ライフサイエンスコーパス: sickle hemoglobin

1 hemia in a transgenic mouse expressing human sickle hemoglobin.

2 ttempt to alter the solubility properties of sickle hemoglobin.

3 s was achieved after correction of the human sickle hemoglobin allele by gene-specific targeting.

4 er some protection against polymerization of sickle hemoglobin and exert a reversible antiplatelet ef

5 olymerization by laser photolysis of carboxy sickle hemoglobin and observing stochastic variation of

6 The binding of CO to the sickle hemoglobin and the simultaneous melting of the he

7 Recognizing the qualitative abnormality of sickle hemoglobin as a prototype, Pauling & Castle estab

8 le RBC ROS generation has been attributed to sickle hemoglobin auto-oxidation and Fenton chemistry re

9 that affects the heterogeneous nucleation of sickle hemoglobin by using convex particle theory.

10 homozygous sickle cell anemia (HbSS), 7 with sickle hemoglobin C (HbSC), 7 with sickle/beta-thalassem

11 beta degrees -thalassemia (S beta degrees ), sickle-hemoglobin C disease (SC), or sickle-beta(+)-thal

12 We tested the hypothesis that sickle hemoglobin disrupts cdB3-based regulatory protein

13 In experiments using sickle hemoglobin droplets suspended in oil, it has been

14 ated 70 kDa dextran lowers the solubility of sickle hemoglobin, due to molecular crowding, and provid

15 utation plus the natural genetic mutation of sickle hemoglobin, E6V(beta).

16 If sickle hemoglobin fibers fail to depolymerize fully duri

17 of a very significant material anisotropy in sickle hemoglobin fibers, as might arise from the differ

18 entire class of linear aggregates, not just sickle hemoglobin fibers.

19 studied the variations of twist and bend in sickle hemoglobin fibers.

20 Sickle hemoglobin forms long, multistranded polymers tha

21 el method for measuring the microrheology of sickle hemoglobin gels, based on magnetically driven com

22 Given the recently determined stiffness of sickle hemoglobin gels, the observed obstruction seen in

23 by a variant of the beta-globin gene called sickle hemoglobin (Hb S).

24 Three novel recombinant mutants of sickle hemoglobin (Hb S, beta 6Glu-->Val) have been cons

25 homogeneous and heterogeneous nucleation on sickle hemoglobin (HbS beta 6 Glu-->Val) additionally mo

26 on the sites that promote polymerization of sickle hemoglobin (HbS) after formation of the initial h

27 hemoglobin (HbF) decreases polymerization of sickle hemoglobin (HbS) and improves outcomes in sickle

28 rstanding of intracellular polymerization of sickle hemoglobin (HbS) and subsequent interaction with

29 n standard treatment (N = 66) maintained 30% sickle hemoglobin (HbS) and tolerated deferasirox at 28.

30 n red blood cell (RBC) polymorphisms such as sickle hemoglobin (HbS) are known to protect against mal

31 s may be acting to prevent polymerization of sickle hemoglobin (HbS) by binding to and stabilizing li

32 kle cell anemia has been that replacement of sickle hemoglobin (HbS) by fetal hemoglobin (HbF) would

33 ed healthy hemoglobin A (HbA) and homozygous sickle hemoglobin (HbS) containing RBCs using whole bloo

34 We apply this analysis to a system of sickle hemoglobin (HbS) fibers that laterally attract on

35 ous and heterogeneous nucleation kinetics of sickle hemoglobin (HbS) have been studied for various de

36 y-free paper-based test capable of detecting sickle hemoglobin (HbS) in newborn blood samples with a

37 lity, is driven by polymerization of mutated sickle hemoglobin (HbS) in red blood cells (RBCs).

38 Sickle hemoglobin (HbS) is a point mutation of the two b

39 Polymerization of sickle hemoglobin (HbS) is the primary pathogenic event

40 een on transfusions aimed at maintaining the sickle hemoglobin (HbS) level below 30%.

41 sing blood samples from 25 SCD patients with sickle hemoglobin (HbS) levels varying from 64 to 90.1%,

42 at possesses the beta6 Glu-->Val mutation of sickle hemoglobin (HbS) plus beta73 Asp-->Asn.

43 Sickle hemoglobin (HbS) polymerization occurs when the c

44 pe of sickle cell anemia by inhibiting deoxy sickle hemoglobin (HbS) polymerization.

