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  1. Book: La pervivència del rei En Jaume

    Quintana i Torres, Antoni J / Calafat i Vila, Rosa M

    (Menjavents ; 5)

    1992  

    Author's details Antoni J. Quintana ; Rosa M. Calafat
    Series title Menjavents ; 5
    Language Catalan
    Size 194 S, Ill.
    Edition 1. ed
    Publisher Ed. Documenta Balear
    Publishing place Palma
    Document type Book
    ISBN 8460445631 ; 9788460445630
    Database Former special subject collection: coastal and deep sea fishing

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  2. Article ; Online: GRAU, Vicent, La Segona República a Castelló. Una memoria històrica positiva, pròleg de Rosa Monlleó, Castelló de la Plana, Publicacions de la Universitat Jaume I, 2012, 465 pp.

    Ricard Camil Torres Fabra

    Pasado y Memoria, Iss 11, Pp 307-

    2012  Volume 311

    Keywords Segunda República ; Castellón ; Reseñas bibliográficas ; History (General) and history of Europe ; D
    Language Catalan
    Publishing date 2012-10-01T00:00:00Z
    Publisher Universidad de Alicante
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  3. Article ; Online: Channel Formation in Cry Toxins: An Alphafold-2 Perspective.

    Torres, Jaume / Surya, Wahyu / Boonserm, Panadda

    International journal of molecular sciences

    2023  Volume 24, Issue 23

    Abstract: ... Bacillus ... ...

    Abstract Bacillus thuringiensis
    MeSH term(s) Animals ; Bacillus thuringiensis Toxins ; Furylfuramide/metabolism ; Endotoxins/toxicity ; Hemolysin Proteins/metabolism ; Bacillus thuringiensis/chemistry ; Bacterial Proteins/metabolism ; Larva
    Chemical Substances insecticidal crystal protein, Bacillus Thuringiensis ; Bacillus thuringiensis Toxins ; Furylfuramide (054NR2135Y) ; Endotoxins ; Hemolysin Proteins ; Bacterial Proteins
    Language English
    Publishing date 2023-11-27
    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/ijms242316809
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Reply to: "Carvedilol in patients with compensated cirrhosis: The ongoing benefits of definitive randomised trials over meta-analysis in patients with small varices".

    Villanueva, Càndid / Torres, Ferran / Tripathi, Dhiraj / Bosch, Jaume

    Journal of hepatology

    2023  Volume 79, Issue 1, Page(s) e23–e24

    MeSH term(s) Humans ; Carvedilol/therapeutic use ; Liver Cirrhosis/complications ; Esophageal and Gastric Varices/etiology ; Varicose Veins ; Longitudinal Studies ; Gastrointestinal Hemorrhage ; Randomized Controlled Trials as Topic
    Chemical Substances Carvedilol (0K47UL67F2)
    Language English
    Publishing date 2023-02-25
    Publishing country Netherlands
    Document type Meta-Analysis ; Letter ; Research Support, Non-U.S. Gov't ; Comment
    ZDB-ID 605953-3
    ISSN 1600-0641 ; 0168-8278
    ISSN (online) 1600-0641
    ISSN 0168-8278
    DOI 10.1016/j.jhep.2023.02.025
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Oligomerization-Dependent Beta-Structure Formation in SARS-CoV-2 Envelope Protein.

    Surya, Wahyu / Torres, Jaume

    International journal of molecular sciences

    2022  Volume 23, Issue 21

    Abstract: The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is responsible for the current COVID-19 pandemic. In SARS-CoV-2, the channel-forming envelope (E) protein is almost identical to the E protein in SARS-CoV, and both share an identical α- ... ...

    Abstract The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is responsible for the current COVID-19 pandemic. In SARS-CoV-2, the channel-forming envelope (E) protein is almost identical to the E protein in SARS-CoV, and both share an identical α-helical channel-forming domain. Structures for the latter are available in both detergent and lipid membranes. However, models of the extramembrane domains have only been obtained from solution NMR in detergents, and show no β-strands, in contrast to secondary-structure predictions. Herein, we have studied the conformation of purified SARS-CoV-2 E protein in lipid bilayers that mimic the composition of ER-Golgi intermediate compartment (ERGIC) membranes. The full-length E protein at high protein-to-lipid ratios produced a clear shoulder at 1635 cm
    MeSH term(s) Humans ; SARS-CoV-2 ; Detergents ; Pandemics ; COVID-19 ; Lipid Bilayers/chemistry
    Chemical Substances Detergents ; Lipid Bilayers
    Language English
    Publishing date 2022-10-31
    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/ijms232113285
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Oligomerization-Dependent Beta-Structure Formation in SARS-CoV-2 Envelope Protein

    Wahyu Surya / Jaume Torres

    International Journal of Molecular Sciences, Vol 23, Iss 13285, p

    2022  Volume 13285

    Abstract: The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is responsible for the current COVID-19 pandemic. In SARS-CoV-2, the channel-forming envelope (E) protein is almost identical to the E protein in SARS-CoV, and both share an identical α- ... ...

