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102. Redox-Sensing Under Hypochlorite Stress and Infection Conditions by the Rrf2-Family Repressor HypR inStaphylococcus aureus

Author

Loi, Vu Van, primary, Busche, Tobias, additional, Tedin, Karsten, additional, Bernhardt, Jörg, additional, Wollenhaupt, Jan, additional, Huyen, Nguyen Thi Thu, additional, Weise, Christoph, additional, Kalinowski, Jörn, additional, Wahl, Markus C., additional, Fulde, Marcus, additional, and Antelmann, Haike, additional

Published
2018
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103. The aldehyde dehydrogenase AldA contributes to the hypochlorite defense and is redox-controlled by protein S-bacillithiolation in Staphylococcus aureus

Author

Imber, Marcel, primary, Loi, Vu Van, additional, Reznikov, Sylvia, additional, Fritsch, Verena Nadin, additional, Pietrzyk-Brzezinska, Agnieszka J., additional, Prehn, Janek, additional, Hamilton, Chris, additional, Wahl, Markus C., additional, Bronowska, Agnieszka K., additional, and Antelmann, Haike, additional

Published
2018
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105. ProteinS-Bacillithiolation Functions in Thiol Protection and Redox Regulation of the Glyceraldehyde-3-Phosphate Dehydrogenase Gap inStaphylococcus aureusUnder Hypochlorite Stress

Author

Imber, Marcel, primary, Huyen, Nguyen Thi Thu, additional, Pietrzyk-Brzezinska, Agnieszka J., additional, Loi, Vu Van, additional, Hillion, Melanie, additional, Bernhardt, Jörg, additional, Thärichen, Lena, additional, Kolšek, Katra, additional, Saleh, Malek, additional, Hamilton, Chris J., additional, Adrian, Lorenz, additional, Gräter, Frauke, additional, Wahl, Markus C., additional, and Antelmann, Haike, additional

Published
2018
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106. European contribution to the study of ROS:a summary of the findings and prospects for the future from the COST Action BM1203 (EU-ROS)

Author

Egea, Javier, Fabregat, Isabel, Frapart, Yves M., Ghezzi, Pietro, Görlach, Agnes, Kietzmann, Thomas, Kubaichuk, Kateryna, Knaus, Ulla G., Lopez, Manuela G., Olaso-Gonzalez, Gloria, Petry, Andreas, Schulz, Rainer, Vina, Jose, Winyard, Paul, Abbas, Kahina, Ademowo, Stella, Afonso, Catarina B., Andreadou, Ioanna, Antelmann, Haike, Antunes, Fernando, Aslan, Mutay, Bachschmid, Markus M., Barbosa, Rui M., Belousov, Vsevolod, Berndt, Carsten, Bernlohr, David, Bertrán, Esther, Bindoli, Alberto, Bottari, Serge P., Brito, Paula M., Carrara, Guia, Casas, Ana I., Chatzi, Afroditi, Chondrogianni, Niki, Conrad, Marcus, Cooke, Marcus S., Costa, João G., Cuadrado, Antonio, My-Chan Dang, Pham, De Smet, Barbara, Debelec–butuner, Bilge, Dias, Irundika, Dunn, Joe Dan, Edson, Amanda J., El Assar, Mariam, El-Benna, Jamel, Ferdinandy, Péter, Fernandes, Ana S., Fladmark, Kari E., Förstermann, Ulrich, Giniatullin, Rashid, Giricz, Zoltán, Görbe, Anikó, Griffiths, Helen, Hampl, Vaclav, Hanf, Alina, Herget, Jan, Hernansanz-Agustín, Pablo, Hillion, Melanie, Huang, Jinjing, Ilikay, Serap, Jansen-Dürr, Pidder, Jaquet, Vincent, Joles, Jaap A., Kalyanaraman, Balaraman, Kaminskyy, Danylo, Karbaschi, Mahsa, Kleanthous, Marina, Klotz, Lars-Oliver, Korac, Bato, Korkmaz, Kemal Sami, Koziel, Rafal, Kračun, Damir, Krause, Karl-Heinz, Křen, Vladimír, Krieg, Thomas, Laranjinha, João, Lazou, Antigone, Li, Huige, Martínez-Ruiz, Antonio, Matsui, Reiko, Mcbean, Gethin J., Meredith, Stuart P., Messens, Joris, Miguel, Verónica, Mikhed, Yuliya, Milisav, Irina, Milković, Lidija, Miranda-Vizuete, Antonio, Mojović, Milos, Monsalve, María, Mouthuy, Pierre-Alexis, Mulvey, John, Münzel, Thomas, Muzykantov, Vladimir, Nguyen, Isabel T.N., Oelze, Matthias, Oliveira, Nuno G., Palmeira, Carlos M., Papaevgeniou, Nikoletta, Pavićević, Aleksandra, Pedre, Brandán, Peyrot, Fabienne, Phylactides, Marios, Pircalabioru, Gratiela G., Pitt, Andrew R., Poulsen, Henrik E., Prieto, Ignacio, Rigobello, Maria Pia, Robledinos-Antón, Natalia, Rodríguez-mañas, Leocadio, Rolo, Anabela P., Rousset, Francis, Ruskovska, Tatjana, Saraiva, Nuno, Sasson, Shlomo, Schröder, Katrin, Semen, Khrystyna, Seredenina, Tamara, Shakirzyanova, Anastasia, Smith, Geoffrey L., Soldati, Thierry, Sousa, Bebiana C., Spickett, Corinne M., Stancic, Ana, Stasia, Marie José, Steinbrenner, Holger, Stepanić, Višnja, Steven, Sebastian, Tokatlidis, Kostas, Tuncay, Erkan, Turan, Belma, Ursini, Fulvio, Vacek, Jan, Vajnerova, Olga, Valentová, Kateřina, van Breusegem, Frank, Varisli, Lokman, Veal, Elizabeth A., Yalçın, A. Suha, Yelisyeyeva, Olha, Žarković, Neven, Zatloukalová, Martina, Zielonka, Jacek, Touyz, Rhian M., Papapetropoulos, Andreas, Grune, Tilman, Lamas, Santiago, Schmidt, Harald H.H.W., di Lisa, Fabio, Daiber, Andreas, Egea, Javier, Fabregat, Isabel, Frapart, Yves M., Ghezzi, Pietro, Görlach, Agnes, Kietzmann, Thomas, Kubaichuk, Kateryna, Knaus, Ulla G., Lopez, Manuela G., Olaso-Gonzalez, Gloria, Petry, Andreas, Schulz, Rainer, Vina, Jose, Winyard, Paul, Abbas, Kahina, Ademowo, Stella, Afonso, Catarina B., Andreadou, Ioanna, Antelmann, Haike, Antunes, Fernando, Aslan, Mutay, Bachschmid, Markus M., Barbosa, Rui M., Belousov, Vsevolod, Berndt, Carsten, Bernlohr, David, Bertrán, Esther, Bindoli, Alberto, Bottari, Serge P., Brito, Paula M., Carrara, Guia, Casas, Ana I., Chatzi, Afroditi, Chondrogianni, Niki, Conrad, Marcus, Cooke, Marcus S., Costa, João G., Cuadrado, Antonio, My-Chan Dang, Pham, De Smet, Barbara, Debelec–butuner, Bilge, Dias, Irundika, Dunn, Joe Dan, Edson, Amanda J., El Assar, Mariam, El-Benna, Jamel, Ferdinandy, Péter, Fernandes, Ana S., Fladmark, Kari E., Förstermann, Ulrich, Giniatullin, Rashid, Giricz, Zoltán, Görbe, Anikó, Griffiths, Helen, Hampl, Vaclav, Hanf, Alina, Herget, Jan, Hernansanz-Agustín, Pablo, Hillion, Melanie, Huang, Jinjing, Ilikay, Serap, Jansen-Dürr, Pidder, Jaquet, Vincent, Joles, Jaap A., Kalyanaraman, Balaraman, Kaminskyy, Danylo, Karbaschi, Mahsa, Kleanthous, Marina, Klotz, Lars-Oliver, Korac, Bato, Korkmaz, Kemal Sami, Koziel, Rafal, Kračun, Damir, Krause, Karl-Heinz, Křen, Vladimír, Krieg, Thomas, Laranjinha, João, Lazou, Antigone, Li, Huige, Martínez-Ruiz, Antonio, Matsui, Reiko, Mcbean, Gethin J., Meredith, Stuart P., Messens, Joris, Miguel, Verónica, Mikhed, Yuliya, Milisav, Irina, Milković, Lidija, Miranda-Vizuete, Antonio, Mojović, Milos, Monsalve, María, Mouthuy, Pierre-Alexis, Mulvey, John, Münzel, Thomas, Muzykantov, Vladimir, Nguyen, Isabel T.N., Oelze, Matthias, Oliveira, Nuno G., Palmeira, Carlos M., Papaevgeniou, Nikoletta, Pavićević, Aleksandra, Pedre, Brandán, Peyrot, Fabienne, Phylactides, Marios, Pircalabioru, Gratiela G., Pitt, Andrew R., Poulsen, Henrik E., Prieto, Ignacio, Rigobello, Maria Pia, Robledinos-Antón, Natalia, Rodríguez-mañas, Leocadio, Rolo, Anabela P., Rousset, Francis, Ruskovska, Tatjana, Saraiva, Nuno, Sasson, Shlomo, Schröder, Katrin, Semen, Khrystyna, Seredenina, Tamara, Shakirzyanova, Anastasia, Smith, Geoffrey L., Soldati, Thierry, Sousa, Bebiana C., Spickett, Corinne M., Stancic, Ana, Stasia, Marie José, Steinbrenner, Holger, Stepanić, Višnja, Steven, Sebastian, Tokatlidis, Kostas, Tuncay, Erkan, Turan, Belma, Ursini, Fulvio, Vacek, Jan, Vajnerova, Olga, Valentová, Kateřina, van Breusegem, Frank, Varisli, Lokman, Veal, Elizabeth A., Yalçın, A. Suha, Yelisyeyeva, Olha, Žarković, Neven, Zatloukalová, Martina, Zielonka, Jacek, Touyz, Rhian M., Papapetropoulos, Andreas, Grune, Tilman, Lamas, Santiago, Schmidt, Harald H.H.W., di Lisa, Fabio, and Daiber, Andreas

