UB Paderborn / Katalog / Suche / in CDI

Selection and characterization of DNA aptamers with binding selectivity to Campylobacter jejuni using whole-cell SELEX

Applied microbiology and biotechnology, 2010-08, Vol.87 (6), p.2323-2334

2010

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Single Molecule Studies of Enzyme Mechanisms

Chemical reviews, 2006-08, Vol.106 (8), p.3080-3094

2006

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The effects of competition from non-pathogenic foodborne bacteria during the selective enrichment of Listeria monocytogenes using buffered Listeria enrichment broth

Food microbiology, 2014-12, Vol.44, p.173-179

2014

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16S rRNA partial gene sequencing for the differentiation and molecular subtyping of Listeria species

Food microbiology, 2013-12, Vol.36 (2), p.231-240

2013

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Postenrichment Population Differentials Using Buffered Listeria Enrichment Broth: Implications of the Presence of Listeria innocua on Listeria monocytogenes in Food Test Samples

Journal of food protection, 2013-11, Vol.76 (11), p.1854-1862

2013

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Selection of DNA aptamers for capture and detection of Salmonella Typhimurium using a whole-cell SELEX approach in conjunction with cell sorting

Applied microbiology and biotechnology, 2013-04, Vol.97 (8), p.3677-3686

2013

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Single-molecule measurements of the opening and closing of the DNA gate by eukaryotic topoisomerase II

Proceedings of the National Academy of Sciences - PNAS, 2007-03, Vol.104 (12), p.4840-4845

2007

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Contribution of Selective Conditions to Microbial Competition in Four Listeria Selective Enrichment Formulations

Journal of food protection, 2016-11, Vol.79 (11), p.1904-1910

2016

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Comparison of Listeria monocytogenes recoveries from spiked mung bean sprouts by the enrichment methods of three regulatory agencies

Food microbiology, 2017-09, Vol.66, p.40-47

2017

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Effect of Listeria seeligeri or Listeria welshimeri on Listeria monocytogenes detection in and recovery from buffered Listeria enrichment broth

Food microbiology, 2015-04, Vol.46, p.528-534

2015

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Conformation Coupled Enzyme Catalysis: Single-Molecule and Transient Kinetics Investigation of Dihydrofolate Reductase

Biochemistry (Easton), 2005-12, Vol.44 (51), p.16835-16843

2005

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âCatch 222,â the Effects of Symmetry on Ligand Binding and Catalysis in R67 Dihydrofolate Reductase as Determined by Mutations at Tyr-69

The Journal of biological chemistry, 2004-11, Vol.279 (45), p.47003-47009

2004

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Single-Molecule Investigation of the T4 Bacteriophage DNA Polymerase Holoenzyme: Multiple Pathways of Holoenzyme Formation

Biochemistry (Easton), 2006-07, Vol.45 (26), p.7990-7997

2006

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Role of Ionic Interactions in Ligand Binding and Catalysis of R67 Dihydrofolate Reductase

Biochemistry (Easton), 2003-09, Vol.42 (36), p.10569-10578

2003

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Calorimetric Studies of Ligand Binding in R67 Dihydrofolate Reductase

Biochemistry (Easton), 2005-09, Vol.44 (37), p.12420-12433

2005

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Defining the Binding Site of Homotetrameric R67 Dihydrofolate Reductase and Correlating Binding Enthalpy with Catalysis

Biochemistry (Easton), 2004-06, Vol.43 (23), p.7403-7412

2004

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Breaking Symmetry: Mutations Engineered into R67 Dihydrofolate Reductase, a D2 Symmetric Homotetramer Possessing a Single Active Site Pore

Biochemistry (Easton), 2002-12, Vol.41 (52), p.15664-15675

2002

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Intact Protein Analysis for Site-Directed Mutagenesis Overexpression Products: Plasmid-Encoded R67 Dihydrofolate Reductase

Analytical biochemistry, 2002-06, Vol.305 (1), p.68-81

2002

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One site fits both: a model for the ternary complex of folate + NADPH in R67 dihydrofolate reductase, a D2 symmetric enzyme

Journal of computer-aided molecular design, 2001-11, Vol.15 (11), p.1035

2001

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Single Molecule Studies of Enzyme Mechanisms

Chemical reviews, 2006-08, Vol.106 (8), p.3080

2006

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Breaking Symmetry: Mutations Engineered into R67 Dihydrofolate Reductase, a D 2 Symmetric Homotetramer Possessing a Single Active Site Pore

Biochemistry (Easton), 2002-12, Vol.41 (52), p.15664-15675

2002

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Role of S65, Q67, I68, and Y69 Residues in Homotetrameric R67 Dihydrofolate Reductase

Biochemistry (Easton), 2001-09, Vol.40 (38), p.11344-11352

2001

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Single Molecule Studies on Enzyme Mechanisms

ChemInform, 2006-10, Vol.37 (43), p.no-no

2006

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Selection and characterization of DNA aptamers with binding selectivity to Campylobacter jejuni using whole-cell SELEX

Single Molecule Studies of Enzyme Mechanisms

The effects of competition from non-pathogenic foodborne bacteria during the selective enrichment of Listeria monocytogenes using buffered Listeria enrichment broth

16S rRNA partial gene sequencing for the differentiation and molecular subtyping of Listeria species

Postenrichment Population Differentials Using Buffered Listeria Enrichment Broth: Implications of the Presence of Listeria innocua on Listeria monocytogenes in Food Test Samples

Selection of DNA aptamers for capture and detection of Salmonella Typhimurium using a whole-cell SELEX approach in conjunction with cell sorting

Single-molecule measurements of the opening and closing of the DNA gate by eukaryotic topoisomerase II

Contribution of Selective Conditions to Microbial Competition in Four Listeria Selective Enrichment Formulations

Comparison of Listeria monocytogenes recoveries from spiked mung bean sprouts by the enrichment methods of three regulatory agencies

Effect of Listeria seeligeri or Listeria welshimeri on Listeria monocytogenes detection in and recovery from buffered Listeria enrichment broth

Conformation Coupled Enzyme Catalysis: Single-Molecule and Transient Kinetics Investigation of Dihydrofolate Reductase

âCatch 222,â the Effects of Symmetry on Ligand Binding and Catalysis in R67 Dihydrofolate Reductase as Determined by Mutations at Tyr-69

Single-Molecule Investigation of the T4 Bacteriophage DNA Polymerase Holoenzyme: Multiple Pathways of Holoenzyme Formation

Role of Ionic Interactions in Ligand Binding and Catalysis of R67 Dihydrofolate Reductase

Calorimetric Studies of Ligand Binding in R67 Dihydrofolate Reductase

Defining the Binding Site of Homotetrameric R67 Dihydrofolate Reductase and Correlating Binding Enthalpy with Catalysis

Breaking Symmetry: Mutations Engineered into R67 Dihydrofolate Reductase, a D2 Symmetric Homotetramer Possessing a Single Active Site Pore

Intact Protein Analysis for Site-Directed Mutagenesis Overexpression Products: Plasmid-Encoded R67 Dihydrofolate Reductase

One site fits both: a model for the ternary complex of folate + NADPH in R67 dihydrofolate reductase, a D2 symmetric enzyme

Single Molecule Studies of Enzyme Mechanisms

Breaking Symmetry: Mutations Engineered into R67 Dihydrofolate Reductase, a D 2 Symmetric Homotetramer Possessing a Single Active Site Pore

Role of S65, Q67, I68, and Y69 Residues in Homotetrameric R67 Dihydrofolate Reductase

Single Molecule Studies on Enzyme Mechanisms

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