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1
The T4 DNA polymerase accessory proteins form an ATP-dependent complex on a primer-template junction
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The T4 DNA polymerase accessory proteins form an ATP-dependent complex on a primer-template junction

MUNN, M. M ; ALBERTS, B. M

The Journal of biological chemistry, 1991-10, Vol.266 (30), p.20024-20033 [Periódico revisado por pares]

Bethesda, MD: American Society for Biochemistry and Molecular Biology

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2
DNA footprinting studies of the complex formed by the T4 DNA polymerase holoenzyme at a primer-template junction
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DNA footprinting studies of the complex formed by the T4 DNA polymerase holoenzyme at a primer-template junction

MUNN, M. M ; ALBERTS, B. M

The Journal of biological chemistry, 1991-10, Vol.266 (30), p.20034-20044 [Periódico revisado por pares]

Bethesda, MD: American Society for Biochemistry and Molecular Biology

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3
The mechanism of homologous DNA strand exchange catalyzed by the bacteriophage T4 uvsX and gene 32 proteins
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The mechanism of homologous DNA strand exchange catalyzed by the bacteriophage T4 uvsX and gene 32 proteins

Kodadek, T ; Wong, M L ; Alberts, B M

The Journal of biological chemistry, 1988-07, Vol.263 (19), p.9427-9436 [Periódico revisado por pares]

Bethesda, MD: Elsevier Inc

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4
Studies of the DNA helicase-RNA primase unit from bacteriophage T4. A trinucleotide sequence on the DNA template starts RNA primer synthesis
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Studies of the DNA helicase-RNA primase unit from bacteriophage T4. A trinucleotide sequence on the DNA template starts RNA primer synthesis

Cha, T A ; Alberts, B M

The Journal of biological chemistry, 1986-05, Vol.261 (15), p.7001-7010 [Periódico revisado por pares]

Bethesda, MD: Elsevier Inc

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5
Overexpression, purification, sequence analysis, and characterization of the T4 bacteriophage dda DNA helicase
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Overexpression, purification, sequence analysis, and characterization of the T4 bacteriophage dda DNA helicase

HACKER, K. J ; ALBERTS, B. M

The Journal of biological chemistry, 1992-10, Vol.267 (29), p.20674-20681 [Periódico revisado por pares]

Bethesda, MD: American Society for Biochemistry and Molecular Biology

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6
The bacteriophage T4 insertion/substitution vector system. A method for introducing site-specific mutations into the virus chromosome
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The bacteriophage T4 insertion/substitution vector system. A method for introducing site-specific mutations into the virus chromosome

Selick, H E ; Kreuzer, K N ; Alberts, B M

The Journal of biological chemistry, 1988-08, Vol.263 (23), p.11336-11347 [Periódico revisado por pares]

Bethesda, MD: Elsevier Inc

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7
The UvsY protein of bacteriophage T4 modulates recombination-dependent DNA synthesis in vitro
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The UvsY protein of bacteriophage T4 modulates recombination-dependent DNA synthesis in vitro

MORRICAL, S. W ; ALBERTS, B. M

The Journal of biological chemistry, 1990-09, Vol.265 (25), p.15096-15103 [Periódico revisado por pares]

Bethesda, MD: American Society for Biochemistry and Molecular Biology

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8
Site-specific recognition of bacteriophage T4 DNA by T4 type II DNA topoisomerase and Escherichia coli DNA gyrase
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Site-specific recognition of bacteriophage T4 DNA by T4 type II DNA topoisomerase and Escherichia coli DNA gyrase

Kreuzer, K N ; Alberts, B M

The Journal of biological chemistry, 1984-04, Vol.259 (8), p.5339-5346 [Periódico revisado por pares]

Bethesda, MD: Elsevier Inc

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9
Amplification of snap-back DNA synthesis reactions by the uvsX recombinase of bacteriophage T4
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Amplification of snap-back DNA synthesis reactions by the uvsX recombinase of bacteriophage T4

MORRICAL, S. W ; MEI LIE WONG ; ALBERTS, B. M

The Journal of biological chemistry, 1991-07, Vol.266 (21), p.14031-14038 [Periódico revisado por pares]

Bethesda, MD: American Society for Biochemistry and Molecular Biology

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10
The 3‘-5‘ proofreading exonuclease of bacteriophage T4 DNA polymerase is stimulated by other T4 DNA replication proteins
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The 3‘-5‘ proofreading exonuclease of bacteriophage T4 DNA polymerase is stimulated by other T4 DNA replication proteins

Bedinger, P ; Alberts, B M

The Journal of biological chemistry, 1983-08, Vol.258 (16), p.9649-9656 [Periódico revisado por pares]

Bethesda, MD: Elsevier Inc

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