NMR-Derived Models of Amidopyrine and Its Metabolites in Complexes with Rabbit Cytochrome P450 2B4 Reveal a Structural Mechanism of Sequential N-Dealkylation
NMR-Derived Models of Amidopyrine and Its Metabolites in Complexes with Rabbit Cytochrome P450 2B4 Reveal a Structural Mechanism of Sequential N-Dealkylation
A Large-scale Comparison of Computational Models on the Residue Flexibility for NMR-derived Proteinss.
A Large-scale Comparison of Computational Models on the Residue Flexibility for NMR-derived Proteinss.
A Large-scale Comparison of Computational Models on the Residue Flexibility for NMR-derived Proteinss.
Protein Pept Lett. 2011 Sep 20;
Authors: Zhang H, Shi H, Hanlon M
Abstract
As an alternative to X-ray crystallography, nuclear magnetic resonance (NMR) has also emerged as the method of choice for studying both protein structure and dynamics in solution. However, little work using computational models such as Gaussian network model...
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09-22-2011 04:25 PM
NMR-derived models of amidopyrine and its metabolites in complexes with rabbit cytochrome P450 2B4 reveal a structural mechanism of sequential N-dealkylation.
NMR-derived models of amidopyrine and its metabolites in complexes with rabbit cytochrome P450 2B4 reveal a structural mechanism of sequential N-dealkylation.
NMR-derived models of amidopyrine and its metabolites in complexes with rabbit cytochrome P450 2B4 reveal a structural mechanism of sequential N-dealkylation.
Biochemistry. 2011 Mar 29;50(12):2123-34
Authors: Roberts AG, Sjögren SE, Fomina N, Vu KT, Almutairi A, Halpert JR
To understand the molecular basis of sequential N-dealkylation by cytochrome P450 2B enzymes, we studied the binding of...
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05-20-2011 11:26 AM
Structural Features of Cytochromes P450 and Ligands that Affect Drug Metabolism as Re
Structural Features of Cytochromes P450 and Ligands that Affect Drug Metabolism as Revealed by X-ray Crystallography and NMR.
Structural Features of Cytochromes P450 and Ligands that Affect Drug Metabolism as Revealed by X-ray Crystallography and NMR.
Future Med Chem. 2010 Sep 1;2(9):1451-1468
Authors: Gay SC, Roberts AG, Halpert JR
Cytochromes P450 (P450s) play a major role in the clearance of drugs, toxins, and environmental pollutants. Additionally, metabolism by P450s can result in toxic or carcinogenic products. The metabolism of...
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11-26-2010 05:32 PM
[NMR paper] High-quality homology models derived from NMR and X-ray structures of E. coli protein
High-quality homology models derived from NMR and X-ray structures of E. coli proteins YgdK and Suf E suggest that all members of the YgdK/Suf E protein family are enhancers of cysteine desulfurases.
Related Articles High-quality homology models derived from NMR and X-ray structures of E. coli proteins YgdK and Suf E suggest that all members of the YgdK/Suf E protein family are enhancers of cysteine desulfurases.
Protein Sci. 2005 Jun;14(6):1597-608
Authors: Liu G, Li Z, Chiang Y, Acton T, Montelione GT, Murray D, Szyperski T
The structural...
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11-25-2010 08:21 PM
[NMR paper] SOMO (SOlution MOdeler) differences between X-Ray- and NMR-derived bead models sugges
SOMO (SOlution MOdeler) differences between X-Ray- and NMR-derived bead models suggest a role for side chain flexibility in protein hydrodynamics.
Related Articles SOMO (SOlution MOdeler) differences between X-Ray- and NMR-derived bead models suggest a role for side chain flexibility in protein hydrodynamics.
Structure. 2005 May;13(5):723-34
Authors: Rai N, Nöllmann M, Spotorno B, Tassara G, Byron O, Rocco M
Reduced numbers of frictional/scattering centers are essential for tractable hydrodynamic and small-angle scattering data modeling. We...
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[NMR paper] The substrate binding site of human liver cytochrome P450 2C9: an NMR study.
The substrate binding site of human liver cytochrome P450 2C9: an NMR study.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles The substrate binding site of human liver cytochrome P450 2C9: an NMR study.
Biochemistry. 1997 Oct 21;36(42):12672-82
Authors: Poli-Scaife S, Attias R, Dansette PM, Mansuy D
Purified recombinant human liver cytochrome P450 2C9 was produced, from expression of the corresponding cDNA in yeast, in quantities large enough for UV-visible and 1H NMR experiments. Its...
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08-22-2010 05:08 PM
[NMR paper] A model for human cytochrome P450 2D6 based on homology modeling and NMR studies of s
A model for human cytochrome P450 2D6 based on homology modeling and NMR studies of substrate binding.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles A model for human cytochrome P450 2D6 based on homology modeling and NMR studies of substrate binding.
Biochemistry. 1996 Apr 9;35(14):4540-50
Authors: Modi S, Paine MJ, Sutcliffe MJ, Lian LY, Primrose WU, Wolf CR, Roberts GC
The cytochrome P450 responsible for the debrisoquine/sparteine polymorphism (P450 2D6) has been produced in large...
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08-22-2010 02:27 PM
[NMR paper] 1H-NMR study of reduced heme proteins myoglobin and cytochrome P450.
1H-NMR study of reduced heme proteins myoglobin and cytochrome P450.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles 1H-NMR study of reduced heme proteins myoglobin and cytochrome P450.
Eur J Biochem. 1993 Jul 15;215(2):431-7
Authors: Banci L, Bertini I, Marconi S, Pierattelli R
The 1H-NMR spectra of deoxymyoglobin and reduced cytochrome P450 are analyzed by NOE spectroscopy. Progress has been made in the assignment of the...