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  1. Article ; Online: SARS-CoV-2 spike protein: flexibility as a new target for fighting infection.

    Pierri, Ciro Leonardo

    Signal transduction and targeted therapy

    2020  Volume 5, Issue 1, Page(s) 254

    MeSH term(s) Betacoronavirus ; COVID-19 ; Coronavirus Infections ; Humans ; Pandemics ; Pneumonia, Viral ; SARS-CoV-2 ; Spike Glycoprotein, Coronavirus/genetics
    Chemical Substances Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2
    Keywords covid19
    Language English
    Publishing date 2020-10-30
    Publishing country England
    Document type Journal Article ; Comment
    ZDB-ID 2886872-9
    ISSN 2059-3635 ; 2095-9907
    ISSN (online) 2059-3635
    ISSN 2095-9907
    DOI 10.1038/s41392-020-00369-3
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: SARS-CoV-2 spike protein

    Ciro Leonardo Pierri

    Signal Transduction and Targeted Therapy, Vol 5, Iss 1, Pp 1-

    flexibility as a new target for fighting infection

    2020  Volume 3

    Keywords Medicine ; R ; Biology (General) ; QH301-705.5
    Language English
    Publishing date 2020-10-01T00:00:00Z
    Publisher Nature Publishing Group
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  3. Article: Supercritical Fluid Extraction of Bioactive Components from Apple Peels and Their Modulation of Complex I Activity in Isolated Mitochondria.

    Aresta, Antonella / De Vietro, Nicoletta / Cotugno, Pietro / Pierri, Ciro Leonardo / Trisolini, Lucia / Zambonin, Carlo

    Antioxidants (Basel, Switzerland)

    2024  Volume 13, Issue 3

    Abstract: Supercritical fluid extraction (SFE) was used to extract bioactive compounds from apple ( ...

    Abstract Supercritical fluid extraction (SFE) was used to extract bioactive compounds from apple (
    Language English
    Publishing date 2024-03-01
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2704216-9
    ISSN 2076-3921
    ISSN 2076-3921
    DOI 10.3390/antiox13030307
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: The Mycotoxin Patulin Inhibits the Mitochondrial Carnitine/Acylcarnitine Carrier (SLC25A20) by Interaction with Cys136 Implications for Human Health.

    Giangregorio, Nicola / Tonazzi, Annamaria / Calvano, Cosima Damiana / Pierri, Ciro Leonardo / Incampo, Giovanna / Cataldi, Tommaso R I / Indiveri, Cesare

    International journal of molecular sciences

    2023  Volume 24, Issue 3

    Abstract: The effect of mycotoxin patulin (4-hydroxy-4H-furo [3,2c] pyran-2 [6H] -one) on the mitochondrial carnitine/acylcarnitine carrier (CAC, SLC25A20) was investigated. Transport function was measured as [ ...

    Abstract The effect of mycotoxin patulin (4-hydroxy-4H-furo [3,2c] pyran-2 [6H] -one) on the mitochondrial carnitine/acylcarnitine carrier (CAC, SLC25A20) was investigated. Transport function was measured as [
    MeSH term(s) Humans ; Animals ; Rats ; Patulin ; Escherichia coli/metabolism ; Cysteine/metabolism ; Sulfhydryl Reagents/pharmacology ; Carnitine/pharmacology ; Carnitine/metabolism ; Glutathione/metabolism ; Membrane Transport Proteins
    Chemical Substances Patulin (95X2BV4W8R) ; acylcarnitine ; Cysteine (K848JZ4886) ; Sulfhydryl Reagents ; Carnitine (S7UI8SM58A) ; Glutathione (GAN16C9B8O) ; SLC25A20 protein, human (EC 2.3.1.) ; Membrane Transport Proteins
    Language English
    Publishing date 2023-01-23
    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/ijms24032228
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Sweet as honey, bitter as bile: Mitochondriotoxic peptides and other therapeutic proteins isolated from animal tissues, for dealing with mitochondrial apoptosis.