45 located at axial and lateral contacts of the sickle hemoglobin (HbS) polymers and strongly inhibit de

46 d comparatively little toxicity, and reduced sickle hemoglobin (HbS) synthesis as well as sickling of

47 ification agents that reduce the tendency of sickle hemoglobin (HbS) to aggregate represents an impor

48 Sickle hemoglobin (HbS), as a result of its polymer-rela

49 To create mice expressing exclusively human sickle hemoglobin (HbS), transgenic mice expressing huma

50 nitrite reductase activity of unpolymerized sickle hemoglobin (HbS), whose oxygen affinity and coope

51 ion results on the self-assembly behavior of sickle hemoglobin (HbS).

52 abinoids in transgenic mice expressing human sickle hemoglobin (HbS).

53 by reducing intracellular polymerization of sickle hemoglobin (HbS).

54 (SCD) is the polymerization of deoxygenated sickle hemoglobin (HbS).

55 ing the solubilizing effect of iron nitrosyl sickle hemoglobin (HbS-NO).

56 and F. A. Ferrone, in which up to 50% of the sickle hemoglobin is substituted by cross-linked hemoglo

57 moderate strength recommendation to maintain sickle hemoglobin levels of less than 30% prior to the n

58 all known free energies of polymerization of sickle hemoglobin measured in the presence of dextran.

59 ce between the association behavior of deoxy sickle hemoglobin molecules (HbS), which can polymerize

60 Sickle hemoglobin molecules assemble into polymers compo

61 Sickle hemoglobin nucleation occurs in solution as a hom

62 ar to but slightly greater than that seen in sickle hemoglobin nucleation.

63 emia [6 HbS/beta0, 1 HbS/beta+]), and 2 with sickle hemoglobin OArab (HbS/OArab).

64 s insight into the mechanism and kinetics of sickle hemoglobin polymer melting.

65 an effect mediated by its exclusion from the sickle hemoglobin polymer.

66 n hemoglobin (HBB) gene engineered to impede sickle hemoglobin polymerization (HBBAS3) to transduce h

67 n are both well described as consequences of sickle hemoglobin polymerization acting as a Brownian ra

68 of sickle cell disease, leading to increased sickle hemoglobin polymerization and decreased red blood

69 dissolution, and find that oxygen-dependent sickle hemoglobin polymerization and melting alone are s

70 Sickle hemoglobin polymerization exhibits a striking sen

71 Sickle hemoglobin polymerizes by two types of nucleation

72 a precise method of measuring the growth of sickle hemoglobin polymers by observing the time require

73 erstanding of the ligand binding kinetics of sickle hemoglobin polymers could have pathophysiological

74 ygous state of normal hemoglobin A (HbA) and sickle hemoglobin S (HbS), confers protection against ma

75 e rigidities are found to be consistent with sickle hemoglobin "single" fibers 20 nm in diameter, des

76 e evaluated children with SCD homozygous for sickle hemoglobin (SS disease) and controls (n = 65) and

77 travital microscopy in mice expressing human sickle hemoglobin (SS) that SS red blood cells (RBCs) bi

78 By photolysing droplets of sickle hemoglobin suspended in oil we find that polymeri

79 effort to map the most important regions of sickle hemoglobin that are involved in polymerization, w

80 Although the molecular defect in sickle hemoglobin that produces sickle cell disease has

81 In a solution of sickle hemoglobin, the molecules in the gel contribute n

82 n phenotype also reflects the instability of sickle hemoglobin, the release of heme, and the inductio

83 globin (HbF), which reduces the tendency for sickle hemoglobin to polymerize, thereby reducing the fr

84 trate abnormal (O2-dependent) association of sickle hemoglobin to RBC membrane that interferes with s

85 al NO synthase deletion (dNOS(-/-)) or human sickle hemoglobin transgenic expression (Sickle).

86 A sickle hemoglobin triple mutant with three amino acid su

87 nes on the rate of homogeneous nucleation in sickle hemoglobin, using preparations of open ghosts (OG

88 mutation (rd1) independent from that causing sickle hemoglobin was an incidental finding in some Berk

89 When transgenic mice that expressed human sickle hemoglobin were mated with mice having knockout m

90 e generated that expressed exclusively human sickle hemoglobin with 3 levels of HbF using their previ

91 ood vessels because of polymerization of the sickle hemoglobin within the red cells.