Abstract

The European Cooperation in Science and Technology (COST) provides an ideal framework to establish multi-disciplinary research networks. COST Action BM1203 (EU-ROS) represents a consortium of researchers from different disciplines who are dedicated to providing new insights and tools for better understanding redox biology and medicine and, in the long run, to finding new therapeutic strategies to target dysregulated redox processes in various diseases. This report highlights the major achievements of EU-ROS as well as research updates and new perspectives arising from its members. The EU-ROS consortium comprised more than 140 active members who worked together for four years on the topics briefly described below. The formation of reactive oxygen and nitrogen species (RONS) is an established hallmark of our aerobic environment and metabolism but RONS also act as messengers via redox regulation of essential cellular processes. The fact that many diseases have been found to be associated with oxidative stress established the theory of oxidative stress as a trigger of diseases that can be corrected by antioxidant therapy. However, while experimental studies support this thesis, clinical studies still generate controversial results, due to complex pathophysiology of oxidative stress in humans. For future improvement of antioxidant therapy and better understanding of redox-associated disease progression detailed knowledge on the sources and targets of RONS formation and discrimination of their detrimental or beneficial roles is required. In order to advance this important area of biology and medicine, highly synergistic approaches combining a variety of diverse and contrasting disciplines are needed.

Published
2017

107. European contribution to the study of ROS : A summary of the findings and prospects for the future from the COST action BM1203 (EU-ROS)

