Статті в журналах з теми "Iron-sulfur Protein Assembly"
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Liu, Jian She, Lin Qian, and Chun Li Zheng. "Biogenesis and Transfer of Iron-Sulfur Clusters from Acidithiobacillus ferrooxidans." Advanced Materials Research 825 (October 2013): 198–201. http://dx.doi.org/10.4028/www.scientific.net/amr.825.198.
Повний текст джерелаSong, Daisheng, and Frank S. Lee. "Mouse Knock-out of IOP1 Protein Reveals Its Essential Role in Mammalian Cytosolic Iron-Sulfur Protein Biogenesis." Journal of Biological Chemistry 286, no. 18 (March 2, 2011): 15797–805. http://dx.doi.org/10.1074/jbc.m110.201731.
Повний текст джерелаDos Santos, Patricia C., Archer D. Smith, Jeverson Frazzon, Valerie L. Cash, Michael K. Johnson, and Dennis R. Dean. "Iron-Sulfur Cluster Assembly." Journal of Biological Chemistry 279, no. 19 (March 1, 2004): 19705–11. http://dx.doi.org/10.1074/jbc.m400278200.
Повний текст джерелаSrour, Batoul, Sylvain Gervason, Beata Monfort, and Benoit D’Autréaux. "Mechanism of Iron–Sulfur Cluster Assembly: In the Intimacy of Iron and Sulfur Encounter." Inorganics 8, no. 10 (October 3, 2020): 55. http://dx.doi.org/10.3390/inorganics8100055.
Повний текст джерелаBalk, Janneke, Daili J. Aguilar Netz, Katharina Tepper, Antonio J. Pierik, and Roland Lill. "The Essential WD40 Protein Cia1 Is Involved in a Late Step of Cytosolic and Nuclear Iron-Sulfur Protein Assembly." Molecular and Cellular Biology 25, no. 24 (December 15, 2005): 10833–41. http://dx.doi.org/10.1128/mcb.25.24.10833-10841.2005.
Повний текст джерелаLu, Jianxin, Juanjuan Yang, Guoqiang Tan, and Huangen Ding. "Complementary roles of SufA and IscA in the biogenesis of iron–sulfur clusters in Escherichia coli." Biochemical Journal 409, no. 2 (December 21, 2007): 535–43. http://dx.doi.org/10.1042/bj20071166.
Повний текст джерелаStehling, Oliver, Daili J. A. Netz, Brigitte Niggemeyer, Ralf Rösser, Richard S. Eisenstein, Helene Puccio, Antonio J. Pierik, and Roland Lill. "Human Nbp35 Is Essential for both Cytosolic Iron-Sulfur Protein Assembly and Iron Homeostasis." Molecular and Cellular Biology 28, no. 17 (June 23, 2008): 5517–28. http://dx.doi.org/10.1128/mcb.00545-08.
Повний текст джерелаLu, Jianxin, Jacob P. Bitoun, Guoqiang Tan, Wu Wang, Wenguang Min, and Huangen Ding. "Iron-binding activity of human iron–sulfur cluster assembly protein hIscA1." Biochemical Journal 428, no. 1 (April 28, 2010): 125–31. http://dx.doi.org/10.1042/bj20100122.
Повний текст джерелаIshiyama, Akihiko, Chika Sakai, Yuichi Matsushima, Satoru Noguchi, Satomi Mitsuhashi, Yukari Endo, Yukiko K. Hayashi, et al. "IBA57 mutations abrogate iron-sulfur cluster assembly leading to cavitating leukoencephalopathy." Neurology Genetics 3, no. 5 (September 8, 2017): e184. http://dx.doi.org/10.1212/nxg.0000000000000184.
Повний текст джерелаBernard, Delphine G., Daili J. A. Netz, Thibaut J. Lagny, Antonio J. Pierik, and Janneke Balk. "Requirements of the cytosolic iron–sulfur cluster assembly pathway in Arabidopsis." Philosophical Transactions of the Royal Society B: Biological Sciences 368, no. 1622 (July 19, 2013): 20120259. http://dx.doi.org/10.1098/rstb.2012.0259.
