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Nam J.L.,University of Leeds | Ramiro S.,University of Amsterdam | Gaujoux-Viala C.,University of Nimes | Takase K.,University of Leeds | And 8 more authors.
Annals of the Rheumatic Diseases | Year: 2014

Objectives To update the evidence for the efficacy of biological disease-modifying antirheumatic drugs (bDMARD) in patients with rheumatoid arthritis (RA) to inform the European League Against Rheumatism (EULAR) Task Force treatment recommendations. Methods Medline, Embase and Cochrane databases were searched for articles published between January 2009 and February 2013 on infliximab, etanercept, adalimumab, certolizumab-pegol, golimumab, anakinra, abatacept, rituximab, tocilizumab and biosimilar DMARDs (bsDMARDs) in phase 3 development. Abstracts from 2011 to 2012 American College of Rheumatology (ACR) and 2011-2013 EULAR conferences were obtained. Results Fifty-one full papers, and 57 abstracts were identified. The randomised controlled trials (RCT) confirmed the efficacy of bDMARD+conventional synthetic DMARDs (csDMARDs) versus csDMARDs alone (level 1B evidence). There was some additional evidence for the use of bDMARD monotherapy, however bDMARD and MTX combination therapy for all bDMARD classes was more efficacious (1B). Clinical and radiographic responses were high with treat-to-target strategies. Earlier improvement in signs and symptoms were seen with more intensive initial treatment strategies, but outcomes were similar upon addition of bDMARDs in patients with insufficient response to MTX. In general, radiographic progression was lower with bDMARD use, mainly due to initial treatment effects. Although patients may achieve bDMARD- and drug-free remission, maintenance of clinical responses was higher with bDMARD continuation (1B), but bDMARD dose reduction could be applied (1B). There was still no RCT data for bDMARD switching. Conclusions The systematic literature review confirms efficacy of biological DMARDs in RA. It addresses different treatment strategies with the potential for reduction in therapy, particularly with early disease control, and highlights emerging therapies. Source


Omnus D.J.,Hannover Medical School | Omnus D.J.,University of Stockholm | Mehrtens S.,Hannover Medical School | Ritter B.,Hannover Medical School | And 5 more authors.
Journal of Molecular Biology | Year: 2011

Heterogeneous nuclear ribonucleoprotein D-like protein (JKTBP) 1 was implicated in cap-independent translation by binding to the internal ribosome entry site in the 5′ untranslated region (UTR) of NF-κB-repressing factor (NRF). Two different NRF mRNAs have been identified so far, both sharing the common 5′ internal ribosome entry site but having different length of 3′ UTRs. Here, we used a series of DNA and RNA luciferase reporter constructs comprising 5′, 3′ or both NRF UTRs to study the effect of JKTBP1 on translation of NRF mRNA variants. The results indicate that JKTBP1 regulates the level of NRF protein expression by binding to both NRF 5′ and 3′ UTRs. Using successive deletion and point mutations as well as RNA binding studies, we define two distinct JKTBP1 binding elements in NRF 5′ and 3′ UTRs. Furthermore, JKTBP1 requires two distinct RNA binding domains to interact with NRF UTRs and a short C-terminal region for its effect on NRF expression. Together, our study shows that JKTBP1 contributes to NRF protein expression via two disparate mechanisms: mRNA stabilization and cap-independent translation. By binding to 5′ UTR, JKTBP1 increases the internal translation initiation in both NRF mRNA variants, whereas its binding to 3′ UTR elevated primarily the stability of the major NRF mRNA. Thus, JKTBP1 is a key regulatory factor linking two pivotal control mechanisms of NRF gene expression: the cap-independent translation initiation and mRNA stabilization. © 2011 Elsevier Ltd. Source


Shevtsova V.,MRC | Mialdun A.,MRC | Kawamura H.,Tokyo University of Science | Ueno I.,Tokyo University of Science | And 2 more authors.
Fluid Dynamics and Materials Processing | Year: 2011

The experimental results from nine benchmark test cases conducted by five different groups are presented. The goal of this study is to build an experimental database for validation of numerical models in liquid bridge geometry. The need arises as comparison of numerical results with a single experiment can lead to a large discrepancy due to specific experimental conditions. Perfectly conducting rigid walls and, especially, idealized boundary conditions at the free surface employed in numerical studies are not always realized in experiments. The experimental benchmark has emphasized strong sensitivity of the threshold of instability to the liquid bridge shape. A clear distinction should be made between results belonging to the different disturbance patterns, i.e. different wave numbers. The results of benchmark contributors are in a satisfactory agreement when they are associated with the stability branch with an identical wave number. In this case the discrepancy of the results for determination of the critical parameters is about ±15%-18% and they can be used for the validation of numerical models. © 2011 Tech Science Press. Source


Iwai T.,Kanagawa University | Matsui Y.,Kagawa University | Omura S.,Yokohama University | Tohnai I.,Kanagawa University
Journal of Craniofacial Surgery | Year: 2012

Because navigational guidance can localize the operative site 3-dimensionally during maxillofacial surgery and provide precision, reliability, and safety for surgeons, we report Le Fort I osteotomy under navigational guidance for posterior repositioning of the maxilla. Copyright © 2012 Mutaz B. Habal, MD. Source


Recent development of protein crystallography allows us to understand protein function at atomic level. However, protein is always in motion in solution, which is of great importance to the function. Here, we show a novel method using solution X-ray scattering (SXS) and molecular dynamics (MD) simulation to characterize protein dynamics in solution. © 2011 Hie Society of Polymer Science. Source

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