Author

Egea, Javier, Fabregat, Isabel, Frapart, Yves M, Ghezzi, Pietro, Görlach, Agnes, Kietzmann, Thomas, Kubaichuk, Kateryna, Knaus, Ulla G, Lopez, Manuela G, Olaso-Gonzalez, Gloria, Petry, Andreas, Schulz, Rainer, Vina, Jose, Winyard, Paul J, Abbas, Kahina, Ademowo, Opeyemi S, Afonso, Catarina B, Andreadou, Ioanna, Antelmann, Haike, Antunes, Fernando, Aslan, Mutay, Bachschmid, Markus M, Barbosa, Rui M, Belousov, Vsevolod, Berndt, Carsten, Bernlohr, David, Bertrán, Esther, Bindoli, Alberto, Bottari, Serge P, Brito, Paula M, Carrara, Guia, Casas, Ana I, Chatzi, Afroditi, Chondrogianni, Niki, Conrad, Marcus, Cooke, Marcus S, Costa, João G, Cuadrado, Antonio, My-Chan Dang, Pham, De Smet, Barbara, Debelec-Butuner, Bilge, Dias, Irundika H K, Dunn, Joe Dan, Edson, Amanda J, El Assar, Mariam, El-Benna, Jamel, Ferdinandy, Péter, Fernandes, Ana S, Fladmark, Kari E, Förstermann, Ulrich, Giniatullin, Rashid, Giricz, Zoltán, Görbe, Anikó, Griffiths, Helen L, Hampl, Vaclav, Hanf, Alina, Herget, Jan, Hernansanz-Agustín, Pablo, Hillion, Melanie, Huang, Jingjing, Ilikay, Serap, Jansen-Dürr, Pidder, Jaquet, Vincent, Joles, Jaap A, Kalyanaraman, Balaraman, Kaminskyy, Danylo, Karbaschi, Mahsa, Kleanthous, Marina, Klotz, Lars-Oliver, Korac, Bato, Korkmaz, Kemal Sami, Koziel, Rafal, Kračun, Damir, Krause, Karl-Heinz, Křen, Vladimír, Krieg, Thomas, Laranjinha, João, Lazou, Antigone, Li, Huige, Martínez-Ruiz, Antonio, Matsui, Reiko, McBean, Gethin J, Meredith, Stuart P, Messens, Joris, Miguel, Verónica, Mikhed, Yuliya, Milisav, Irina, Milković, Lidija, Miranda-Vizuete, Antonio, Mojović, Miloš, Monsalve, María, Mouthuy, Pierre-Alexis, Mulvey, John, Münzel, Thomas, Muzykantov, Vladimir, Nguyen, Isabel T N, Oelze, Matthias, Oliveira, Nuno G, Palmeira, Carlos M, Papaevgeniou, Nikoletta, Pavićević, Aleksandra, Pedre, Brandán, Peyrot, Fabienne, Phylactides, Marios, Pircalabioru, Gratiela G, Pitt, Andrew R, Poulsen, Henrik E, Prieto, Ignacio, Rigobello, Maria Pia, Robledinos-Antón, Natalia, Rodríguez-Mañas, Leocadio, Rolo, Anabela P, Rousset, Francis, Ruskovska, Tatjana, Saraiva, Nuno, Sasson, Shlomo, Schröder, Katrin, Semen, Khrystyna, Seredenina, Tamara, Shakirzyanova, Anastasia, Smith, Geoffrey L, Soldati, Thierry, Sousa, Bebiana C, Spickett, Corinne M, Stancic, Ana, Stasia, Marie José, Steinbrenner, Holger, Stepanić, Višnja, Steven, Sebastian, Tokatlidis, Kostas, Tuncay, Erkan, Turan, Belma, Ursini, Fulvio, Vacek, Jan, Vajnerova, Olga, Valentová, Kateřina, Van Breusegem, Frank, Varisli, Lokman, Veal, Elizabeth A, Yalçın, A Suha, Yelisyeyeva, Olha, Žarković, Neven, Zatloukalová, Martina, Zielonka, Jacek, Touyz, Rhian M, Papapetropoulos, Andreas, Grune, Tilman, Lamas, Santiago, Schmidt, Harald H H W, Di Lisa, Fabio, Daiber, Andreas, Egea, Javier, Fabregat, Isabel, Frapart, Yves M, Ghezzi, Pietro, Görlach, Agnes, Kietzmann, Thomas, Kubaichuk, Kateryna, Knaus, Ulla G, Lopez, Manuela G, Olaso-Gonzalez, Gloria, Petry, Andreas, Schulz, Rainer, Vina, Jose, Winyard, Paul J, Abbas, Kahina, Ademowo, Opeyemi S, Afonso, Catarina B, Andreadou, Ioanna, Antelmann, Haike, Antunes, Fernando, Aslan, Mutay, Bachschmid, Markus M, Barbosa, Rui M, Belousov, Vsevolod, Berndt, Carsten, Bernlohr, David, Bertrán, Esther, Bindoli, Alberto, Bottari, Serge P, Brito, Paula M, Carrara, Guia, Casas, Ana I, Chatzi, Afroditi, Chondrogianni, Niki, Conrad, Marcus, Cooke, Marcus S, Costa, João G, Cuadrado, Antonio, My-Chan Dang, Pham, De Smet, Barbara, Debelec-Butuner, Bilge, Dias, Irundika H K, Dunn, Joe Dan, Edson, Amanda J, El Assar, Mariam, El-Benna, Jamel, Ferdinandy, Péter, Fernandes, Ana S, Fladmark, Kari E, Förstermann, Ulrich, Giniatullin, Rashid, Giricz, Zoltán, Görbe, Anikó, Griffiths, Helen L, Hampl, Vaclav, Hanf, Alina, Herget, Jan, Hernansanz-Agustín, Pablo, Hillion, Melanie, Huang, Jingjing, Ilikay, Serap, Jansen-Dürr, Pidder, Jaquet, Vincent, Joles, Jaap A, Kalyanaraman, Balaraman, Kaminskyy, Danylo, Karbaschi, Mahsa, Kleanthous, Marina, Klotz, Lars-Oliver, Korac, Bato, Korkmaz, Kemal Sami, Koziel, Rafal, Kračun, Damir, Krause, Karl-Heinz, Křen, Vladimír, Krieg, Thomas, Laranjinha, João, Lazou, Antigone, Li, Huige, Martínez-Ruiz, Antonio, Matsui, Reiko, McBean, Gethin J, Meredith, Stuart P, Messens, Joris, Miguel, Verónica, Mikhed, Yuliya, Milisav, Irina, Milković, Lidija, Miranda-Vizuete, Antonio, Mojović, Miloš, Monsalve, María, Mouthuy, Pierre-Alexis, Mulvey, John, Münzel, Thomas, Muzykantov, Vladimir, Nguyen, Isabel T N, Oelze, Matthias, Oliveira, Nuno G, Palmeira, Carlos M, Papaevgeniou, Nikoletta, Pavićević, Aleksandra, Pedre, Brandán, Peyrot, Fabienne, Phylactides, Marios, Pircalabioru, Gratiela G, Pitt, Andrew R, Poulsen, Henrik E, Prieto, Ignacio, Rigobello, Maria Pia, Robledinos-Antón, Natalia, Rodríguez-Mañas, Leocadio, Rolo, Anabela P, Rousset, Francis, Ruskovska, Tatjana, Saraiva, Nuno, Sasson, Shlomo, Schröder, Katrin, Semen, Khrystyna, Seredenina, Tamara, Shakirzyanova, Anastasia, Smith, Geoffrey L, Soldati, Thierry, Sousa, Bebiana C, Spickett, Corinne M, Stancic, Ana, Stasia, Marie José, Steinbrenner, Holger, Stepanić, Višnja, Steven, Sebastian, Tokatlidis, Kostas, Tuncay, Erkan, Turan, Belma, Ursini, Fulvio, Vacek, Jan, Vajnerova, Olga, Valentová, Kateřina, Van Breusegem, Frank, Varisli, Lokman, Veal, Elizabeth A, Yalçın, A Suha, Yelisyeyeva, Olha, Žarković, Neven, Zatloukalová, Martina, Zielonka, Jacek, Touyz, Rhian M, Papapetropoulos, Andreas, Grune, Tilman, Lamas, Santiago, Schmidt, Harald H H W, Di Lisa, Fabio, and Daiber, Andreas

