Masako Nagai
Overview
Explore the profile of Masako Nagai including associated specialties, affiliations and a list of published articles.
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Articles
27
Citations
135
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Recent Articles
1.
Nagatomo S, Shoji M, Terada T, Nakatani K, Shigeta Y, Hirota S, et al.
Biophys J
. 2022 Jun;
121(14):2767-2780.
PMID: 35689380
Hemoglobins M (Hbs M) are human hemoglobin variants in which either the α or β subunit contains a ferric heme in the αβ tetramer. Though the ferric subunit cannot bind...
2.
Nagatomo S, Nagai M, Kitagawa T
Biophys Rev
. 2022 May;
14(2):483-498.
PMID: 35528033
This mini-review, mainly based on our resonance Raman studies on the structural origin of cooperative O binding in human adult hemoglobin (HbA), aims to answering why HbA is a tetramer...
3.
Nagatomo S, Kitagawa T, Nagai M
Biophys J
. 2021 Jun;
120(13):2734-2745.
PMID: 34087219
Using various mutants, we investigated to date the roles of the Fe-histidine (F8) bonds in cooperative O binding of human hemoglobin (Hb) and differences in roles between α- and β-subunits...
4.
Nagai M, Mizusawa N, Kitagawa T, Nagatomo S
Biophys Rev
. 2017 Dec;
10(2):271-284.
PMID: 29260461
Structural changes of heme side-chains of human adult hemoglobin (Hb A) upon ligand (O or CO) dissociation have been studied by circular dichroism (CD) and resonance Raman (RR) spectroscopies. We...
5.
Nagatomo S, Saito K, Yamamoto K, Ogura T, Kitagawa T, Nagai M
Biochemistry
. 2017 Oct;
56(46):6125-6136.
PMID: 29064674
Following a previous detailed investigation of the β subunit of αβ human adult hemoglobin (Hb A), this study focuses on the α subunit by using three natural valency hybrid α(Fe-deoxy/O)β(Fe)...
6.
Nagatomo S, Okumura M, Saito K, Ogura T, Kitagawa T, Nagai M
Biochemistry
. 2017 Feb;
56(9):1261-1273.
PMID: 28199095
Regulation of the oxygen affinity of human adult hemoglobin (Hb A) at high pH, known as the alkaline Bohr effect, is essential for its physiological function. In this study, structural...
7.
Nagai M, Nagai Y, Aki Y, Sakurai H, Mizusawa N, Ogura T, et al.
Chirality
. 2016 Jul;
28(8):585-92.
PMID: 27427792
Native human adult hemoglobin (Hb A) has mostly normal orientation of heme, whereas recombinant Hb A (rHb A) expressed in E. coli contains both normal and reversed orientations of heme....
8.
Neya S, Nagai M, Nagatomo S, Hoshino T, Yoneda T, Kawaguchi A
Biochim Biophys Acta
. 2015 Oct;
1857(5):582-588.
PMID: 26435388
Myoglobin reconstitution with various synthetic heme analogues was reviewed to follow the consequences of modified heme-globin interactions. Utility of dimethyl sulfoxide as the solvent for water-insoluble hemes was emphasized. Proton...
9.
Nagatomo S, Nagai Y, Aki Y, Sakurai H, Imai K, Mizusawa N, et al.
PLoS One
. 2015 Aug;
10(8):e0135080.
PMID: 26244770
Human hemoglobin (Hb), which is an α2β2 tetramer and binds four O2 molecules, changes its O2-affinity from low to high as an increase of bound O2, that is characterized by...
10.
Nagai M, Kobayashi C, Nagai Y, Imai K, Mizusawa N, Sakurai H, et al.
J Phys Chem B
. 2014 Dec;
119(4):1275-87.
PMID: 25525834
Incorporation of the heme into globin induces a prominent circular dichroism (CD) band in the Soret region. The appearance of heme optical activity is widely believed to arise from the...