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457 related items for PubMed ID: 18444665
1. Critical role of arginine 160 of the EutB protein subunit for active site structure and radical catalysis in coenzyme B12-dependent ethanolamine ammonia-lyase. Sun L, Groover OA, Canfield JM, Warncke K. Biochemistry; 2008 May 20; 47(20):5523-35. PubMed ID: 18444665 [Abstract] [Full Text] [Related]
2. The structural model of Salmonella typhimurium ethanolamine ammonia-lyase directs a rational approach to the assembly of the functional [(EutB-EutC)₂]₃ oligomer from isolated subunits. Bovell AM, Warncke K. Biochemistry; 2013 Feb 26; 52(8):1419-28. PubMed ID: 23374068 [Abstract] [Full Text] [Related]
3. Characterization of the product radical structure in the Co(II)-product radical pair state of coenzyme B12-dependent ethanolamine deaminase by using three-pulse 2H ESEEM spectroscopy. Warncke K. Biochemistry; 2005 Mar 08; 44(9):3184-93. PubMed ID: 15736929 [Abstract] [Full Text] [Related]
4. Active site reactant center geometry in the Co(II)-product radical pair state of coenzyme B12-dependent ethanolamine deaminase determined by using orientation-selection electron spin-echo envelope modulation spectroscopy. Canfield JM, Warncke K. J Phys Chem B; 2005 Feb 24; 109(7):3053-64. PubMed ID: 16851320 [Abstract] [Full Text] [Related]
5. Comparative model of EutB from coenzyme B12-dependent ethanolamine ammonia-lyase reveals a beta8alpha8, TIM-barrel fold and radical catalytic site structural features. Sun L, Warncke K. Proteins; 2006 Aug 01; 64(2):308-19. PubMed ID: 16688781 [Abstract] [Full Text] [Related]
6. Kinetic and thermodynamic characterization of Co(II)-substrate radical pair formation in coenzyme B12-dependent ethanolamine ammonia-lyase in a cryosolvent system by using time-resolved, full-spectrum continuous-wave electron paramagnetic resonance spectroscopy. Wang M, Warncke K. J Am Chem Soc; 2008 Apr 09; 130(14):4846-58. PubMed ID: 18341340 [Abstract] [Full Text] [Related]
7. Interaction of the substrate radical and the 5'-deoxyadenosine-5'-methyl group in vitamin B(12) coenzyme-dependent ethanolamine deaminase. Warncke K, Utada AS. J Am Chem Soc; 2001 Sep 05; 123(35):8564-72. PubMed ID: 11525664 [Abstract] [Full Text] [Related]
18. Isotope effects in the transient phases of the reaction catalyzed by ethanolamine ammonia-lyase: determination of the number of exchangeable hydrogens in the enzyme-cofactor complex. Bandarian V, Reed GH. Biochemistry; 2000 Oct 03; 39(39):12069-75. PubMed ID: 11009622 [Abstract] [Full Text] [Related]
19. Deuterium Kinetic Isotope Effects Resolve Low-Temperature Substrate Radical Reaction Pathways and Steps in B12-Dependent Ethanolamine Ammonia-Lyase. Kohne M, Li W, Zhu C, Warncke K. Biochemistry; 2019 Sep 03; 58(35):3683-3690. PubMed ID: 31419122 [Abstract] [Full Text] [Related]
20. Probing nitrogen-sensitive steps in the free-radical-mediated deamination of amino alcohols by ethanolamine ammonia-lyase. Poyner RR, Anderson MA, Bandarian V, Cleland WW, Reed GH. J Am Chem Soc; 2006 Jun 07; 128(22):7120-1. PubMed ID: 16734439 [Abstract] [Full Text] [Related] Page: [Next] [New Search]