National Center for Biotechnology

Madrid, Spain

National Center for Biotechnology

Madrid, Spain
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— The Global Diabetic Footwear Market was valued at US$ 5331.8 million in 2016, according to a new report published by Coherent Market Insights. Diabetes is a prolonged medical condition that is caused due to the lack or lower levels of insulin in the body. A person suffering from this condition is susceptible to conditions such as sores and other external injuries, predominantly in feet. Diabetic footwear has evolved as a medicinal revolution that helps avoid the feet of a person suffering from diabetes prone to such injuries. Therefore, using the suitable diabetic footwear helps diabetic patients with significant result with respect to prevention and treatment of the condition. Diabetes can result in permanent blindness and can result in a stroke and amputation of the legs. According to WHO, an estimated 1.6 million deaths were directly caused by diabetes in 2015. Diabetes can be classified as Type 1, Type 2, and gestational diabetes. Though Type 2 diabetes was diagnosed only in adults, recently it is also being found in children. To know the latest trends and insights prevalent in this market, click the link below: https://www.coherentmarketinsights.com/market-insight/diabetic-footwear-market-744 Key Trends and Analysis of the Diabetic Footwear Market: Men dominated the end user segment in 2016, according to the stats provided by Coherent Market Insights. The reason for the same is the prevalence of diabetes among men as compared to women. According to International Diabetes Federation (IDF), there were about 15.6 Mn more men than women with diabetes (215.2 million men vs 199.5 million women) in 2015. According to WHO, the prevalence of diabetes among adults has risen from 4.7% in 1980 to 8.5% in 2014 globally. According to a report published by the National Health Service, men are prone to diabetes twice as compared to females. Asia Pacific dominated the market in 2016 and the trend is expected to remain the same during 2017-2025. This is due to the presence of a large population in China and India suffering from diabetes. WHO states that Type 2 diabetes is up to six times more prevalent in people of South Asian descent and up to three times more common among those of African and African-Caribbean origin. According to a study published by National Center for Biotechnology Information, around 79.4 million deaths are expected due to diabetes by 2025 in India alone. China is expected to account for around 42.3 million deaths due to diabetes during the forecast period. The reason behind such huge rates is genetic factors coupled with environmental influences such as obesity — associated with increasing disposable incomes, steady urban migration, and lifestyle changes. Rising spread of awareness regarding the prevention and cure of diabetes by various government bodies is expected to drive the growth of diabetic footwear market in the Asia Pacific region. According to National Center for Biotechnology, between 5% and 10% of India’s health budget is spent on the prevention and treatment of diabetes every year. The Europe market for diabetic footwear is expected to grow at a CAGR of 7.43% during the forecast period. The market was valued at US$ 4 million in 2016. Awareness among the population has resulted in an increasing demand for diabetic footwear in the region. According to WHO, there are about 60 Mn people with diabetes in this region, out of which, 10.3% are men and 9.6% are women aged 25 years and above. Main causes of diabetics in this region are obesity, unhealthy diet, and reduced physical activity. Podartis S.r.l., Aetrex Worldwide Inc., Orthofeet Inc., Etonic Shoes, Drew Shoe, Dr. Comfort, DARCO International, Duna S.r.l, and Hong Kong Grace Shoes among others are a few key players operating in the global diabetic footwear market. There are various organic and inorganic growth strategies, which are being followed by the leading players in the market. For instance, to retain their market share globally, Podartis S.r.l is intensifying its portfolio by introducing innovative products, Aetrex Worldwide, Inc. has increased its production capacity, while Orthofeet Inc. is focusing on revolutionizing its products via product development and increased R&D, and DARCO International Inc. is planning on entering untapped markets in the Asia Pacific. Coherent Market Insights is a prominent market research and consulting firm offering action-ready syndicated research reports, custom market analysis, consulting services, and competitive analysis through various recommendations related to emerging market trends, technologies, and potential absolute dollar opportunity. For more information, please visit https://www.coherentmarketinsights.com/press-release/global-diabetic-footwear-market-to-surpass-us-102-billion-by-2025-buoyed-by-increasing-diabetes-cases-323


de Castro I.F.,CSIC - National Center for Biotechnology | Zamora P.F.,Vanderbilt University | Ooms L.,Vanderbilt University | Fernandez J.J.,National Center for Biotechnology | And 4 more authors.
mBio | Year: 2014

