {IFZ imported},
  number = {Suppl. 1},
  pages = {S28},
  timestamp = {2008-10-14T16:07:18.000+0200},
  title = {Quantitative proteomics of Plasmodium falciparum protein expression following drug exposure},
  volume = 38,
  year = 2008
}

@article{Morin.20080807,
  abstract = {Various aza-analogues of 1,4-naphthoquinone and menadione were prepared and tested as inhibitors and substrates of the plasmodial thioredoxin and glutathione reductases as well as the human glutathione reductase. The replacement of one to two carbons at the phenyl ring of the 1,4-naphthoquinone core by one to two nitrogen atoms led to an increased oxidant character of the molecules in accordance with both the redox potential values and the substrate efficiencies. Compared to the 1,4-naphthoquinone and menadione, the quinoline-5,8-dione 1 and both quinoxaline-5,8-diones 5 and 6 behaved as the most efficient subversive substrates of the three NADPH-dependent disulfide reductases tested. Modulation of these parameters was observed by alkylation of the aza-naphthoquinone core.},
  added-at = {2008-10-14T16:07:18.000+0200},
  author = {Morin, Christophe and Besset, Tatiana and Moutet, Jean-Claude and Fayolle, Martine and Br�ckner, Margit and Limosin, Dani?le and Becker, Katja and Davioud-Charvet, Elisabeth},
  biburl = {http://www.bibsonomy.org/bibtex/2779c9c2f3b4c8f40238339774a3d4832/nutribiochem},
  interhash = {cb6d834081706d5b015c38539d4dd4ad},
  intrahash = {779c9c2f3b4c8f40238339774a3d4832},
  issn = {1477-0520},
  journal = {Org Biomol Chem},
  keywords = {IFZ imported},
  number = 15,
  pages = {2731-2742},
  timestamp = {2008-10-14T16:07:18.000+0200},
  title = {The aza-analogues of 1,4-naphthoquinones are potent substrates and inhibitors of plasmodial thioredoxin and glutathione reductases and of human erythrocyte glutathione reductase},
  volume = 6,
  year = {2008/08/07/}
}

@article{Hu.200710,
  abstract = {We studied the effects of sulfur-containing chemopreventive agents, including allyl sulfides and isothiocyanates, on human redox networks. Isothiocyanates inhibited isolated redox-active enzymes in a time- and dose-dependent manner. As shown for the most active compound, benzyl isothiocyanate (BITC), on thioredoxin reductase, the inhibition has an initial competitive part (Ki=6.1+/-1.0 microM) followed by a time-dependent irreversible inhibition (k2=72.8+/-25.5 M(-1) s(-1)). Also, glutathione reductase and glutathione S-transferase were irreversibly modified by BITC. Sulforaphane led to irreversible inhibition of the studied redox enzymes, but with 5-10 times lower k2 values. In contrast, allyl sulfides had only moderate effects on the tested enzymes. However, diallyl disulfide was found to react directly with reduced glutathione (k2=100 M(-2) s(-1)). This reaction might contribute to enhanced oxidative stress and the induction of the selenoprotein glutathione peroxidase as determined },
  added-at = {2008-10-14T16:07:18.000+0200},
  author = {Hu, Ying and Urig, Sabine and Koncarevic, Sasa and Wu, Xinjiang and Fischer, Marina and Rahlfs, Stefan and Mersch-Sundermann, Volker and Becker, Katja},
  biburl = {http://www.bibsonomy.org/bibtex/208e03de016eac0326ebb47c3922bbc3d/nutribiochem},
  interhash = {5cc54ebfcc4e6e07c7650f4055370545},
  intrahash = {08e03de016eac0326ebb47c3922bbc3d},
  journal = {Biol Chem},
  keywords = {2'-disulfonic_Acid 4-Acetamido-4'-isothiocyanatostilbene-2 Allyl_Compounds Anticarcinogenic_Agents Cell_Cycle Cell_Line Cell_Proliferation Disulfides Dose-Response_Relationship Drug Glutathione Glutathione_Transferase Humans IFZ Oxidation-Reduction Sulfur_Compounds Thioredoxin-Disulfide_Reductase Thioredoxins Tumor Up-Regulation glutathione_peroxidase isothiocyanates},
  number = 10,
  pages = {1069-1081},
  timestamp = {2008-10-14T16:07:18.000+0200},
  title = {Glutathione- and thioredoxin-related enzymes are modulated by sulfur-containing chemopreventive agents},
  volume = 388,
  year = {2007/10//}
}

