Effect of Boronizing on Operating Stability of Steel AISI 304L under Erosion Impact of Hard Particles

Metal Science and Heat Treatment - The effect of solid boronizing at 950°C for 2 and 4 h on the phase composition, microstructure, hardness and abrasive wear of steel AISI 304L is studied...     

On keys' meanings and modes: the impact of different key solutions on children's efficiency using a mobile phone

The present study investigates the impact of different key solutions of mobile phones on users' effectiveness and efficiency using the devices. In the first experiment, 36 children (9 - 14 years) and in the second experiment 45 young adults (19 - 33 years) completed four common phone tasks twice consecutively on three simulated phones that had identical menus, but different key solutions. An approach was undertaken to quantify the complexity of keys in three models, incorporating different factors contributing to the keys' complexity (number of key options, number of modes and number of modes with a semantically dissimilar meaning), in order to predict users' performance decrements. As a further main factor, the degree of the users' locus of control (LOC) was measured and interactions with performance outcomes were studied. As dependent measures, the number of inefficient keystrokes, the number of tasks solved and the processing time were determined. Results showed a significant effect of control key solutions on users' efficiency and effectiveness for both children and young adults. Moreover, children's LOC values significantly interacted with performance: children with low LOC values showed the lowest performance and no learnability, especially when using keys with a high complexity. From the three factors contributing to the complexity of keys, keys exerting different functions with semantically inconsistent meanings had the worst effect on performance. It is concluded that in mobile user interface design keys with semantically inconsistent meanings should be generally avoided.     

Fabrication of Schottky barrier MOSFETs using self-assembly CoSi2 nanopatterning and spacer gate technologies

A self-assembly patterning method for generation of epitaxial CoSi₂ nanostructures was used to fabricate 50 nm channel-length MOSFETs. The transistors have either a symmetric structure with Schottky source and drain or an asymmetric structure with n⁺-source and Schottky drain. The patterning technique is based on anisotropic diffusion of Co/Si atoms in a strain field during rapid thermal oxidation. The strain field is generated along the edges of a mask consisting of 20 nm SiO₂ and 300 nm Si₃N₄. During rapid thermal oxinitridation (RTON) of the masked silicide structure, a well-defined separation of the silicide layer forms along the edge of the mask. These highly uniform gaps define the channel region of the fabricated device. The separated silicide layers act as metal source and drain. A poly-Si spacer was used as the gate contact. The asymmetric transistor was fabricated by ion implantation into the unprotected CoSi₂ layer and a subsequent out-diffusion process to form the n⁺-source. I–V characteristics of both the symmetric and asymmetric transistor structures have been investigated.     

Identification of glycoprotein 330 as an endocytic receptor for apolipoprotein J/clusterin

Glycoprotein 330 (gp330) is a member of a family of endocytic receptors related to the low density lipoprotein receptor. gp330 has previously been shown to bind a number of ligands in common with its family member, the low density lipoprotein receptor-related protein (LRP). To identify ligands specific for gp330 and relevant to its localization on epithelia such as in the mammary gland, gp330-Sepharose affinity chromatography was performed. As a result, a 70-kDa protein was selected from human milk and identified by protein sequencing to be apolipoprotein J/clusterin (apoJ). Solid-phase binding assays confirmed that gp330 bound to apoJ with high affinity (Kd = 14.2 nM). Similarly, gp330 bound to apoJ transferred to nitrocellulose after SDS-polyacrylamide gel electrophoresis. LRP, however, showed no binding to apoJ in either type of assay. The binding of gp330 to apoJ could be competitively inhibited with excess apoJ as well as with the gp330 ligands apolipoprotein E, lipoprotein lipase, and the receptor-associated protein, a 39-kDa protein that acts to antagonize binding of all known ligands for gp330 and LRP. Several cultured cell lines that express gp330 and ones that do not express the receptor were examined for their ability to bind and internalize 125I-apoJ. Only cells that expressed gp330 endocytosed and degraded radiolabeled apoJ. Furthermore, F9 cells treated with retinoic acid and dibutyryl cyclic AMP to increase expression levels of gp330 displayed an increased capacity to internalize and degrade apoJ. Cellular internalization and degradation of radiolabeled apoJ could be inhibited with unlabeled apoJ, receptor-associated protein, and gp330 antibodies. The results indicate that gp330 but not LRP can bind to apoJ in vitro and that gp330 expressed by cells can mediate apoJ endocytosis leading to lysosomal degradation.     

