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Biochemistry
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September 26, 1995
The nature of the transition state for enzyme-catalyzed phosphoryl transfer. Hydrolysis of O-aryl phosphorothioates by alkaline phosphatase
F Hollfelder, D Herschlag
The Journal of Organic Chemistry
|
August 21, 2001
On the magnitude and specificity of medium effects in enzyme-like catalysts for proton transfer
F Hollfelder, A J Kirby, D S Tawfik
Applied Biochemistry and Biotechnology
|
May 29, 2000
Nonspecific catalysis by protein surfaces
A J Kirby, F Hollfelder, D S Tawfik
Protein Engineering, Design & Selection : PEDS
|
November 10, 2009
USER friendly DNA recombination (USERec): a simple and flexible near homology-independent method for gene library construction
B R M Villiers, V Stein, F Hollfelder
Nature
|
September 5, 1996
Off-the-shelf proteins that rival tailor-made antibodies as catalysts
F Hollfelder, A J Kirby, D S Tawfik
Organic Letters
|
May 18, 2000
Vesicles accelerate proton transfer from carbon up to 850-fold
J Pérez-Juste, F Hollfelder, A J Kirby, et al.
Proceedings of the National Academy of Sciences of the United States of America
|
June 28, 2001
In vitro characterization of DNA gyrase inhibition by microcin B17 analogs with altered bisheterocyclic sites
D B Zamble, D A Miller, J G Heddle, et al.
Chemical Communications (Cambridge, England)
|
March 16, 2007
Quantitative detection of protein expression in single cells using droplet microfluidics
A Huebner, M Srisa-Art, D Holt, et al.
Biochemistry
|
October 3, 1999
Impaired transition state complementarity in the hydrolysis of O-arylphosphorothioates by protein-tyrosine phosphatases
Y L Zhang, F Hollfelder, S J Gordon, et al.
Journal of Molecular Biology
|
April 9, 2001
The antibiotic microcin B17 is a DNA gyrase poison: characterisation of the mode of inhibition
J G Heddle, S J Blance, D B Zamble, et al.
Page
of 1
Search research articles
Search
Showing results (1-10 of 10) with videos related to
Sort By:
Page
of 1
Biochemistry
|
September 26, 1995
The nature of the transition state for enzyme-catalyzed phosphoryl transfer. Hydrolysis of O-aryl phosphorothioates by alkaline phosphatase
F Hollfelder, D Herschlag
The Journal of Organic Chemistry
|
August 21, 2001
On the magnitude and specificity of medium effects in enzyme-like catalysts for proton transfer
F Hollfelder, A J Kirby, D S Tawfik
Applied Biochemistry and Biotechnology
|
May 29, 2000
Nonspecific catalysis by protein surfaces
A J Kirby, F Hollfelder, D S Tawfik
Protein Engineering, Design & Selection : PEDS
|
November 10, 2009
USER friendly DNA recombination (USERec): a simple and flexible near homology-independent method for gene library construction
B R M Villiers, V Stein, F Hollfelder
Nature
|
September 5, 1996
Off-the-shelf proteins that rival tailor-made antibodies as catalysts
F Hollfelder, A J Kirby, D S Tawfik
Organic Letters
|
May 18, 2000
Vesicles accelerate proton transfer from carbon up to 850-fold
J Pérez-Juste, F Hollfelder, A J Kirby, et al.
Proceedings of the National Academy of Sciences of the United States of America
|
June 28, 2001
In vitro characterization of DNA gyrase inhibition by microcin B17 analogs with altered bisheterocyclic sites
D B Zamble, D A Miller, J G Heddle, et al.
Chemical Communications (Cambridge, England)
|
March 16, 2007
Quantitative detection of protein expression in single cells using droplet microfluidics
A Huebner, M Srisa-Art, D Holt, et al.
Biochemistry
|
October 3, 1999
Impaired transition state complementarity in the hydrolysis of O-arylphosphorothioates by protein-tyrosine phosphatases
Y L Zhang, F Hollfelder, S J Gordon, et al.
Journal of Molecular Biology
|
April 9, 2001
The antibiotic microcin B17 is a DNA gyrase poison: characterisation of the mode of inhibition
J G Heddle, S J Blance, D B Zamble, et al.
Page
of 1