Повний текст джерелаBoyd, Jeffrey M., Randy M. Drevland, Diana M. Downs, and David E. Graham. "Archaeal ApbC/Nbp35 Homologs Function as Iron-Sulfur Cluster Carrier Proteins." Journal of Bacteriology 191, no. 5 (December 29, 2008): 1490–97. http://dx.doi.org/10.1128/jb.01469-08.
Повний текст джерелаLill, Roland, and Sven-A. Freibert. "Mechanisms of Mitochondrial Iron-Sulfur Protein Biogenesis." Annual Review of Biochemistry 89, no. 1 (June 20, 2020): 471–99. http://dx.doi.org/10.1146/annurev-biochem-013118-111540.
Повний текст джерелаWang, Wu, Hao Huang, Guoqiang Tan, Fan Si, Min Liu, Aaron P. Landry, Jianxin Lu, and Huangen Ding. "In vivo evidence for the iron-binding activity of an iron–sulfur cluster assembly protein IscA in Escherichia coli." Biochemical Journal 432, no. 3 (November 25, 2010): 429–36. http://dx.doi.org/10.1042/bj20101507.
Повний текст джерелаBian, Shumin, and J. A. Cowan. "Protein-bound iron–sulfur centers. Form, function, and assembly." Coordination Chemistry Reviews 190-192 (September 1999): 1049–66. http://dx.doi.org/10.1016/s0010-8545(99)00157-5.
Повний текст джерелаMühlenhoff, Ulrich, Nadine Richhardt, Jana Gerber, and Roland Lill. "Characterization of Iron-Sulfur Protein Assembly in Isolated Mitochondria." Journal of Biological Chemistry 277, no. 33 (June 13, 2002): 29810–16. http://dx.doi.org/10.1074/jbc.m204675200.
Повний текст джерелаConte, Laura, and Vincenzo Zara. "The Rieske Iron-Sulfur Protein: Import and Assembly into the Cytochrome Complex of Yeast Mitochondria." Bioinorganic Chemistry and Applications 2011 (2011): 1–9. http://dx.doi.org/10.1155/2011/363941.
Повний текст джерелаTokumoto, U., S. Nomura, Y. Minami, H. Mihara, S. i. Kato, T. Kurihara, N. Esaki, H. Kanazawa, H. Matsubara, and Y. Takahashi. "Network of Protein-Protein Interactions among Iron-Sulfur Cluster Assembly Proteins in Escherichia coli1." Journal of Biochemistry 131, no. 5 (May 1, 2002): 713–19. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a003156.
Повний текст джерелаCai, Kai, and John Markley. "NMR as a Tool to Investigate the Processes of Mitochondrial and Cytosolic Iron-Sulfur Cluster Biosynthesis." Molecules 23, no. 9 (August 31, 2018): 2213. http://dx.doi.org/10.3390/molecules23092213.
Повний текст джерелаCherak, Stephana J., and Raymond J. Turner. "Assembly pathway of a bacterial complex iron sulfur molybdoenzyme." Biomolecular Concepts 8, no. 3-4 (September 26, 2017): 155–67. http://dx.doi.org/10.1515/bmc-2017-0011.
Повний текст джерелаKeller, Rebecca, Jeanine de Keyzer, Arnold J. M. Driessen, and Tracy Palmer. "Co-operation between different targeting pathways during integration of a membrane protein." Journal of Cell Biology 199, no. 2 (October 8, 2012): 303–15. http://dx.doi.org/10.1083/jcb.201204149.
Повний текст джерелаSchwenkert, Serena, Daili J. A. Netz, Jeverson Frazzon, Antonio J. Pierik, Eckhard Bill, Jeferson Gross, Roland Lill, and Jörg Meurer. "Chloroplast HCF101 is a scaffold protein for [4Fe-4S] cluster assembly." Biochemical Journal 425, no. 1 (December 14, 2009): 207–18. http://dx.doi.org/10.1042/bj20091290.