    Colella, Francesco / Scillitani, Giovanni / Pierri, Ciro Leonardo

    Toxicology

    2020  Volume 447, Page(s) 152612

    Abstract: Mitochondria are subcellular organelles involved in cell metabolism and cell life-cycle. Their role in apoptosis regulation makes them an interesting target of new drugs for dealing with cancer or rare diseases. Several peptides and proteins isolated ... ...

    Abstract Mitochondria are subcellular organelles involved in cell metabolism and cell life-cycle. Their role in apoptosis regulation makes them an interesting target of new drugs for dealing with cancer or rare diseases. Several peptides and proteins isolated from animal and plant sources are known for their therapeutic properties and have been tested on cancer cell-lines and xenograft murine models, highlighting their ability in inducing cell-death by triggering mitochondrial apoptosis. Some of those molecules have been even approved as drugs. Conversely, many other bioactive compounds are still under investigation for their proapoptotic properties. In this review we report about a group of peptides, isolated from animal venoms, with potential therapeutic properties related to their ability in triggering mitochondrial apoptosis. This class of compounds is known with different names, such as mitochondriotoxins or mitocans.
    MeSH term(s) Amino Acid Sequence ; Animals ; Apoptosis/drug effects ; Apoptosis/physiology ; Bile ; Biological Factors/chemistry ; Biological Factors/isolation & purification ; Biological Factors/toxicity ; Honey ; Humans ; Intercellular Signaling Peptides and Proteins/chemistry ; Intercellular Signaling Peptides and Proteins/isolation & purification ; Intercellular Signaling Peptides and Proteins/toxicity ; Mitochondria/chemistry ; Mitochondria/metabolism ; Neoplasms/drug therapy ; Neoplasms/metabolism ; Peptide Fragments/chemistry ; Peptide Fragments/isolation & purification ; Peptide Fragments/toxicity ; Protein Structure, Secondary ; Wasp Venoms/chemistry ; Wasp Venoms/isolation & purification ; Wasp Venoms/toxicity
    Chemical Substances Biological Factors ; Intercellular Signaling Peptides and Proteins ; Peptide Fragments ; Wasp Venoms ; mastoparan (72093-21-1)
    Language English
    Publishing date 2020-11-07
    Publishing country Ireland
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 184557-3
    ISSN 1879-3185 ; 0300-483X
    ISSN (online) 1879-3185
    ISSN 0300-483X
    DOI 10.1016/j.tox.2020.152612
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article: Sweet as honey, bitter as bile: Mitochondriotoxic peptides and other therapeutic proteins isolated from animal tissues, for dealing with mitochondrial apoptosis

    Colella, Francesco / Scillitani, Giovanni / Pierri, Ciro Leonardo

    Toxicology. 2021 Jan. 15, v. 447

    2021  

    Abstract: Mitochondria are subcellular organelles involved in cell metabolism and cell life-cycle. Their role in apoptosis regulation makes them an interesting target of new drugs for dealing with cancer or rare diseases. Several peptides and proteins isolated ... ...

    Abstract Mitochondria are subcellular organelles involved in cell metabolism and cell life-cycle. Their role in apoptosis regulation makes them an interesting target of new drugs for dealing with cancer or rare diseases. Several peptides and proteins isolated from animal and plant sources are known for their therapeutic properties and have been tested on cancer cell-lines and xenograft murine models, highlighting their ability in inducing cell-death by triggering mitochondrial apoptosis. Some of those molecules have been even approved as drugs. Conversely, many other bioactive compounds are still under investigation for their proapoptotic properties. In this review we report about a group of peptides, isolated from animal venoms, with potential therapeutic properties related to their ability in triggering mitochondrial apoptosis. This class of compounds is known with different names, such as mitochondriotoxins or mitocans.
    Keywords animal models ; animal tissues ; animals ; apoptosis ; bioactive compounds ; biopharmaceuticals ; cell lines ; medicinal properties ; metabolism ; mitochondria ; neoplasms ; new drugs ; peptides ; venoms ; xenotransplantation
    Language English
    Dates of publication 2021-0115
    Publishing place Elsevier B.V.
    Document type Article
    ZDB-ID 184557-3
    ISSN 1879-3185 ; 0300-483X
    ISSN (online) 1879-3185
    ISSN 0300-483X
    DOI 10.1016/j.tox.2020.152612
    Database NAL-Catalogue (AGRICOLA)

