bluuebunny/crossref_metadata_2025_split huggingface dataset:
Understanding Furniture Design Choices Using a 3D Virtual Showroom
Authors: Yoon So–Yeon , Oh Hyunjoo , Cho Ji Young 
Published: April 2010

This study is a Web–based investigation that utilizes virtual reality technology to understand the factors considered for residential furniture purchase and furniture style preference. In residential interior design, furniture has significant financial and symbolic meaning. From a broader perspective, residential furniture is important to the domestic furniture industry as well as to woodworking and textile markets. Despite this importance, little is known about how consumers make residential furniture choices and what designs or styles are preferred. The purpose of this study is to understand the most important factors involved in choosing living room furniture and to identify preferences for furniture style using an online virtual showroom application. In this survey, 301 college participants responded to questions regarding priorities and style preferences when purchasing living room furniture. The participants evaluated 117 living room furniture items representing three style categories: traditional, modern, and casual. The survey results demonstrated significant differences between males and females in their priority considerations, style preferences for furniture, and the number of possibilities they try before making final choices. This empirical study is an effort to provide important information on consumer characteristics and their furniture choices for interior practitioners and furniture industry personnel in a three–dimensional virtual furniture showroom constructed for the study.
Comparison of thrice‐daily lispro 50/50 vs thrice‐daily lispro in combination with sulfonylurea as initial insulin therapy for type 2 diabetes
Authors: Yamashiro Keiko , Ikeda Fuki , Fujitani Yoshio , Watada Hirotaka , Kawamori Ryuzo , Hirose Takahisa 
Published: April 2010

AbstractAims/Introduction:  Basal–bolus intensive insulin therapy has been believed to achieve best the glycemic control, but is also complicated as a result of the number of injections required and the type of insulin. This study compared the effect of thrice‐daily lispro 50/50 (prandial premixed therapy [PPT]) with thrice daily lispro given in combination with sulfonylureas (prandial bolus therapy with sulfonylurea [PBTS]) as initial insulin therapy for type 2 diabetes.Materials and Methods:  This 24‐week, observational, parallel trial comprised a 12‐week screening period and a 24‐week intervention period for 31 diabetes patients who were poorly controlled with submaximal sulfonylurea. At the start of the intervention period, we commenced thrice‐daily insulin injections and divided the 31 patients into either lispro 50/50 with discontinuation of sulfonylurea (PPT, n = 15) or lispro added to sulfonylurea (PBTS, n = 16). The same dose‐adjustment algorithm was used for analyzing both groups; HbA1c, plasma glucose, insulin daily dose, bodyweight and number of hypoglycemic episodes were evaluated.Results:  At the end of the study, HbA1c was significantly improved in both groups (P < 0.00001), but no difference was apparent between the groups. The daily doses of PPT were more than those of PBTS, albeit the difference was statistically insignificant (P = 0.051). There were significantly fewer hypoglycemic episodes encountered with PPT than with PBTS.Conclusions:  Thrice‐daily injections of lispro 50/50 provide an effective and safe regimen as initial insulin therapy for type 2 diabetes. (J Diabetes Invest, doi: 10.1111/j.2040‐1124.2010.00025.x, 2010)
Generation and Characterization of Chimeric Antibodies against NS3, NS4, NS5, and Core Antigens of Hepatitis C Virus
Authors: Tu Bailin , Ziemann Robert N. , Tieman Bryan C. , Hawksworth David J. , Tyner Joan , Scheffel James , Pinkus Mary S. , Brophy Susan E. , Werneke Jeffrey M. , Gutierrez Robin , White Michael 
Published: April 2010

ABSTRACT

Mouse-human chimeric antibodies (cAbs) against hepatitis C virus (HCV) core, NS3 (nonstructural), NS4, and NS5 antigens were developed as quality control (QC) reagents to replace the use of human sera/plasma for Abbott HCV immunoassays. The cAb retains the mouse monoclonal antibody (MAb) specificity and affinity but still reacts in the existing HCV assay format, which measures human anti-HCV immunoglobulin. Mouse heavy-chain (V
H
) and light-chain (V
L
) variable regions of anti-HCV core, NS3, NS4, and NS5 antigens were PCR amplified from hybridoma lines and then cloned with human IgG1 heavy-chain (C
H
) and light-chain (C
L
) constant regions, respectively. A single mammalian expression plasmid containing both heavy-chain and light-chain immunoglobulin genes was constructed and transfected into dihydrofolate reductase (DHFR)-deficient Chinese hamster ovary (CHO) cells. The transfected CHO cells were selected using hypoxanthine- and thymidine-free medium and screened by an enzyme immunoassay (EIA). The clone secreting the highest level of antibody was isolated from the CHO transfectants and further subcloned. Each cAb-expressing CHO cell line was weaned into serum-free medium, and the cAb was purified by protein A affinity chromatography. The levels of cAb production for the various CHO cell lines varied from 10 to 20 mg/liter. Purified anti-HCV cAbs were tested with Abbott HCV immunoassays and showed reactivity. Moreover, yeast surface display combined with alanine-scanning mutagenesis was used to map the epitope at the individual amino acid level. Our results suggest that these HCV cAbs are ideal controls, calibrators, and/or QC reagents for HCV assay standardization.
Implantable Cardiac Defibrillator Pocket Infection Due to a Previously Undescribed
Cupriavidus
Species
Authors: Christensen Joshua B. , Vitko Nicholas P. , Voskuil Martin I. , Castillo-Mancilla Jose R. 
Published: April 2010

ABSTRACT

The genus
Cupriavidus
consists of Gram-negative, nonfermenting bacteria most of which are environmental organisms, though some species have been associated with human disease. We report the recovery and identification of an isolate that represents a previously undescribed species of
Cupriavidus
from an implantable cardiac defibrillator pocket infection.
Role of Interferon Antagonist Activity of Rabies Virus Phosphoprotein in Viral Pathogenicity
Authors: Ito Naoto , Moseley Gregory W. , Blondel Danielle , Shimizu Kenta , Rowe Caitlin L. , Ito Yuki , Masatani Tatsunori , Nakagawa Keisuke , Jans David A. , Sugiyama Makoto 
Published: April 2010

ABSTRACT
The fixed rabies virus (RV) strain Nishigahara kills adult mice after intracerebral inoculation, whereas the chicken embryo fibroblast cell-adapted strain Ni-CE causes nonlethal infection in adult mice. We previously reported that the chimeric CE(NiP) strain, which has the phosphoprotein (P protein) gene from the Nishigahara strain in the genetic background of the Ni-CE strain, causes lethal infection in adult mice, indicating that the P gene is responsible for the different pathogenicities of the Nishigahara and Ni-CE strains. Previous studies demonstrated that RV P protein binds to the interferon (IFN)-activated transcription factor STAT1 and blocks IFN signaling by preventing its translocation to the nucleus. In this study, we examine the molecular mechanism by which RV P protein determines viral pathogenicity by comparing the IFN antagonist activities of the Nishigahara and Ni-CE P proteins. The results, obtained from both RV-infected cells and cells transfected to express P protein only, show that Ni-CE P protein is significantly impaired for its capacity to block IFN-activated STAT1 nuclear translocation and, consequently, inhibits IFN signaling less efficiently than Nishigahara P protein. Further, it was demonstrated that a defect in the nuclear export of Ni-CE P protein correlates with a defect in its ability to cause the mislocalization of STAT1. These data provide the first evidence that the capacity of the RV P protein to inhibit STAT1 nuclear translocation and IFN signaling correlates with the viral pathogenicity.
Mechanism of Initiation Site Selection Promoted by the Human Rhinovirus 2 Internal Ribosome Entry Site
Authors: Kaminski Ann , Pöyry Tuija A. A. , Skene Peter J. , Jackson Richard J. 
Published: April 2010

ABSTRACT
Translation initiation site usage on the human rhinovirus 2 internal ribosome entry site (IRES) has been examined in a mixed reticulocyte lysate/HeLa cell extract system. There are two relevant AUG triplets, both in a base-paired hairpin structure (domain VI), with one on the 5′ side at nucleotide (nt) 576, base paired with the other at nt 611, which is the initiation site for polyprotein synthesis. A single residue was inserted in the apical loop to put AUG-576 in frame with AUG-611, and in addition another in-frame AUG was introduced at nt 593. When most of the IRES was deleted to generate a monocistronic mRNA, the use of these AUGs conformed to the scanning ribosome model: improving the AUG-576 context increased initiation at this site and decreased initiation at downstream sites, whereas the converse was seen when AUG-576 was mutated to GUA; and AUG-593, when present, took complete precedence over AUG-611. Under IRES-dependent conditions, by contrast, much less initiation occurred at AUG-576 than in a monocistronic mRNA with the same AUG-576 context, mutation of AUG-576 decreased initiation at downstream sites by ∼70%, and introduction of AUG-593 did not completely abrogate initiation at AUG-611, unless the apical base pairing in domain VI was destroyed by point mutations. These results indicate that ribosomes first bind at the AUG-576 site, but instead of initiating there, most of them are transferred to AUG-611, the majority by strictly linear scanning and a substantial minority by direct transfer, which is possibly facilitated by the occasional persistence of base pairing in the apical part of the domain VI stem.
The Virion Host Shutoff Endonuclease (UL41) of Herpes Simplex Virus Interacts with the Cellular Cap-Binding Complex eIF4F
Authors: Page Heidi G. , Read G. Sullivan 
Published: April 2010

