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Heme photolysis occurs by ultrafast excited state metal-to-ring charge transfer.
Franzen S, Kiger L, Poyart C, Martin JL. Franzen S, et al. Among authors: poyart c. Biophys J. 2001 May;80(5):2372-85. doi: 10.1016/S0006-3495(01)76207-8. Biophys J. 2001. PMID: 11325737 Free PMC article.
Effectors of hemoglobin. Separation of allosteric and affinity factors.
Marden MC, Bohn B, Kister J, Poyart C. Marden MC, et al. Among authors: poyart c. Biophys J. 1990 Mar;57(3):397-403. doi: 10.1016/S0006-3495(90)82556-X. Biophys J. 1990. PMID: 2306490 Free PMC article.
Coupling of ferric iron spin and allosteric equilibrium in hemoglobin.
Marden MC, Kiger L, Kister J, Bohn B, Poyart C. Marden MC, et al. Among authors: poyart c. Biophys J. 1991 Oct;60(4):770-6. doi: 10.1016/S0006-3495(91)82111-7. Biophys J. 1991. PMID: 1742452 Free PMC article.
Oxygen and CO binding to triply NO and asymmetric NO/CO hemoglobin hybrids.
Kiger L, Poyart C, Marden MC. Kiger L, et al. Among authors: poyart c. Biophys J. 1993 Sep;65(3):1050-8. doi: 10.1016/S0006-3495(93)81164-0. Biophys J. 1993. PMID: 8241385 Free PMC article.
Evidence for sub-picosecond heme doming in hemoglobin and myoglobin: a time-resolved resonance Raman comparison of carbonmonoxy and deoxy species.
Franzen S, Bohn B, Poyart C, Martin JL. Franzen S, et al. Among authors: poyart c. Biochemistry. 1995 Jan 31;34(4):1224-37. doi: 10.1021/bi00004a016. Biochemistry. 1995. PMID: 7827072
Heme-CO as a probe of the conformational state of calmodulin.
Marden MC, Leclerc L, Poyart C. Marden MC, et al. Among authors: poyart c. FEBS Lett. 1990 Oct 29;273(1-2):188-90. doi: 10.1016/0014-5793(90)81081-x. FEBS Lett. 1990. PMID: 2226852
Trematode hemoglobins show exceptionally high oxygen affinity.
Kiger L, Rashid AK, Griffon N, Haque M, Moens L, Gibson QH, Poyart C, Marden MC. Kiger L, et al. Among authors: poyart c. Biophys J. 1998 Aug;75(2):990-8. doi: 10.1016/S0006-3495(98)77587-3. Biophys J. 1998. PMID: 9675199 Free PMC article.
Whereas oxygen can be displaced on a millisecond time scale from human Hb at 25 degrees C, the dissociation of oxygen from trematode Hb may require a few seconds to over 20 s (for Hb Pe). ...
Whereas oxygen can be displaced on a millisecond time scale from human Hb at 25 degrees C, the dissociation of oxygen from trematode …
Functional aspects of ultra-rapid heme doming in hemoglobin, myoglobin, and the myoglobin mutant H93G.
Franzen S, Bohn B, Poyart C, DePillis G, Boxer SG, Martin JL. Franzen S, et al. Among authors: poyart c. J Biol Chem. 1995 Jan 27;270(4):1718-20. doi: 10.1074/jbc.270.4.1718. J Biol Chem. 1995. PMID: 7829506
Hemoglobin Saverne: a new variant with elongated beta chains: structural and functional properties.
Delanoe-Garin J, Blouquit Y, Arous N, Kister J, Poyart C, North ML, Bardakdjian J, Lacombe C, Rosa J, Galacteros F. Delanoe-Garin J, et al. Among authors: poyart c. Hemoglobin. 1988;12(4):337-52. doi: 10.3109/03630268808998034. Hemoglobin. 1988. PMID: 3170236
Structural analysis of the abnormal beta chain showed an elongated C-terminal segment. Histidine 143 is replaced by a proline and the C-terminal sequence is identical to the corresponding segment of Hb Cranston. ...
Structural analysis of the abnormal beta chain showed an elongated C-terminal segment. Histidine 143 is replaced by a proline and the …
Increased oxygen affinity with normal heterotropic effects in hemoglobin Loire [alpha 88(F9)Ala----Ser].
Baklouti F, Baudin-Chich V, Kister J, Marden M, Teyssier G, Poyart C, Delaunay J, Wajcman H. Baklouti F, et al. Among authors: poyart c. Eur J Biochem. 1988 Nov 1;177(2):307-12. doi: 10.1111/j.1432-1033.1988.tb14377.x. Eur J Biochem. 1988. PMID: 3142772
The functional properties of Hb Loire may be explained by a slight displacement of some key residues of the C-terminal region of the alpha chain destabilizing the T structure....
The functional properties of Hb Loire may be explained by a slight displacement of some key residues of the C-terminal region of the …
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