Most viruses that replicate in the cytoplasm of host cells form neo-organelles that serve as sites of viral genome replication and particle assembly. These highly specialized structures concentrate viral replication proteins and nucleic acids, prevent the activation of cell-intrinsic defenses, and coordinate the release of progeny particles. Despite the importance of inclusion complexes in viral replication, there are key gaps in the knowledge of how these organelles form and mediate their functions. Reoviruses are nonenveloped, double-stranded RNA (dsRNA) viruses that serve as tractable experimental models for studies of dsRNA virus replication and pathogenesis. Following reovirus entry into cells, replication occurs in large cytoplasmic structures termed inclusions that fill with progeny virions. Reovirus inclusions are nucleated by viral nonstructural proteins, which in turn recruit viral structural proteins for genome replication and particle assembly. Components of reovirus inclusions are poorly understood, but these structures are generally thought to be devoid of membranes. We used transmission electron microscopy and three-dimensional image reconstructions to visualize reovirus inclusions in infected cells. These studies revealed that reovirus inclusions form within a membranous network. Viral inclusions contain filled and empty viral particles and microtubules and appose mitochondria and rough endoplasmic reticulum (RER). Immunofluorescence confocal microscopy analysis demonstrated that markers of the ER and ER-Golgi intermediate compartment (ERGIC) codistribute with inclusions during infection, as does dsRNA. dsRNA colocalizes with the viral protein σNS and an ERGIC marker inside inclusions. These findings suggest that cell membranes within reovirus inclusions form a scaffold to coordinate viral replication and assembly. © 2014 Fernández de Castro et al.


Tuleuova N.,University of California at Davis | Tuleuova N.,National Center for Biotechnology | Revzin A.,University of California at Davis
Cellular and Molecular Bioengineering | Year: 2010

Aptamer beacons are DNA or RNA probes that bind proteins or small molecules of interest and emit signal directly upon interaction with the target analyte. This paper describes micropatterning of aptamer beacons for detection of IFN-γ-an important inflammatory cytokine. The beacon consisted of a fluorophore-labeled aptamer strand hybridized with a shorter, quencher-carrying complementary strand. Cytokine molecules were expected to displace quenching strands of the beacon, disrupting FRET effect and resulting in fluorescence signal. The glass substrate was first micropatterned with poly(ethylene glycol) (PEG) hydrogel microwells (35 μm diameter individual wells) so as to define sites for attachment of beacon molecules. PEG microwell arrays were then incubated with avidin followed by biotin-aptamerfluorophore constructs. Subsequent incubation with quencher-carrying complementary strands resulted in formation of DNA duplex and caused quenching of fluorescence due to FRET effect. When exposed to IFN-γ, microwells changed fluorescence from low (quencher hybridized with fluorophore-carrying strand) to high (quenching strand displaced by cytokine molecules). The fluorescence signal was confined to microwells, was changing in real-time and was dependent on the concentration of IFN-γ. In the future, we plan to co-localize aptamer beacons and cells on micropatterned surfaces in order to monitor in real-time cytokine secretion from immune cells in microwells. © 2010 The Author(s).


Liu Y.,University of California at Davis | Tuleouva N.,University of California at Davis | Tuleouva N.,National Center for Biotechnology | Ramanculov E.,National Center for Biotechnology | Revzin A.,University of California at Davis
Analytical Chemistry | Year: 2010

In this paper, we describe the development of an electrochemical DNA aptamer-based biosensor for detection of interferon (IFN)-γ. A DNA hairpin containing IFN-γ-binding aptamer was thiolated, conjugated with methylene blue (MB) redox tag, and immobilized on a gold electrode by self-assembly. Binding of IFN-γ caused the aptamer hairpin to unfold, pushing MB redox molecules away from the electrode and decreasing electron-transfer efficiency. The change in redox current was quantified using square wave voltammetry (SWV) and was found to be highly sensitive to IFN-γ concentration. The limit of detection for optimized biosensor was 0.06 nM with linear response extending to 10 nM. This aptasensor was specific to IFN-γ in the presence of overabundant serum proteins. Importantly, the same aptasensor could be regenerated by disrupting aptamer-IFN-γ complex in urea buffer and reused multiple times. Unlike standard sandwich immunoassays, the aptasensor described here allowed one to detect IFN-γ binding directly without the need for multiple washing steps and reagents. An electrochemical biosensor for simple and sensitive detection of IFN-γ demonstrated in this paper will have future applications in immunology, cancer research, and infectious disease monitoring. © 2010 American Chemical Society.


