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1
The transDSL ligase ribozyme can utilize various forms of modules to clamp its substrate and enzyme units
The transDSL ligase ribozyme can utilize various forms of modules to clamp its substrate and enzyme units
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The transDSL ligase ribozyme can utilize various forms of modules to clamp its substrate and enzyme units

Ishikawa, J., Kyushu Univ., Fukuoka (Japan) ; Isomoto, N ; Fujita, Y ; Furuta, H ; Ikawa, Y

Bioscience, biotechnology, and biochemistry, 2010, Vol.74 (4), p.872-874 [Periódico revisado por pares]

Tokyo: Japan Society for Bioscience, Biotechnology, and Agrochemistry

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2
Purification and properties of hydroquinone hydroxylase, a FAD-dependent monooxygenase involved in the catabolism of 4-hydroxybenzoate in Candida parapsilosis CBS604
Purification and properties of hydroquinone hydroxylase, a FAD-dependent monooxygenase involved in the catabolism of 4-hydroxybenzoate in Candida parapsilosis CBS604
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Purification and properties of hydroquinone hydroxylase, a FAD-dependent monooxygenase involved in the catabolism of 4-hydroxybenzoate in Candida parapsilosis CBS604

Eppink, M.H.M ; Cammaart, E ; Wassenaar, D. van ; Middelhoven, W.J ; Berkel, W.J.H. van

European journal of biochemistry, 2000-12, Vol.267 (23), p.6832-6840 [Periódico revisado por pares]

Oxford, UK: Blackwell Science Ltd

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3
Detailed characterization of the posttranscriptional gene-silencing-related small RNA in a GUS gene-silenced tobacco
Detailed characterization of the posttranscriptional gene-silencing-related small RNA in a GUS gene-silenced tobacco
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Detailed characterization of the posttranscriptional gene-silencing-related small RNA in a GUS gene-silenced tobacco

HUTVÁGNER, GYÖRGY ; MLYNÁROVÁ, LUDMILA ; NAP, JAN-PETER

RNA (Cambridge), 2000-10, Vol.6 (10), p.1445-1454, Article S1355838200001096 [Periódico revisado por pares]

United States: Cambridge University Press

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4
Post-prandial protease activity in the digestive tract of African catfish Clarias gariepinus larvae fed decapsulated cysts of Artemia
Post-prandial protease activity in the digestive tract of African catfish Clarias gariepinus larvae fed decapsulated cysts of Artemia
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Post-prandial protease activity in the digestive tract of African catfish Clarias gariepinus larvae fed decapsulated cysts of Artemia

Garcia-Ortega, A ; Verreth, J ; Segner, H

Fish physiology and biochemistry, 2000-04, Vol.22 (3), p.237-244 [Periódico revisado por pares]

Dordrecht: Springer Nature B.V

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5
Inhibition of the acid lipase activity by apolipoprotein A-I in the presence of lysosomal proteases
Inhibition of the acid lipase activity by apolipoprotein A-I in the presence of lysosomal proteases
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Inhibition of the acid lipase activity by apolipoprotein A-I in the presence of lysosomal proteases

Inoue, Y. (Kagoshima Univ. (Japan). Faculty of Agriculture) ; Ose, T ; Mukai, S ; Ehira, S ; Yonekura, M ; Hou, D.X ; Fujii, M

Bioscience, biotechnology, and biochemistry, 1999-05, Vol.63 (5), p.937-939 [Periódico revisado por pares]

Tokyo: Japan Society for Bioscience, Biotechnology, and Agrochemistry

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6
Ubiquinol:cytochrome c oxidoreductase: effects of inhibitors on reverse electron transfer from the iron-sulfur protein to cytochrome b
Ubiquinol:cytochrome c oxidoreductase: effects of inhibitors on reverse electron transfer from the iron-sulfur protein to cytochrome b
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Ubiquinol:cytochrome c oxidoreductase: effects of inhibitors on reverse electron transfer from the iron-sulfur protein to cytochrome b

Matsuno-Yagi, A. (The Scripps Research Institute, La Jolla CA.) ; Hatefi, Y

The Journal of biological chemistry, 1999-04, Vol.274 (14), p.9283-9288 [Periódico revisado por pares]

United States

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7
Three classes of inhibitors share a common binding domain in mitochondrial complex I (NADH:ubiquinone oxidoreductase)
Three classes of inhibitors share a common binding domain in mitochondrial complex I (NADH:ubiquinone oxidoreductase)
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Three classes of inhibitors share a common binding domain in mitochondrial complex I (NADH:ubiquinone oxidoreductase)

Okun, J.G. (Universitatsklinikum Frankfurt, Germany.) ; Lummen, P ; Brandt, U

The Journal of biological chemistry, 1999-01, Vol.274 (5), p.2625-2630 [Periódico revisado por pares]

United States: American Society for Biochemistry and Molecular Biology

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8
Functional analysis of the DXDDTA motif in squalene-hopene cyclase by site-directed mutagenesis experiments: Initiation site of the polycyclization reaction and stabilization site of the carbocation intermediate of the initially cyclized A-ring
Functional analysis of the DXDDTA motif in squalene-hopene cyclase by site-directed mutagenesis experiments: Initiation site of the polycyclization reaction and stabilization site of the carbocation intermediate of the initially cyclized A-ring
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Functional analysis of the DXDDTA motif in squalene-hopene cyclase by site-directed mutagenesis experiments: Initiation site of the polycyclization reaction and stabilization site of the carbocation intermediate of the initially cyclized A-ring

Sato, T. (Niigata Univ. (Japan)) ; Hoshino, T

Bioscience, biotechnology, and biochemistry, 1999-01, Vol.63 (12), p.2189-2198 [Periódico revisado por pares]

Tokyo: Japan Society for Bioscience, Biotechnology, and Agrochemistry

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9
Topology of Euglena Chloroplast Protein Precursors within Endoplasmic Reticulum to Golgi to Chloroplast Transport Vesicles
Topology of Euglena Chloroplast Protein Precursors within Endoplasmic Reticulum to Golgi to Chloroplast Transport Vesicles
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Topology of Euglena Chloroplast Protein Precursors within Endoplasmic Reticulum to Golgi to Chloroplast Transport Vesicles

Sulli, Chidananda ; Fang, ZhiWei ; Muchhal, Umesh ; Schwartzbach, Steven D.

The Journal of biological chemistry, 1999-01, Vol.274 (1), p.457-463 [Periódico revisado por pares]

United States: Elsevier Inc

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10
Y'-Help1, a DNA helicase encoded by the yeast subtelomeric Y' element, is induced in survivors defective for telomerase
Y'-Help1, a DNA helicase encoded by the yeast subtelomeric Y' element, is induced in survivors defective for telomerase
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Y'-Help1, a DNA helicase encoded by the yeast subtelomeric Y' element, is induced in survivors defective for telomerase

Yamada, M. (Tokyo Institute of Technology, Yokohama, Japan.) ; Hayatsu, N ; Matsuura, A ; Ishikawa, F

The Journal of biological chemistry, 1998-12, Vol.273 (50), p.33360-33366 [Periódico revisado por pares]

United States

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