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John B. Hays

Researcher at University of Maryland, Baltimore County

Publications -  19
Citations -  508

John B. Hays is an academic researcher from University of Maryland, Baltimore County. The author has contributed to research in topics: Recombination & Bacteriophage. The author has an hindex of 10, co-authored 19 publications receiving 502 citations.

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Journal ArticleDOI

T4 endonuclease VII cleaves holliday structures

Kiyoshi Mizuuchi, +3 more
- 01 Jun 1982 - 
TL;DR: Observations account for the role of endonuclease VII in the DNA metabolism of phage T4, and provide the first example of an enzyme that acts specifically on branch points in duplex DNA.
Journal ArticleDOI

Selective inhibition of Escherichia coli RecBC activities by plasmid-encoded GamS function of phage lambda

Stanley A. Friedman, +1 more
- 01 Jan 1986 - 
TL;DR: expression of gamS+, but not gamS201, inhibited Escherichia coli RecBC nuclease in vivo; the criteria were inhibition of chromosomal DNA degradation after UV irradiation and plating of T4 gene 2- phages.
Journal ArticleDOI

Partially deficient methylation of cytosine in DNA at CCTAGG sites stimulates genetic recombination of bacteriophage lambda

Brent E. Korba, +1 more
- 01 Mar 1982 - 
TL;DR: It is hypothesize that hemimethylated CCATGG sites in "Arl-" DNA are necessary and sufficient for enhanced recombination, and necessary but not sufficient for S1 sensitivity.
Book ChapterDOI

Repair and recombination of uv-irradiated phage lambda

John B. Hays, +1 more
- 01 Jan 1978 - 
TL;DR: Intracellular lambda DNA was extracted from infected rec+ bacteria and scored for infectivity and recombination (loss of duplication) by transfection of recA recB spheroplasts and subsequent assay for EDTA resistance.
Journal ArticleDOI

Initial Characterization of Hexose and Hexitol Phosphoenolpyruvate-Dependent Phosphotransferases of Staphylococcus aureus

Stanley A. Friedman, +1 more
- 01 Jun 1977 - 
TL;DR: The phosphoenolpyruvate sugar phosphotransferases of Staphylococcus aureus were surveyed biochemically to determine substrate range, inducibility and constitutivity, and requirements for soluble sugar-specific proteins.