Year |
Citation |
Score |
2018 |
Schorsch M, Kramer M, Goss T, Eisenhut M, Robinson N, Osman D, Wilde A, Sadaf S, Brückler H, Walder L, Scheibe R, Hase T, Hanke GT. A unique ferredoxin acts as a player in the low-iron response of photosynthetic organisms. Proceedings of the National Academy of Sciences of the United States of America. PMID 30514818 DOI: 10.1073/Pnas.1810379115 |
0.313 |
|
2018 |
Schorsch M, Kramer M, Goss T, Eisenhut M, Robinson N, Osman D, Wilde A, Sadaf S, Brückler H, Walder L, Scheibe R, Hase T, Hanke GT. A unique ferredoxin acts as a player in the low-iron response of photosynthetic organisms. Proceedings of the National Academy of Sciences of the United States of America. PMID 30514818 DOI: 10.1073/Pnas.1810379115 |
0.313 |
|
2017 |
Shinohara F, Kurisu G, Hanke G, Bowsher C, Hase T, Kimata-Ariga Y. Structural basis for the isotype-specific interactions of ferredoxin and ferredoxin: NADP oxidoreductase: an evolutionary switch between photosynthetic and heterotrophic assimilation. Photosynthesis Research. 134: 281-289. PMID 28093652 DOI: 10.1007/s11120-016-0331-1 |
0.305 |
|
2017 |
Shinohara F, Kurisu G, Hanke G, Bowsher C, Hase T, Kimata-Ariga Y. Structural basis for the isotype-specific interactions of ferredoxin and ferredoxin: NADP oxidoreductase: an evolutionary switch between photosynthetic and heterotrophic assimilation. Photosynthesis Research. 134: 281-289. PMID 28093652 DOI: 10.1007/s11120-016-0331-1 |
0.305 |
|
2016 |
Kim JY, Nakayama M, Toyota H, Kurisu G, Hase T. Structural and mutational studies of an electron transfer complex of maize sulfite reductase and ferredoxin. Journal of Biochemistry. PMID 26920048 DOI: 10.1093/jb/mvw016 |
0.337 |
|
2016 |
Kim JY, Nakayama M, Toyota H, Kurisu G, Hase T. Structural and mutational studies of an electron transfer complex of maize sulfite reductase and ferredoxin. Journal of Biochemistry. PMID 26920048 DOI: 10.1093/jb/mvw016 |
0.337 |
|
2015 |
Okutani S, Iwai T, Iwatani S, Matsuno K, Takahashi Y, Hase T. Response of Fe-S cluster assembly machinery of Escherichia coli to mechanical stress in a model of amino-acid crystal fermentation. Journal of Bioscience and Bioengineering. PMID 25682519 DOI: 10.1016/j.jbiosc.2015.01.011 |
0.319 |
|
2015 |
Okutani S, Iwai T, Iwatani S, Matsuno K, Takahashi Y, Hase T. Response of Fe-S cluster assembly machinery of Escherichia coli to mechanical stress in a model of amino-acid crystal fermentation. Journal of Bioscience and Bioengineering. PMID 25682519 DOI: 10.1016/j.jbiosc.2015.01.011 |
0.319 |
|
2010 |
Hase T, Mizutani S, Mukohata Y. Expression of Maize Ferredoxin cDNA in Escherichia coli: Comparison of Photosynthetic and Nonphotosynthetic Ferredoxin Isoproteins and their Chimeric Molecule. Plant Physiology. 97: 1395-401. PMID 16668562 DOI: 10.1104/PP.97.4.1395 |
0.326 |
|
2010 |
Suzuki S, Izumihara K, Hase T. Plastid import and iron-sulfur cluster assembly of photosynthetic and nonphotosynthetic ferredoxin isoproteins in maize. Plant Physiology. 97: 375-80. PMID 16668395 DOI: 10.1104/PP.97.1.375 |
0.306 |
|
2010 |
Takahashi Y, Mitsui A, Hase T, Matsubara H. Formation of the iron-sulfur cluster of ferredoxin in isolated chloroplasts. Proceedings of the National Academy of Sciences of the United States of America. 83: 2434-7. PMID 16593686 DOI: 10.1073/PNAS.83.8.2434 |
0.335 |
|
2007 |
Rouhier N, Unno H, Bandyopadhyay S, Masip L, Kim SK, Hirasawa M, Gualberto JM, Lattard V, Kusunoki M, Knaff DB, Georgiou G, Hase T, Johnson MK, Jacquot JP. Functional, structural, and spectroscopic characterization of a glutathione-ligated [2Fe-2S] cluster in poplar glutaredoxin C1. Proceedings of the National Academy of Sciences of the United States of America. 104: 7379-84. PMID 17460036 DOI: 10.1073/Pnas.0702268104 |