Published
2017

108. European contribution to the study of ROS: A summary of the findings and prospects for the future from the COST action BM1203 (EU-ROS)

Author

MS Nefrologie, Regenerative Medicine and Stem Cells, Circulatory Health, Nefro Vasculaire Geneeskunde, Other research (not in main researchprogram), Egea, Javier, Fabregat, Isabel, Frapart, Yves M, Ghezzi, Pietro, Görlach, Agnes, Kietzmann, Thomas, Kubaichuk, Kateryna, Knaus, Ulla G, Lopez, Manuela G, Olaso-Gonzalez, Gloria, Petry, Andreas, Schulz, Rainer, Vina, Jose, Winyard, Paul J, Abbas, Kahina, Ademowo, Opeyemi S, Afonso, Catarina B, Andreadou, Ioanna, Antelmann, Haike, Antunes, Fernando, Aslan, Mutay, Bachschmid, Markus M, Barbosa, Rui M, Belousov, Vsevolod, Berndt, Carsten, Bernlohr, David, Bertrán, Esther, Bindoli, Alberto, Bottari, Serge P, Brito, Paula M, Carrara, Guia, Casas, Ana I, Chatzi, Afroditi, Chondrogianni, Niki, Conrad, Marcus, Cooke, Marcus S, Costa, João G, Cuadrado, Antonio, My-Chan Dang, Pham, De Smet, Barbara, Debelec-Butuner, Bilge, Dias, Irundika H K, Dunn, Joe Dan, Edson, Amanda J, El Assar, Mariam, El-Benna, Jamel, Ferdinandy, Péter, Fernandes, Ana S, Fladmark, Kari E, Förstermann, Ulrich, Giniatullin, Rashid, Giricz, Zoltán, Görbe, Anikó, Griffiths, Helen L, Hampl, Vaclav, Hanf, Alina, Herget, Jan, Hernansanz-Agustín, Pablo, Hillion, Melanie, Huang, Jingjing, Ilikay, Serap, Jansen-Dürr, Pidder, Jaquet, Vincent, Joles, Jaap A, Kalyanaraman, Balaraman, Kaminskyy, Danylo, Karbaschi, Mahsa, Kleanthous, Marina, Klotz, Lars-Oliver, Korac, Bato, Korkmaz, Kemal Sami, Koziel, Rafal, Kračun, Damir, Krause, Karl-Heinz, Křen, Vladimír, Krieg, Thomas, Laranjinha, João, Lazou, Antigone, Li, Huige, Martínez-Ruiz, Antonio, Matsui, Reiko, McBean, Gethin J, Meredith, Stuart P, Messens, Joris, Miguel, Verónica, Mikhed, Yuliya, Milisav, Irina, Milković, Lidija, Miranda-Vizuete, Antonio, Mojović, Miloš, Monsalve, María, Mouthuy, Pierre-Alexis, Mulvey, John, Münzel, Thomas, Muzykantov, Vladimir, Nguyen, Isabel T N, Oelze, Matthias, Oliveira, Nuno G, Palmeira, Carlos M, Papaevgeniou, Nikoletta, Pavićević, Aleksandra, Pedre, Brandán, Peyrot, Fabienne, Phylactides, Marios, Pircalabioru, Gratiela G, Pitt, Andrew R, Poulsen, Henrik E, Prieto, Ignacio, Rigobello, Maria Pia, Robledinos-Antón, Natalia, Rodríguez-Mañas, Leocadio, Rolo, Anabela P, Rousset, Francis, Ruskovska, Tatjana, Saraiva, Nuno, Sasson, Shlomo, Schröder, Katrin, Semen, Khrystyna, Seredenina, Tamara, Shakirzyanova, Anastasia, Smith, Geoffrey L, Soldati, Thierry, Sousa, Bebiana C, Spickett, Corinne M, Stancic, Ana, Stasia, Marie José, Steinbrenner, Holger, Stepanić, Višnja, Steven, Sebastian, Tokatlidis, Kostas, Tuncay, Erkan, Turan, Belma, Ursini, Fulvio, Vacek, Jan, Vajnerova, Olga, Valentová, Kateřina, Van Breusegem, Frank, Varisli, Lokman, Veal, Elizabeth A, Yalçın, A Suha, Yelisyeyeva, Olha, Žarković, Neven, Zatloukalová, Martina, Zielonka, Jacek, Touyz, Rhian M, Papapetropoulos, Andreas, Grune, Tilman, Lamas, Santiago, Schmidt, Harald H H W, Di Lisa, Fabio, Daiber, Andreas, MS Nefrologie, Regenerative Medicine and Stem Cells, Circulatory Health, Nefro Vasculaire Geneeskunde, Other research (not in main researchprogram), Egea, Javier, Fabregat, Isabel, Frapart, Yves M, Ghezzi, Pietro, Görlach, Agnes, Kietzmann, Thomas, Kubaichuk, Kateryna, Knaus, Ulla G, Lopez, Manuela G, Olaso-Gonzalez, Gloria, Petry, Andreas, Schulz, Rainer, Vina, Jose, Winyard, Paul J, Abbas, Kahina, Ademowo, Opeyemi S, Afonso, Catarina B, Andreadou, Ioanna, Antelmann, Haike, Antunes, Fernando, Aslan, Mutay, Bachschmid, Markus M, Barbosa, Rui M, Belousov, Vsevolod, Berndt, Carsten, Bernlohr, David, Bertrán, Esther, Bindoli, Alberto, Bottari, Serge P, Brito, Paula M, Carrara, Guia, Casas, Ana I, Chatzi, Afroditi, Chondrogianni, Niki, Conrad, Marcus, Cooke, Marcus S, Costa, João G, Cuadrado, Antonio, My-Chan Dang, Pham, De Smet, Barbara, Debelec-Butuner, Bilge, Dias, Irundika H K, Dunn, Joe Dan, Edson, Amanda J, El Assar, Mariam, El-Benna, Jamel, Ferdinandy, Péter, Fernandes, Ana S, Fladmark, Kari E, Förstermann, Ulrich, Giniatullin, Rashid, Giricz, Zoltán, Görbe, Anikó, Griffiths, Helen L, Hampl, Vaclav, Hanf, Alina, Herget, Jan, Hernansanz-Agustín, Pablo, Hillion, Melanie, Huang, Jingjing, Ilikay, Serap, Jansen-Dürr, Pidder, Jaquet, Vincent, Joles, Jaap A, Kalyanaraman, Balaraman, Kaminskyy, Danylo, Karbaschi, Mahsa, Kleanthous, Marina, Klotz, Lars-Oliver, Korac, Bato, Korkmaz, Kemal Sami, Koziel, Rafal, Kračun, Damir, Krause, Karl-Heinz, Křen, Vladimír, Krieg, Thomas, Laranjinha, João, Lazou, Antigone, Li, Huige, Martínez-Ruiz, Antonio, Matsui, Reiko, McBean, Gethin J, Meredith, Stuart P, Messens, Joris, Miguel, Verónica, Mikhed, Yuliya, Milisav, Irina, Milković, Lidija, Miranda-Vizuete, Antonio, Mojović, Miloš, Monsalve, María, Mouthuy, Pierre-Alexis, Mulvey, John, Münzel, Thomas, Muzykantov, Vladimir, Nguyen, Isabel T N, Oelze, Matthias, Oliveira, Nuno G, Palmeira, Carlos M, Papaevgeniou, Nikoletta, Pavićević, Aleksandra, Pedre, Brandán, Peyrot, Fabienne, Phylactides, Marios, Pircalabioru, Gratiela G, Pitt, Andrew R, Poulsen, Henrik E, Prieto, Ignacio, Rigobello, Maria Pia, Robledinos-Antón, Natalia, Rodríguez-Mañas, Leocadio, Rolo, Anabela P, Rousset, Francis, Ruskovska, Tatjana, Saraiva, Nuno, Sasson, Shlomo, Schröder, Katrin, Semen, Khrystyna, Seredenina, Tamara, Shakirzyanova, Anastasia, Smith, Geoffrey L, Soldati, Thierry, Sousa, Bebiana C, Spickett, Corinne M, Stancic, Ana, Stasia, Marie José, Steinbrenner, Holger, Stepanić, Višnja, Steven, Sebastian, Tokatlidis, Kostas, Tuncay, Erkan, Turan, Belma, Ursini, Fulvio, Vacek, Jan, Vajnerova, Olga, Valentová, Kateřina, Van Breusegem, Frank, Varisli, Lokman, Veal, Elizabeth A, Yalçın, A Suha, Yelisyeyeva, Olha, Žarković, Neven, Zatloukalová, Martina, Zielonka, Jacek, Touyz, Rhian M, Papapetropoulos, Andreas, Grune, Tilman, Lamas, Santiago, Schmidt, Harald H H W, Di Lisa, Fabio, and Daiber, Andreas

