His scientific interests lie mostly in Biochemistry, Cell biology, Protein structure, Ezrin and FERM domain. Toshio Hakoshima frequently studies issues relating to Crystal structure and Biochemistry. In his study, which falls under the umbrella issue of Cell biology, HMG-box, DNA-binding domain and Transcription factor is strongly linked to Binding site.
His studies in Protein structure integrate themes in fields like Genetics, Alpha helix, Biophysics, Peptide sequence and Stereochemistry. When carried out as part of a general Ezrin research project, his work on Moesin and Radixin is frequently linked to work in Phosphotyrosine-binding domain and Peptide binding, therefore connecting diverse disciplines of study. His research integrates issues of Sequence motif, Beta sheet, Pleckstrin homology domain and Immunoglobulin superfamily in his study of FERM domain.
His primary scientific interests are in Biochemistry, Crystallography, Crystal structure, Biophysics and Stereochemistry. His Biophysics study combines topics from a wide range of disciplines, such as Moesin, Ezrin, Radixin and FERM domain. His work in Radixin tackles topics such as Cell adhesion molecule which are related to areas like Beta sheet.
His FERM domain study combines topics in areas such as Cytoplasm, Cell biology and Signal transducing adaptor protein. He has included themes like Nucleotide, Guanine, Polyamine, Hydrogen bond and Ribonuclease T1 in his Stereochemistry study. His Protein structure research incorporates elements of Genetics, Binding site and Rho-associated protein kinase.
Biochemistry, Cell biology, Biophysics, Stereochemistry and Plasma protein binding are his primary areas of study. His study connects Polyhydroxyalkanoates and Biochemistry. His Cell biology research includes themes of Receptor, Karrikin and Strigolactone.
His study in Biophysics is interdisciplinary in nature, drawing from both Cell migration, Haptotaxis and Helix. His Stereochemistry research incorporates themes from Crystallography, Catalytic triad, Active site, Cupriavidus necator and Protein structure. Toshio Hakoshima interconnects Moesin, Ezrin, Radixin and Cullin in the investigation of issues within FERM domain.
His main research concerns Plasma protein binding, Biochemistry, Stereochemistry, Biophysics and Hydrolase. His research in Plasma protein binding intersects with topics in Protein domain, Auxin, Phosphorylation and Helix. The study incorporates disciplines such as Protein structure, Catalytic triad and Cupriavidus necator, Polyhydroxyalkanoates in addition to Stereochemistry.
His biological study spans a wide range of topics, including Stereoisomerism, Cereblon, Glutarimide, Enantiomer and Binding site. His Biophysics research integrates issues from Cytoplasm and Gravitropism, Polar auxin transport, Arabidopsis. His research investigates the link between Enzyme and topics such as Cell biology that cross with problems in Zinc finger.
This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.
Gibberellin-induced DELLA recognition by the gibberellin receptor GID1
Kohji Murase;Yoshinori Hirano;Tai-ping Sun;Toshio Hakoshima.
Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain.
Keisuke Hamada;Toshiyuki Shimizu;Takeshi Matsui;Shoichiro Tsukita.
The EMBO Journal (2000)
Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding protein 23 kDa/proliferation-associated gene product
Shoko Hirotsu;Yasuko Abe;Kengo Okada;Noriyuki Nagahara.
Proceedings of the National Academy of Sciences of the United States of America (1999)
The Molecular Structure of a DNA-Triostin A Complex
A. H.-J. Wang;G. Ughetto;G. J. Quigley;T. Hakoshima.
Structure of the human Cereblon–DDB1–lenalidomide complex reveals basis for responsiveness to thalidomide analogs
Philip P Chamberlain;Antonia Lopez-Girona;Karen Miller;Gilles Carmel.
Nature Structural & Molecular Biology (2014)
Structural basis for recruitment of human flap endonuclease 1 to PCNA.
Shigeru Sakurai;Ken Kitano;Hiroto Yamaguchi;Keisuke Hamada.
The EMBO Journal (2005)
Crystal structure of human RhoA in a dominantly active form complexed with a GTP analogue.
Kentaro Ihara;Sachiko Muraguchi;Masato Kato;Toshiyuki Shimizu.
Journal of Biological Chemistry (1998)
Crystal structure of an IRF-DNA complex reveals novel DNA recognition and cooperative binding to a tandem repeat of core sequences.
Yoshifumi Fujii;Toshiyuki Shimizu;Masahiro Kusumoto;Yoshimasa Kyogoku.
The EMBO Journal (1999)
Structures of D14 and D14L in the strigolactone and karrikin signaling pathways
Megumi Kagiyama;Yoshinori Hirano;Tomoyuki Mori;Sun Yong Kim.
Genes to Cells (2013)
Structural basis for the specific inhibition of heterotrimeric Gq protein by a small molecule.
Akiyuki Nishimura;Ken Kitano;Jun Takasaki;Masatoshi Taniguchi.
Proceedings of the National Academy of Sciences of the United States of America (2010)
If you think any of the details on this page are incorrect, let us know.
We appreciate your kind effort to assist us to improve this page, it would be helpful providing us with as much detail as possible in the text box below: