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— Pancreatic Cancer Diagnostic Tests - Medical Devices Pipeline Assessment, report provides an overview of Pancreatic Cancer Diagnostic Tests currently in pipeline stage. The report reviews major players involved in the pipeline product development. It also provides information about clinical trials in progress, which includes trial phase, trial status, trial start and end dates, and, the number of trials for the key Pancreatic Cancer Diagnostic Tests pipeline products Complete report on Pancreatic Cancer Diagnostic Tests - Medical Devices Pipeline Assessment, 2016 spread across 175 pages is available at http://www.reportsnreports.com/reports/773014-pancreatic-cancer-diagnostic-tests-medical-devices-pipeline-assessment-2016.html The report reviews the major players involved in the development of Pancreatic Cancer Diagnostic Tests and list all their pipeline projects. The report provides key clinical trial data of ongoing trials specific to pipeline products List of Tables: • Pancreatic Cancer Diagnostic Tests Products under Development • Pancreatic Cancer Diagnostic Tests - Pipeline Products under Development by Companies • Pancreatic Cancer Diagnostic Tests Companies and Product Overview • Pancreatic Cancer Diagnostic Tests - Recent Developments • Pancreatic Cancer Diagnostic Tests - Ongoing Clinical Trials • Pancreatic Cancer Companies - Pipeline Products by Stage of Development • Pancreatic Cancer Diagnostic Tests - Pipeline Products by Stage of Development • ImmunoCellular Therapeutics Announces Third Quarter 2016 Financial Results and Provides Research and Development Update • 2016: VolitionRx Announces Third Quarter 2016 Financial Results and Business Update • 2016: Merrimack Reports Third Quarter 2016 Financial Results • 2016: Exact Sciences Appoints Jeff Elliott Chief Financial Officer • 2016: OPKO Health Reports Third Quarter Financial and Operating Results • 2016: Halozyme Reports Third Quarter 2016 Financial Results • 2016: Clovis Oncology Announces Q3 2016 Operating Results and Corporate Update Company Discussed In Report: A&G Pharmaceutical Inc, Abcodia Ltd Company, BioMarker Strategies, Matrix-Bio, US Biomarkers Inc, , PeriRx LLC, Oxford Gene Technology Ltd, Asuragen, Inc, BioMarker Strategies, Cleveland Diagnostics, CompanDX Ltd, German Cancer Research Center, IV Diagnostics Scope Extensive coverage of the Pancreatic Cancer Diagnostic Tests under development. The report reviews details of major pipeline products which include, product description, licensing and collaboration details and other developmental activities. The report reviews the major players involved in the development of Pancreatic Cancer Diagnostic Tests and list all their pipeline projects. The coverage of pipeline products based on various stages of development ranging from Early Development to Approved / Issued stage. The report provides key clinical trial data of ongoing trials specific to pipeline products. Recent developments in the segment / industry Reasons to Buy Formulate significant competitor information, analysis, and insights to improve R&D strategies Identify emerging players with potentially strong product portfolio and create effective counter-strategies to gain competitive advantage. Identify and understand important and diverse types of Pancreatic Cancer Diagnostic Tests under development Develop market-entry and market expansion strategies. Plan mergers and acquisitions effectively by identifying major players with the most promising pipeline. In-depth analysis of the product's current stage of development, territory and estimated launch date About Us: Reportsnreports.com is an online database of market research reports offer in-depth analysis of over 5000 market segments. The library has syndicated reports by leading market research publishers across the globe and also offer customized market research reports for multiple industries. For more information, please visit http://www.reportsnreports.com/reports/773014-pancreatic-cancer-diagnostic-tests-medical-devices-pipeline-assessment-2016.html


Ferreira L.A.,Cleveland Diagnostics | Breydo L.,University of South Florida | Reichardt C.,University of Marburg | Uversky V.N.,Russian Academy of Sciences | Zaslavsky B.Y.,Cleveland Diagnostics
Journal of Biomolecular Structure and Dynamics | Year: 2016

The solvatochromic solvent features of water (dipolarity/polarizability, π*, hydrogen bond donor acidity, α, and hydrogen bond acceptor basicity, β) of water have been determined in aqueous solutions of erythritol, glucose, inositol, sarcosine, xylitol and urea with concentrations from 0 to ~3 M and higher. The concentration effects of the osmolytes on the solvent features of water were characterized and compared with those reported previously for sorbitol, sucrose, trimethylamine N-oxide (TMAO), and trehalose. The solvent features of water in solutions of all osmolytes except TMAO and sarcosine were established to be linearly interrelated. It is shown that the concentration effects of essentially all nonionic osmolytes depend on osmolytes’ lipophilicity, molecular polarizability, and polar surface area. It is demonstrated that solubility of various compounds in aqueous solutions of glucose, sucrose, sorbitol, and urea of varied concentrations may be described in terms of solvent dipolarity/polarizability of water in these solutions. Surface tension of aqueous solutions of sucrose and sorbitol may also be described in the same terms. The relative permittivity of aqueous solutions of glucose and sucrose may be described in terms of the solvent hydrogen bond donor acidity of water. It is suggested that the effects of nonionic osmolytes on behavior of proteins and nucleic acids in aqueous media may be considered in terms of the altered solvent features of water instead of “nano-molecular crowding” effect. © 2016 Informa UK Limited, trading as Taylor & Francis Group