Повний текст джерелаNetz, Daili J. A., Antonio J. Pierik, Martin Stümpfig, Eckhard Bill, Anil K. Sharma, Leif J. Pallesen, William E. Walden, and Roland Lill. "A Bridging [4Fe-4S] Cluster and Nucleotide Binding Are Essential for Function of the Cfd1-Nbp35 Complex as a Scaffold in Iron-Sulfur Protein Maturation." Journal of Biological Chemistry 287, no. 15 (February 23, 2012): 12365–78. http://dx.doi.org/10.1074/jbc.m111.328914.
Повний текст джерелаCamponeschi, Francesca, Simone Ciofi-Baffoni, Vito Calderone, and Lucia Banci. "Molecular Basis of Rare Diseases Associated to the Maturation of Mitochondrial [4Fe-4S]-Containing Proteins." Biomolecules 12, no. 7 (July 21, 2022): 1009. http://dx.doi.org/10.3390/biom12071009.
Повний текст джерелаMühlenhoff, Ulrich, Joseph J. Braymer, Stefan Christ, Nicole Rietzschel, Marta A. Uzarska, Benjamin D. Weiler, and Roland Lill. "Glutaredoxins and iron-sulfur protein biogenesis at the interface of redox biology and iron metabolism." Biological Chemistry 401, no. 12 (November 26, 2020): 1407–28. http://dx.doi.org/10.1515/hsz-2020-0237.
Повний текст джерелаCampbell, Courtney J., Ashley E. Pall, Akshata R. Naik, Lindsey N. Thompson, and Timothy L. Stemmler. "Molecular Details of the Frataxin–Scaffold Interaction during Mitochondrial Fe–S Cluster Assembly." International Journal of Molecular Sciences 22, no. 11 (June 2, 2021): 6006. http://dx.doi.org/10.3390/ijms22116006.
Повний текст джерелаElchennawi, Ingie, and Sandrine Ollagnier de Choudens. "Iron–Sulfur Clusters toward Stresses: Implication for Understanding and Fighting Tuberculosis." Inorganics 10, no. 10 (October 18, 2022): 174. http://dx.doi.org/10.3390/inorganics10100174.
Повний текст джерелаQian, Lin, Chunli Zheng, and Jianshe Liu. "Characterization of iron-sulfur cluster assembly protein isca from Acidithiobacillus ferrooxidans." Biochemistry (Moscow) 78, no. 3 (March 2013): 244–51. http://dx.doi.org/10.1134/s000629791303005x.
Повний текст джерелаWu, Gong, Sheref S. Mansy, Shu-pao Wu, Kristene K. Surerus, Matthew W. Foster, and J. A. Cowan. "Characterization of an Iron−Sulfur Cluster Assembly Protein (ISU1) fromSchizosaccharomyces pombe†." Biochemistry 41, no. 15 (April 2002): 5024–32. http://dx.doi.org/10.1021/bi016073s.
Повний текст джерелаCiesielski, Szymon J., Brenda Schilke, Jaroslaw Marszalek, and Elizabeth A. Craig. "Protection of scaffold protein Isu from degradation by the Lon protease Pim1 as a component of Fe–S cluster biogenesis regulation." Molecular Biology of the Cell 27, no. 7 (April 2016): 1060–68. http://dx.doi.org/10.1091/mbc.e15-12-0815.
Повний текст джерелаMühlenhoff, Ulrich, Mathias J. Gerl, Birgit Flauger, Heike M. Pirner, Sandra Balser, Nadine Richhardt, Roland Lill, and Jürgen Stolz. "The Iron-Sulfur Cluster Proteins Isa1 and Isa2 Are Required for the Function but Not for the De Novo Synthesis of the Fe/S Clusters of Biotin Synthase in Saccharomyces cerevisiae." Eukaryotic Cell 6, no. 3 (January 26, 2007): 495–504. http://dx.doi.org/10.1128/ec.00191-06.
Повний текст джерелаCrooks, Daniel R., Manik C. Ghosh, Ronald G. Haller, Wing-Hang Tong, and Tracey A. Rouault. "Posttranslational stability of the heme biosynthetic enzyme ferrochelatase is dependent on iron availability and intact iron-sulfur cluster assembly machinery." Blood 115, no. 4 (January 28, 2010): 860–69. http://dx.doi.org/10.1182/blood-2009-09-243105.