@article{Hu.200702,
  abstract = {Resveratrol is a polyphenolic chemopreventive agent that has been shown to influence cellular redox reactions. As a systematic approach to elucidating the complex effects of resveratrol on eukaryotic cells, we studied its dose-dependent effects on the transcript levels of genes and activities of enzymes related to redox metabolism, cell cycle regulation, and apoptotic cascades in the cancer cell line A549. Glutathione peroxidase (GPx)1 mRNA levels, as well as GPx and thioredoxin reductase (TrxR) activities, were significantly increased after resveratrol treatment, whereas total glutathione concentrations decreased. Increased transcript levels were also detected for selenophosphate synthetase 2 and superoxide dismutase 2. However, mRNA levels of thioredoxin, TrxR, glutathione reductase, glutathione S-transferase, superoxide dismutase 1, and catalase were not altered. Among the 12 genes studied that are related to the cell cycle, differentiation and apoptosis, mRNA levels of six genes, i},
  added-at = {2008-10-14T16:07:18.000+0200},
  author = {Hu, Ying and Rahlfs, Stefan and Mersch-Sundermann, Volker and Becker, Katja},
  biburl = {http://www.bibsonomy.org/bibtex/2678af63d13353f09e47f49eeee29f469/nutribiochem},
  interhash = {2e22181c6ee4abceafeea07147b1cd28},
  intrahash = {678af63d13353f09e47f49eeee29f469},
  journal = {Biol Chem},
  keywords = {Apoptosis Carcinoma Cell_Count Cell_Cycle Cell_Proliferation Cultured Dose-Response_Relationship Drug Genetic Glutathione Humans IFZ Lung_Neoplasms Messenger Non-Small-Cell_Lung Oxidation-Reduction Phosphotransferases RNA Reverse_Transcriptase_Polymerase_Chain_Reaction Sensitivity_and_Specificity Stilbenes Structure-Activity_Relationship Transcription Tumor_Cells glutathione_peroxidase},
  number = 2,
  pages = {207-219},
  timestamp = {2008-10-14T16:07:18.000+0200},
  title = {Resveratrol modulates mRNA transcripts of genes related to redox metabolism and cell proliferation in non-small-cell lung carcinoma cells},
  volume = 388,
  year = {2007/02//}
}

@article{Kamerbeek.20070415,
  abstract = {Hereditary glutathione reductase (GR) deficiency was found in only 2 cases when testing more than 15 000 blood samples. We have investigated the blood cells of 2 patients (1a and 1b) in a previously described family suffering from favism and cataract and of a novel patient (2) presenting with severe neonatal jaundice. Red blood cells and leukocytes of the patients in family 1 did not contain any GR activity, and the GR protein was undetectable by Western blotting. Owing to a 2246-bp deletion in the patients' DNA, translated GR is expected to lack almost the complete dimerization domain, which results in unstable and inactive enzyme. The red blood cells from patient 2 did not exhibit GR activity either, but the patient's leukocytes contained some residual activity that correlated with a weak protein expression. Patient 2 was found to be a compound heterozygote, with a premature stop codon on one allele and a substitution of glycine 330, a highly conserved residue in the superfamily of N},
  added-at = {2008-10-14T16:07:18.000+0200},
  author = {Kamerbeek, M. Nanne and van Zwieten, Rob and Boer, Martin and Morren, Gert and Vuil, Herma and Bannink, Natalja and Lincke, Carsten and Dolman, M. Koert and Becker, Katja and Schirmer, Heiner R. and Gromer, Stephan and Roos, Dirk},
  biburl = {http://www.bibsonomy.org/bibtex/24cd883fd4676fcbf70bc4e397511dbf0/nutribiochem},
  interhash = {7e388501bb202f099317eac21d95c0c5},
  intrahash = {4cd883fd4676fcbf70bc4e397511dbf0},
  journal = {Blood},
  keywords = {Alleles Amino_Acid_Substitution Cataract Child Codon Erythrocytes Favism Female Genetic_Diseases Glutathione_Reductase Heterozygote Humans IFZ Inborn Infant Jaundice Leukocytes Male Middle_Aged Neonatal Newborn Nonsense Preschool Protein_Structure Quaternary Sequence_Deletion Tertiary},
  number = 8,
  pages = {3560-3566},
  timestamp = {2008-10-14T16:07:18.000+0200},
  title = {Molecular basis of glutathione reductase deficiency in human blood cells},
  volume = 109,
  year = {2007/04/15/}
}