    Abstract The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is responsible for the current COVID-19 pandemic. In SARS-CoV-2, the channel-forming envelope (E) protein is almost identical to the E protein in SARS-CoV, and both share an identical α-helical channel-forming domain. Structures for the latter are available in both detergent and lipid membranes. However, models of the extramembrane domains have only been obtained from solution NMR in detergents, and show no β-strands, in contrast to secondary-structure predictions. Herein, we have studied the conformation of purified SARS-CoV-2 E protein in lipid bilayers that mimic the composition of ER–Golgi intermediate compartment (ERGIC) membranes. The full-length E protein at high protein-to-lipid ratios produced a clear shoulder at 1635 cm −1 , consistent with the β-structure, but this was absent when the E protein was diluted, which instead showed a band at around 1688 cm −1 , usually assigned to β-turns. The results were similar with a mixture of POPC:POPG (2-oleoyl-1-palmitoyl-sn-glycero-3-phosphocholine/3-glycerol) and also when using an E-truncated form (residues 8–65). However, the latter only showed β-structure formation at the highest concentration tested, while having a weaker oligomerization tendency in detergents than in full-length E protein. Therefore, we conclude that E monomer–monomer interaction triggers formation of the β-structure from an undefined structure (possibly β-turns) in at least about 15 residues located at the C-terminal extramembrane domain. Due to its proximity to the channel, this β-structure domain could modulate channel activity or modify membrane structure at the time of virion formation inside the cell.
    Keywords envelope protein ; SARS-CoV-2 ; ion channel ; Fourier-transform infrared spectroscopy ; analytical ultracentrifugation ; conformational change ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
    Subject code 572
    Language English
    Publishing date 2022-10-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  7. Article ; Online: The cytoplasmic N-terminal tail of Zika virus NS4A protein forms oligomers in the absence of detergent or lipids.

    Surya, Wahyu / Liu, Yiting / Torres, Jaume

    Scientific reports

    2023  Volume 13, Issue 1, Page(s) 7360

    Abstract: The non-structural (NS) NS4A protein in flaviviruses has three predicted transmembrane domains, is critical for virulence and participates in membrane morphogenesis. In Dengue virus (DENV), both hydrophylic N-terminal tail and its first transmembrane ... ...

    Abstract The non-structural (NS) NS4A protein in flaviviruses has three predicted transmembrane domains, is critical for virulence and participates in membrane morphogenesis. In Dengue virus (DENV), both hydrophylic N-terminal tail and its first transmembrane domain participate in the formation of oligomers which are important for pathogenicity. However, the relative importance of the N-terminal domain in oligomerization has been under debate. In particular, since in the absence of detergent or lipids, this domain (residues 1-48) in both DENV and Zika virus (ZIKV) NS4A, was found to be disordered. Recently, however, we reported preliminary data that showed that peptide ZIKV NS4A 4-58 adopts a defined secondary structure in aqueous solution and forms oligomers, signaling its importance for full length NS4A oligomerization. Herein we have performed detailed analytical ultracentrifugation experiments to further characterize the oligomerization of this peptide and also a shorter variant (residues 4-44). In both cases, sedimentation velocity produced a single species with concentration-dependent sedimentation coefficient, consistent with a fast equilibrium between at least two species. Combining sedimentation velocity and equilibrium experiments, data is best fitted to a monomer-dimer-trimer equilibrium. Possible models of NS4A oligomers obtained with AlphaFold-2 predict the stabilizing role for residues in this N-terminal domain, such as Arg20, Asn27, Ala44 and Glu50, all at highly conserved positions in flavivirus NS4A proteins. Our results are thus consistent with N-terminal domain interactions acting as one of the driving forces for NS4A homo-oligomerization.
    MeSH term(s) Humans ; Zika Virus/metabolism ; Detergents/metabolism ; Dengue Virus/metabolism ; Zika Virus Infection ; Viral Nonstructural Proteins/metabolism ; Lipids
    Chemical Substances Detergents ; Viral Nonstructural Proteins ; Lipids
    Language English
    Publishing date 2023-05-05
    Publishing country England
    Document type Journal Article
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-023-34621-x
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Engineering Ultra-Permeable and Antifouling Water Channel-based Biomimetic Membranes toward Sustainable Water Purification

    Xuesong Li / Linyan Yang / Jaume Torres / Rong Wang

    Journal of Membrane Science Letters, Vol 3, Iss 2, Pp 100049- (2023)

    2023  

    Abstract: Water channel-based biomimetic membranes (WBMs) are gaining increasing attention due to the effectiveness of water channels in enhancing water permeability and breaking the permselectivity trade-off. However, the ultra-permeable WBMs may suffer from ... ...

