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512 results on '"Driessen, Arnold J.M."'

5. Structural and Functional Insights into an Archaeal Lipid Synthase

Author

Ren, Sixue, de Kok, Niels A.W., Gu, Yijun, Yan, Weizhu, Sun, Qiu, Chen, Yunying, He, Jun, Tian, Lejin, Andringa, Ruben L.H., Zhu, Xiaofeng, Tang, Mei, Qi, Shiqian, Xu, Heng, Ren, Haiyan, Fu, Xianghui, Minnaard, Adriaan J., Yang, Shengyong, Zhang, Wanjiang, Li, Weimin, Wei, Yuquan, Driessen, Arnold J.M., and Cheng, Wei

Published
2020
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6. Extremophiles in a changing world

Author

Cowan, Don, Albers, Sonja Verena, Antranikian, Garabed, Atomi, Haruyuki, Averhoff, Beate, Basen, Mirko, Driessen, Arnold J.M., Jebbar, Mohamed, Kelman, Zvi, Kerou, Melina, Littlechild, Jennifer Ann, Müller, Volker Steffen, Schönheit, Peter, Siebers, Bettina, Vorgias, Konstantinos E., Cowan, Don, Albers, Sonja Verena, Antranikian, Garabed, Atomi, Haruyuki, Averhoff, Beate, Basen, Mirko, Driessen, Arnold J.M., Jebbar, Mohamed, Kelman, Zvi, Kerou, Melina, Littlechild, Jennifer Ann, Müller, Volker Steffen, Schönheit, Peter, Siebers, Bettina, and Vorgias, Konstantinos E.

Abstract

Extremophiles and their products have been a major focus of research interest for over 40 years. Through this period, studies of these organisms have contributed hugely to many aspects of the fundamental and applied sciences, and to wider and more philosophical issues such as the origins of life and astrobiology. Our understanding of the cellular adaptations to extreme conditions (such as acid, temperature, pressure and more), of the mechanisms underpinning the stability of macromolecules, and of the subtleties, complexities and limits of fundamental biochemical processes has been informed by research on extremophiles. Extremophiles have also contributed numerous products and processes to the many fields of biotechnology, from diagnostics to bioremediation. Yet, after 40 years of dedicated research, there remains much to be discovered in this field. Fortunately, extremophiles remain an active and vibrant area of research. In the third decade of the twenty-first century, with decreasing global resources and a steadily increasing human population, the world’s attention has turned with increasing urgency to issues of sustainability. These global concerns were encapsulated and formalized by the United Nations with the adoption of the 2030 Agenda for Sustainable Development and the presentation of the seventeen Sustainable Development Goals (SDGs) in 2015. In the run-up to 2030, we consider the contributions that extremophiles have made, and will in the future make, to the SDGs.

Published
2024

7. SecYEG-mediated translocation in a model synthetic cell

Author

Schoenmakers, Ludo L.J., Uijl, Max J. den, Postma, Jelle L., Akker, Tim A.P. van den, Huck, Wilhelm T.S., Driessen, Arnold J.M., Schoenmakers, Ludo L.J., Uijl, Max J. den, Postma, Jelle L., Akker, Tim A.P. van den, Huck, Wilhelm T.S., and Driessen, Arnold J.M.

Abstract

Contains fulltext : 307202.pdf (Publisher’s version ) (Open Access)

Published
2024

38. Structural and Functional Insights into an Archaeal Lipid Synthase

Author

Ren, Sixue, de Kok, Niels A.W., Gu, Yijun, Yan, Weizhu, Sun, Qiu, Chen, Yunying, He, Jun, Tian, Lejin, Andringa, Ruben L.H., Zhu, Xiaofeng, Tang, Mei, Qi, Shiqian, Xu, Heng, Ren, Haiyan, Fu, Xianghui, Minnaard, Adriaan J., Yang, Shengyong, Zhang, Wanjiang, Li, Weimin, Wei, Yuquan, Driessen, Arnold J.M., and Cheng, Wei

Published
2021
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41. The 2008 update of the Aspergillus nidulans genome annotation: A community effort