Published
2017

109. Monitoring global protein thiol-oxidation and protein S-mycothiolation in Mycobacterium smegmatis under hypochlorite stress

Author

Massachusetts Institute of Technology. Department of Biology, Rueckert, Christian, Hillion, Melanie, Busche, Tobias, Rossius, Martina, Rawat, Mamta, Wirtz, Markus, Antelmann, Haike, Bernhardt, Jorg, Maas, Sandra, Becher, Dorte, Hell, Ruediger, Kalinowski, Jorn, Massachusetts Institute of Technology. Department of Biology, Rueckert, Christian, Hillion, Melanie, Busche, Tobias, Rossius, Martina, Rawat, Mamta, Wirtz, Markus, Antelmann, Haike, Bernhardt, Jorg, Maas, Sandra, Becher, Dorte, Hell, Ruediger, and Kalinowski, Jorn

Abstract

Mycothiol (MSH) is the major low molecular weight (LMW) thiol in Actinomycetes. Here, we used shotgun proteomics, OxICAT and RNA-seq transcriptomics to analyse protein S-mycothiolation, reversible thiol-oxidations and their impact on gene expression in Mycobacterium smegmatis under hypochlorite stress. In total, 58 S-mycothiolated proteins were identified under NaOCl stress that are involved in energy metabolism, fatty acid and mycolic acid biosynthesis, protein translation, redox regulation and detoxification. Protein S-mycothiolation was accompanied by MSH depletion in the thiol-metabolome. Quantification of the redox state of 1098 Cys residues using OxICAT revealed that 381 Cys residues (33.6%) showed >10% increased oxidations under NaOCl stress, which overlapped with 40 S-mycothiolated Cys-peptides. The absence of MSH resulted in a higher basal oxidation level of 338 Cys residues (41.1%). The RseA and RshA anti-sigma factors and the Zur and NrdR repressors were identified as NaOCl-sensitive proteins and their oxidation resulted in an up-regulation of the SigH, SigE, Zur and NrdR regulons in the RNA-seq transcriptome. In conclusion, we show here that NaOCl stress causes widespread thiol-oxidation including protein S-mycothiolation resulting in induction of antioxidant defense mechanisms in M. smegmatis. Our results further reveal that MSH is important to maintain the reduced state of protein thiols.

Published
2017

110. European contribution to the study of ROS: A summary of the findings and prospects for the future from the COST action BM1203 (EU-ROS)