Pazos F.,Computational Systems Biology Group | Pietrosemoli N.,Computational Systems Biology Group | Garcia-Martin J.A.,National Center for Biotechnology | Garcia-Martin J.A.,Boston College | Solano R.,National Center for Biotechnology
Frontiers in Plant Science | Year: 2013

To some extent contradicting the classical paradigm of the relationship between protein 3D structure and function, now it is clear that large portions of the proteomes, especially in higher organisms, lack a fixed structure and still perform very important functions. Proteins completely or partially unstructured in their native (functional) form are involved in key cellular processes underlain by complex networks of protein interactions. The intrinsic conformational flexibility of these disordered proteins allows them to bind multiple partners in transient interactions of high specificity and low affinity. In concordance, in plants this type of proteins has been found in processes requiring these complex and versatile interaction networks. These include transcription factor networks, where disordered proteins act as integrators of different signals or link different transcription factor subnetworks due to their ability to interact (in many cases simultaneously) with different partners. Similarly, they also serve as signal integrators in signaling cascades, such as those related to response to external stimuli. Disordered proteins have also been found in plants in many stress-response processes, acting as protein chaperones or protecting other cellular components and structures. In plants, it is especially important to have complex and versatile networks able to quickly and efficiently respond to changing environmental conditions since these organisms cannot escape and have no other choice than adapting to them. Consequently, protein disorder can play an especially important role in plants, providing them with a fast mechanism to obtain complex, interconnected and versatile molecular networks. © 2013 Pazos, Pietrosemoli, García-Martín and Solano.


Tuleuova N.,University of California at Davis | Tuleuova N.,National Center for Biotechnology | Jones C.N.,University of California at Davis | Yan J.,University of California at Davis | And 3 more authors.
Analytical Chemistry | Year: 2010

Traditional antibody-based affinity sensing strategies employ multiple reagents and washing steps and are unsuitable for real-time detection of analyte binding. Aptamers, on the other hand, may be designed to monitor binding events directly, in real-time, without the need for secondary labels. The goal of the present study was to design an aptamer beacon for fluorescence resonance energy transfer (FRET)based detection of interferon-gamma (IFN-γ)-an important inflammatory cytokine. Variants of DNA aptamer modified with biotin moieties and spacers were immobilized on avidin-coated surfaces and characterized by surface plasmon resonance (SPR). The SPR studies showed that immobilization of aptamer via the 3' end resulted in the best binding IFN-γ (Kd = 3.44 nM). This optimal aptamer variant was then used to construct a beacon by hybridizing fluorophore-labeled aptamer with an antisense oligonucleotide strand carrying a quencher. SPR studies revealed that IFN-γ binding with an aptamer beacon occurred within 15 min of analyte introduction-suggesting dynamic replacement of the quencher-complementary strand by IFN-γ molecules. To further highlight biosensing applications, aptamer beacon molecules were immobilized inside microfluidic channels and challenged with varying concentration of analyte. Fluorescence microscopy revealed low fluorescence in the absence of analyte and high fluorescence after introduction of IFN-γ. Importantly, unlike traditional antibody-based immunoassays, the signal was observed directly upon binding of analyte without the need for multiple washing steps, The surface immobilized aptamer beacon had a linear range from 5 to 100 nM and a lower limit of detection of 5 nM IFN-γ. In conclusion, we designed a FRET-based aptamer beacon for monitoring of an inflammatory cytokine-IFNy. In the future, this biosensing strategy will be employed to monitor dynamics of cytokine production by the immune cells. © 2010 American Chemical Society.


Tuleuova N.,University of California at Davis | Tuleuova N.,National Center for Biotechnology | Lee J.Y.,University of California at Davis | Lee J.,University of California at Davis | And 3 more authors.
Biomaterials | Year: 2010

The success in driving embryonic stem cells towards hepatic lineage has been confounded by the complexity and cost of differentiation protocols that employ large quantities of expensive growth factors (GFs). Instead of supplementing culture media with soluble GFs, we investigated cultivation and differentiation of mouse embryonic stem cells (mESCs) on printed arrays of GFs. Hepatocyte growth factor (HGF), basic fibroblast growth factor (bFGF) and bone morphogenetic protein (BMP4) were mixed in solution with fibronectin and collagen (I) and then printed onto silane-modified glass slides to form 500 μm diameter protein spots. mESCs were cultured on top of GF spots for up to 12 days and analyzed by RT-PCR and immunostaining at different time points. The stem cells residing on HGF-containing combinations of GFs exhibited requisite features of hepatic differentiation including pronounced loss in pluripotency (Oct4), transient (up and down) expression of endoderm (Sox17) and upregulation of early hepatic markers - albumin and alpha-fetoprotein. The hepatic differentiation was enhanced further by adding hepatic stellate cells to surfaces that already contained mESCs on GF spots. A combination of co-culture with non-parenchymal liver cells and the optimal GF stimulation was found to induce endoderm and hepatic phenotype earlier and to a much greater extent than the GF arrays or micropatterned co-cultures used individually. While this paper investigated hepatic differentiation of mouse ESCs, our findings and stem cell culture approaches are likely to be relevant for human ESC cultivation. Overall, the platform combining printed GF arrays and heterotypic co-cultures will be broadly applicable for identifying the composition of the microenvironment niche for ESC differentiation into various tissue types. © 2010 Elsevier Ltd.