Ferreira L.A.,Cleveland Diagnostics | Madeira P.P.,University of Porto | Breydo L.,University of South Florida | Reichardt C.,University of Marburg | And 3 more authors.
Journal of Biomolecular Structure and Dynamics | Year: 2016

Analysis of the macromolecular crowding effects in polymer solutions show that the excluded volume effect is not the only factor affecting the behavior of biomolecules in a crowded environment. The observed inconsistencies are commonly explained by the so-called soft interactions, such as electrostatic, hydrophobic, and van der Waals interactions, between the crowding agent and the protein, in addition to the hard nonspecific steric interactions. We suggest that the changes in the solvent properties of aqueous media induced by the crowding agents may be the root of these "soft" interactions. To check this hypothesis, the solvatochromic comparison method was used to determine the solvent dipolarity/polarizability, hydrogen-bond donor acidity, and hydrogen-bond acceptor basicity of aqueous solutions of different polymers (dextran, poly(ethylene glycol), Ficoll, Ucon, and polyvinylpyrrolidone) with the polymer concentration up to 40% typically used as crowding agents. Polymer-induced changes in these features were found to be polymer type and concentration specific, and, in case of polyethylene glycol (PEG), molecular mass specific. Similarly sized polymers PEG and Ucon producing different changes in the solvent properties of water in their solutions induced morphologically different α-synuclein aggregates. It is shown that the crowding effects of some polymers on protein refolding and stability reported in the literature can be quantitatively described in terms of the established solvent features of the media in these polymers solutions. These results indicate that the crowding agents do induce changes in solvent properties of aqueous media in crowded environment. Therefore, these changes should be taken into account for crowding effect analysis. © 2015 Taylor and Francis.


PubMed | University of Porto, University of Marburg, University of South Florida and Cleveland Diagnostics
Type: Journal Article | Journal: Journal of biomolecular structure & dynamics | Year: 2016

Analysis of the macromolecular crowding effects in polymer solutions show that the excluded volume effect is not the only factor affecting the behavior of biomolecules in a crowded environment. The observed inconsistencies are commonly explained by the so-called soft interactions, such as electrostatic, hydrophobic, and van der Waals interactions, between the crowding agent and the protein, in addition to the hard nonspecific steric interactions. We suggest that the changes in the solvent properties of aqueous media induced by the crowding agents may be the root of these soft interactions. To check this hypothesis, the solvatochromic comparison method was used to determine the solvent dipolarity/polarizability, hydrogen-bond donor acidity, and hydrogen-bond acceptor basicity of aqueous solutions of different polymers (dextran, poly(ethylene glycol), Ficoll, Ucon, and polyvinylpyrrolidone) with the polymer concentration up to 40% typically used as crowding agents. Polymer-induced changes in these features were found to be polymer type and concentration specific, and, in case of polyethylene glycol (PEG), molecular mass specific. Similarly sized polymers PEG and Ucon producing different changes in the solvent properties of water in their solutions induced morphologically different -synuclein aggregates. It is shown that the crowding effects of some polymers on protein refolding and stability reported in the literature can be quantitatively described in terms of the established solvent features of the media in these polymers solutions. These results indicate that the crowding agents do induce changes in solvent properties of aqueous media in crowded environment. Therefore, these changes should be taken into account for crowding effect analysis.


Zaslavsky B.Y.,Cleveland Diagnostics | Uversky V.N.,University of South Florida | Chait A.,Cleveland Diagnostics
Expert Review of Proteomics | Year: 2015

Proteins have several measurable features in biological fluids that may change under pathological conditions. The current disease biomarker discovery is mostly based on protein concentration in the sample as the measurable feature. Changes in protein structures, such as post-translational modifications and in protein–partner interactions are known to accompany pathological processes. Changes in glycosylation profiles are well-established for many plasma proteins in various types of cancer and other diseases. The solvent interaction analysis method is based on protein partitioning in aqueous two-phase systems and is highly sensitive to changes in protein structure and protein–protein- and protein–partner interactions while independent of the protein concentration in the biological sample. It provides quantitative index: partition coefficient representing changes in protein structure and interactions with partners. The fundamentals of the method are presented with multiple examples of applications of the method to discover and monitor structural protein biomarkers as disease-specific diagnostic indicators. © 2015 Taylor & Francis


Myers T.R.,Cleveland Diagnostics | Tomasio L.,Cleveland Diagnostics
Respiratory Care | Year: 2011