Author

Egea, Javier, primary, Fabregat, Isabel, additional, Frapart, Yves M., additional, Ghezzi, Pietro, additional, Görlach, Agnes, additional, Kietzmann, Thomas, additional, Kubaichuk, Kateryna, additional, Knaus, Ulla G., additional, Lopez, Manuela G., additional, Olaso-Gonzalez, Gloria, additional, Petry, Andreas, additional, Schulz, Rainer, additional, Vina, Jose, additional, Winyard, Paul, additional, Abbas, Kahina, additional, Ademowo, Opeyemi S., additional, Afonso, Catarina B., additional, Andreadou, Ioanna, additional, Antelmann, Haike, additional, Antunes, Fernando, additional, Aslan, Mutay, additional, Bachschmid, Markus M., additional, Barbosa, Rui M., additional, Belousov, Vsevolod, additional, Berndt, Carsten, additional, Bernlohr, David, additional, Bertrán, Esther, additional, Bindoli, Alberto, additional, Bottari, Serge P., additional, Brito, Paula M., additional, Carrara, Guia, additional, Casas, Ana I., additional, Chatzi, Afroditi, additional, Chondrogianni, Niki, additional, Conrad, Marcus, additional, Cooke, Marcus S., additional, Costa, João G., additional, Cuadrado, Antonio, additional, My-Chan Dang, Pham, additional, De Smet, Barbara, additional, Debelec–Butuner, Bilge, additional, Dias, Irundika H.K., additional, Dunn, Joe Dan, additional, Edson, Amanda J., additional, El Assar, Mariam, additional, El-Benna, Jamel, additional, Ferdinandy, Péter, additional, Fernandes, Ana S., additional, Fladmark, Kari E., additional, Förstermann, Ulrich, additional, Giniatullin, Rashid, additional, Giricz, Zoltán, additional, Görbe, Anikó, additional, Griffiths, Helen, additional, Hampl, Vaclav, additional, Hanf, Alina, additional, Herget, Jan, additional, Hernansanz-Agustín, Pablo, additional, Hillion, Melanie, additional, Huang, Jingjing, additional, Ilikay, Serap, additional, Jansen-Dürr, Pidder, additional, Jaquet, Vincent, additional, Joles, Jaap A., additional, Kalyanaraman, Balaraman, additional, Kaminskyy, Danylo, additional, Karbaschi, Mahsa, additional, Kleanthous, Marina, additional, Klotz, Lars-Oliver, additional, Korac, Bato, additional, Korkmaz, Kemal Sami, additional, Koziel, Rafal, additional, Kračun, Damir, additional, Krause, Karl-Heinz, additional, Křen, Vladimír, additional, Krieg, Thomas, additional, Laranjinha, João, additional, Lazou, Antigone, additional, Li, Huige, additional, Martínez-Ruiz, Antonio, additional, Matsui, Reiko, additional, McBean, Gethin J., additional, Meredith, Stuart P., additional, Messens, Joris, additional, Miguel, Verónica, additional, Mikhed, Yuliya, additional, Milisav, Irina, additional, Milković, Lidija, additional, Miranda-Vizuete, Antonio, additional, Mojović, Miloš, additional, Monsalve, María, additional, Mouthuy, Pierre-Alexis, additional, Mulvey, John, additional, Münzel, Thomas, additional, Muzykantov, Vladimir, additional, Nguyen, Isabel T.N., additional, Oelze, Matthias, additional, Oliveira, Nuno G., additional, Palmeira, Carlos M., additional, Papaevgeniou, Nikoletta, additional, Pavićević, Aleksandra, additional, Pedre, Brandán, additional, Peyrot, Fabienne, additional, Phylactides, Marios, additional, Pircalabioru, Gratiela G., additional, Pitt, Andrew R., additional, Poulsen, Henrik E., additional, Prieto, Ignacio, additional, Rigobello, Maria Pia, additional, Robledinos-Antón, Natalia, additional, Rodríguez-Mañas, Leocadio, additional, Rolo, Anabela P., additional, Rousset, Francis, additional, Ruskovska, Tatjana, additional, Saraiva, Nuno, additional, Sasson, Shlomo, additional, Schröder, Katrin, additional, Semen, Khrystyna, additional, Seredenina, Tamara, additional, Shakirzyanova, Anastasia, additional, Smith, Geoffrey L., additional, Soldati, Thierry, additional, Sousa, Bebiana C., additional, Spickett, Corinne M., additional, Stancic, Ana, additional, Stasia, Marie José, additional, Steinbrenner, Holger, additional, Stepanić, Višnja, additional, Steven, Sebastian, additional, Tokatlidis, Kostas, additional, Tuncay, Erkan, additional, Turan, Belma, additional, Ursini, Fulvio, additional, Vacek, Jan, additional, Vajnerova, Olga, additional, Valentová, Kateřina, additional, Van Breusegem, Frank, additional, Varisli, Lokman, additional, Veal, Elizabeth A., additional, Yalçın, A. Suha, additional, Yelisyeyeva, Olha, additional, Žarković, Neven, additional, Zatloukalová, Martina, additional, Zielonka, Jacek, additional, Touyz, Rhian M., additional, Papapetropoulos, Andreas, additional, Grune, Tilman, additional, Lamas, Santiago, additional, Schmidt, Harald H.H.W., additional, Di Lisa, Fabio, additional, and Daiber, Andreas, additional

Published
2017
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111. The glyceraldehyde-3-phosphate dehydrogenase GapDH of Corynebacterium diphtheriae is redox-controlled by protein S-mycothiolation under oxidative stress

Author

Hillion, Melanie, primary, Imber, Marcel, additional, Pedre, Brandán, additional, Bernhardt, Jörg, additional, Saleh, Malek, additional, Loi, Vu Van, additional, Maaß, Sandra, additional, Becher, Dörte, additional, Astolfi Rosado, Leonardo, additional, Adrian, Lorenz, additional, Weise, Christoph, additional, Hell, Rüdiger, additional, Wirtz, Markus, additional, Messens, Joris, additional, and Antelmann, Haike, additional

Published
2017
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113. Monitoring global protein thiol-oxidation and protein S-mycothiolation in Mycobacterium smegmatis under hypochlorite stress

Author

Hillion, Melanie, primary, Bernhardt, Jörg, additional, Busche, Tobias, additional, Rossius, Martina, additional, Maaß, Sandra, additional, Becher, Dörte, additional, Rawat, Mamta, additional, Wirtz, Markus, additional, Hell, Rüdiger, additional, Rückert, Christian, additional, Kalinowski, Jörn, additional, and Antelmann, Haike, additional

Published
2017
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114. Proteomics of protein in secretion by bacillus subtilis: separating the 'secrets' of the secretome

Author

Antelmann, Haike, Tjalsma, Harold, Braun, Peter G., Jongbloed, Jan D.H., Dorenbos, Ronald, Darmon, Elise, Westers, Helga, Zanen, Geeske, Quax, Wim J., Diji, Jan Maarten van, Hecker, Michael, Bron, Sierd, and Kuipers, Oscar P.

Subjects
Proteomics -- Research, Proteins -- Research, Bacillus subtilis -- Research, Biological sciences
Abstract

Secretory proteins perform a variety of important 'remote-control' functions for bacterial survival in the environment. The study concludes that proteomics has yielded a variety of novel leads for the analysis of protein traffic in B.subtilis and other gram-positive bacteria.