Author

Wortman, Jennifer Russo, Gilsenan, Jane Mabey, Joardar, Vinita, Deegan, Jennifer, Clutterbuck, John, Andersen, Mikael R., Archer, David, Bencina, Mojca, Braus, Gerhard, Coutinho, Pedro, Döhren, Hans von, Doonan, John, Driessen, Arnold J.M., Durek, Pawel, Espeso, Eduardo, Fekete, Erzsébet, Flipphi, Michel, Estrada, Carlos Garcia, Geysens, Steven, Goldman, Gustavo, de Groot, Piet W.J., Hansen, Kim, Harris, Steven D., Heinekamp, Thorsten, Helmstaedt, Kerstin, Henrissat, Bernard, Hofmann, Gerald, Homan, Tim, Horio, Tetsuya, Horiuchi, Hiroyuki, James, Steve, Jones, Meriel, Karaffa, Levente, Karányi, Zsolt, Kato, Masashi, Keller, Nancy, Kelly, Diane E., Kiel, Jan A.K.W., Kim, Jung-Mi, van der Klei, Ida J., Klis, Frans M., Kovalchuk, Andriy, Kraševec, Nada, Kubicek, Christian P., Liu, Bo, MacCabe, Andrew, Meyer, Vera, Mirabito, Pete, Miskei, Márton, Mos, Magdalena, Mullins, Jonathan, Nelson, David R., Nielsen, Jens, Oakley, Berl R., Osmani, Stephen A., Pakula, Tiina, Paszewski, Andrzej, Paulsen, Ian, Pilsyk, Sebastian, Pócsi, István, Punt, Peter J., Ram, Arthur F.J., Ren, Qinghu, Robellet, Xavier, Robson, Geoff, Seiboth, Bernhard, van Solingen, Piet, Specht, Thomas, Sun, Jibin, Taheri-Talesh, Naimeh, Takeshita, Norio, Ussery, Dave, vanKuyk, Patricia A., Visser, Hans, van de Vondervoort, Peter J.I., de Vries, Ronald P., Walton, Jonathan, Xiang, Xin, Xiong, Yi, Zeng, An Ping, Brandt, Bernd W., Cornell, Michael J., van den Hondel, Cees A.M.J.J., Visser, Jacob, Oliver, Stephen G., and Turner, Geoffrey

Published
2009
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43. Reshaping of the conformational search of a protein by the chaperone trigger factor

Author

Mashaghi, Alireza, Kramer, Gunter, Bechtluft, Philipp, Zachmann-Brand, Beate, Driessen, Arnold J.M., Bukau, Bernd, and Tans, Sander J.

Subjects
Research, Properties, Methods, Protein folding -- Research, Conformational analysis -- Methods, Molecular chaperones -- Properties, Binding proteins -- Properties
Abstract

Atomic force microscopes and optical tweezers can be used to study protein folding at the single-molecule level (13,14). By pulling proteins at their ends while accurately monitoring lengths and forces, [...], Protein folding is often described as a search process, in which polypeptides explore different conformations to find their native structure. Molecular chaperones are known to improve folding yields by suppressing aggregation between polypeptides before this conformational search starts (1,2), as well as by rescuing misfolds after it ends (1,3). Although chaperones have long been speculated to also affect the conformational search itself--by reshaping the underlying folding landscape along the folding trajectory (4,5)--direct experimental evidence has been scarce so far. In Escherichiacoli, the general chaperone trigger factor (6-8) (TF) couldplaysucharole. TF has been shown to interact with nascent chains at the ribosome (9,10), with polypeptides released from the ribosome into the cytosol (11), and with fully folded proteins before their assembly into larger complexes (12). To investigate the effect of TF from E. coli on the conformational search of polypeptides to their native state, we investigated individual maltose binding protein (MBP) molecules using optical tweezers. Here we show that TF binds folded structures smaller than one domain, which are then stable for seconds and ultimately convert to the native state. Moreover, TF stimulates native folding in constructs of repeated MBP domains. The results indicate that TF promotes correct folding by protecting partially folded states from distant interactions that produce stable misfolded states. As TF interacts with most newly synthesized proteins in E. coli, we expect these findings to be of general importance in understanding protein folding pathways.

Published
2013

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