    Abstract Water channel-based biomimetic membranes (WBMs) are gaining increasing attention due to the effectiveness of water channels in enhancing water permeability and breaking the permselectivity trade-off. However, the ultra-permeable WBMs may suffer from severe membrane fouling issue because a high-water flux tends to result in an accelerated fouling and thus compromises the benefits gained from the usage of water channels. Herein, a novel in-situ modification protocol was proposed to enhance the antifouling performance of ultra-permeable WBMs. The nanovesicles incorporated with aquaporin (AQP) water channels were functionalized with polyethylene glycol brushes (i.e., PEGylation) via a facile self-assembly approach and subsequently encapsulated in the selective layer of thin-film composite membranes through interfacial polymerization. The modification had minimal impact on the function of AQPs, resulting in WBMs with a high water permeance (∼8.2 LMH/bar) and good NaCl rejection (96.4%) comparable to the unmodified WBMs. Moreover, the in-situ modification drastically enhanced the surface hydrophilicity, which endowed the membrane with a superior fouling resistance to organic foulants. The improved fouling resistance ensured a more sustainable operation of ultra-permeable WBMs, particularly in scenarios that favor high water fluxes. This facile modification strategy provides an efficient way to fabricate ultra-permeable and antifouling WBMs for sustainable water purification.
    Keywords water channel ; highly permeable membranes ; antifouling performance ; in-situ modification ; PEGylation ; Chemistry ; QD1-999
    Subject code 550
    Language English
    Publishing date 2023-11-01T00:00:00Z
    Publisher Elsevier
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  9. Article ; Online: Channel Formation in Cry Toxins

    Jaume Torres / Wahyu Surya / Panadda Boonserm

    International Journal of Molecular Sciences, Vol 24, Iss 23, p

    An Alphafold-2 Perspective

    2023  Volume 16809

    Abstract: Bacillus thuringiensis (Bt) strains produce pore-forming toxins (PFTs) that attack insect pests. Information for pre-pore and pore structures of some of these Bt toxins is available. However, for the three-domain (I-III) crystal (Cry) toxins, the most ... ...

    Abstract Bacillus thuringiensis (Bt) strains produce pore-forming toxins (PFTs) that attack insect pests. Information for pre-pore and pore structures of some of these Bt toxins is available. However, for the three-domain (I-III) crystal (Cry) toxins, the most used Bt toxins in pest control, this crucial information is still missing. In these Cry toxins, biochemical data have shown that 7-helix domain I is involved in insertion in membranes, oligomerization and formation of a channel lined mainly by helix α4, whereas helices α1 to α3 seem to have a dynamic role during insertion. In the case of Cry1Aa, toxic against Manduca sexta larvae, a tetrameric oligomer seems to precede membrane insertion. Given the experimental difficulty in the elucidation of the membrane insertion steps, we used Alphafold-2 (AF2) to shed light on possible oligomeric structural intermediates in the membrane insertion of this toxin. AF2 very accurately (<1 Å RMSD) predicted the crystal monomeric and trimeric structures of Cry1Aa and Cry4Ba. The prediction of a tetramer of Cry1Aa, but not Cry4Ba, produced an ‘extended model’ where domain I helices α3 and α2b form a continuous helix and where hydrophobic helices α1 and α2 cluster at the tip of the bundle. We hypothesize that this represents an intermediate that binds the membrane and precedes α4/α5 hairpin insertion, together with helices α6 and α7. Another Cry1Aa tetrameric model was predicted after deleting helices α1 to α3, where domain I produced a central cavity consistent with an ion channel, lined by polar and charged residues in helix α4. We propose that this second model corresponds to the ‘membrane-inserted’ structure. AF2 also predicted larger α4/α5 hairpin n-mers (14 ≤ n ≤ 17) with high confidence, which formed even larger (~5 nm) pores. The plausibility of these models is discussed in the context of available experimental data and current paradigms.
    Keywords Cry toxins ; Alphafold ; pore formation ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
    Subject code 612
    Language English
    Publishing date 2023-11-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  10. Article ; Online: Positive cooperativity in the activation of E. coli aquaporin Z by cardiolipin: Potential for lipid-based aquaporin modulators.

    Tan, Cephas Li-Jie / Torres, Jaume

    Biochimica et biophysica acta. Molecular and cell biology of lipids

    2021  Volume 1866, Issue 5, Page(s) 158899

    MeSH term(s) Aquaporins/genetics ; Aquaporins/metabolism ; Cardiolipins/genetics ; Cardiolipins/metabolism ; Cell Membrane/genetics ; Cell Membrane/metabolism ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/metabolism
    Chemical Substances Aquaporins ; Cardiolipins ; Escherichia coli Proteins ; aqpZ protein, E coli
    Language English
    Publishing date 2021-02-11
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 60-7
    ISSN 1879-2618 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1879-2618 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2650
    ISSN 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbalip.2021.158899
    Database MEDical Literature Analysis and Retrieval System OnLINE

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