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  1. Article ; Online: Morphine infusor pump switch to oral methadone.

    Santos Suárez, Juan / Del Valle Arnáez, Gema

    BMJ supportive & palliative care

    2019  Volume 10, Issue 1, Page(s) 1–3

    Abstract: Between 2014 and 2017, four patients with widespread cancer were referred to a home palliative care team from a hospital in Oviedo (Spain) with subcutaneous elastomeric infusion pump containing 180-260 mg/day of morphine for previously uncontrolled pain. ...

    Abstract Between 2014 and 2017, four patients with widespread cancer were referred to a home palliative care team from a hospital in Oviedo (Spain) with subcutaneous elastomeric infusion pump containing 180-260 mg/day of morphine for previously uncontrolled pain. 3-4 rotations were performed over 5-11 days, gradually substituting morphine for oral methadone (three times a day) to minimise the risks of rapid conversion, with a highly variable final subcutaneous morphine:oral methadone ratio (5:1 to 17:1), guided by the absence of pain, and to enhance the patient's functional capacity avoiding device dependence. The final methadone dose varied between 15 and 39 mg/day. There was daily telephone supervision and visits every 2-4 days. Patient demise occurred 56, 111, 168 and 350 days following the opioid conversion, and methadone was maintained until then. In all cases and prior to concluding the rotation, pain was controlled and sleepiness had subsided.
    MeSH term(s) Administration, Oral ; Aged ; Analgesics, Opioid/administration & dosage ; Cancer Pain/drug therapy ; Dose-Response Relationship, Drug ; Drug Substitution/methods ; Fatal Outcome ; Female ; Humans ; Infusion Pumps ; Infusions, Subcutaneous ; Male ; Methadone/administration & dosage ; Middle Aged ; Morphine/administration & dosage ; Palliative Care/methods ; Spain
    Chemical Substances Analgesics, Opioid ; Morphine (76I7G6D29C) ; Methadone (UC6VBE7V1Z)
    Language English
    Publishing date 2019-04-03
    Publishing country England
    Document type Case Reports ; Journal Article
    ISSN 2045-4368
    ISSN (online) 2045-4368
    DOI 10.1136/bmjspcare-2018-001760
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: SGnn: A Web Server for the Prediction of Prion-Like Domains Recruitment to Stress Granules Upon Heat Stress.

    Iglesias, Valentín / Santos, Jaime / Santos-Suárez, Juan / Pintado-Grima, Carlos / Ventura, Salvador

    Frontiers in molecular biosciences

    2021  Volume 8, Page(s) 718301

    Abstract: Proteins bearing prion-like domains (PrLDs) are essential players in stress granules (SG) assembly. Analysis of data on heat stress-induced recruitment of yeast PrLDs to SG suggests that this propensity might be connected with three defined protein ... ...

    Abstract Proteins bearing prion-like domains (PrLDs) are essential players in stress granules (SG) assembly. Analysis of data on heat stress-induced recruitment of yeast PrLDs to SG suggests that this propensity might be connected with three defined protein biophysical features: aggregation propensity, net charge, and the presence of free cysteines. These three properties can be read directly in the PrLDs sequences, and their combination allows to predict protein recruitment to SG under heat stress. On this basis, we implemented SGnn, an online predictor of SG recruitment that exploits a feed-forward neural network for high accuracy classification of the assembly behavior of PrLDs. The simplicity and precision of our strategy should allow its implementation to identify heat stress-induced SG-forming proteins in complete proteomes.
    Language English
    Publishing date 2021-08-18
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2814330-9
    ISSN 2296-889X
    ISSN 2296-889X
    DOI 10.3389/fmolb.2021.718301
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: DispHred: A Server to Predict pH-Dependent Order-Disorder Transitions in Intrinsically Disordered Proteins.

    Santos, Jaime / Iglesias, Valentín / Pintado, Carlos / Santos-Suárez, Juan / Ventura, Salvador

    International journal of molecular sciences

    2020  Volume 21, Issue 16

    Abstract: The natively unfolded nature of intrinsically disordered proteins (IDPs) relies on several physicochemical principles, of which the balance between a low sequence hydrophobicity and a high net charge appears to be critical. Under this premise, it is well- ...

