GLORIA

GEOMAR Library Ocean Research Information Access

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
  • Future Science Ltd  (3)
  • 1
    Online Resource
    Online Resource
    Future Science Ltd ; 2015
    In:  Future Science OA Vol. 1, No. 2 ( 2015-09)
    In: Future Science OA, Future Science Ltd, Vol. 1, No. 2 ( 2015-09)
    Type of Medium: Online Resource
    ISSN: 2056-5623
    Language: English
    Publisher: Future Science Ltd
    Publication Date: 2015
    detail.hit.zdb_id: 2863457-3
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
  • 2
    In: Future Science OA, Future Science Ltd, Vol. 1, No. 2 ( 2015-09)
    Abstract: The main therapeutic and prophylactic tools against malaria have been locked for more than a century in the classical approaches of using drugs targeting metabolic processes of the causing agent, the protist Plasmodium spp., and of designing vaccines against chosen antigens found on the parasite's surface. Given the extraordinary resources exhibited by Plasmodium to escape these traditional strategies, which have not been able to free humankind from the scourge of malaria despite much effort invested in them, new concepts have to be explored in order to advance toward eradication of the disease. In this context, amyloid-forming proteins and peptides found in the proteome of the pathogen should perhaps cease being regarded as mere anomalous molecules. Their likely functionality in the pathophysiology of Plasmodium calls for attention being paid to them as a possible Achilles’ heel of malaria. Here we will give an overview of Plasmodium-encoded amyloid-forming polypeptides as potential therapeutic targets and toxic elements, particularly in relation to cerebral malaria and the blood–brain barrier function. We will also discuss the recent finding that the genome of the parasite contains an astonishingly high proportion of prionogenic domains.
    Type of Medium: Online Resource
    ISSN: 2056-5623
    Language: English
    Publisher: Future Science Ltd
    Publication Date: 2015
    detail.hit.zdb_id: 2863457-3
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
  • 3
    Online Resource
    Online Resource
    Future Science Ltd ; 2015
    In:  Future Science OA Vol. 1, No. 2 ( 2015-09)
    In: Future Science OA, Future Science Ltd, Vol. 1, No. 2 ( 2015-09)
    Abstract: Misfolding and aggregation of proteins in tissues is linked to the onset of a diverse set of human neurodegenerative disorders, including Alzheimer's and Parkinson's diseases. In these pathologies proteins usually aggregate into highly ordered and β-sheet enriched amyloid fibrils. However, the formation of these toxic structures is not restricted to a reduced set of polypeptides but rather an intrinsic property of proteins. This suggests that the number of proteins involved in conformational disorders might be much larger than previously thought. The propensity of a protein to form amyloid assemblies is imprinted in its sequence and can be read using computational approaches. Here, we exploit four of these algorithms to analyze the presence of aggregation-prone regions in the sequence and structure of the extracellular domains of several neuroreceptors, with the idea of identifying patches that can interact anomalously with other aggregation-prone molecules such as the amyloid-β peptide or promote their self-assembly. The number of amyloidogenic regions in these domains is rather low but they are significantly exposed to solvent and therefore are suitable for interactions. We find a significant overlap between aggregation-prone regions and receptors interfaces and/or ligand-binding sites, which illustrates an unavoidable competition between the formation of functional native interactions and that of dangerous amyloid-like contacts leading to disease.
    Type of Medium: Online Resource
    ISSN: 2056-5623
    Language: English
    Publisher: Future Science Ltd
    Publication Date: 2015
    detail.hit.zdb_id: 2863457-3
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...