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  1. Article ; Online: The p38 MAPK Signaling Activation in Colorectal Cancer upon Therapeutic Treatments

    Angelina Pranteda / Valentina Piastra / Lorenzo Stramucci / Deborah Fratantonio / Gianluca Bossi

    International Journal of Molecular Sciences, Vol 21, Iss 2773, p

    2020  Volume 2773

    Abstract: Pharmacological treatment of colorectal carcinoma currently proceeds through the administration of a combination of different chemotherapeutic agents. In the case of rectal carcinoma, radiation therapy also represents a therapeutic strategy. In an ... ...

    Abstract Pharmacological treatment of colorectal carcinoma currently proceeds through the administration of a combination of different chemotherapeutic agents. In the case of rectal carcinoma, radiation therapy also represents a therapeutic strategy. In an attempt at translating much-needed new targeted therapy to the clinics, p38 mitogen activated protein kinase (MAPK) inhibitors have been tested in clinical trials involving colorectal carcinoma patients, especially in combination with chemotherapy; however, despite the high expectations raised by a clear involvement of the p38 MAPK pathway in the response to therapeutic treatments, poor results have been obtained so far. In this work, we review recent insights into the exact role of the p38 MAPK pathway in response to currently available therapies for colorectal carcinoma, depicting an intricate scenario in which the p38 MAPK node presents many opportunities, as well as many challenges, for its perspective exploitation for clinical purposes.
    Keywords p38 MAPK ; colorectal cancer ; therapeutic treatments ; 5-fluorouracil ; oxaliplatin ; irinotecan ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
    Language English
    Publishing date 2020-04-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  2. Article ; Online: Identification of relevant conformational epitopes on the HER2 oncoprotein by using Large Fragment Phage Display (LFPD).

    Federico Gabrielli / Roberto Salvi / Chiara Garulli / Cristina Kalogris / Serena Arima / Luca Tardella / Paolo Monaci / Serenella M Pupa / Elda Tagliabue / Maura Montani / Elena Quaglino / Lorenzo Stramucci / Claudia Curcio / Cristina Marchini / Augusto Amici

    PLoS ONE, Vol 8, Iss 3, p e

    2013  Volume 58358

    Abstract: We developed a new phage-display based approach, the Large Fragment Phage Display (LFPD), that can be used for mapping conformational epitopes on target molecules of immunological interest. LFPD uses a simplified and more effective phage-display approach ...

    Abstract We developed a new phage-display based approach, the Large Fragment Phage Display (LFPD), that can be used for mapping conformational epitopes on target molecules of immunological interest. LFPD uses a simplified and more effective phage-display approach in which only a limited set of larger fragments (about 100 aa in length) are expressed on the phage surface. Using the human HER2 oncoprotein as a target, we identified novel B-cell conformational epitopes. The same homologous epitopes were also detected in rat HER2 and all corresponded to the epitopes predicted by computational analysis (PEPITO software), showing that LFPD gives reproducible and accurate results. Interestingly, these newly identified HER2 epitopes seem to be crucial for an effective immune response against HER2-overexpressing breast cancers and might help discriminating between metastatic breast cancer and early breast cancer patients. Overall, the results obtained in this study demonstrated the utility of LFPD and its potential application to the detection of conformational epitopes on many other molecules of interest, as well as, the development of new and potentially more effective B-cell conformational epitopes based vaccines.
    Keywords Medicine ; R ; Science ; Q
    Subject code 500
    Language English
    Publishing date 2013-01-01T00:00:00Z
    Publisher Public Library of Science (PLoS)
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  3. Article ; Online: Correction

    Silvia Grasso / Jennifer Chapelle / Vincenzo Salemme / Simona Aramu / Isabella Russo / Nicoletta Vitale / Ludovica Verdun di Cantogno / Katiuscia Dallaglio / Isabella Castellano / Augusto Amici / Giorgia Centonze / Nanaocha Sharma / Serena Lunardi / Sara Cabodi / Federica Cavallo / Alessia Lamolinara / Lorenzo Stramucci / Enrico Moiso / Paolo Provero /
    Adriana Albini / Anna Sapino / Johan Staaf / Pier Paolo Di Fiore / Giovanni Bertalot / Salvatore Pece / Daniela Tosoni / Stefano Confalonieri / Manuela Iezzi / Paola Di Stefano / Emilia Turco / Paola Defilippi

    Nature Communications, Vol 9, Iss 1, Pp 1-

    Author Correction: The scaffold protein p140Cap limits ERBB2-mediated breast cancer progression interfering with Rac GTPase-controlled circuitries

    2018  Volume 1

    Abstract: Nature Communications 8: Article number: 14797 (2017); Published online 16 March 2017; Updated 30 March 2018 In the original version of this Article, the affiliation details for Anna Sapino were incorrectly given as Department of Medical Sciences, ... ...

    Abstract Nature Communications 8: Article number: 14797 (2017); Published online 16 March 2017; Updated 30 March 2018 In the original version of this Article, the affiliation details for Anna Sapino were incorrectly given as Department of Medical Sciences, University of Torino, 10126 Torino, Italy instead ofCandiolo Cancer Institute-FPO, IRCCS, Str.
    Keywords Science ; Q
    Language English
    Publishing date 2018-03-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  4. Article ; Online: The scaffold protein p140Cap limits ERBB2-mediated breast cancer progression interfering with Rac GTPase-controlled circuitries

    Silvia Grasso / Jennifer Chapelle / Vincenzo Salemme / Simona Aramu / Isabella Russo / Nicoletta Vitale / Ludovica Verdun di Cantogno / Katiuscia Dallaglio / Isabella Castellano / Augusto Amici / Giorgia Centonze / Nanaocha Sharma / Serena Lunardi / Sara Cabodi / Federica Cavallo / Alessia Lamolinara / Lorenzo Stramucci / Enrico Moiso / Paolo Provero /
    Adriana Albini / Anna Sapino / Johan Staaf / Pier Paolo Di Fiore / Giovanni Bertalot / Salvatore Pece / Daniela Tosoni / Stefano Confalonieri / Manuela Iezzi / Paola Di Stefano / Emilia Turco / Paola Defilippi

    Nature Communications, Vol 8, Iss 1, Pp 1-

    2017  Volume 16

    Abstract: p140Cap adaptor proteins interfere with adhesion and growth factor-dependent signalling in cancer cells but the mechanisms are unclear. Here the authors show that p140Cap interferes with ERBB2-dependent activation of Rac GTPase-controlled circuitries ... ...

    Abstract p140Cap adaptor proteins interfere with adhesion and growth factor-dependent signalling in cancer cells but the mechanisms are unclear. Here the authors show that p140Cap interferes with ERBB2-dependent activation of Rac GTPase-controlled circuitries reducing metastasis and cancer progression.
    Keywords Science ; Q
    Language English
    Publishing date 2017-03-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

    Full text online

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    Inter-library loan at ZB MED

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