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  Journal of Integrated OMICS
  This is an Open Access Journal Open Access journal
   ISSN (Print) 2182-0287 - ISSN (Online) 2182-0287
   Published by Proteomass Homepage  [1 journal]
  • Editorial board

    • Authors: José Luís Capelo Martínez
      PubDate: 2014-12-31
      Issue No: Vol. 4 (2014)
  • VOL 4, NO 2 (2014)

    • Authors: José Luís Capelo Martínez
      PubDate: 2014-12-31
      Issue No: Vol. 4 (2014)
  • Quantitative mass spectrometry of urinary biomarkers

    • Authors: Marina Jerebtsova, Sergei Nekhai
      Abstract: The effectiveness of treatment of renal diseases is limited because the lack of diagnostic, prognostic and therapeutic markers. Despite the more than a decade of intensive investigation of urinary biomarkers, no new clinical biomarkers were approved. This is in part because the early expectations toward proteomics in biomarkers discovery were significantly higher than the capability of technology at the time. However, during the last decade, proteomic technology has made dramatic progress in both the hardware and software methods. In this review we are discussing modern quantitative methods of mass-spectrometry and providing several examples of their applications for discovery and validation of renal disease biomarkers. We are optimistic about future prospects for the development of novel of specific clinical urinary biomarkers.
      PubDate: 2014-12-08
      Issue No: Vol. 4 (2014)
  • Characterization of temperature-sensing and PIP2-regulation of TRPV1 ion
           channel at the C-terminal domain using NMR spectroscopy and Molecular
           Dynamics Simulations

    • Authors: Kelly A. Raymond, Edward C. Twomey, Yufeng Wei
      Abstract: Transient receptor potential (TRP) channels are receptors of stimulating signals, such as temperature, taste, odor, and chemo- and mechano-stimuli. Temperature sensing TRP channels coincidently function as pain receptors, and are potential targets for substances of abuse, including alcohol and illicit drugs. TRP vanilloid type 1 (TRPV1) channel is activated by heat (>43 °C) and capsaicin under the tight regulation of membrane-associated second messenger, PIP2 (phosphatidylinositol-4,5-bisphosphate), responds to noxious stimuli and inflammatory substances, and could potentially modulate effects of alcohol and drugs of abuse. Despite the crucial roles in mediating signal transductions at both peripheral and central nervous systems, TRP channels are poorly understood in the context of structures and mechanisms. In this letter, we describe our initial structural characterization of the TRPV1 C-terminal domain, the putative temperature sensing and PIP2-regulatory domain, using NMR spectroscopy and molecular dynamics simulations. Both experimental and computational models suggest the C-terminal domain is intrinsically unstructured at room temperature with and without lipid bicelles. Elevated temperature and PIP2-binding can induce substantial conformational changes and formation of considerable secondary structural components in the C-terminal domain, which could be transduced to the transmembrane domain to potentially sensitize the channel.
      PubDate: 2014-10-02
      Issue No: Vol. 4 (2014)
  • Proteomic identification of muscle-associated biomarkers of amyotrophic
           lateral sclerosis using the wobbler mouse model of primary motor

    • Authors: Ashling Holland, Kay Ohlendieck
      Abstract: Motor neuron disease is a major group of inherited or spontaneous disorders that are associated with muscular atrophy. Recently, muscle preparations from the genetic wobbler mouse model of primary motor neuronopathy have been analyzed by mass spectrometry-based proteomics. The progressive degeneration of individual motor neurons was shown to cause complex alterations in the concentration or isoform expression pattern of muscle proteins involved in the excitation-contraction-relaxation cycle, the cytoskeleton, ion handling, cellular signaling, the stress response and energy metabolism. In this article, we compare the panel of potential new muscle-associated biomarkers that have been obtained by two different, but complementary, bioanalytical approaches, i.e. label-free mass spectrometric analysis versus fluorescence two-dimensional difference-in gel electrophoresis. The complex disease-associated changes in the muscle proteome are considerably different to the more unilateral skeletal muscle transitions observed in experimentally denervated fibers or disuse-related muscular atrophy. The apparent subtype-specific vulnerability of neuromuscular synapses and compensatory mechanisms of fiber type shifting in motor neuron disease is discussed, and contrasted to other forms of muscular atrophy.
      PubDate: 2014-09-24
      Issue No: Vol. 4 (2014)
  • High-throughput genomic technology in research of virulence and
           antimicrobial resistance in microorganisms causing nosocomial infections

    • Authors: Nuno Silva, Gilberto Igrejas, Patrícia Poeta
      Abstract: Most hospital-acquired infections are caused by organisms common in the general population, in which are relatively harmless. Infection by nosocomial pathogenic bacteria is increasingly becoming a major threat to the patients in the hospital. Molecular diagnosis of antibiotic resistant organisms such as Clostridium difficile Infections (CDI) Methicillin Resistant Staphylococcus aureus (MRSA), Extended-Spectrum β-lactamase (ESBL) Escherichia coli, Vancomycin Resistant Enterococcus (VRE), Carbapenem-Resistant Klebsiella (CRK) among others is vital for prevention of healthcare-acquired infections in acute care facilities. DNA microarray besides being a promising diagnosis tool may also provide valuable information about the mechanisms of antimicrobial resistance and pathogenicity of these bacteria. This review aims to highlight the prominence of high-throughput genomic tools in research of virulence and antimicrobial resistance in microorganisms causing nosocomial infections.
      PubDate: 2014-09-24
      Issue No: Vol. 4 (2014)
School of Mathematical and Computer Sciences
Heriot-Watt University
Edinburgh, EH14 4AS, UK
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