@article{Tripathi.2007,
  abstract = {BACKGROUND: In contrast to many other organisms, the malarial parasite Plasmodium falciparum possesses only one typical glutathione S-transferase. This enzyme, PfGST, cannot be assigned to any of the known GST classes and represents a most interesting target for antimalarial drug development. The PfGST under native conditions forms non-covalently linked higher aggregates with major population (approximately 98%) being tetramer. However, in the presence of 2 mM GSH, a dimer of PfGST is observed. Recently reported study on binding and catalytic properties of PfGST indicated a GSH dependent low-high affinity transition with simultaneous binding of two GSH molecules to PfGST dimer suggesting that GSH binds to low affinity inactive enzyme dimer converting it to high affinity functionally active dimer. In order to understand the role of GSH in tetramer-dimer transition of PfGST as well as in modulation of functional activity of the enzyme, detailed structural, functional and stability studie},
  added-at = {2008-10-14T16:07:18.000+0200},
  author = {Tripathi, Timir and Rahlfs, Stefan and Becker, Katja and Bhakuni, Vinod},
  biburl = {http://www.bibsonomy.org/bibtex/2e50b48ede2d548f29c9be36590f6947a/nutribiochem},
  interhash = {f677b27e4c9526aa511fc2989c3da8f8},
  intrahash = {e50b48ede2d548f29c9be36590f6947a},
  issn = {1472-6807},
  journal = {BMC Struct Biol},
  keywords = {Animals Biopolymers Dimerization Electrophoresis Glutathione Glutathione_Transferase IFZ Plasmodium_falciparum Polyacrylamide_Gel Protein_Conformation Protein_Denaturation Recombinant_Proteins},
  pages = {67-67},
  timestamp = {2008-10-14T16:07:18.000+0200},
  title = {Glutathione mediated regulation of oligomeric structure and functional activity of Plasmodium falciparum glutathione S-transferase},
  volume = 7,
  year = 2007
}

@article{Maiorino.20070126,
  abstract = {Some members of the glutathione peroxidase (GPx) family have been reported to accept thioredoxin as reducing substrate. However, the selenocysteine-containing ones oxidise thioredoxin (Trx), if at all, at extremely slow rates. In contrast, the Cys homolog of Drosophila melanogaster exhibits a clear preference for Trx, the net forward rate constant, k'(+2), for reduction by Trx being 1.5x10(6) M(-1) s(-1), but only 5.4 M(-1) s(-1) for glutathione. Like other CysGPxs with thioredoxin peroxidase activity, Drosophila melanogaster (Dm)GPx oxidized by H(2)O(2) contained an intra-molecular disulfide bridge between the active-site cysteine (C45; C(P)) and C91. Site-directed mutagenesis of C91 in DmGPx abrogated Trx peroxidase activity, but increased the rate constant for glutathione by two orders of magnitude. In contrast, a replacement of C74 by Ser or Ala only marginally affected activity and specificity of DmGPx. Furthermore, LC-MS/MS analysis of oxidized DmGPx exposed to a reduced Trx C35S},
  added-at = {2008-10-14T16:07:18.000+0200},
  author = {?},
  biburl = {http://www.bibsonomy.org/bibtex/2482c03361f814d195909dd986d35fd68/nutribiochem},
  interhash = {4d10ba897691efb358377cddd30906b3},
  intrahash = {482c03361f814d195909dd986d35fd68},
  journal = {J Mol Biol},
  keywords = {Amino_Acid Amino_Acid_Sequence Animals Chemical Dimerization Disulfides Drosophila_melanogaster IFZ Kinetics Models Molecular Molecular_Sequence_Data Mutagenesis Peroxidases Peroxiredoxins Sequence_Homology Site-Directed Substrate_Specificity Thioredoxins glutathione_peroxidase},
  number = 4,
  pages = {1033-1046},
  timestamp = {2008-10-14T16:07:18.000+0200},
  title = {The thioredoxin specificity of Drosophila GPx: a paradigm for a peroxiredoxin-like mechanism of many glutathione peroxidases},
  volume = 365,
  year = {2007/01/26/}
}

@article{Frosch.20070920,
  abstract = {Raman microspectroscopy was applied for an in situ localization of the malaria pigment hemozoin in Plasmodium falciparum-infected erythrocytes. The Raman spectra (lambdaexc=633 nm) of hemozoin show very intense signals with a very good signal-to-noise ratio. These in situ Raman signals of hemozoin were compared to Raman spectra of extracted hemozoin, of the synthetic analogue beta-hematin, and of hematin and hemin. beta-Hematin was synthesized according to the acid-catalyzed dehydration of hematin and the anhydrous dehydrohalogenation of hemin which lead to good crystals with lengths of about 5-30 microm. The Raman spectra (lambdaexc=1064 nm) of hemozoin and beta-hematin show almost identical behaviors, while some low wavenumber modes might be used to distinguish between the morphology of differently synthesized beta-hematin samples. The intensity pattern of the resonance Raman spectra (lambdaexc=568 nm) of hemozoin and beta-hematin differ significantly from those of hematin and hemin.},
  added-at = {2008-10-14T16:07:18.000+0200},
  author = {Frosch, Torsten and Koncarevic, Sasa and Zedler, Linda and Schmitt, Michael and Schenzel, Karla and Becker, Katja and Popp, J�rgen},
  biburl = {http://www.bibsonomy.org/bibtex/2ca1c6a601bdcd01ec74326eee3a78393/nutribiochem},
  interhash = {9b5f64ac3d03bbcedf196bf3b99af632},
  intrahash = {ca1c6a601bdcd01ec74326eee3a78393},
  issn = {1520-6106},
  journal = {J Phys Chem B},
  keywords = {Animals Erythrocytes Hemeproteins Humans IFZ Malaria Molecular_Structure Plasmodium_falciparum Raman Spectrum_Analysis Trophozoites},
  number = 37,
  pages = {11047-11056},
  timestamp = {2008-10-14T16:07:18.000+0200},
  title = {In situ localization and structural analysis of the malaria pigment hemozoin},
  volume = 111,
  year = {2007/09/20/}
}

