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Laboratory and controlled field experiments using potassium permanganate to remediate trichloroethylene and perchloroethylene DNAPLs in porous media

Journal of contaminant hydrology, 1998-02, Vol.29 (3), p.205-224

1998

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Two pairs of oppositely charged amino acids from Jun and Fos confer heterodimerization to GCN4 leucine zipper

The Journal of biological chemistry, 1994-06, Vol.269 (23), p.16247-16253

1994

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DNA binding properties of the LexA repressor

Biochimie, 1991-04, Vol.73 (4), p.423-431

1991

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DNA binding of Jun and Fos bZip domains: homodimers and heterodimers induce a DNA conformational change in solution

Nucleic acids research, 1996-11, Vol.24 (22), p.4487-4494

1996

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Transformation and Transactivation Suppressor Activity of the c-Jun Leucine Zipper Fused to a Bacterial Repressor

Proceedings of the National Academy of Sciences - PNAS, 1992-05, Vol.89 (10), p.4236-4239

1992

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A LexA mutant repressor with a relaxed inter‐domain linker

Protein science, 1998-02, Vol.7 (2), p.512-515

1998

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Contacts between the LexA repressor–or its DNA‐binding domain–and the backbone of the recA operator DNA

The EMBO journal, 1988-01, Vol.7 (1), p.269-275

1988

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Fos Leucine Zipper Variants with Increased Association Capacity

The Journal of biological chemistry, 1995-09, Vol.270 (39), p.22721-22730

1995

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Nucleosome assembly on the human c-fos promoter interferes with transcription factor binding

Nucleic acids research, 1996-12, Vol.24 (23), p.4751-4758

1996

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DNA binding and transactivation properties of Fos variants with homodimerization capacity

Nucleic acids research, 1997-08, Vol.25 (15), p.3026-3033

1997

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Orientation of the LexA DNA-Binding Motif on Operator DNA as Inferred from Cysteine-Mediated Phenyl Azide Crosslinking

Proceedings of the National Academy of Sciences - PNAS, 1993-03, Vol.90 (5), p.2030-2034

1993

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Interaction of a regulatory protein with a DNA target containing two overlapping binding sites

The Journal of biological chemistry, 1991-02, Vol.266 (4), p.2303-2312

1991

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Large-scale purification, oligomerization equilibria, and specific interaction of the LexA repressor of Escherichia coli

Biochemistry (Easton), 1985-05, Vol.24 (11), p.2812-2818

1985

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In vitro binding of LexA repressor to DNA: evidence for the involvement of the amino‐terminal domain

The EMBO journal, 1986-04, Vol.5 (4), p.793-798

1986

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Structure of the LexA Repressor−DNA Complex Probed by Affinity Cleavage and Affinity Photo-Cross-Linking

Biochemistry (Easton), 1996-04, Vol.35 (14), p.4279-4286

1996

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Construction, purification, and characterization of a hybrid protein comprising the DNA binding domain of the LexA repressor and the Jun leucine zipper: a circular dichroism and mutagenesis study

Biochemistry (Easton), 1991-10, Vol.30 (40), p.9657-9664

1991

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Purification and biochemical characterization of Escherichia coli RecA proteins mutated in the putative DNA binding site

The Journal of biological chemistry, 1994-03, Vol.269 (11), p.8246-8254

1994

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Spacing Requirements Between LexA Operator Half-sites can be Relaxed by Fusing the LexA DNA Binding Domain with some Alternative Dimerization Domains

Journal of molecular biology, 1993-01, Vol.229 (1), p.1-7

1993

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Two pairs of oppositely charged amino acids from Jun and Fos confer heterodimerization to CGN4 leucine zipper

The Journal of biological chemistry, 1994, Vol.269 (23), p.16247-16253

1994

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Isolation and characterization of LexA mutant repressors with enhanced DNA binding affinity

Journal of molecular biology, 1992-06, Vol.225 (3), p.609-620

1992

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The carboxy-terminal domain of the LexA repressor oligomerises essentially as the entire protein

FEBS letters, 1988-07, Vol.234 (1), p.56-60

1988

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The LexA repressor and its isolated amino-terminal domain interact cooperatively with poly[d(A-T)], a contiguous pseudo-operator, but not with random DNA: a circular dichroism study

Biochemistry (Easton), 1990-02, Vol.29 (7), p.1961-1970

1990

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The Amino-Terminal Domain of LexA Repressor is α -helical but Differs from Canonical Helix-Turn-Helix Proteins: A Two-Dimensional 1H NMR Study

Proceedings of the National Academy of Sciences - PNAS, 1989-09, Vol.86 (18), p.6863-6867

1989

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DNA sequence determinants of LexA-induced DNA bending

Nucleic acids research, 1993-05, Vol.21 (10), p.2363-2367

1993

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A new LexA-based genetic system for monitoring and analyzing protein heterodimerization in Escherichia coli

Molecular & general genetics, 1998-01, Vol.257 (2), p.205-212

1998

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Laboratory and controlled field experiments using potassium permanganate to remediate trichloroethylene and perchloroethylene DNAPLs in porous media

Two pairs of oppositely charged amino acids from Jun and Fos confer heterodimerization to GCN4 leucine zipper

DNA binding properties of the LexA repressor

DNA binding of Jun and Fos bZip domains: homodimers and heterodimers induce a DNA conformational change in solution

Transformation and Transactivation Suppressor Activity of the c-Jun Leucine Zipper Fused to a Bacterial Repressor

A LexA mutant repressor with a relaxed inter‐domain linker

Contacts between the LexA repressor–or its DNA‐binding domain–and the backbone of the recA operator DNA

Fos Leucine Zipper Variants with Increased Association Capacity

Nucleosome assembly on the human c-fos promoter interferes with transcription factor binding

DNA binding and transactivation properties of Fos variants with homodimerization capacity

Orientation of the LexA DNA-Binding Motif on Operator DNA as Inferred from Cysteine-Mediated Phenyl Azide Crosslinking

Interaction of a regulatory protein with a DNA target containing two overlapping binding sites

Large-scale purification, oligomerization equilibria, and specific interaction of the LexA repressor of Escherichia coli

In vitro binding of LexA repressor to DNA: evidence for the involvement of the amino‐terminal domain

Structure of the LexA Repressor−DNA Complex Probed by Affinity Cleavage and Affinity Photo-Cross-Linking

Construction, purification, and characterization of a hybrid protein comprising the DNA binding domain of the LexA repressor and the Jun leucine zipper: a circular dichroism and mutagenesis study

Purification and biochemical characterization of Escherichia coli RecA proteins mutated in the putative DNA binding site

Spacing Requirements Between LexA Operator Half-sites can be Relaxed by Fusing the LexA DNA Binding Domain with some Alternative Dimerization Domains

Two pairs of oppositely charged amino acids from Jun and Fos confer heterodimerization to CGN4 leucine zipper

Isolation and characterization of LexA mutant repressors with enhanced DNA binding affinity

The carboxy-terminal domain of the LexA repressor oligomerises essentially as the entire protein

The LexA repressor and its isolated amino-terminal domain interact cooperatively with poly[d(A-T)], a contiguous pseudo-operator, but not with random DNA: a circular dichroism study

The Amino-Terminal Domain of LexA Repressor is α -helical but Differs from Canonical Helix-Turn-Helix Proteins: A Two-Dimensional 1H NMR Study

DNA sequence determinants of LexA-induced DNA bending

A new LexA-based genetic system for monitoring and analyzing protein heterodimerization in Escherichia coli

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