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Refinado por: Nome da Publicação: Journal of Bacteriology remover assunto: Mutation remover
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1
Simple, rapid, and quantitative release of periplasmic proteins by chloroform
Simple, rapid, and quantitative release of periplasmic proteins by chloroform
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Simple, rapid, and quantitative release of periplasmic proteins by chloroform

Ames, G F ; Prody, C ; Kustu, S

Journal of Bacteriology, 1984-12, Vol.160 (3), p.1181-1183 [Periódico revisado por pares]

Washington, DC: American Society for Microbiology

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2
D-histidine utilization in Salmonella typhimurium is controlled by the leucine-responsive regulatory protein (Lrp)
D-histidine utilization in Salmonella typhimurium is controlled by the leucine-responsive regulatory protein (Lrp)
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D-histidine utilization in Salmonella typhimurium is controlled by the leucine-responsive regulatory protein (Lrp)

Hecht, K ; Zhang, S ; Klopotowski, T ; Ames, G F

Journal of Bacteriology, 1996-01, Vol.178 (2), p.327-331 [Periódico revisado por pares]

United States: American Society for Microbiology

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3
Amplification of bacterial genomic DNA by the polymerase chain reaction and direct sequencing after asymmetric amplification: application to the study of periplasmic permeases
Amplification of bacterial genomic DNA by the polymerase chain reaction and direct sequencing after asymmetric amplification: application to the study of periplasmic permeases
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Amplification of bacterial genomic DNA by the polymerase chain reaction and direct sequencing after asymmetric amplification: application to the study of periplasmic permeases

Shyamala, V ; Ames, G F

Journal of Bacteriology, 1989-03, Vol.171 (3), p.1602-1608 [Periódico revisado por pares]

Washington, DC: American Society for Microbiology

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4
Utilization by Saccharomyces cerevisiae of 5'-methylthioadenosine as a source of both purine and methionine
Utilization by Saccharomyces cerevisiae of 5'-methylthioadenosine as a source of both purine and methionine
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Utilization by Saccharomyces cerevisiae of 5'-methylthioadenosine as a source of both purine and methionine

Cone, M.C ; Marchitto, K ; Zehfus, B ; Ferro, A.J

Journal of Bacteriology, 1982-07, Vol.151 (1), p.510-515 [Periódico revisado por pares]

United States: American Society for Microbiology

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5
Salmonella typhimurium histidine periplasmic permease mutations that allow transport in the absence of histidine-binding proteins
Salmonella typhimurium histidine periplasmic permease mutations that allow transport in the absence of histidine-binding proteins
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Salmonella typhimurium histidine periplasmic permease mutations that allow transport in the absence of histidine-binding proteins

SPEISER, D. M ; FERRO-LUZZI AMES, G

Journal of Bacteriology, 1991-02, Vol.173 (4), p.1444-1451 [Periódico revisado por pares]

Washington, DC: American Society for Microbiology

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6
Fine-structure genetic map of the maltose transport operon of Salmonella typhimurium
Fine-structure genetic map of the maltose transport operon of Salmonella typhimurium
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Fine-structure genetic map of the maltose transport operon of Salmonella typhimurium

SCHNEIDER, E ; BISHOP, L ; ALFANDARY, V ; FERRO-LUZZI AMES, G

Journal of Bacteriology, 1989-11, Vol.171 (11), p.5860-5865 [Periódico revisado por pares]

Washington, DC: American Society for Microbiology

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7
Protein Composition of the Outer Membrane of Salmonella typhimurium: Effect of Lipopolysaccharide Mutations
Protein Composition of the Outer Membrane of Salmonella typhimurium: Effect of Lipopolysaccharide Mutations
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Protein Composition of the Outer Membrane of Salmonella typhimurium: Effect of Lipopolysaccharide Mutations

Ames, G F ; Spudich, E N ; Nikaido, H

Journal of Bacteriology, 1974-02, Vol.117 (2), p.406-416 [Periódico revisado por pares]

United States: American Society for Microbiology

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8
The hisP Protein, a Known Histidine Transport Component in Salmonella typhimurium, Is Also an Arginine Transport Component
The hisP Protein, a Known Histidine Transport Component in Salmonella typhimurium, Is Also an Arginine Transport Component
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The hisP Protein, a Known Histidine Transport Component in Salmonella typhimurium, Is Also an Arginine Transport Component

Kustu, S G ; Ames, G F

Journal of Bacteriology, 1973-10, Vol.116 (1), p.107-113 [Periódico revisado por pares]

United States: American Society for Microbiology

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9
Analysis of promoter mutations in the histidine transport operon of Salmonella typhimurium: use of hybrid M13 bacteriophages for cloning, transformation, and sequencing
Analysis of promoter mutations in the histidine transport operon of Salmonella typhimurium: use of hybrid M13 bacteriophages for cloning, transformation, and sequencing
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Analysis of promoter mutations in the histidine transport operon of Salmonella typhimurium: use of hybrid M13 bacteriophages for cloning, transformation, and sequencing

Lee, G S ; Ames, G F

Journal of Bacteriology, 1984-09, Vol.159 (3), p.1000-1005 [Periódico revisado por pares]

Washington, DC: American Society for Microbiology

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10
Duplications of histidine transport genes in Salmonella typhimurium and their use for the selection of deletion mutants
Duplications of histidine transport genes in Salmonella typhimurium and their use for the selection of deletion mutants
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Duplications of histidine transport genes in Salmonella typhimurium and their use for the selection of deletion mutants

Ames, G F ; Biek, D P ; Spudich, E N

Journal of Bacteriology, 1978-12, Vol.136 (3), p.1094-1108 [Periódico revisado por pares]

United States: American Society for Microbiology

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