192 related articles for article (PubMed ID: 6704402)
1. A proton nuclear magnetic resonance investigation of human hemoglobin A2. Implications on the intermolecular contacts in sickle hemoglobin fibers and on the Bohr effect of human normal adult hemoglobin.
Russu IM; Lin AK; Ferro-Dosch S; Ho C
Biochim Biophys Acta; 1984 Mar; 785(3):123-31. PubMed ID: 6704402
[TBL] [Abstract][Full Text] [Related]
2. A proton nuclear magnetic resonance investigation of histidyl residues in sickle hemoglobin.
Russu IM; Ho C
Biochemistry; 1982 Sep; 21(20):5044-51. PubMed ID: 6291599
[TBL] [Abstract][Full Text] [Related]
3. A proton nuclear magnetic resonance investigation of histidyl residues in human normal adult hemoglobin.
Russu IM; Ho NT; Ho C
Biochemistry; 1982 Sep; 21(20):5031-43. PubMed ID: 6291598
[TBL] [Abstract][Full Text] [Related]
4. Contribution of surface histidyl residues in the alpha-chain to the Bohr effect of human normal adult hemoglobin: roles of global electrostatic effects.
Sun DP; Zou M; Ho NT; Ho C
Biochemistry; 1997 Jun; 36(22):6663-73. PubMed ID: 9184146
[TBL] [Abstract][Full Text] [Related]
5. Roles of the beta 146 histidyl residue in the molecular basis of the Bohr effect of hemoglobin: a proton nuclear magnetic resonance study.
Busch MR; Mace JE; Ho NT; Ho C
Biochemistry; 1991 Feb; 30(7):1865-77. PubMed ID: 1993201
[TBL] [Abstract][Full Text] [Related]
6. Assessment of roles of surface histidyl residues in the molecular basis of the Bohr effect and of beta 143 histidine in the binding of 2,3-bisphosphoglycerate in human normal adult hemoglobin.
Fang TY; Zou M; Simplaceanu V; Ho NT; Ho C
Biochemistry; 1999 Oct; 38(40):13423-32. PubMed ID: 10529219
[TBL] [Abstract][Full Text] [Related]
7. Proton longitudinal relaxation investigation of histidyl residues of normal human adult and sickle deoxyhemoglobin: evidence for the existence of pregelation aggregates in sickle deoxyhemoglobin solutions.
Russu IM; Ho C
Proc Natl Acad Sci U S A; 1980 Nov; 77(11):6577-81. PubMed ID: 6256747
[TBL] [Abstract][Full Text] [Related]
8. Assessment of role of beta 146-histidyl and other histidyl residues in the Bohr effect of human normal adult hemoglobin.
Russu IM; Ho C
Biochemistry; 1986 Apr; 25(7):1706-16. PubMed ID: 3707904
[TBL] [Abstract][Full Text] [Related]
9. High-resolution proton nuclear magnetic resonance studies of sickle cell hemoglobin.
Fung LW; Lin KL; Ho C
Biochemistry; 1975 Jul; 14(15):3424-30. PubMed ID: 238591
[TBL] [Abstract][Full Text] [Related]
10. Role of the beta 146 histidyl residue in the alkaline Bohr effect of hemoglobin.
Russu IM; Ho NT; Ho C
Biochemistry; 1980 Mar; 19(5):1043-52. PubMed ID: 7356961
[TBL] [Abstract][Full Text] [Related]
11. A high-resolution proton nuclear-magnetic-resonance investigation of carp hemoglobin. Conformational differences between carp and human normal adult hemoglobins in solution.
Dalvit C; Miura S; de Young A; Noble RW; Cerdonio M; Ho C
Eur J Biochem; 1984 Jun; 141(2):255-9. PubMed ID: 6329750
[TBL] [Abstract][Full Text] [Related]
12. Molecular basis for the anti-sickling activity of aromatic amino acids and related compounds: a proton nuclear magnetic resonance investigation.
Russu IM; Lin AK; Yang CP; Ho C
Biochemistry; 1986 Feb; 25(4):808-15. PubMed ID: 3964645
[TBL] [Abstract][Full Text] [Related]
13. High resolution NMR studies of histidine-substituted and histidine-perturbed hemoglobin variants. Histidine assignments, electrostatic interactions at the protein surface, and implications for hemoglobin S polymerization.
Craescu CT; Schaeffer C; Mispelter J; Garin J; Rosa J
J Biol Chem; 1986 Jun; 261(17):7894-901. PubMed ID: 3711114
[TBL] [Abstract][Full Text] [Related]
14. A proton nuclear magnetic resonance investigation of the anion Bohr effect of human normal adult hemoglobin.
Russu IM; Wu SS; Ho NT; Kellogg GW; Ho C
Biochemistry; 1989 Jun; 28(12):5298-306. PubMed ID: 2765535
[TBL] [Abstract][Full Text] [Related]
15. 1H and 31P nuclear magnetic resonance investigation of the interaction between 2,3-diphosphoglycerate and human normal adult hemoglobin.
Russu IM; Wu SS; Bupp KA; Ho NT; Ho C
Biochemistry; 1990 Apr; 29(15):3785-92. PubMed ID: 2340273
[TBL] [Abstract][Full Text] [Related]
16. A proton nuclear magnetic resonance investigation of proximal histidyl residues in human normal and abnormal hemoglobins. A probe for the heme pocket.
Takahashi S; Lin AK; Ho C
Biophys J; 1982 Jul; 39(1):33-40. PubMed ID: 7104448
[TBL] [Abstract][Full Text] [Related]
17. Effects of anions on the molecular basis of the Bohr effect of hemoglobin.
Busch MR; Ho CE
Biophys Chem; 1990 Aug; 37(1-3):313-22. PubMed ID: 2285794
[TBL] [Abstract][Full Text] [Related]
18. Conformational changes in the hemoglobin S system as seen by proton binding.
Scholberg HP; Fronticelli C; Bucci E
J Biol Chem; 1980 Sep; 255(18):8592-8. PubMed ID: 7410379
[TBL] [Abstract][Full Text] [Related]
19. Structural bases of the inhibitory effects of hemoglobin F and hemoglobin A2 on the polymerization of hemoglobin S.
Nagel RL; Bookchin RM; Johnson J; Labie D; Wajcman H; Isaac-Sodeye WA; Honig GR; SchilirĂ² G; Crookston JH; Matsutomo K
Proc Natl Acad Sci U S A; 1979 Feb; 76(2):670-2. PubMed ID: 284392
[TBL] [Abstract][Full Text] [Related]
20. Proton nuclear Overhauser effect investigation of the heme pockets in ligated hemoglobin: conformational differences between oxy and carbonmonoxy forms.
Dalvit C; Ho C
Biochemistry; 1985 Jul; 24(14):3398-407. PubMed ID: 4041419
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]