ABSTRACT
The herpes simplex virus Vhs endonuclease degrades host and viral mRNAs. Isolated Vhs cuts any RNA at many sites. Yet, within cells, it targets mRNAs and cuts at preferred sites, including regions of translation initiation. Previous studies have shown that Vhs binds the translation factors eIF4A and eIF4H. Here, we show that Vhs binds the cap-binding complex eIF4F. Association with eIF4F correlated with the ability of Vhs to bind eIF4A but not eIF4H. All Vhs proteins that degrade mRNAs associated with eIF4F. However, simply tethering an active endonuclease to eIF4F is not sufficient to degrade mRNAs. Binding to eIF4H may also be required.
Suppression of a Morphogenic Mutant in Rous Sarcoma Virus Capsid Protein by a Second-Site Mutation: a Cryoelectron Tomography Study
Authors: Butan Carmen , Lokhandwala Parvez M. , Purdy John G. , Cardone Giovanni , Craven Rebecca C. , Steven Alasdair C. 
Published: April 2010

ABSTRACT

Retrovirus assembly is driven by polymerization of the Gag polyprotein as nascent virions bud from host cells. Gag is then processed proteolytically, releasing the capsid protein (CA) to assemble
de novo
inside maturing virions. CA has N-terminal and C-terminal domains (NTDs and CTDs, respectively) whose folds are conserved, although their sequences are divergent except in the 20-residue major homology region (MHR) in the CTD. The MHR is thought to play an important role in assembly, and some mutations affecting it, including the F167Y substitution, are lethal. A temperature-sensitive second-site suppressor mutation in the NTD, A38V, restores infectivity. We have used cryoelectron tomography to investigate the morphotypes of this double mutant. Virions produced at the nonpermissive temperature do not assemble capsids, although Gag is processed normally; moreover, they are more variable in size than the wild type and have fewer glycoprotein spikes. At the permissive temperature, virions are similar in size and spike content as in the wild type and capsid assembly is restored, albeit with altered polymorphisms. The mutation F167Y-A38V (referred to as FY/AV in this paper) produces fewer tubular capsids than wild type and more irregular polyhedra, which tend to be larger than in the wild type, containing ∼30% more CA subunits. It follows that FY/AV CA assembles more efficiently
in situ
than in the wild type and has a lower critical concentration, reflecting altered nucleation properties. However, its infectivity is lower than that of the wild type, due to a 4-fold-lower budding efficiency. We conclude that the wild-type CA protein sequence represents an evolutionary compromise between competing requirements for optimization of Gag assembly (of the immature virion) and CA assembly (in the maturing virion).
Glycosylation at 158N of the Hemagglutinin Protein and Receptor Binding Specificity Synergistically Affect the Antigenicity and Immunogenicity of a Live Attenuated H5N1 A/Vietnam/1203/2004 Vaccine Virus in Ferrets
Authors: Wang Weijia , Lu Bin , Zhou Helen , Suguitan Amorsolo L. , Cheng Xing , Subbarao Kanta , Kemble George , Jin Hong 
Published: April 2010