@article{Chen.20070215,
  abstract = {Brain metastases are among the most feared complications in breast cancer, as no therapy exists that prevents or eliminates breast cancer spreading to the brain. New therapeutic strategies depend on specific knowledge of tumor cell properties that allow breast cancer cell growth within the brain tissue. To provide information in this direction, we established a human breast cancer cell model for brain metastasis based on circulating tumor cells from a breast cancer patient and variants of these cells derived from bone or brain lesions in immunodeficient mice. The brain-derived cells showed an increased potential for brain metastasis in vivo and exhibited a unique protein expression profile identified by large-scale proteomic analysis. This protein profile is consistent with either a selection of predisposed cells or bioenergetic adaptation of the tumor cells to the unique energy metabolism of the brain. Increased expression of enzymes involved in glycolysis, tricarboxylic acid cycle, a},
  added-at = {2008-10-14T16:07:18.000+0200},
  author = {Chen, I. Emily and Hewel, Johannes and Krueger, S. Joseph and Tiraby, Claire and Weber, R. Martin and Kralli, Anastasia and Becker, Katja and Yates, R. John and Felding-Habermann, Brunhilde},
  biburl = {http://www.bibsonomy.org/bibtex/2b1ec0fa05f47269651b25ab8ed7eaad5/nutribiochem},
  interhash = {fabd294c85a1d5e39799c33cf6d40d98},
  intrahash = {b1ec0fa05f47269651b25ab8ed7eaad5},
  journal = {Cancer Res},
  keywords = {Animal Animals Brain_Neoplasms Breast_Neoplasms Cell_Growth_Processes Citric_Acid_Cycle Disease_Models Energy_Metabolism Female Glutathione Glycolysis Humans IFZ Mice Mitochondria Oxidation-Reduction Oxygen_Consumption Pentose_Phosphate_Pathway Proteomics SCID},
  number = 4,
  pages = {1472-1486},
  timestamp = {2008-10-14T16:07:18.000+0200},
  title = {Adaptation of energy metabolism in breast cancer brain metastases},
  volume = 67,
  year = {2007/02/15/}
}

@article{Tripathi.200806,
  abstract = {Recently discovered monothiol glutaredoxins with CXXS-active site sequence share a common structural motif and biochemical mechanism of action and are involved in multiple cellular functions. Here we report first studies on the structural and stability characterization of a monothiol glutaredoxin, in particular--PfGLP1. Our results demonstrate that in the native conformation, the enzyme has a compact core structure with a relatively flexible N-terminal portion having an open configuration. Comparative functional studies with the full-length and N-terminal truncated protein demonstrate that the flexible N-terminal portion does not play any significant role in functional activity of the protein. In contrast to other Grxs, PfGLP1 does not contain a Fe-S cluster. The pH dependent studies demonstrate that the protein is resistant to alkaline pH but highly sensitive to acidic pH and undergoes significant unfolding between pH 4 and 5. However, acidic conditions also do not induce complete unf},
  added-at = {2008-10-14T16:07:18.000+0200},
  author = {Tripathi, Timir and Rahlfs, Stefan and Becker, Katja and Bhakuni, Vinod},
  biburl = {http://www.bibsonomy.org/bibtex/2f7da19c92c1723c8c603d5019cf616ec/nutribiochem},
  interhash = {77215f346e3cf72265b3785720f76246},
  intrahash = {f7da19c92c1723c8c603d5019cf616ec},
  issn = {0006-3002},
  journal = {Biochim Biophys Acta},
  keywords = {Amino_Acid Amino_Acid_Sequence Animals Circular_Dichroism Glutaredoxins IFZ Molecular_Sequence_Data Molecular_Weight Plasmodium_falciparum Protein_Binding Protein_Denaturation Protons Protozoan_Proteins Sequence_Homology Temperature},
  number = 6,
  pages = {946-952},
  timestamp = {2008-10-14T16:07:18.000+0200},
  title = {Structural and stability characteristics of a monothiol glutaredoxin: glutaredoxin-like protein 1 from Plasmodium falciparum},
  volume = 1784,
  year = {2008/06//}
}