Asthma is a multifactorial, chronic inflammatory disease of the airways. The knowledge that asthma is an inflammatory disorder has become a core fundamental in the definition of asthma. Asthma's chief features include a variable degree of air-flow obstruction and bronchial hyper-responsiveness, in addition to the underlying chronic airways inflammation. This underlying chronic airway inflammation substantially contributes to airway hyper-responsiveness, air-flow limitation, respiratory symptoms, and disease chronicity. However, this underlying chronic airway inflammation has implications for the diagnosis, management, and potential prevention of the disease. This review for the respiratory therapy community summarizes these developments as well as providing an update on asthma epidemiology, natural history, cause, and pathogenesis. This paper also provides an overview on appropriate diagnostic and monitoring strategies for asthma, pharmacology, and newer therapies for the future as well as relevant management of acute and ambulatory asthma, and a brief review of educational approaches. © 2011 Daedalus Enterprises.


Zaslavsky B.Y.,Cleveland Diagnostics | Uversky V.N.,University of South Florida | Chait A.,Cleveland Diagnostics
Biochimica et Biophysica Acta - Proteins and Proteomics | Year: 2016

This review covers the fundamentals of protein partitioning in aqueous two-phase systems (ATPS). Included is a review of advancements in the analytical application of solute partitioning in ATPS over the last two decades, with multiple examples of experimental data providing evidence that phase-forming polymers do not interact with solutes partitioned in ATPS. The partitioning of solutes is governed by the differences in solute interactions with aqueous media in the two phases. Solvent properties of the aqueous media in these two phases may be characterized and manipulated. The solvent interaction analysis (SIA) method, based on the solute partitioning in ATPS, may be used for characterization and analysis of individual proteins and their interactions with different partners. The current state of clinical proteomics regarding the discovery and monitoring of new protein biomarkers is discussed, and it is argued that the protein expression level in a biological fluid may be not the optimal focus of clinical proteomic research. Multiple examples of application of the SIA method for discovery of changes in protein structure and protein-partner interactions in biological fluids are described. The SIA method reveals new opportunities for discovery and monitoring structure-based protein biomarkers. © 2016 Elsevier B.V. All rights reserved.


PubMed | University of Porto, Russian Academy of Sciences and Cleveland Diagnostics
Type: Journal Article | Journal: Journal of biomolecular structure & dynamics | Year: 2016

Solvent properties of aqueous media (dipolarity/polarizability, hydrogen bond donor acidity, and hydrogen bond acceptor basicity) were measured in the coexisting phases of Dextran-PEG aqueous two-phase systems (ATPSs) containing .5 and 2.0M urea. The differences between the electrostatic and hydrophobic properties of the phases in the ATPSs were quantified by analysis of partitioning of the homologous series of sodium salts of dinitrophenylated amino acids with aliphatic alkyl side chains. Furthermore, partitioning of eleven different proteins in the ATPSs was studied. The analysis of protein partition behavior in a set of ATPSs with protective osmolytes (sorbitol, sucrose, trehalose, and TMAO) at the concentration of .5M, in osmolyte-free ATPS, and in ATPSs with .5 or 2.0M urea in terms of the solvent properties of the phases was performed. The results show unambiguously that even at the urea concentration of .5M, this denaturant affects partitioning of all proteins (except concanavalin A) through direct urea-protein interactions and via its effect on the solvent properties of the media. The direct urea-protein interactions seem to prevail over the urea effects on the solvent properties of water at the concentration of .5M urea and appear to be completely dominant at 2.0M urea concentration.


PubMed | Cleveland Diagnostics
Type: | Journal: Frontiers in pharmacology | Year: 2016

The physiological link between circulating high density lipoprotein (HDL) levels and cardiovascular disease is well-documented, albeit its intricacies are not well-understood. An improved appreciation of HDL function and overall role in vascular health and disease requires at its foundation a better understanding of the lipoproteins molecular structure, its formation, and its process of maturation through interactions with various plasma enzymes and cell receptors that intervene along the pathway of reverse cholesterol transport. This review focuses on summarizing recent developments in the field of lipid free apoA-I and HDL structure, with emphasis on new insights revealed by newly published nascent and spherical HDL models constructed by combining low resolution structures obtained from small angle neutron scattering (SANS) with contrast variation and geometrical constraints derived from hydrogen-deuterium exchange (HDX), crosslinking mass spectrometry, electron microscopy, Frster resonance energy transfer, and electron spin resonance. Recently published low resolution structures of nascent and spherical HDL obtained from SANS with contrast variation and isotopic labeling of apolipoprotein A-I (apoA-I) will be critically reviewed and discussed in terms of how they accommodate existing biophysical structural data from alternative approaches. The new low resolution structures revealed and also provided some answers to long standing questions concerning lipid organization and particle maturation of lipoproteins. The review will discuss the merits of newly proposed SANS based all atom models for nascent and spherical HDL, and compare them with accepted models. Finally, naturally occurring and bioengineered mutations in apoA-I, and their impact on HDL phenotype, are reviewed and discuss together with new therapeutics employed for restoring HDL function.


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