Published
2004

115. Binding of sigma (super)A and sigma (super)B to core RNA polymerase after environmental stress in Bacillus subtilis

Author

Rollenhagen, Claudia, Antelmann, Haike, Kirstein, Janine, Delumeau, Olivier, Hecker, Michael, and Yudkin, Michael D.

Subjects
Bacteriology -- Research, RNA polymerases -- Genetic aspects, Bacillus subtilis -- Genetic aspects, Bacillus subtilis -- Physiological aspects, Biological sciences
Abstract

Research has been conducted on response of Bacillus subtilis sigma factor (super)B to environmental stress. Results indicate that sigma (super)B concentration after stress cannot compensate for its low affinity for core RNA polymerase.

Published
2003

119. Comparative Secretome Analyses of Human and Zoonotic Staphylococcus aureusIsolates CC8, CC22, and CC398*

Author

Busche, Tobias, Hillion, Mélanie, Van Loi, Vu, Berg, David, Walther, Birgit, Semmler, Torsten, Strommenger, Birgit, Witte, Wolfgang, Cuny, Christiane, Mellmann, Alexander, Holmes, Mark A., Kalinowski, Jörn, Adrian, Lorenz, Bernhardt, Jörg, and Antelmann, Haike

Abstract

The proteogenomes and secretomes of dominant human and zoonotic S. aureuslineages CC8, CC22 and CC398 were compared revealing genomic and regulatory differences in the secretion of 869 proteins. In the core secretome, 101 secreted or cell surface anchored virulence factors contribute with 82.4% to total secretome abundance. CC398 isolates showed higher secretion of α- and ß-hemolysins and lower secretion of surface proteins resulting in strong hemolysis and decreased biofilm formation because of lower SigB activity compared to human-specific CC8 and CC22.

Published
2018
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120. The Tat pathway exports multiple virulence proteins in the plant pathogen Streptomyces scabies

Author

Joshi, Madhumita V, Mann, Stefan G, Antelmann, Haike, Widdick, David, Fyans, Joanna K, Chandra, Govind, Hutchings, Matthew I, Toth, Ian, Hecker, Michael, Loria, Rosemary, Palmer, Tracy, Plant Pathology, Cornell University [New York], Molecular Microbiology, John Innes Centre [Norwich], Universität Greifswald - University of Greifswald, University of Dundee, School of Biological Sciences, University of East Anglia [Norwich] (UEA), Scottish Crop Research Institute, Department of Microbial Physiology, Institute for Microbiology, Department of Plant Pathology, and College of Life Sciences

Subjects
Life Sciences
Abstract

International audience; Streptomyces scabies is one of a group of organisms that causes the economically important disease potato scab. Analysis of the S. scabies genome sequence indicates that it is likely to secrete many proteins via the twin arginine protein transport (Tat) pathway, including several proteins whose coding sequences may have been acquired through horizontal gene transfer and share a common ancestor with proteins in other plant pathogens. Inactivation of the S. scabies Tat pathway resulted in pleiotropic phenotypes including slower growth rate and increased permeability of the cell envelope. Comparison of the extracellular proteome of the wild type and ΔtatC strains identified 73 predicted secretory proteins that were present in reduced amounts in the tatC mutant strain, and 47 Tat substrates were verified using a Tat reporter assay. The ΔtatC strain was almost completely avirulent on Arabidopsis seedlings and was delayed in attaching to the root tip relative to the wild type strain. Genes encoding 14 candidate Tat substrates were individually inactivated, and seven of these mutants were reduced in virulence compared to the wild type strain. We conclude that the Tat pathway secretes multiple proteins that are required for full virulence.

Published
2010

123. Protein S-Mycothiolation Functions as Redox-Switch and Thiol Protection Mechanism in Corynebacterium glutamicum Under Hypochlorite Stress

Author

Chi, Bui Khanh, Busche, Tobias, Van Laer, Koen, Baesell, Katrin, Becher, Doerte, Clermont, Lina, Seibold, Gerd M., Persicke, Marcus, Kalinowski, Joern, Messens, Joris, Antelmann, Haike, Chi, Bui Khanh, Busche, Tobias, Van Laer, Koen, Baesell, Katrin, Becher, Doerte, Clermont, Lina, Seibold, Gerd M., Persicke, Marcus, Kalinowski, Joern, Messens, Joris, and Antelmann, Haike

Abstract

Aims: Protein S-bacillithiolation was recently discovered as important thiol protection and redox-switch mechanism in response to hypochlorite stress in Firmicutes bacteria. Here we used transcriptomics to analyze the NaOCl stress response in the mycothiol (MSH)-producing Corynebacterium glutamicum. We further applied thiol-redox proteomics and mass spectrometry (MS) to identify protein S-mycothiolation. Results: Transcriptomics revealed the strong upregulation of the disulfide stress sigma(H) regulon by NaOCl stress in C. glutamicum, including genes for the anti sigma factor (rshA), the thioredoxin and MSH pathways (trxB1, trxC, cg1375, trxB, mshC, mca, mtr) that maintain the redox balance. We identified 25 S-mycothiolated proteins in NaOCl-treated cells by liquid chromatography-tandem mass spectrometry (LC-MS/MS), including 16 proteins that are reversibly oxidized by NaOCl in the thiol-redox proteome. The S-mycothiolome includes the methionine synthase (MetE), the maltodextrin phosphorylase (MalP), the myoinositol-1-phosphate synthase (Ino1), enzymes for the biosynthesis of nucleotides (GuaB1, GuaB2, PurL, NadC), and thiamine (ThiD), translation proteins (TufA, PheT, RpsF, RplM, RpsM, RpsC), and antioxidant enzymes (Tpx, Gpx, MsrA). We further show that S-mycothiolation of the thiol peroxidase (Tpx) affects its peroxiredoxin activity in vitro that can be restored by mycoredoxin1. LC-MS/MS analysis further identified 8 proteins with S-cysteinylations in the mshC mutant suggesting that cysteine can be used for S-thiolations in the absence of MSH. Innovation and Conclusion: We identified widespread protein S-mycothiolations in the MSH-producing C. glutamicum and demonstrate that S-mycothiolation reversibly affects the peroxidase activity of Tpx. Interestingly, many targets are conserved S-thiolated across bacillithiol- and MSH-producing bacteria, which could become future drug targets in related pathogenic Gram-positives.