Management, Market, and Financial Factors Separating Winners and Losers in E-Business

There have been many successful e‐businesses as well as many failed e‐businesses. The methods and practices that were evident in the development of both surviving e‐businesses and failed ones have much to teach us. Why did some e‐businesses fail while others survived? At present few guidelines exist to assist e‐business owners and managers wanting to succeed in their Internet‐based ventures. This study empirically investigated factors that may lead to e‐business success or failure; these were categorized as management, market, and financial factors. The results of a survey were combined with one‐on‐one interviews of venture capitalists who funded successful and failed e‐businesses. The results indicate that certain factors deemed applicable to an e‐business may have contributed to the firm’s eventual success or failure.     

Mutational analysis of the three cysteines and active-site aspartic acid 103 of ketosteroid isomerase from Pseudomonas putida biotype B

In order to clarify the roles of three cysteines in ketosteroid isomerase (KSI) from Pseudomonas putida biotype B, each of the cysteine residues has been changed to a serine residue (C69S, C81S, and C97S) by site-directed mutagenesis. All cysteine mutations caused only a slight decrease in the k(cat) value, with no significant change of Km for the substrate. Even modification of the sulfhydryl group with 5,5'-dithiobis(2-nitrobenzoic acid) has almost no effect on enzyme activity. These results demonstrate that none of the cysteines in the KSI from P. putida is critical for catalytic activity, contrary to the previous identification of a cysteine in an active-site-directed photoinactivation study of KSI. Based on the three-dimensional structures of KSIs with and without dienolate intermediate analog equilenin, as determined by X-ray crystallography at high resolution, Asp-103 was found to be located within the range of the hydrogen bond to the equilenin. To assess the role of Asp-103 in catalysis, Asp-103 has been replaced with either asparagine (D103N) or alanine (D103A) by site-directed mutagenesis. For D103A mutant KSI there was a significant decrease in the k(cat) value: the k(cat) of the mutant was 85-fold lower than that of the wild-type enzyme; however, for the D103N mutant, which retained some hydrogen bonding capability, there was a minor decrease in the k(cat) value. These findings support the idea that aspartic acid 103 in the active site is an essential catalytic residue involved in catalysis by hydrogen bonding to the dienolate intermediate.     

Association of INAD with NORPA is essential for controlled activation and deactivation of Drosophila phototransduction in vivo

Visual transduction in Drosophila is a G protein-coupled phospholipase C-mediated process that leads to depolarization via activation of the transient receptor potential (TRP) calcium channel. Inactivation-no-afterpotential D (INAD) is an adaptor protein containing PDZ domains known to interact with TRP. Immunoprecipitation studies indicate that INAD also binds to eye-specific protein kinase C and the phospholipase C, no-receptor-potential A (NORPA). By overlay assay and site-directed mutagenesis we have defined the essential elements of the NORPA-INAD association and identified three critical residues in the C-terminal tail of NORPA that are required for the interaction. These residues, Phe-Cys-Ala, constitute a novel binding motif distinct from the sequences recognized by the PDZ domain in INAD. To evaluate the functional significance of the INAD-NORPA association in vivo, we generated transgenic flies expressing a modified NORPA, NORPAC1094S, that lacks the INAD interaction. The transgenic animals display a unique electroretinogram phenotype characterized by slow activation and prolonged deactivation. Double mutant analysis suggests a possible inaccessibility of eye-specific protein kinase C to NORPAC1094S, undermining the observed defective deactivation, and that delayed activation may similarly result from NORPAC1094S being unable to localize in close proximity to the TRP channel. We conclude that INAD acts as a scaffold protein that facilitates NORPA-TRP interactions required for gating of the TRP channel in photoreceptor cells.