K. Harada

Osaka University of Economics — Japan

Medicine · Health Sciences

16h-index652citations60works0.02yr avg
OpenAlex↗Google Scholar↗Lab page↗

Accepting Students?

No reports yet. Know if this professor is taking students?

Research Topics

Advanced MRI Techniques and Applications(8), Hemoglobin structure and function(7), Advanced Neuroimaging Techniques and Applications(6), Pharmacogenetics and Drug Metabolism(5), Nuclear physics research studies(4)

Publications60 total

1P095 Substrate access to slow substrate binding P450cam with mutation at the proposed gate for water egress/ingress from/to the active site(02. Heme proteins,Poster)
Seibutsu Butsuri·2013Open Access
2I1536 Water expelling pathway of cytochrome P450cam : Effect of mutation of a gate forming Asp297 to Leu on D-camphor binding(Heme proteins 2,The 48th Annual Meeting of the Biophysical Society of Japan)
Seibutsu Butsuri·2011Open Access
2I1548 Reaction of norcamphor with cytochrome P450cam mutated at the gate forming Asp297 for putative water expelling pathway(Heme proteins 2,The 48th Annual Meeting of the Biophysical Society of Japan)
Seibutsu Butsuri·2011Open Access
3P113 Substrate binding excludes water cluster from active site of cytochrome P450cam - mutation analysis of water expelling system(Heme proteins,The 48th Annual Meeting of the Biophysical Society of Japan)
Seibutsu Butsuri·2010Open Access
3P-076 チトクロムP450camの活性部位からの水クラスター排出機構(ヘム蛋白質,第47回日本生物物理学会年会)
生物物理·2009
A Role of the Heme-7-Propionate Side Chain in Cytochrome P450cam as a Gate for Regulating the Access of Water Molecules to the Substrate-Binding Site
Journal of the American Chemical Society·2009· 48 cited
3P-076 Mechanism of the water exclusion from the active site of cytochrome P450cam(Heme proteins,The 47th Annual Meeting of the Biophysical Society of Japan)
Seibutsu Butsuri·2009Open Access
1P-121 チトクロムP450camの基質結合反応における活性部位近傍Asp297の役割(ヘム蛋白質,第46回日本生物物理学会年会)
生物物理·2008
Roles of heme-6-propionate side chain in monooxygenase cytochrome P450cam
Acta Crystallographica Section A Foundations of Crystallography·2008Open Access
Elucidation of Functional Roles of Heme-Propionate Side Chains in Hemoproteins
2008
1P-121 Roles of Asp297 in the vicinity of the active site of cytochrome P450cam in substrate binding(The 46th Annual Meeting of the Biophysical Society of Japan)
Seibutsu Butsuri·2008Open Access
Evaluation of the Functional Role of the Heme-6-propionate Side Chain in Cytochrome P450cam
Journal of the American Chemical Society·2007· 24 cited
Structure and Ligand Binding Properties of Myoglobins Reconstituted with Monodepropionated Heme:  Functional Role of Each Heme Propionate Side Chain<sup>,</sup>
Biochemistry·2007· 44 cited
Isospin structure of<mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML" display="inline"><mml:mrow><mml:msup><mml:mi>J</mml:mi><mml:mrow><mml:mi>π</mml:mi></mml:mrow></mml:msup><mml:mo>=</mml:mo><mml:msup><mml:mn>1</mml:mn><mml:mrow><mml:mo>+</mml:mo></mml:mrow></mml:msup></mml:mrow></mml:math>states in<mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML" display="inline"><mml:mmultiscripts><mml:mi mathvariant="normal">Ni</mml:mi><mml:mprescripts/><mml:none/><mml:mrow><mml:mn>58</mml:mn></mml:mrow></mml:mmultiscripts></mml:math>and<mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML" display="inline"><mml:mmultiscripts><mml:mi mathvariant="normal">Cu</mml:mi><mml:mprescripts/><mml:none/><mml:mrow><mml:mn>58</mml:mn></mml:mrow></mml:mmultiscripts></mml:math>studied by<mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML" display="inline"><mml:mmultiscripts><mml:mi mathvariant="normal">Ni</mml:mi><mml:mprescripts/><mml:none/><mml:mrow><mml:mn>58</mml:mn></mml:mrow></mml:mmultiscripts></mml:math>(<mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML" display="inline"><mml:mrow><mml:mi>p</mml:mi><mml:mo>,</mml:mo><mml:msup><mml:mi>p</mml:mi><mml:mrow><mml:mo>'</mml:mo></mml:mrow></mml:msup></mml:mrow></mml:math>) and<mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML" display="inline"><mml:mmultiscripts><mml:mi mathvariant="normal">Ni</mml:mi><mml:mprescripts/><mml:none/><mml:mrow><mml:mn>58</mml:mn></mml:mrow></mml:mmultiscripts></mml:math>(<mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML" display="inline"><mml:mmultiscripts><mml:mi mathvariant="normal">He</mml:mi><mml:mprescripts/><mml:none/><mml:mrow><mml:mn>3</mml:mn></mml:mrow></mml:mmultiscripts></mml:math>,<mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML" display="inline"><mml:mrow><mml:mi>t</mml:mi></mml:mrow></mml:math>)<mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML" display="inline"><mml:mmultiscripts><mml:mi mathvariant="normal">Cu</mml:mi><mml:mprescripts/><mml:none/><mml:mrow><mml:mn>58</mml:mn></mml:mrow></mml:mmultiscripts></mml:math>measurements
Physical Review C·2007· 46 cited
Isospin structure of J(pi)=1(+) states in Ni-58 and Cu-58 studied by Ni-58(p,p(')) and Ni-58(He-3,t)Cu-58 measurements
2007
Time-resolved Raman evidence for energy ‘funneling’ through propionate side chains in heme ‘cooling’ upon photolysis of carbonmonoxy myoglobin
Chemical Physics Letters·2006· 38 cited
Pathway of Information Transmission from Heme to Protein upon Ligand Binding/Dissociation in Myoglobin Revealed by UV Resonance Raman Spectroscopy
Journal of Biological Chemistry·2006· 21 citedOpen Access
MRI artifact cancellation algorithms for 2-D translational motion
2005· 3 cited
Chemical Properties of Sperm Whale Myoglobins Reconstituted with Monopropionate Hemins
Chemistry Letters·2004· 9 cited
Role of heme-propionate side chains in myoglobin function
Journal of Inorganic Biochemistry·2003· 3 cited
page 1 of 3Next →

Frequent Co-authors

T Kozuka(17), Takashi Hayashi(13), Keisuke Sakurai(8), Kosuke Sakurai(8), Hideo Shimada(7), Naonobu Fujita(7), Y Akai(5), Hiroyuki Naito(4), J Arisawa(4), Shun Hirota(4), A.D. Bacher(4), G.P.A. Berg(4), T. Black(4), H. Fujimura(4), K. Hatanaka(4), K. Katori(4), Y. Shimbara(4), Kunitoshi Shimokata(4), Hiroshi Yamagami(3), Shota Tamura(3)