0.533 |
|
2006 |
Feng Y, Zhong N, Rouhier N, Hase T, Kusunoki M, Jacquot JP, Jin C, Xia B. Structural insight into poplar glutaredoxin C1 with a bridging iron-sulfur cluster at the active site. Biochemistry. 45: 7998-8008. PMID 16800625 DOI: 10.1021/Bi060444T |
0.506 |
|
2005 |
Kurisu G, Nishiyama D, Kusunoki M, Fujikawa S, Katoh M, Hanke GT, Hase T, Teshima K. A structural basis of Equisetum arvense ferredoxin isoform II producing an alternative electron transfer with ferredoxin-NADP+ reductase. The Journal of Biological Chemistry. 280: 2275-81. PMID 15513928 DOI: 10.1074/jbc.M408904200 |
0.348 |
|
2005 |
Kurisu G, Nishiyama D, Kusunoki M, Fujikawa S, Katoh M, Hanke GT, Hase T, Teshima K. A structural basis of Equisetum arvense ferredoxin isoform II producing an alternative electron transfer with ferredoxin-NADP+ reductase. The Journal of Biological Chemistry. 280: 2275-81. PMID 15513928 DOI: 10.1074/jbc.M408904200 |
0.348 |
|
2005 |
Takahashi Y, Unno H, Hase T, Kusunoki M, Rouhier N, Jacquot J. Crystal structure of glutaredoxin of CxxC1 type from poplar Acta Crystallographica Section a Foundations of Crystallography. 61: c205-c205. DOI: 10.1107/S0108767305091257 |
0.369 |
|
2001 |
Kurisu G, Kusunoki M, Katoh E, Yamazaki T, Teshima K, Onda Y, Kimata-Ariga Y, Hase T. Structure of the electron transfer complex between ferredoxin and ferredoxin-NADP(+) reductase. Nature Structural Biology. 8: 117-21. PMID 11175898 DOI: 10.1038/84097 |
0.317 |
|
2001 |
Nakayama M, Akashi T, Hase T. Plant sulfite reductase: molecular structure, catalytic function and interaction with ferredoxin. Journal of Inorganic Biochemistry. 82: 27-32. PMID 11132635 DOI: 10.1016/S0162-0134(00)00138-0 |
0.333 |
|
2001 |
Bick J, Nakayama M, Setterdahl A, Leustek T, Hase T, Knaff D. Oxidation-reduction properties of two enzymes involved in reductive sulfate assimilation in plants Science Access. 3. DOI: 10.1071/Sa0403459 |
0.322 |
|
1988 |
Fukuyama K, Nagahara Y, Tsukihara T, Katsube Y, Hase T, Matsubara H. Tertiary structure of Bacillus thermoproteolyticus [4Fe-4S] ferredoxin. Evolutionary implications for bacterial ferredoxins. Journal of Molecular Biology. 199: 183-93. PMID 3351918 DOI: 10.1016/0022-2836(88)90388-9 |
0.35 |
|
1983 |
Tsukihara T, Kobayashi M, Nakamura M, Katsube Y, Fukuyama K, Hase T, Wada K, Matsubara H. Structure-function relationship of [2Fe-2S] ferredoxins and design of a model molecule. Bio Systems. 15: 243-57. PMID 7139087 DOI: 10.1016/0303-2647(82)90009-0 |
0.311 |
|
1983 |
Ozaki Y, Nagayama K, Kyogoku Y, Hase T, Matsubara H. Resonance Raman spectroscopic study on the iron-sulfur proteins containing [2Fe-2S] clusters Febs Letters. 152: 236-240. DOI: 10.1016/0014-5793(83)80387-1 |
0.335 |
|
1981 |
Tsukihira T, Fukuyama K, Nakamura M, Katsube Y, Tanaka N, Kakudo M, Wada K, Hase T, Matsubara H. X-ray analysis of a [2Fe-2S] ferrodoxin from Spirulina platensis. Main chain fold and location of side chains at 2.5 A resolution. Journal of Biochemistry. 90: 1763-73. PMID 6801028 DOI: 10.1093/Oxfordjournals.Jbchem.A133654 |
0.301 |
|
1980 |
Fukuyama K, Hase T, Matsumoto S, Tsukihara T, Katsube Y, Tanaka N, Kakudo M, Wada K, Matsubara H. Structure of S. platensis [2Fe-2S] ferredoxin and evolution of chloroplast-type ferredoxins Nature. 286: 522-524. DOI: 10.1038/286522A0 |
0.307 |
|
1979 |
Hase T, Wakabayashi S, Matsubara H, Imai T, Matsumoto T, Tobari J. Mycobacterium smegmatis ferredoxin: a unique distribution of cysteine residues constructing iron--sulfur clusters. Febs Letters. 103: 224-8. PMID 467663 DOI: 10.1016/0014-5793(79)81332-0 |
0.328 |
|
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