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C-terminal processing of tyrosinase is responsible for activation of Pholiota microspora proenzyme.
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- Applied Microbiology & Biotechnology, 2011, v. 90, n. 1, p. 227, doi. 10.1007/s00253-010-3039-8
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- Article
Kinetic study on myoglobin refolding monitored by five optical probe stopped-flow methods.
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- Proteins, 1994, v. 19, n. 2, p. 110, doi. 10.1002/prot.340190204
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- Article
Stability of immobilized α-chymotrypsin.
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- Biotechnology & Bioengineering, 1981, v. 23, n. 6, p. 1219, doi. 10.1002/bit.260230605
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- Article
Metabolomics Profiling of Roasted Stem Tea Using Gas Chromatography- Mass Spectrometry and a Sensory Test.
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- Food Science & Technology Research, 2018, v. 24, n. 6, p. 1059, doi. 10.3136/fstr.24.1059
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- Article
FER and LecRK show haplotype-dependent cold-responsiveness and mediate freezing tolerance in Lotus japonicus.
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- Plant Physiology, 2023, v. 191, n. 2, p. 1138, doi. 10.1093/plphys/kiac533
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- Article
Purification, Characterization, and Molecular Cloning of Tyrosinase from Pholiota nameko.
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- Bioscience, Biotechnology & Biochemistry, 2007, v. 71, n. 7, p. 1752, doi. 10.1271/bbb.70171
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- Article
The pro-enzyme C-terminal processing domain of Pholiota nameko tyrosinase is responsible for folding of the N-terminal catalytic domain.
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- Applied Microbiology & Biotechnology, 2015, v. 99, n. 13, p. 5499, doi. 10.1007/s00253-015-6597-y
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- Article
Extreme genetic signatures of local adaptation during Lotus japonicus colonization of Japan.
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- Nature Communications, 2020, v. 11, n. 1, p. 1, doi. 10.1038/s41467-019-14213-y
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- Article
Remarkable Functional Aspects of Myoglobin Induced by Diazaheme Prosthetic Group1.
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- Journal of Biochemistry, 1997, v. 121, n. 4, p. 654, doi. 10.1093/oxfordjournals.jbchem.a021636
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- Article
Kinetic Characterization of Antibody-Catalyzed Insertion of a Metal Ion into Porphyrin.
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- Journal of Biochemistry, 1996, v. 119, n. 5, p. 857, doi. 10.1093/oxfordjournals.jbchem.a021322
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- Article