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  7. Article ; Online: The Mycotoxin Patulin Inhibits the Mitochondrial Carnitine/Acylcarnitine Carrier (SLC25A20) by Interaction with Cys136 Implications for Human Health

    Nicola Giangregorio / Annamaria Tonazzi / Cosima Damiana Calvano / Ciro Leonardo Pierri / Giovanna Incampo / Tommaso R. I. Cataldi / Cesare Indiveri

    International Journal of Molecular Sciences, Vol 24, Iss 2228, p

    2023  Volume 2228

    Abstract: The effect of mycotoxin patulin (4-hydroxy-4H-furo [3,2c] pyran-2 [6H] -one) on the mitochondrial carnitine/acylcarnitine carrier (CAC, SLC25A20) was investigated. Transport function was measured as [ 3 H]-carnitine ex /carnitine in antiport in ... ...

    Abstract The effect of mycotoxin patulin (4-hydroxy-4H-furo [3,2c] pyran-2 [6H] -one) on the mitochondrial carnitine/acylcarnitine carrier (CAC, SLC25A20) was investigated. Transport function was measured as [ 3 H]-carnitine ex /carnitine in antiport in proteoliposomes reconstituted with the native protein extracted from rat liver mitochondria or with the recombinant CAC over-expressed in E. coli . Patulin (PAT) inhibited both the mitochondrial native and recombinant transporters. The inhibition was not reversed by physiological and sulfhydryl-reducing reagents, such as glutathione (GSH) or dithioerythritol (DTE). The IC 50 derived from the dose–response analysis indicated that PAT inhibition was in the range of 50 µM both on the native and on rat and human recombinant protein. The kinetics process revealed a competitive type of inhibition. A substrate protection experiment confirmed that the interaction of PAT with the protein occurred within a protein region, including the substrate-binding area. The mechanism of inhibition was identified using the site-directed mutagenesis of CAC. No inhibition was observed on Cys mutants in which only the C136 residue was mutated. Mass spectrometry studies and in silico molecular modeling analysis corroborated the outcomes derived from the biochemical assays.
    Keywords mitochondria ; carnitine carrier ; patulin ; cysteines ; inhibition ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
    Subject code 570
    Language English
    Publishing date 2023-01-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  8. Article ; Online: 3D structures inferred from cDNA clones identify the CD1D-Restricted γδ T cell receptor in dromedaries.

    Linguiti, Giovanna / Tragni, Vincenzo / Pierri, Ciro Leonardo / Massari, Serafina / Lefranc, Marie-Paule / Antonacci, Rachele / Ciccarese, Salvatrice

    Frontiers in immunology

    2022  Volume 13, Page(s) 928860

    Abstract: The Camelidae species occupy an important immunological niche within the humoral as well as cell mediated immune response. Although recent studies have highlighted that the somatic hypermutation (SHM) shapes the T cell receptor gamma (TRG) and delta (TRD) ...

