Chemical nucleases

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Artificial nucleases.

Chembiochem : a European journal of chemical biology·2002

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Oligoribonucleotide-based gene-specific transcription inhibitors that target the open complex.

Methods (San Diego, Calif.)·2001

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An approach to gene-specific transcription inhibition using oligonucleotides complementary to the template strand of the open complex.

Proceedings of the National Academy of Sciences of the United States of America·2000

Same author

Scission of DNA at a preselected sequence using a single-strand-specific chemical nuclease.

Chemistry & biology·1998

Same author

Protease activity of 1,10-phenanthroline-copper(I). Targeted scission of the catalytic site of carbonic anhydrase.

Biochemistry·1998

Same author

Variable structures of Fis-DNA complexes determined by flanking DNA-protein contacts.

Journal of molecular biology·1996

Same journal

Aromatic Cage-Directed Azide-Methyllysine Photochemistry for Profiling Nonhistone Interacting Partners of the MeCP2 Methyl-CpG-Binding Domain.

Biochemistry·2026

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Differential Hydroxypyruvate Processing by E. coli and P. aeruginosa DXP Synthases Reveals Preferential Xylulose 5-Phosphate Formation by the P. aeruginosa Enzyme.

Biochemistry·2026

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Structural and Functional Characterization of Heterologous Nitrogenase Complexes.

Biochemistry·2026

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Discovery of Bacterial Unspecific Peroxygenases.

Biochemistry·2026

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Lactate Biology: Subcellular Routing and Chemical Form Define Function.

Biochemistry·2026

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Nature's Anaerobic Toolkit: Glycyl Radical Enzymes and Their Expanding Functional and Mechanistic Diversity.

Biochemistry·2026

Related Experiment Videos

Chemical nucleases

Related Concept Videos

Artificial nucleases.

Oligoribonucleotide-based gene-specific transcription inhibitors that target the open complex.

An approach to gene-specific transcription inhibition using oligonucleotides complementary to the template strand of the open complex.

Scission of DNA at a preselected sequence using a single-strand-specific chemical nuclease.

Protease activity of 1,10-phenanthroline-copper(I). Targeted scission of the catalytic site of carbonic anhydrase.

Variable structures of Fis-DNA complexes determined by flanking DNA-protein contacts.

Aromatic Cage-Directed Azide-Methyllysine Photochemistry for Profiling Nonhistone Interacting Partners of the MeCP2 Methyl-CpG-Binding Domain.

Differential Hydroxypyruvate Processing by <i>E. coli</i> and <i>P. aeruginosa</i> DXP Synthases Reveals Preferential Xylulose 5-Phosphate Formation by the <i>P. aeruginosa</i> Enzyme.

Structural and Functional Characterization of Heterologous Nitrogenase Complexes.

Discovery of Bacterial Unspecific Peroxygenases.

Lactate Biology: Subcellular Routing and Chemical Form Define Function.

Nature's Anaerobic Toolkit: Glycyl Radical Enzymes and Their Expanding Functional and Mechanistic Diversity.

Related Experiment Videos

Chemical nucleases

Related Concept Videos

Related Articles

Artificial nucleases.

Oligoribonucleotide-based gene-specific transcription inhibitors that target the open complex.

An approach to gene-specific transcription inhibition using oligonucleotides complementary to the template strand of the open complex.

Scission of DNA at a preselected sequence using a single-strand-specific chemical nuclease.

Protease activity of 1,10-phenanthroline-copper(I). Targeted scission of the catalytic site of carbonic anhydrase.

Variable structures of Fis-DNA complexes determined by flanking DNA-protein contacts.

Aromatic Cage-Directed Azide-Methyllysine Photochemistry for Profiling Nonhistone Interacting Partners of the MeCP2 Methyl-CpG-Binding Domain.

Differential Hydroxypyruvate Processing by <i>E. coli</i> and <i>P. aeruginosa</i> DXP Synthases Reveals Preferential Xylulose 5-Phosphate Formation by the <i>P. aeruginosa</i> Enzyme.

Structural and Functional Characterization of Heterologous Nitrogenase Complexes.

Discovery of Bacterial Unspecific Peroxygenases.

Lactate Biology: Subcellular Routing and Chemical Form Define Function.

Nature's Anaerobic Toolkit: Glycyl Radical Enzymes and Their Expanding Functional and Mechanistic Diversity.