Golan G.,Hebrew University of Jerusalem | Ishchenko A.A.,University Paris - Sud | Khassenov B.,National Center for Biotechnology | Shoham G.,Hebrew University of Jerusalem | Saparbaev M.K.,University Paris - Sud
Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis | Year: 2010

Aerobic respiration generates reactive oxygen species (ROS) as a by-product of cellular metabolism which can damage DNA. The complex nature of oxidative DNA damage requires actions of several repair pathways. Oxidized DNA bases are substrates for two overlapping pathways: base excision repair (BER) and nucleotide incision repair (NIR). In the BER pathway a DNA glycosylase cleaves the N-glycosylic bond between the abnormal base and deoxyribose, leaving either an abasic site or single-stranded DNA break. Alternatively, in the NIR pathway, an apurinic/apyrimidinic (AP) endonuclease incises duplex DNA 5′ next to oxidatively damaged nucleotide. The multifunctional Escherichia coli endonuclease IV (Nfo) is involved in both BER and NIR pathways. Nfo incises duplex DNA 5′ of a damaged residue but also possesses an intrinsic 3′ → 5′ exonuclease activity. Herein, we demonstrate that Nfo-catalyzed NIR and exonuclease activities can generate a single-strand gap at the 5′ side of 5,6-dihydrouracil residue. Furthermore, we show that Nfo mutants carrying amino acid substitutions H69A and G149D are deficient in both NIR and exonuclease activities, suggesting that these two functions are genetically linked and governed by the same amino acid residues. The crystal structure of Nfo-H69A mutant reveals the loss of one of the active site zinc atoms (Zn1) and rearrangements of the catalytic site, but no gross changes in the overall enzyme conformation. We hypothesize that these minor changes strongly affect the DNA binding of Nfo. Decreased affinity may lead to a different kinking angle of the DNA helix and this in turn thwart nucleotide incision and exonuclease activities of Nfo mutants but to lesser extent of their AP endonuclease function. Based on the biochemical and genetic data we propose a model where nucleotide incision coupled to 3′ → 5′ exonuclease activity prevents formation of lethal double-strand breaks when repairing bi-stranded clustered DNA damage. © 2009 Elsevier B.V. All rights reserved.


News Article | November 17, 2016
Site: marketersmedia.com

— Learn Bones, one of the web’s premier resources for anatomy students and those looking to learn more about the human musculoskeletal system, recently announced the publication of their new bone health guide. The site aims to help their readers understand the underlying causes of osteoporosis and learn about the steps they can take to keep this debilitating condition at bay. The newly-published guide is currently available on the home page of the Learn Bones website at http://www.learnbones.com/. “According to the National Center for Biotechnology information, nearly 50 million U.S. citizens aged 50 and over currently suffer from osteoporosis or have bone density problems that could lead to the disease. Unfortunately, having an aging population means the problem is only expected to get worse,” said James Thompson of Learn Bones. “This is why we’ve developed and released our newest bone health guide. We want people to know that there are steps they can take to reduce their risk of developing osteoporosis and other bone conditions and give them the tools to live long, healthy, active lives,” Thompson went on to say. The recently-published bone health guide at http://www.learnbones.com/ begins with an in-depth explanation of osteoporosis and its underlying causes. The guide then goes on to explain what steps people can take right now to reduce their risk of developing it, including getting regular exercise and ensuring that they get adequate doses of daily vitamins. For those who have already developed weakness in their bones, Learn Bones’ new guide will give them tips on what to expect when it comes to possible treatments for their condition. As Thompson continued, “While everyone wants to believe that they’ll never be negatively affected by osteoporosis, the truth is that keeping our bones strong over the long haul requires us to start treating our bodies well right now. We just want to help people take control of their bone health so that they can enjoy their lives for many more years to come.” Those who would like to get a glimpse of Learn Bones’ newest bone health guide or see how they help both anatomy students and the general population better understand the human body can visit http://www.learnbones.com/ for more information. Learnbones.com is a premier resource for students of anatomy. The site offers relevant information on the bones of the human body in a concise and pertinent manner. Many of the images displayed are from Gray's Anatomy, the ultimate text book for students. In addition to information about the human skeletal system, the site also offers resources for those who want to learn about bone diseases and the muscles of the human body. For more information, please visit http://www.learnbones.com


Fernandez A.F.,University of Oviedo | Fraga M.F.,University of Oviedo | Fraga M.F.,National Center for Biotechnology
Epigenetics | Year: 2011

The physiological effects of the dietary polyphenol resveratrol are being extensively studied. Resveratrol has been proposed to promote healthy aging and to increase lifespan, primarily through the activation of the class III histone deacetylases (sirtuins). Although its positive effects are evident in yeast and mice, they still have to be confirmed in humans. The molecular mechanisms involved in the processes are not fully understood because resveratrol may have other targets than sirtuins and the direct activation of sirtuins by resveratrol is under debate. © 2011 Landes Bioscience.

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