    Abstract The Camelidae species occupy an important immunological niche within the humoral as well as cell mediated immune response. Although recent studies have highlighted that the somatic hypermutation (SHM) shapes the T cell receptor gamma (TRG) and delta (TRD) repertoire in
    MeSH term(s) Animals ; Antigens, CD1d/genetics ; Camelus ; Clone Cells ; Complementarity Determining Regions/genetics ; DNA, Complementary ; Humans ; Receptors, Antigen, T-Cell, gamma-delta/chemistry ; Receptors, Antigen, T-Cell, gamma-delta/genetics
    Chemical Substances Antigens, CD1d ; CD1D protein, human ; Complementarity Determining Regions ; DNA, Complementary ; Receptors, Antigen, T-Cell, gamma-delta
    Language English
    Publishing date 2022-08-09
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2606827-8
    ISSN 1664-3224 ; 1664-3224
    ISSN (online) 1664-3224
    ISSN 1664-3224
    DOI 10.3389/fimmu.2022.928860
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Major antigen and paramyosin proteins as candidate biomarkers for serodiagnosis of canine infection by zoonotic Onchocerca lupi.

    Latrofa, Maria Stefania / Palmisano, Giuseppe / Annoscia, Giada / Pierri, Ciro Leonardo / Chandrashekar, Ramaswamy / Otranto, Domenico

    PLoS neglected tropical diseases

    2021  Volume 15, Issue 2, Page(s) e0009027

    Abstract: Onchocerca lupi (Spirurida: Onchocercidae) is a filarial worm parasitizing domestic carnivores and humans. Adult nematodes usually localize beneath in the sclera or in the ocular retrobulbar of infected animals, whilst microfilariae are found in the skin. ...

    Abstract Onchocerca lupi (Spirurida: Onchocercidae) is a filarial worm parasitizing domestic carnivores and humans. Adult nematodes usually localize beneath in the sclera or in the ocular retrobulbar of infected animals, whilst microfilariae are found in the skin. Therefore, diagnosis of O. lupi is achieved by microscopic and/or molecular detection of microfilariae from skin biopsy and/or surgical removal of adults from ocular tissues of infected hosts. An urgent non-invasive diagnostic tool for the diagnosis of O. lupi in dog is mandatory. In this study, an immunoproteomic analyses was performed using a combination of immunoblotting and mass spectrometry techniques. Onchocerca lupi major antigen (Ol-MJA) and paramyosin (Ol-PARA) proteins were identified as potential biomarkers for serodiagnosis. Linear epitopes were herein scanned for both proteins using high-density peptide microarray. Sera collected from dog infected with O. lupi and healthy animal controls led to the identification of 11 immunodominant antigenic peptides (n = 7 for Ol-MJA; n = 4 for Ol-PARA). These peptides were validated using sera of dogs uniquely infected with the most important filarioids infesting dogs either zoonotic (Dirofilaria repens, Dirofilaria immitis) or not (Acanthocheilonema reconditum and Cercopithifilaria bainae). Overall, six antigenic peptides, three for Ol-MJA and for Ol-PARA, respectively, were selected as potential antigens for the serological detection of canine O. lupi infection. The molecular and proteomic dataset herein reported should provide a useful resource for studies on O. lupi toward supporting the development of new interventions (drugs, vaccines and diagnostics) against canine onchocercosis.
    MeSH term(s) Animals ; Biomarkers/blood ; Dog Diseases/diagnosis ; Dog Diseases/parasitology ; Dogs ; Female ; Male ; Microfilariae/genetics ; Microfilariae/isolation & purification ; Onchocerca/chemistry ; Onchocerca/immunology ; Onchocerca/isolation & purification ; Onchocerciasis/diagnosis ; Onchocerciasis/immunology ; Onchocerciasis/parasitology ; Onchocerciasis, Ocular/blood ; Onchocerciasis, Ocular/diagnosis ; Onchocerciasis, Ocular/immunology ; Onchocerciasis, Ocular/parasitology ; Serologic Tests ; Tropomyosin/blood ; Tropomyosin/genetics ; Tropomyosin/immunology ; Tropomyosin/isolation & purification
    Chemical Substances Biomarkers ; Tropomyosin
    Language English
    Publishing date 2021-02-10
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2429704-5
    ISSN 1935-2735 ; 1935-2727
    ISSN (online) 1935-2735
    ISSN 1935-2727
    DOI 10.1371/journal.pntd.0009027
    Database MEDical Literature Analysis and Retrieval System OnLINE

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