Search research articles
Contact Us
Filters
Showing results (31-40 of 289) with videos related to
Page
of 29
Sort By:
Bioinformatics (Oxford, England)
|
September 15, 2005
A comparison study: applying segmentation to array CGH data for downstream analyses
Hanni Willenbrock, Jane Fridlyand
Journal of the American Association of Nurse Practitioners
|
December 11, 2024
Validation of the Nurse Practitioner Knowledge and Attitudes of Patient Obesity Scale: A pilot study
Donna Willenbrock, Sage Rose
The Biochemical Journal
|
September 15, 1984
Natural structural variation in enzymes as a tool in the study of mechanism exemplified by a comparison of the catalytic-site structure and characteristics of cathepsin B and papain. pH-dependent kinetics of the reactions of cathepsin B from bovine spleen and from rat liver with a thiol-specific two-protonic-state probe (2,2'-dipyridyl disulphide) and with a specific synthetic substrate (N-alpha-benzyloxycarbonyl-L-arginyl-L-arginine 2-naphthylamide)
F Willenbrock, K Brocklehurst
Methods in Molecular Biology (Clifton, N.J.)
|
February 24, 2001
Kinetic analysis of the inhibition of matrix metalloproteinases by tissue inhibitor of metalloproteinases (TIMP)
M Hutton, F Willenbrock
American Journal of Respiratory and Critical Care Medicine
|
December 1, 1994
Structure-function relationships in the tissue inhibitors of metalloproteinases
F Willenbrock, G Murphy
The Biochemical Journal
|
April 15, 1985
Preparation of cathepsins B and H by covalent chromatography and characterization of their catalytic sites by reaction with a thiol-specific two-protonic-state reactivity probe. Kinetic study of cathepsins B and H extending into alkaline media and a rapid spectroscopic titration of cathepsin H at pH 3-4
F Willenbrock, K Brocklehurst
The Biochemical Journal
|
April 15, 1985
A general framework of cysteine-proteinase mechanism deduced from studies on enzymes with structurally different analogous catalytic-site residues Asp-158 and -161 (papain and actinidin), Gly-196 (cathepsin B) and Asn-165 (cathepsin H). Kinetic studies up to pH 8 of the hydrolysis of N-alpha-benzyloxycarbonyl-L-arginyl-L-arginine 2-naphthylamide catalysed by cathepsin B and of L-arginine 2-naphthylamide catalysed by cathepsin H
F Willenbrock, K Brocklehurst
Physical Review. D, Particles and Fields
|
July 1, 1989
Weak-boson production at Fermilab Tevatron energies
Berger, Halzen, Kim, et al.
The Biochemical Journal
|
August 15, 1986
Chemical evidence for the pH-dependent control of ion-pair geometry in cathepsin B. Benzofuroxan as a reactivity probe sensitive to differences in the mutual disposition of the thiolate and imidazolium components of cysteine proteinase catalytic sites
F Willenbrock, K Brocklehurst
Genome Biology
|
December 4, 2004
Chromatin architecture and gene expression in Escherichia coli
Hanni Willenbrock, David W Ussery
Page
of 29
Search research articles
Search
Showing results (31-40 of 289) with videos related to
Sort By:
Page
of 29
Bioinformatics (Oxford, England)
|
September 15, 2005
A comparison study: applying segmentation to array CGH data for downstream analyses
Hanni Willenbrock, Jane Fridlyand
Journal of the American Association of Nurse Practitioners
|
December 11, 2024
Validation of the Nurse Practitioner Knowledge and Attitudes of Patient Obesity Scale: A pilot study
Donna Willenbrock, Sage Rose
The Biochemical Journal
|
September 15, 1984
Natural structural variation in enzymes as a tool in the study of mechanism exemplified by a comparison of the catalytic-site structure and characteristics of cathepsin B and papain. pH-dependent kinetics of the reactions of cathepsin B from bovine spleen and from rat liver with a thiol-specific two-protonic-state probe (2,2'-dipyridyl disulphide) and with a specific synthetic substrate (N-alpha-benzyloxycarbonyl-L-arginyl-L-arginine 2-naphthylamide)
F Willenbrock, K Brocklehurst
Methods in Molecular Biology (Clifton, N.J.)
|
February 24, 2001
Kinetic analysis of the inhibition of matrix metalloproteinases by tissue inhibitor of metalloproteinases (TIMP)
M Hutton, F Willenbrock
American Journal of Respiratory and Critical Care Medicine
|
December 1, 1994
Structure-function relationships in the tissue inhibitors of metalloproteinases
F Willenbrock, G Murphy
The Biochemical Journal
|
April 15, 1985
Preparation of cathepsins B and H by covalent chromatography and characterization of their catalytic sites by reaction with a thiol-specific two-protonic-state reactivity probe. Kinetic study of cathepsins B and H extending into alkaline media and a rapid spectroscopic titration of cathepsin H at pH 3-4
F Willenbrock, K Brocklehurst
The Biochemical Journal
|
April 15, 1985
A general framework of cysteine-proteinase mechanism deduced from studies on enzymes with structurally different analogous catalytic-site residues Asp-158 and -161 (papain and actinidin), Gly-196 (cathepsin B) and Asn-165 (cathepsin H). Kinetic studies up to pH 8 of the hydrolysis of N-alpha-benzyloxycarbonyl-L-arginyl-L-arginine 2-naphthylamide catalysed by cathepsin B and of L-arginine 2-naphthylamide catalysed by cathepsin H
F Willenbrock, K Brocklehurst
Physical Review. D, Particles and Fields
|
July 1, 1989
Weak-boson production at Fermilab Tevatron energies
Berger, Halzen, Kim, et al.
The Biochemical Journal
|
August 15, 1986
Chemical evidence for the pH-dependent control of ion-pair geometry in cathepsin B. Benzofuroxan as a reactivity probe sensitive to differences in the mutual disposition of the thiolate and imidazolium components of cysteine proteinase catalytic sites
F Willenbrock, K Brocklehurst
Genome Biology
|
December 4, 2004
Chromatin architecture and gene expression in Escherichia coli
Hanni Willenbrock, David W Ussery
Page
of 29