Повний текст джерелаLeimkühler, Silke. "The Biosynthesis of the Molybdenum Cofactor in Escherichia coli and Its Connection to FeS Cluster Assembly and the Thiolation of tRNA." Advances in Biology 2014 (April 29, 2014): 1–21. http://dx.doi.org/10.1155/2014/808569.
Повний текст джерелаBerteau, Olivier. "A missed Fe-S cluster handoff causes a metabolic shakeup." Journal of Biological Chemistry 293, no. 21 (May 25, 2018): 8312–13. http://dx.doi.org/10.1074/jbc.h118.002883.
Повний текст джерелаMoseler, Anna, Isabel Aller, Stephan Wagner, Thomas Nietzel, Jonathan Przybyla-Toscano, Ulrich Mühlenhoff, Roland Lill, et al. "The mitochondrial monothiol glutaredoxin S15 is essential for iron-sulfur protein maturation in Arabidopsis thaliana." Proceedings of the National Academy of Sciences 112, no. 44 (October 19, 2015): 13735–40. http://dx.doi.org/10.1073/pnas.1510835112.
Повний текст джерелаWang, Jian, Carine Fillebeen, Guohua Chen, Annette Biederbick, Roland Lill, and Kostas Pantopoulos. "Iron-Dependent Degradation of Apo-IRP1 by the Ubiquitin-Proteasome Pathway." Molecular and Cellular Biology 27, no. 7 (January 22, 2007): 2423–30. http://dx.doi.org/10.1128/mcb.01111-06.
Повний текст джерелаDuarte, Margarida, and Arnaldo Videira. "Respiratory Chain Complex I Is Essential for Sexual Development in Neurospora and Binding of Iron Sulfur Clusters Are Required for Enzyme Assembly." Genetics 156, no. 2 (October 1, 2000): 607–15. http://dx.doi.org/10.1093/genetics/156.2.607.
Повний текст джерелаStehling, Oliver, Jae-Hun Jeoung, Sven A. Freibert, Viktoria D. Paul, Sebastian Bänfer, Brigitte Niggemeyer, Ralf Rösser, Holger Dobbek, and Roland Lill. "Function and crystal structure of the dimeric P-loop ATPase CFD1 coordinating an exposed [4Fe-4S] cluster for transfer to apoproteins." Proceedings of the National Academy of Sciences 115, no. 39 (September 10, 2018): E9085—E9094. http://dx.doi.org/10.1073/pnas.1807762115.
Повний текст джерелаManicki, Mateusz, Julia Majewska, Szymon Ciesielski, Brenda Schilke, Anna Blenska, Jacek Kominek, Jaroslaw Marszalek, Elizabeth A. Craig, and Rafal Dutkiewicz. "Overlapping Binding Sites of the Frataxin Homologue Assembly Factor and the Heat Shock Protein 70 Transfer Factor on the Isu Iron-Sulfur Cluster Scaffold Protein." Journal of Biological Chemistry 289, no. 44 (September 16, 2014): 30268–78. http://dx.doi.org/10.1074/jbc.m114.596726.
Повний текст джерелаElchennawi, Ingie, Philippe Carpentier, Christelle Caux, Marine Ponge, and Sandrine Ollagnier de Choudens. "Structural and Biochemical Characterization of Mycobacterium tuberculosis Zinc SufU-SufS Complex." Biomolecules 13, no. 5 (April 24, 2023): 732. http://dx.doi.org/10.3390/biom13050732.
Повний текст джерелаLaGier, Michael J., Jan Tachezy, Frantisek Stejskal, Katerina Kutisova, and Janet S. Keithly. "Mitochondrial-type iron–sulfur cluster biosynthesis genes (IscS and IscU) in the apicomplexan Cryptosporidium parvum." Microbiology 149, no. 12 (December 1, 2003): 3519–30. http://dx.doi.org/10.1099/mic.0.26365-0.
