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  1. Book: Enhancing plant water use efficiency to meet future food production

    Chaves, Maria Manuela / Vaz, M. / Torrecillas, A. / Pereira, J. S.

    (Agricultural water management ; Volume 164 (31 January 2016))

    2016  

    Author's details Edited by M. Vaz, A. Torrecillas and J. S. Pereira
    Series title Agricultural water management ; Volume 164 (31 January 2016)
    Collection
    Language English
    Size V, 196 Seiten, Illustrationen
    Publisher Elsevier
    Publishing place Amsterdam
    Publishing country Netherlands
    Document type Book
    HBZ-ID HT018867947
    Database Catalogue ZB MED Nutrition, Environment, Agriculture

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    In stock of ZB MED Bonn / Germany

    Shelf markLoan statusLocation
    Z 3189 (164) available for loan (reading room) Freihandmagazin (U1)

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  2. Article ; Online: O pensamento antropolóxico de Manuel M. Murguía. Raza e cultura

    Pereira González, Fernando

    Cuadernos de Estudios Gallegos, Vol 47, Iss 113, Pp 327-

    2000  Volume 382

    Abstract: Not avalaible No ... ...

    Abstract Not avalaible No disponible
    Keywords History of Spain ; DP1-402 ; History (General) and history of Europe ; D ; DOAJ:History ; DOAJ:History and Archaeology
    Language English
    Publishing date 2000-12-01T00:00:00Z
    Publisher Consejo Superior de Investigaciones Científicas
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

    Full text online

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  3. Article ; Online: The protein family of pyruvate:quinone oxidoreductases: Amino acid sequence conservation and taxonomic distribution.

    Sousa, Filipe M / Fernandes, Bárbara / Pereira, Manuela M

    Biochimica et biophysica acta. Bioenergetics

    2023  Volume 1864, Issue 2, Page(s) 148958

    Abstract: Pyruvate:quinone oxidoreductases (PQOs) catalyse the oxidative decarboxylation of pyruvate to acetate and concomitant reduction of quinone to quinol with the release of ... ...

    Abstract Pyruvate:quinone oxidoreductases (PQOs) catalyse the oxidative decarboxylation of pyruvate to acetate and concomitant reduction of quinone to quinol with the release of CO
    MeSH term(s) Amino Acid Sequence ; Pyruvic Acid ; Flavin-Adenine Dinucleotide/metabolism ; Proteins ; Quinone Reductases/metabolism ; Amino Acids ; NAD(P)H Dehydrogenase (Quinone)/metabolism ; Quinones
    Chemical Substances Pyruvic Acid (8558G7RUTR) ; Flavin-Adenine Dinucleotide (146-14-5) ; Proteins ; Quinone Reductases (EC 1.6.99.-) ; Amino Acids ; NAD(P)H Dehydrogenase (Quinone) (EC 1.6.5.2) ; Quinones
    Language English
    Publishing date 2023-02-07
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 60-7
    ISSN 1879-2650 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 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) 1879-2650 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618
    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.bbabio.2023.148958
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

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  4. Article: Valorisation of Wasted Immature Tomato to Innovative Fermented Functional Foods.

    Pereira, Nelson / Farrokhi, Mahsa / Vida, Manuela / Lageiro, Manuela / Ramos, Ana Cristina / Vieira, Margarida C / Alegria, Carla / Gonçalves, Elsa M / Abreu, Marta

    Foods (Basel, Switzerland)

    2023  Volume 12, Issue 7

    Abstract: In this study, the lactic fermentation of immature tomatoes as a tool for food ingredient production was evaluated as a circular economy-oriented alternative for valorising industrial tomatoes that are unsuitable for processing and which have wasted away ...

    Abstract In this study, the lactic fermentation of immature tomatoes as a tool for food ingredient production was evaluated as a circular economy-oriented alternative for valorising industrial tomatoes that are unsuitable for processing and which have wasted away in large quantities in the field. Two lactic acid bacteria (LAB) were assessed as starter cultures in an immature tomato pulp fermentation to produce functional food ingredients with probiotic potential. The first trial evaluated the probiotic character of
    Language English
    Publishing date 2023-04-04
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2704223-6
    ISSN 2304-8158
    ISSN 2304-8158
    DOI 10.3390/foods12071532
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Exploring substrate interaction in respiratory alternative complex III from Rhodothermus marinus.

