L O Narhi
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Explore the profile of L O Narhi including associated specialties, affiliations and a list of published articles.
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Recent Articles
21.
Narhi L, Aoki K, Philo J, Arakawa T
J Protein Chem
. 1997 Apr;
16(3):213-25.
PMID: 9155092
Erythropoietin (EPO) is a glycoprotein hormone which belongs to the four-helical-bundle cytokine family and regulates the level of circulating red blood cells. The EPO receptor (EPOR) belongs to the cytokine-receptor...
22.
Hsu Y, Wu G, Mendiaz E, Syed R, Wypych J, Toso R, et al.
J Biol Chem
. 1997 Mar;
272(10):6406-15.
PMID: 9045664
Soluble Escherichia coli-derived recombinant human stem cell factor (rhSCF) forms a non-covalently associated dimer. We have determined a dimer association constant (Ka) of 2-4 x 10(8) M-1, using sedimentation equilibrium...
23.
Formation of an active dimer during storage of interleukin-1 receptor antagonist in aqueous solution
Chang B, Beauvais R, Arakawa T, Narhi L, Dong A, Aparisio D, et al.
Biophys J
. 1996 Dec;
71(6):3399-406.
PMID: 8968609
The degradation products of recombinant human interleukin-1 receptor antagonist (rhIL-1ra) formed during storage at 30 degrees C in aqueous solution were characterized. Cationic exchange chromatography of the stored sample showed...
24.
Narhi L, Philo J, Li T, Zhang M, Samal B, Arakawa T
Biochemistry
. 1996 Sep;
35(35):11454-60.
PMID: 8784201
Acid-induced unfolding of proteins often results in an intermediate structure, called the molten globule structure or "A" state, which retains at least partial secondary structure but lacks a rigid tertiary...
25.
Narhi L, Philo J, Li T, Zhang M, Samal B, Arakawa T
Biochemistry
. 1996 Sep;
35(35):11447-53.
PMID: 8784200
The unfolding and refolding of alpha-helical proteins has been extensively studied, demonstrating formation of intermediate structures which retain the native-like alpha-helix but lack the tertiary structure. Studies on the folding...
26.
Lu H, Hsu Y, Narhi L, Karkare S, Lin F
Protein Expr Purif
. 1996 Sep;
8(2):227-37.
PMID: 8812867
We report here the expression of recombinant human prokallikrein and kallikrein in engineered Chinese hamster ovary cells transfected with a human genomic gene encoding preprokallikrein. At high expression levels, recombinant...
27.
Hsu Y, Narhi L, Spahr C, Langley K, Lu H
Protein Sci
. 1996 Jun;
5(6):1165-73.
PMID: 8762148
The effect of oxidation of the methionine residues of Escherichia coli-derived recombinant human stem cell factor (huSCF) to methionine sulfoxide on the structure and activity of SCF was examined. Oxidation...
28.
Lu H, Jones M, Shieh J, Mendiaz E, Feng D, Watler P, et al.
J Biol Chem
. 1996 May;
271(19):11309-16.
PMID: 8626683
Distinct from the noncovalently linked recombinant human stem call factor (rhSCF) dimer, we report here the isolation and identification of an SDS-nondissociable dimer produced during folding/oxidation of rhSCF. Experimental evidence...
29.
Jones M, Narhi L, Chang W, Lu H
J Biol Chem
. 1996 May;
271(19):11301-8.
PMID: 8626682
Oxidative folding of recombinant human stem cell factor (rhSCF) produced in Escherichia coli was investigated in vitro. Folding of denatured and reduced rhSCF involves at least five intermediate forms, I-1...
30.
Philo J, Aoki K, Arakawa T, Narhi L, Wen J
Biochemistry
. 1996 Feb;
35(5):1681-91.
PMID: 8634300
Although there is considerable evidence that signaling by the erythropoietin (EPO) receptor is initiated when it is dimerized by binding EPO, it has been previously reported that the soluble extracellular...