Refine your search:     
Report No.
 - 
Search Results: Records 1-2 displayed on this page of 2
  • 1

Presentation/Publication Type

Initialising ...

Refine

Journal/Book Title

Initialising ...

Meeting title

Initialising ...

First Author

Initialising ...

Keyword

Initialising ...

Language

Initialising ...

Publication Year

Initialising ...

Held year of conference

Initialising ...

Save select records

Journal Articles

Static tensile deformation behavior of a lean duplex stainless steel studied by in situ neutron diffraction and synchrotron radiation white X-rays

Tsuchida, Noriyuki*; Kawahata, Takuji*; Ishimaru, Eiichiro*; Takahashi, Akihiko*; Suzuki, Hiroshi; Shobu, Takahisa

ISIJ International, 53(7), p.1260 - 1267, 2013/07

 Times Cited Count:24 Percentile:73.74(Metallurgy & Metallurgical Engineering)

To investigate the tensile deformation behavior of a lean duplex stainless steel (S32101) from the viewpoints of plastic deformability among phases or grains, we performed static tensile tests, in situ neutron diffraction, and white X-ray diffraction experiments at room temperature. From the experimental results of synchrotron radiation white X-ray diffraction experiments, the hard phase of S32101 was changed from the ferrite phase to austenite one during tensile deformation. This led to a larger stress partitioning between the phases at the latter stage of deformation. From the experimental results of in situ neutron diffraction, it was found that the stress partitioning of the $$gamma$$ phase in the S32101 was the largest among the present results. Therefore, the larger work hardening rate of S32101 can be explained by the large stress partitioning of the $$gamma$$ phase, that between $$gamma$$ and $$alpha$$ phases and $$gamma$$ volume fraction.

Journal Articles

Enlarged FAMSBAS; Protein 3D structure models of genome sequences for 41 species

Yamaguchi, Akihiro*; Iwadate, Mitsuo*; Suzuki, Eiichiro*; Yura, Kei; Kawakita, Shigetsune*; Umeyama, Hideaki*; Go, Michiko*

Nucleic Acids Research, 31(1), p.463 - 468, 2003/01

 Times Cited Count:15 Percentile:25.22(Biochemistry & Molecular Biology)

Enlarged FAMSBASE is a relational database of comparative protein structure models for the whole genome of 41 species, presented in the GTOP database. The models are calculated by FAMS, Full Automatic Modeling System. Enlarged FAMSBASE provides a wide range of query keys, such as name of ORF (open reading frame), ORF keywords, PDB ID, PDB heterogen atoms, and sequence similarity. Heterogen atoms in PDB include cofactors, ligands, and other factors that interact with proteins, and are a good starting point for analyzing interactions between proteins and other molecules. The data may also work as a template for drug design. The present number of ORFs with protein 3D models in FAMSBASE is 183,805, and the database includes an average of three models for each ORF. FAMSBASE is available at http://famsbase.bio.nagoya-u.ac.jp/famsbase/.

2 (Records 1-2 displayed on this page)
  • 1