Повний текст джерелаRydz, Leszek, Maria Wróbel, and Halina Jurkowska. "Sulfur Administration in Fe–S Cluster Homeostasis." Antioxidants 10, no. 11 (October 29, 2021): 1738. http://dx.doi.org/10.3390/antiox10111738.
Повний текст джерелаLa, Ping, Valentina Ghiaccio, Jianbing Zhang, and Stefano Rivella. "An Orchestrated Balance between Mitochondria Biogenesis, Iron-Sulfur Cluster Synthesis and Cellular Iron Acquisition." Blood 132, Supplement 1 (November 29, 2018): 1048. http://dx.doi.org/10.1182/blood-2018-99-112198.
Повний текст джерелаMendel, Ralf R., Thomas W. Hercher, Arkadiusz Zupok, Muhammad A. Hasnat, and Silke Leimkühler. "The Requirement of Inorganic Fe-S Clusters for the Biosynthesis of the Organometallic Molybdenum Cofactor." Inorganics 8, no. 7 (July 16, 2020): 43. http://dx.doi.org/10.3390/inorganics8070043.
Повний текст джерелаBoutigny, Sylvain, Avneesh Saini, Edward E. K. Baidoo, Natasha Yeung, Jay D. Keasling, and Gareth Butland. "Physical and Functional Interactions of a Monothiol Glutaredoxin and an Iron Sulfur Cluster Carrier Protein with the Sulfur-donating Radical S-Adenosyl-l-methionine Enzyme MiaB." Journal of Biological Chemistry 288, no. 20 (March 29, 2013): 14200–14211. http://dx.doi.org/10.1074/jbc.m113.460360.
Повний текст джерелаGerber, Jana, Karina Neumann, Corinna Prohl, Ulrich Mühlenhoff, and Roland Lill. "The Yeast Scaffold Proteins Isu1p and Isu2p Are Required inside Mitochondria for Maturation of Cytosolic Fe/S Proteins." Molecular and Cellular Biology 24, no. 11 (June 1, 2004): 4848–57. http://dx.doi.org/10.1128/mcb.24.11.4848-4857.2004.
Повний текст джерелаLill, Roland. "From the discovery to molecular understanding of cellular iron-sulfur protein biogenesis." Biological Chemistry 401, no. 6-7 (May 26, 2020): 855–76. http://dx.doi.org/10.1515/hsz-2020-0117.
Повний текст джерелаBogenhagen, Daniel F., and John D. Haley. "Pulse-chase SILAC–based analyses reveal selective oversynthesis and rapid turnover of mitochondrial protein components of respiratory complexes." Journal of Biological Chemistry 295, no. 9 (January 23, 2020): 2544–54. http://dx.doi.org/10.1074/jbc.ra119.011791.
Повний текст джерелаChillappagari, Shashi, Andreas Seubert, Hein Trip, Oscar P. Kuipers, Mohamed A. Marahiel, and Marcus Miethke. "Copper Stress Affects Iron Homeostasis by Destabilizing Iron-Sulfur Cluster Formation in Bacillus subtilis." Journal of Bacteriology 192, no. 10 (March 16, 2010): 2512–24. http://dx.doi.org/10.1128/jb.00058-10.
Повний текст джерелаRybniker, Jan, Florence Pojer, Jan Marienhagen, Gaëlle S. Kolly, Jeffrey M. Chen, Edeltraud van Gumpel, Pia Hartmann, and Stewart T. Cole. "The cysteine desulfurase IscS of Mycobacterium tuberculosis is involved in iron–sulfur cluster biogenesis and oxidative stress defence." Biochemical Journal 459, no. 3 (April 11, 2014): 467–78. http://dx.doi.org/10.1042/bj20130732.
Повний текст джерелаVogel, Frank, Carsten Bornhövd, Walter Neupert, and Andreas S. Reichert. "Dynamic subcompartmentalization of the mitochondrial inner membrane." Journal of Cell Biology 175, no. 2 (October 16, 2006): 237–47. http://dx.doi.org/10.1083/jcb.200605138.
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