A. Matsuoka

发表

1H NMR study of dynamics and thermodynamics of acid-alkaline transition in ferric hemoglobin of a midge larva (Tokunagayusurika akamusi).

K. Shikama, Y. Yamamoto, K. Koshikawa, 1998, Biochimica et biophysica acta.

The swinging movement of the distal histidine residue and the autoxidation reaction for midge larval hemoglobins.

K. Shikama, K. Imai, S. Kamimura, 2003, European journal of biochemistry.

Human haemoglobin: a new paradigm for oxygen binding involving two types of alphabeta contacts.

K. Shikama, A. Matsuoka, 2003, European journal of biochemistry.

The α1β1 contact of human hemoglobin plays a key role in stabilizing the bound dioxygen

K. Shikama, T. Ichikawa, A. Matsuoka, 2002 .

L-arginine and calmodulin regulation of the heme iron reactivity in neuronal nitric oxide synthase.

M. Ikeda-Saito, J. Olson, D. Stuehr, 1994, The Journal of biological chemistry.

Isolation and autoxidation profile of fish myoglobin from hoki (Macruronus magellanicus).

T. Mizuguchi, A. Matsuoka, G. Kobayashi, 2014, Fukushima journal of medical science.

Identification and Characterization of a Redox Sensor Phosphodiesterase from Ferrovum sp. PN-J185 Containing Bacterial Hemerythrin and HD-GYP Domains.

Kenichi Kitanishi, J. Igarashi, A. Matsuoka, 2020, Biochemistry.

Spectral properties unique to the myoglobins lacking the usual distal histidine residue.

K. Shikama, A. Matsuoka, 1989, Journal of molecular biology.

Relationship between oxygen affinity and autoxidation of myoglobin.

K. Imai, S. Nagao, S. Hirota, 2012, Inorganic chemistry.

Stability properties of Aplysia oxymyoglobin: effect of esterification of the heme propionates.

K. Shikama, A. Matsuoka, 1992, Biochimica et biophysica acta.

Dual nature of the distal histidine residue in the autoxidation reaction of myoglobin and hemoglobin comparison of the H64 mutants.

K. Shikama, A. Matsuoka, T. Suzuki, 2000, European journal of biochemistry.

African elephant myoglobin with an unusual autoxidation behavior: comparison with the H64Q mutant of sperm whale myoglobin.

K. Shikama, M. Ikeda-Saito, A. Matsuoka, 1998, Biochimica et biophysica acta.

The unique structures of protozoan myoglobin and yeast hemoglobin: an evolutionary diversity.

H. Iwaasa, K. Shikama, A. Matsuoka, 1995, The international journal of biochemistry & cell biology.

Role of globin moiety in the autoxidation reaction of oxymyoglobin: effect of 8 M urea.

K. Shikama, A. Matsuoka, Y. Sugawara, 1995, Biophysical journal.

Hydrogen peroxide plays a key role in the oxidation reaction of myoglobin by molecular oxygen. A computer simulation.

K. Shikama, T. Wazawa, A. Matsuoka, 1992, Biophysical journal.

Protozoan myoglobin from Paramecium caudatum. Its autoxidation reaction and hemichrome formation.

K. Shikama, Y. Tsubamoto, A. Matsuoka, 1990, European journal of biochemistry.

Autoxidation of myoglobin from bigeye tuna fish (Thunnus obesus).

K. Shikama, Y. Kitahara, N. Kobayashi, 1990, Biochimica et biophysica acta.

Aplysia oxymyoglobin with an unusual stability property: involvement of two kinds of carboxyl groups.

K. Shikama, A. Matsuoka, 1988, Biochimica et biophysica acta.

Stability properties of oxymyoglobin from chicken gizzard smooth muscle.

T. Takagi, H. Iwaasa, K. Shikama, 1987, Comparative biochemistry and physiology. B, Comparative biochemistry.

Aplysia oxymyoglobin with an unusual stability property: kinetic analysis of the pH dependence

K. Shikama, A. Matsuoka, 1986 .

1H-NMR study of dynamics and thermodynamics of Cl- binding to ferric hemoglobin of a midge larva (Tokunagayusurika akamusi).

K. Shikama, Yasuhiko Yamamoto, K. Koshikawa, 2003, Biochimica et biophysica acta.

The dimer-monomer conversion of Cerithidea myoglobin coupled with the heme iron oxidation

K. Shikama, K. Imai, A. Matsuoka, 1996 .

The Soret magnetic circular dichroism of ferric high-spin myoglobins. A probe for the distal histidine residue.

K. Shikama, N. Kobayashi, A. Matsuoka, 1992, European journal of biochemistry.

Structure-Function Relationships in Unusual Nonvertebrate Globins

K. Shikama, A. Matsuoka, 2004, Critical reviews in biochemistry and molecular biology.

APLYSIA MYOGLOBIN WITH UNUSUAL PROPERTIES: ANOTHER PROTOTYPE IN MYOGLOBIN AND HAEMOGLOBIN BIOCHEMISTRY

K. Shikama, A. Matsuoka, 1994, Biological reviews of the Cambridge Philosophical Society.

Extreme heterogeneous composition of the Paramecium caudatum macronuclear genomic DNA between hemoglobin and nucleosome assembly protein-1 genes.

K. Yamauchi, A. Matsuoka, K. Mikami, 2010, Genes & genetic systems.

A primitive myoglobin from Tetrahymena pyriformis: its heme environment, autoxidizability, and genomic DNA structure.

K. Shikama, J. Igarashi, A. Matsuoka, 2000, Biochimica et biophysica acta.

The a1b1 contact of human hemoglobin plays a key role in stabilizing the bound dioxygen Further evidence from the iron valency hybrids

Keiji, T. Ichikawa, A. Matsuoka, 2001 .

The Molecular Mechanism of Autoxidation for Human Oxyhemoglobin

K. Shikama, A. Hachimori, A. Matsuoka, 1998, The Journal of Biological Chemistry.

The structure of the Aplysia kurodai gene encoding ADP-ribosyl cyclase, a second-messenger enzyme.

N. Noguchi, S. Takasawa, T. Numakunai, 1995, Gene.

EPR and ENDOR studies of the distal site coordination of shark heart myoglobin

K. Shikama, A. Matsuoka, N. Ohshima, 2007 .

The pH-dependent swinging-out of the distal histidine residue in ferric hemoglobin of a midge larva (Tokunagayusurika akamusi).

K. Shikama, M. Fukuda, N. Kobayashi, 1994, Biochimica et biophysica acta.

Aplysia Myoglobin: Involvement of Two Kinds of Carboxyl Groups in the Autoxidation Reaction

K. Shikama, A. Matsuoka, 1991 .

Aplysia myoglobins with an unusual amino acid sequence.

T. Takagi, K. Shikama, A. Matsuoka, 1984, Journal of Molecular Biology.

A hydrogen-bonding network formed by the B10–E7–E11 residues of a truncated hemoglobin from Tetrahymena pyriformis is critical for stability of bound oxygen and nitric oxide detoxification

J. Igarashi, Kazuo Kobayashi, Kazuo Kobayashi, 2011, JBIC Journal of Biological Inorganic Chemistry.

Yeast Flavohemoglobin from Candida norvegensis

K. Shikama, A. Matsuoka, G. Kobayashi, 2002, The Journal of Biological Chemistry.