    Abstract The natively unfolded nature of intrinsically disordered proteins (IDPs) relies on several physicochemical principles, of which the balance between a low sequence hydrophobicity and a high net charge appears to be critical. Under this premise, it is well-known that disordered proteins populate a defined region of the charge-hydropathy (C-H) space and that a linear boundary condition is sufficient to distinguish between folded and disordered proteins, an approach widely applied for the prediction of protein disorder. Nevertheless, it is evident that the C-H relation of a protein is not unalterable but can be modulated by factors extrinsic to its sequence. Here, we applied a C-H-based analysis to develop a computational approach that evaluates sequence disorder as a function of pH, assuming that both protein net charge and hydrophobicity are dependent on pH solution. On that basis, we developed DispHred, the first pH-dependent predictor of protein disorder. Despite its simplicity, DispHred displays very high accuracy in identifying pH-induced order/disorder protein transitions. DispHred might be useful for diverse applications, from the analysis of conditionally disordered segments to the synthetic design of disorder tags for biotechnological applications. Importantly, since many disorder predictors use hydrophobicity as an input, the here developed framework can be implemented in other state-of-the-art algorithms.
    MeSH term(s) Algorithms ; Hydrogen-Ion Concentration ; Hydrophobic and Hydrophilic Interactions ; Internet ; Intrinsically Disordered Proteins/chemistry ; Reproducibility of Results ; User-Computer Interface
    Chemical Substances Intrinsically Disordered Proteins
    Language English
    Publishing date 2020-08-13
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms21165814
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: pH-Dependent Aggregation in Intrinsically Disordered Proteins Is Determined by Charge and Lipophilicity.

    Santos, Jaime / Iglesias, Valentín / Santos-Suárez, Juan / Mangiagalli, Marco / Brocca, Stefania / Pallarès, Irantzu / Ventura, Salvador

    Cells

    2020  Volume 9, Issue 1

    Abstract: Protein aggregation is associated with an increasing number of human disorders and premature aging. Moreover, it is a central concern in the manufacturing of recombinant proteins for biotechnological and therapeutic applications. Nevertheless, the unique ...

    Abstract Protein aggregation is associated with an increasing number of human disorders and premature aging. Moreover, it is a central concern in the manufacturing of recombinant proteins for biotechnological and therapeutic applications. Nevertheless, the unique architecture of protein aggregates is also exploited by nature for functional purposes, from bacteria to humans. The relevance of this process in health and disease has boosted the interest in understanding and controlling aggregation, with the concomitant development of a myriad of algorithms aimed to predict aggregation propensities. However, most of these programs are blind to the protein environment and, in particular, to the influence of the pH. Here, we developed an empirical equation to model the pH-dependent aggregation of intrinsically disordered proteins (IDPs) based on the assumption that both the global protein charge and lipophilicity depend on the solution pH. Upon its parametrization with a model IDP, this simple phenomenological approach showed unprecedented accuracy in predicting the dependence of the aggregation of both pathogenic and functional amyloidogenic IDPs on the pH. The algorithm might be useful for diverse applications, from large-scale analysis of IDPs aggregation properties to the design of novel reversible nanofibrillar materials.
    MeSH term(s) Humans ; Hydrogen-Ion Concentration ; Hydrophobic and Hydrophilic Interactions ; Intrinsically Disordered Proteins/chemistry ; Intrinsically Disordered Proteins/metabolism ; Protein Aggregates ; Protein Folding
    Chemical Substances Intrinsically Disordered Proteins ; Protein Aggregates
    Language English
    Publishing date 2020-01-08
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2661518-6
    ISSN 2073-4409 ; 2073-4409
    ISSN (online) 2073-4409
    ISSN 2073-4409
    DOI 10.3390/cells9010145
    Database MEDical Literature Analysis and Retrieval System OnLINE

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