ABSTRACT

A live attenuated influenza A/Vietnam/1203/2004 (H5N1) vaccine virus (VN04
ca
) has receptor binding specificity to α2,3-linked sialosides (α2,3SAL), and a single dose induces a minimal serum antibody response in mice and ferrets. In contrast, A/Hong Kong/213/2003 (H5N1) vaccine virus (HK03
ca
) binds to both α2,6SAL and α2,3SAL and generates a stronger serum antibody response in animals. Among the 9 amino acids that differed between the two H5 HA1 proteins, several HK03-specific residues enabled the VN04
ca
virus to bind to both α2,3SAL and α2,6SAL receptors, but only the removal of the 158N glycosylation, together with an S227N change, resulted in more-efficient viral replication in the upper respiratory tract of ferrets and an increased serum antibody response. However, the antibody response was HK03 strain specific and did not significantly cross-neutralize VN04 virus. A second approach was taken to adapt the H5N1 VN04
ca
virus in MDCK cells to select HA variants with larger plaque morphology. Although a number of large-plaque-size HA variants with amino acid changes in the HA receptor binding region were identified, none of these mutations affected virus receptor binding preference and immunogenicity. In addition, the known receptor binding site changes, Q226L and G228S, were introduced into the HA protein of the VN04
ca
virus. Only in conjunction with the removal of the 158N glycosylation did the virus replicate efficiently in the upper respiratory tract of ferrets and became more immunogenic, yet the response was also HK03 specific. Thus, the mask of the antigenic epitopes by 158N glycosylation at the HA globular head and its α2,3SAL binding preference of VN04
ca
virus affect virus antigenicity and replication in the host, resulting in a lower antibody response.
Regulation of Hepatitis C Virus Translation and Infectious Virus Production by the MicroRNA miR-122
Authors: Jangra Rohit K. , Yi MinKyung , Lemon Stanley M. 
Published: April 2010

ABSTRACT
miR-122 is a liver-specific microRNA that positively regulates hepatitis C virus (HCV) RNA abundance and is essential for production of infectious HCV. Using a genetic approach, we show that its ability to enhance yields of infectious virus is dependent upon two miR-122-binding sites near the 5′ end of the HCV genome, S1 and S2. Viral RNA with base substitutions in both S1 and S2 failed to produce infectious virus in transfected cells, while virus production was rescued to near-wild-type levels in cells supplemented with a complementary miR-122 mutant. A comparison of mutants with substitutions in only one site revealed S1 to be dominant, as an S2 but not S1 mutant produced high virus yields in cells supplemented with wild-type miR-122. Translation of HCV RNA was reduced over 50% by mutations in either S1 or S2 and was partially rescued by transfection of the complementary miR-122 mutant. Unlike the case for virus replication, however, both sites function equally in regulating translation. We conclude that miR-122 promotes replication by binding directly to both sites in the genomic RNA and, at least in part, by stimulating internal ribosome entry site (IRES)-mediated translation. However, a comparison of the replication capacities of the double-binding-site mutant and an IRES mutant with a quantitatively equivalent defect in translation suggests that the decrement in translation associated with loss of miR-122 binding is insufficient to explain the profound defect in virus production by the double mutant. miR-122 is thus likely to act at an additional step in the virus life cycle.
Role for Complement in the Development of Seizures following Acute Viral Infection
Authors: Libbey Jane E. , Kirkman Nikki J. , Wilcox Karen S. , White H. Steve , Fujinami Robert S. 
Published: April 2010

ABSTRACTComplement, part of the innate immune system, acts to remove pathogens and unwanted host material. Complement is known to function in all tissues, including the central nervous system (CNS). In this study, we demonstrated the importance of the complement system within the CNS in the development of behavioral seizures following Theiler's murine encephalomyelitis virus (TMEV) infection. C57BL/6 mice, deficient in complement component C3, developed significantly fewer behavioral seizures following TMEV infection, whereas mice depleted of complement component C3 in the periphery through treatment with cobra venom factor had a seizure rate comparable to that of control mice. These studies indicate that C3 participates in the induction of acute seizures during viral encephalitis.
Full-Length Hepatitis B Virus Core Protein Packages Viral and Heterologous RNA with Similarly High Levels of Cooperativity
Authors: Porterfield J. Zachary , Dhason Mary Savari , Loeb Daniel D. , Nassal Michael , Stray Stephen J. , Zlotnick Adam 
Published: April 2010

ABSTRACT

A critical feature of a viral life cycle is the ability to selectively package the viral genome.
In vivo
, phosphorylated hepatitis B virus (HBV) core protein specifically encapsidates a complex of pregenomic RNA (pgRNA) and viral polymerase; it has been suggested that packaging is specific for the complex. Here, we test the hypothesis that core protein has intrinsic specificity for pgRNA, independent of the polymerase. For these studies, we also evaluated the effect of core protein phosphorylation on assembly and RNA binding, using phosphorylated core protein and a phosphorylation mimic in which S155, S162, and S170 were mutated to glutamic acid. We have developed an
in vitro
system where capsids are disassembled and assembly-active core protein dimer is purified. With this protein, we have reassembled empty capsids and RNA-filled capsids. We found that core protein dimer bound and encapsidated both the HBV pregenomic RNA and heterologous RNA with high levels of cooperativity, irrespective of phosphorylation. In direct competition assays, no specificity for pregenomic RNA was observed. This suggests that another factor, such as the viral polymerase, is required for specific packaging. These results also beg the question of what prevents HBV core protein from assembling on nonviral RNA, preserving the protein for virus production.
β1Integrin Expression Increases Susceptibility of Memory B Cells to Epstein-Barr Virus Infection
Authors: Dorner Marcus , Zucol Franziska , Alessi Davide , Haerle Stephan K. , Bossart Walter , Weber Markus , Byland Rahel , Bernasconi Michele , Berger Christoph , Tugizov Sharof , Speck Roberto F. , Nadal David 
Published: April 2010