Published
2014

124. Cell Physiology and Protein Secretion of Bacillus licheniformis Compared to Bacillus subtilis

Author

Voigt, Birgit, Antelmann, Haike, Albrecht, Dirk, Ehrenreich, Armin, Maurer, Karl-Heinz, Evers, Stefan, Gottschalk, Gerhard, van Dijl, Jan Maarten, Schweder, Thomas, Hecker, Michael, University of Groningen, Translational Immunology Groningen (TRIGR), and Scheurink lab

Subjects
LYSIS, GENES, STARVATION RESPONSE, Extracellular proteome, GLUCOSE, CATABOLISM, Bacillus licheniformis, Bacillus subtilis, Cell physiology, Protein secretion, ACETOIN, ARGININE TRANSLOCATION PATHWAY, COMPLETE GENOME SEQUENCE, PROTEOMIC VIEW, TRANSCRIPTION
Abstract

The genome sequence of Bacillus subtilis was published in 1997 and since then many other bacterial genomes have been sequenced, among them Bacillus licheniformis in 2004. B. subtilis and B. licheniformis are closely related and feature similar saprophytic lifestyles in the soil. Both species can secrete numerous proteins into the surrounding medium enabling them to use high-molecular-weight substances, which are abundant in soils, as nutrient sources. The availability of complete genome sequences allows for the prediction of the proteins containing signals for secretion into the extracellular milieu and also of the proteins which form the secretion machinery needed for protein translocation through the cytoplasmic membrane. To confirm the predicted subcellular localization of proteins, proteomics is the best choice. The extracellular proteomes of B. subtilis and B. licheniformis have been analyzed under different growth conditions allowing comparisons of the extracellular proteomes and conclusions regarding similarities and differences of the protein secretion mechanisms between the two species. Copyright (c) 2008 S. Karger AG, Basel

Published
2008

125. Proteomic survey through secretome of Bacillus subtilis

Author

Antelmann, Haike, Van Dijl, Jan Maarten, Bron, Sierd, Hecker, Michael, and Translational Immunology Groningen (TRIGR)

Subjects
Proteomics, Protein Transport, Bacterial Proteins, Cell Wall, Cell Membrane, Lipid Metabolism, Genome, Bacterial, Bacillus subtilis, Protein Structure, Tertiary
Published
2006

129. TheE. colisirtuin CobB shows no preference for enzymatic and nonenzymatic lysine acetylation substrate sites

Author

AbouElfetouh, Alaa, primary, Kuhn, Misty L., additional, Hu, Linda I., additional, Scholle, Michael D., additional, Sorensen, Dylan J., additional, Sahu, Alexandria K., additional, Becher, Dörte, additional, Antelmann, Haike, additional, Mrksich, Milan, additional, Anderson, Wayne F., additional, Gibson, Bradford W., additional, Schilling, Birgit, additional, and Wolfe, Alan J., additional

Published
2014
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132. Protein S-Mycothiolation Functions as Redox-Switch and Thiol Protection Mechanism in Corynebacterium glutamicum Under Hypochlorite Stress

Author

Chi, Bui Khanh, primary, Busche, Tobias, additional, Van Laer, Koen, additional, Bäsell, Katrin, additional, Becher, Dörte, additional, Clermont, Lina, additional, Seibold, Gerd M., additional, Persicke, Marcus, additional, Kalinowski, Jörn, additional, Messens, Joris, additional, and Antelmann, Haike, additional

Published
2014
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134. Molecular architecture of Streptococcus pneumoniae surface thioredoxin-fold lipoproteins crucial for extracellular oxidative stress resistance and maintenance of virulence.

Author

European Synchrotron Radiation Facility, European Commission, Saleh, Malek, Bartual, Sergio G., Abdullah, M.R., Jensch, Inga, Asmat, Tauseef M., Petruschka, L., Pribyl, T., Gellert, Manuela, Lillig, Christopher H., Antelmann, Haike, Hermoso, Juan A., Hammerschmidt, Sven, European Synchrotron Radiation Facility, European Commission, Saleh, Malek, Bartual, Sergio G., Abdullah, M.R., Jensch, Inga, Asmat, Tauseef M., Petruschka, L., Pribyl, T., Gellert, Manuela, Lillig, Christopher H., Antelmann, Haike, Hermoso, Juan A., and Hammerschmidt, Sven

Abstract

The respiratory pathogen Streptococcus pneumoniae has evolved efficient mechanisms to resist oxidative stress conditions and to displace other bacteria in the nasopharynx. Here we character ize at physiological, functional and structural levels two novel surface-exposed thioredoxin-family lipoproteins, Etrx1 and Etrx2. The impact of both Etrx proteins and their r edox partner methionine sulfoxide reductase SpMsrAB2 on pneumococcal pathogenesis was assessed in mouse virulence studies and phagocytosis assays. The results demonstrate that loss of function of either both Etrx proteins or SpMsrAB2 dramatically attenuated pneumococcal virulence in the acute mouse pneumonia model and that Etrx proteins compensate each other. The deficiency of Etrx proteins or SpMsrAB2 further enhanced bacterial uptake by macrophages, and accelerated pneumococcal killing by H2O2 or free methionine sulfoxides (MetSO). Moreover, the absence of both Etrx redox pathways provokes an accumulation of oxidized SpMsrAB2 in vivo. Taken together our results reveal insights into the role of two extracellular electron pathways required for reduction of SpMsrAB2 and surface-exposed MetSO. Identification of this system and its target proteins paves the w ay for the design of novel a ntimicrobials

Published
2013

143. Functional analysis of the sortase YhcS in Bacillus subtilis

Author

Fasehee, Hamidreza, primary, Westers, Helga, additional, Bolhuis, Albert, additional, Antelmann, Haike, additional, Hecker, Michael, additional, Quax, Wim J., additional, Mirlohi, Agha F., additional, van Dijl, Jan Maareten, additional, and Ahmadian, Gholamreza, additional

Published
2011
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144. Environmental Salinity Determines the Specificity and Need for Tat-Dependent Secretion of the YwbN Protein in Bacillus subtilis

Author

van der Ploeg, René, primary, Mäder, Ulrike, additional, Homuth, Georg, additional, Schaffer, Marc, additional, Denham, Emma L., additional, Monteferrante, Carmine G., additional, Miethke, Marcus, additional, Marahiel, Mohamed A., additional, Harwood, Colin R., additional, Winter, Theresa, additional, Hecker, Michael, additional, Antelmann, Haike, additional, and van Dijl, Jan Maarten, additional

Published
2011
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