Nagoya Institute of Technology

About: Nagoya Institute of Technology is a education organization based out in Nagoya, Japan. It is known for research contribution in the topics: Thin film & Turbulence. The organization has 10766 authors who have published 19140 publications receiving 255696 citations. The organization is also known as: Nagoya Kōgyō Daigaku & Nitech.

DSP-based adaptive control of a brushless motor

Abstract: The authors present a method for the software control of a brushless DC motor using parameter identification. Not only speed and current controls, but also a real-time identification of the motor parameter can be implemented by the software, implemented on the digital signal processor (DSP) TMS320C25. The unique current control is performed according to an instantaneous voltage equation of the d-q model of the motor. The control accuracy depends on the motor parameters, so parameter identification with regard to armature inductance and EMF (electromotive force) constant is necessary. The identification algorithm has been verified by both simulation and experiment. The control program, including parameter identification, is of 2.5 K words, and the processing time is 99 mu s. >

Grain refinement in aluminum alloy 2219 during ECAP at 250 °C

Abstract: Grain refinement taking place in a coarse grained 2219 aluminum alloy deformed by equal channel angular pressing (ECAP) at a temperature of 250 °C to a strain of 12 was investigated. The microstructural changes are mainly characterized by the evolution of high density dislocation substructures with relatively low misorientations (∼3–5°) at strains below 2 and deformation bands (DBs) with moderate misorientation angle, which are frequently formed at strains above 3. Repeated ECAP leads to increasing the number and misorientation angle of the boundaries of DBs, so that the misorientation distribution for newly evolved dislocation subboundaries changes from single peak type at low strains to bimodal one at high strains. The fraction of high angle boundaries starts to increase at strain ɛ = 3, then it rapidly rises to about 80% at moderate to high strains and a new fine grains with almost random crystal orientation are fully developed in a whole material. The main mechanism of new fine grained structure formation during ECAP is discussed.

Multi-scale Domain-adversarial Multiple-instance CNN for Cancer Subtype Classification with Unannotated Histopathological Images

Abstract: We propose a new method for cancer subtype classification from histopathological images, which can automatically detect tumor-specific features in a given whole slide image (WSI). The cancer subtype should be classified by referring to a WSI, i.e., a large-sized image (typically 40,000x40,000 pixels) of an entire pathological tissue slide, which consists of cancer and non-cancer portions. One difficulty arises from the high cost associated with annotating tumor regions in WSIs. Furthermore, both global and local image features must be extracted from the WSI by changing the magnifications of the image. In addition, the image features should be stably detected against the differences of staining conditions among the hospitals/specimens. In this paper, we develop a new CNN-based cancer subtype classification method by effectively combining multiple-instance, domain adversarial, and multi-scale learning frameworks in order to overcome these practical difficulties. When the proposed method was applied to malignant lymphoma subtype classifications of 196 cases collected from multiple hospitals, the classification performance was significantly better than the standard CNN or other conventional methods, and the accuracy compared favorably with that of standard pathologists.

FTIR study of the retinal Schiff base and internal water molecules of proteorhodopsin.

Abstract: Proteorhodopsin (PR), an archaeal-type rhodopsin found in marine bacteria, is a light-driven proton pump similar to bacteriorhodopsin (BR). It is known that Asp97, a counterion of the protonated Schiff base, possesses a higher pKa ( approximately 7) compared to that of homologous Asp85 in BR (<3). This suggests that PR has a hydrogen-bonding network different from that of BR. We previously reported that a strongly hydrogen-bonded water molecule is observed only in the alkaline form of PR, where Asp97 is deprotonated (Furutani, Y., Ikeda, D., Shibata, M., and Kandori, H. (2006) Chem. Phys. 324, 705-708). This is probably correlated with the pH-dependent proton pumping activity of PR. In this work, we studied the water-containing hydrogen-bonding network in the Schiff base region of PR by means of Fourier-transform infrared (FTIR) spectroscopy at 77 K. [zeta-15N]Lys-labeling and 18O water were used for assigning the Schiff base N-D and water O-D stretching vibrations in D2O, respectively. The frequency upshift of the N-D stretch in the primary K intermediate is much smaller for PR than for BR, indicating that the Schiff base forms a hydrogen bond after retinal photoisomerization. We then measured FTIR spectra of the mutants of Asp97 (D97N and D97E) and Asp227 (D227N and D227E) to identify the amino acid interacting with the Schiff base in the K state. The PRK minus PR spectra of D97N and D97E were similar to those of the acidic and alkaline forms, respectively, of the wild type implying that the structural changes upon retinal photoisomerization are not influenced by the mutation at Asp97. In contrast, clear spectral differences were observed in D227N and D227E, including vibrational bands of the Schiff base and water molecules. It is concluded that Asp227 plays a crucial role during the photoisomerization process, though Asp97 acts as the primary counterion in the unphotolyzed state of PR.

Synthesis, Structure, and Spectroscopic Properties of [Feiii (tnpa)(OH)(PhCOO)]ClO4 : A Model Complex for an Active Form of Soybean Lipoxygenase-1.

Abstract: The cis configuration between the hydroxo and the carboxylato and the three amino groups of the tetradentate, tripodal ligand tris(6-neopentylamino-2-pyridylmethyl)amine favors the formation of hydrogen bonds which stabilize the hydroxo-Feiii complex 1. Thus, its structure closely resembles that of the active center of Feiii -soybean lipoxygenase-1, which also contains a six-coordinate Feiii atom.