ABSTRACTEpstein-Barr virus (EBV) uses nasal mucosa-associated lymphoid tissue (NALT) as a portal of entry to establish life-long persistence in memory B cells. We previously showed that naïve and memory B cells from NALT are equally susceptible to EBV infection. Here we show that memory B cells from NALT are significantly more susceptible to EBV infection than those from remote lymphatic organs. We identify β1integrin, which is expressed the most by naïve B cells of distinct lymphoid origin and by memory B cells from NALT, as a mediator of increased susceptibility to infection by EBV. Furthermore, we show that BMRF-2-β1integrin interaction and the downstream signal transduction pathway are critical for postbinding events. An increase of β1integrin expression in peripheral blood memory B cells provoked by CD40 stimulation plus B-cell receptor cross-linking increased the susceptibility of non-NALT memory B cells to EBV infection. Thus, EBV seems to utilize the increased activation status of memory B cells residing in the NALT to establish and ensure persistence.
Anticoagulant therapy in critical organ ischaemia/reperfusion injury
Authors: Cate Hugo ten , Spronk Henri M. H. , Loubele Sarah T. B. G. 
Published: April 2010

SummaryIschaemia/reperfusion (I/R) injury is central to a number of pathologies including myocardial infarction and stroke. Several cellular processes are involved in the progress of I/R injury, involving complex interactions between coagulation and inflammatory or apoptotic processes. Besides for their anti-coagulant function, anticoagulant proteins such as activated protein C (APC), active site inhibited factor VIIa (ASIS), tissue factor pathway inhibitor (TFPI), and antithrombin (AT) are also known for their anti-inflammatory or cell protective effects. This review gives an overview of the application of these anti-coagulants in several animal models of I/R injury in critical organs and describes the effects of these proteins on cellular processes including inflammation and apoptosis. The future testing of mutant forms of some of these inhibitors including APC in a clinical setting should be actively explored.
Factor VIIa-antithrombin complexes in patients with arterial and venous thrombosis
Authors: Spiezia Luca , Rossetto Valeria , Campello Elena , Gavasso Sabrina , Woodhams Barry , Tormene Daniela , Simioni Paolo 
Published: April 2010

SummaryAntithrombin (AT), in the presence of heparin, is able to inhibit the catalytic activity of factor VIIa bound to tissue factor (TF) on cell surfaces. The clinical meaning of FVIIa-AT complexes plasma levels is unknown. It was the objective of this study to evaluate FVIIa-AT complexes in subjects with thrombosis. Factor VIIa-AT complexes plasma levels in 154 patients consecutively referred to our Department with arterial or venous thrombosis and in a group of 154 healthy subjects, were measured. Moreover, FVIIa-AT complexes were determined in: i) n = 53 subjects belonging to 10 families with inherited factor VII deficiency; ii) n = 58 subjects belonging to seven families with AT deficiency; iii) n = 49 patients undergoing oral anticoagulant therapy (OAT). Factor VIIaAT levels were determined by a specific ELISA kit (R&D, Diagnostica Stago, Gennevilliers, France). Factor VIIa-AT complexes mean plasma levels were lower in patients with either acute arterial (136 ± 40 pM) or venous (142 ± 53 pM) thrombosis than subjects with previous thrombosis (arterial 164 ± 33 pM and venous 172 ± 61 pM, respectively) and than healthy controls (156 ± 63 pM). Differences between acute and previous thrombosis, were statistically significant (p < 0.05). Subjects with inherited and acquired (under OAT) factor VII deficiency had statistically significant lower FVIIa-AT complexes plasma levels (80 ± 23 pM and 55 ± 22 pM, respectively) than controls (150 ± 51 pM, p < 0.0001 and 156 ± 63 pM, p < 0.00001, respectively). Factor VIIa-AT complexes are positively correlated with plasma factor VII/VIIa levels. Further investigations are needed to verify the possible role of higher FVIIa-AT complex plasma levels in predicting hypercoagulable states and thrombosis.