Gustafsson, 2012 - Google Patents
Biophysical characterization of the* 5 protein variant of human thiopurine methyltransferase by NMR spectroscopyGustafsson, 2012
View PDF- Document ID
- 5415365045599325057
- Author
- Gustafsson R
- Publication year
External Links
Snippet
Human thiopurine methyltransferase (TPMT) is an enzyme involved in the metabolism of thiopurine drugs, which are widely used in leukemia and inflammatory bowel diseases such as ulcerative colitis and Crohns disease. Due to genetic polymorphisms, approximately 30 …
- 102000004377 Thiopurine S-methyltransferases 0 title abstract description 336
Classifications
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01R—MEASURING ELECTRIC VARIABLES; MEASURING MAGNETIC VARIABLES
- G01R33/00—Arrangements or instruments for measuring magnetic variables
- G01R33/20—Arrangements or instruments for measuring magnetic variables involving magnetic resonance
- G01R33/28—Details of apparatus provided for in groups G01R33/44 - G01R33/64
- G01R33/38—Systems for generation, homogenisation or stabilisation of the main or gradient magnetic field
- G01R33/381—Systems for generation, homogenisation or stabilisation of the main or gradient magnetic field using electromagnets
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01R—MEASURING ELECTRIC VARIABLES; MEASURING MAGNETIC VARIABLES
- G01R33/00—Arrangements or instruments for measuring magnetic variables
- G01R33/20—Arrangements or instruments for measuring magnetic variables involving magnetic resonance
- G01R33/28—Details of apparatus provided for in groups G01R33/44 - G01R33/64
- G01R33/30—Sample handling arrangements, e.g. sample cells, spinning mechanisms
- G01R33/31—Temperature control thereof
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01R—MEASURING ELECTRIC VARIABLES; MEASURING MAGNETIC VARIABLES
- G01R33/00—Arrangements or instruments for measuring magnetic variables
- G01R33/20—Arrangements or instruments for measuring magnetic variables involving magnetic resonance
- G01R33/44—Arrangements or instruments for measuring magnetic variables involving magnetic resonance using nuclear magnetic resonance [NMR]
- G01R33/46—NMR spectroscopy
- G01R33/465—NMR spectroscopy applied to biological material, e.g. in vitro testing
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01R—MEASURING ELECTRIC VARIABLES; MEASURING MAGNETIC VARIABLES
- G01R33/00—Arrangements or instruments for measuring magnetic variables
- G01R33/20—Arrangements or instruments for measuring magnetic variables involving magnetic resonance
- G01R33/44—Arrangements or instruments for measuring magnetic variables involving magnetic resonance using nuclear magnetic resonance [NMR]
- G01R33/46—NMR spectroscopy
- G01R33/4625—Processing of acquired signals, e.g. elimination of phase errors, baseline fitting, chemometric analysis
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N24/00—Investigating or analyzing materials by the use of nuclear magnetic resonance, electron paramagnetic resonance or other spin effects
- G01N24/08—Investigating or analyzing materials by the use of nuclear magnetic resonance, electron paramagnetic resonance or other spin effects by using nuclear magnetic resonance
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
- G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/5005—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
- G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay
- G01N33/536—Immunoassay; Biospecific binding assay with immune complex formed in liquid phase
- G01N33/542—Immunoassay; Biospecific binding assay with immune complex formed in liquid phase with steric inhibition or signal modification, e.g. fluorescent quenching
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01R—MEASURING ELECTRIC VARIABLES; MEASURING MAGNETIC VARIABLES
- G01R33/00—Arrangements or instruments for measuring magnetic variables
- G01R33/20—Arrangements or instruments for measuring magnetic variables involving magnetic resonance
- G01R33/44—Arrangements or instruments for measuring magnetic variables involving magnetic resonance using nuclear magnetic resonance [NMR]
- G01R33/48—NMR imaging systems
- G01R33/54—Signal processing systems, e.g. using pulse sequences, Generation or control of pulse sequences ; Operator Console
- G01R33/56—Image enhancement or correction, e.g. subtraction or averaging techniques, e.g. improvement of signal-to-noise ratio and resolution
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01R—MEASURING ELECTRIC VARIABLES; MEASURING MAGNETIC VARIABLES
- G01R33/00—Arrangements or instruments for measuring magnetic variables
- G01R33/02—Measuring direction or magnitude of magnetic fields or magnetic flux
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2500/00—Screening for compounds of potential therapeutic value
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| Stiller et al. | Structure determination of high-energy states in a dynamic protein ensemble | |
| Marion | An introduction to biological NMR spectroscopy | |
| Kay | NMR studies of protein structure and dynamics | |
| Pellecchia et al. | NMR-based structural characterization of large protein-ligand interactions | |
| Pellecchia et al. | NMR in drug discovery | |
| Arcus et al. | A comparison of the pH, urea, and temperature-denatured states of barnase by heteronuclear NMR: implications for the initiation of protein folding | |
| Fejzo et al. | The SHAPES strategy: an NMR-based approach for lead generation in drug discovery | |
| Pellecchia | Solution nuclear magnetic resonance spectroscopy techniques for probing intermolecular interactions | |
| Gladkova et al. | An invisible ubiquitin conformation is required for efficient phosphorylation by PINK1 | |
| Ploskon et al. | A mammalian type I fatty acid synthase acyl carrier protein domain does not sequester acyl chains | |
| Campos-Olivas et al. | Placement of 19F into the center of GB1: effects on structure and stability | |
| Huang et al. | Backbone dynamics of Escherichia coli thioesterase/protease I: evidence of a flexible active-site environment for a serine protease | |
| Lehner et al. | Impact of azidohomoalanine incorporation on protein structure and ligand binding | |
| Goldflam et al. | NMR studies of protein–ligand interactions | |
| US20050234652A1 (en) | Nuclear magnetic resonance-docking of compounds | |
| Ishima | Protein-inhibitor interaction studies using NMR | |
| Cordina et al. | Interdomain orientation of cardiac troponin C characterized by paramagnetic relaxation enhancement NMR reveals a compact state | |
| Sharifahmadian et al. | Monomer‐to‐dimer transition of Brucella suis type IV secretion system component VirB8 induces conformational changes | |
| Gustafsson | Biophysical characterization of the* 5 protein variant of human thiopurine methyltransferase by NMR spectroscopy | |
| Davulcu et al. | Intrinsic domain and loop dynamics commensurate with catalytic turnover in an induced-fit enzyme | |
| Hansen et al. | Binding kinetics of histone chaperone Chz1 and variant histone H2A. Z-H2B by relaxation dispersion NMR spectroscopy | |
| Valadares et al. | Conformational dynamics of tetracenomycin aromatase/cyclase regulate polyketide binding and enzyme aggregation propensity | |
| Breukels et al. | Overview on the use of NMR to examine protein structure | |
| Huang et al. | The solution structure of the Mg2+ form of soybean calmodulin isoform 4 reveals unique features of plant calmodulins in resting cells | |
| Vugmeyster et al. | Effect of subdomain interactions on methyl group dynamics in the hydrophobic core of villin headpiece protein |