    Calisto, Filipa / Todorovic, Smilja / Louro, Ricardo O / Pereira, Manuela M

    Biochimica et biophysica acta. Bioenergetics

    2023  Volume 1864, Issue 3, Page(s) 148983

    Abstract: Rhodothermus marinus is a thermohalophilic organism that has optimized its microaerobic metabolism at 65 °C. We have been exploring its respiratory chain and observed the existence of a quinone:cytochrome c oxidoreductase complex, named Alternative ... ...

    Abstract Rhodothermus marinus is a thermohalophilic organism that has optimized its microaerobic metabolism at 65 °C. We have been exploring its respiratory chain and observed the existence of a quinone:cytochrome c oxidoreductase complex, named Alternative Complex III, structurally different from the bc
    MeSH term(s) Electron Transport Complex III ; Cytochromes c ; Electron Transport ; Oxidoreductases
    Chemical Substances Electron Transport Complex III (EC 7.1.1.8) ; Cytochromes c (9007-43-6) ; Oxidoreductases (EC 1.-)
    Language English
    Publishing date 2023-04-29
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 60-7
    ISSN 1879-2650 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 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) 1879-2650 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618
    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.bbabio.2023.148983
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.247: Show issues Location:
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  6. Article: The Ion-Translocating NrfD-Like Subunit of Energy-Transducing Membrane Complexes.

    Calisto, Filipa / Pereira, Manuela M

    Frontiers in chemistry

    2021  Volume 9, Page(s) 663706

    Abstract: Several energy-transducing microbial enzymes have their peripheral subunits connected to the membrane through an integral membrane protein, that interacts with quinones but does not have redox cofactors, the so-called NrfD-like subunit. The periplasmic ... ...

    Abstract Several energy-transducing microbial enzymes have their peripheral subunits connected to the membrane through an integral membrane protein, that interacts with quinones but does not have redox cofactors, the so-called NrfD-like subunit. The periplasmic nitrite reductase (NrfABCD) was the first complex recognized to have a membrane subunit with these characteristics and consequently provided the family's name: NrfD. Sequence analyses indicate that NrfD homologs are present in many diverse enzymes, such as polysulfide reductase (PsrABC), respiratory alternative complex III (ACIII), dimethyl sulfoxide (DMSO) reductase (DmsABC), tetrathionate reductase (TtrABC), sulfur reductase complex (SreABC), sulfite dehydrogenase (SoeABC), quinone reductase complex (QrcABCD), nine-heme cytochrome complex (NhcABCD), group-2 [NiFe] hydrogenase (Hyd-2), dissimilatory sulfite-reductase complex (DsrMKJOP), arsenate reductase (ArrC) and multiheme cytochrome
    Language English
    Publishing date 2021-04-13
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2711776-5
    ISSN 2296-2646
    ISSN 2296-2646
    DOI 10.3389/fchem.2021.663706
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Modularity of membrane-bound charge-translocating protein complexes.

    Calisto, Filipa / Pereira, Manuela M

    Biochemical Society transactions

    2021  Volume 49, Issue 6, Page(s) 2669–2685

    Abstract: Energy transduction is the conversion of one form of energy into another; this makes life possible as we know it. Organisms have developed different systems for acquiring energy and storing it in useable forms: the so-called energy currencies. A ... ...

    Abstract Energy transduction is the conversion of one form of energy into another; this makes life possible as we know it. Organisms have developed different systems for acquiring energy and storing it in useable forms: the so-called energy currencies. A universal energy currency is the transmembrane difference of electrochemical potential (Δμ~). This results from the translocation of charges across a membrane, powered by exergonic reactions. Different reactions may be coupled to charge-translocation and, in the majority of cases, these reactions are catalyzed by modular enzymes that always include a transmembrane subunit. The modular arrangement of these enzymes allows for different catalytic and charge-translocating modules to be combined. Thus, a transmembrane charge-translocating module can be associated with different catalytic subunits to form an energy-transducing complex. Likewise, the same catalytic subunit may be combined with a different membrane charge-translocating module. In this work, we analyze the modular arrangement of energy-transducing membrane complexes and discuss their different combinations, focusing on the charge-translocating module.
    MeSH term(s) Catalytic Domain ; Cell Membrane/chemistry ; Membrane Proteins/chemistry
    Chemical Substances Membrane Proteins
    Language English
    Publishing date 2021-12-02
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 184237-7
    ISSN 1470-8752 ; 0300-5127
    ISSN (online) 1470-8752
    ISSN 0300-5127
    DOI 10.1042/BST20210462
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 944: Show issues Location:
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    Jg. 1995 - 2021: Lesesall (1.OG)
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  8. Article ; Online: The Ion-Translocating NrfD-Like Subunit of Energy-Transducing Membrane Complexes

    Filipa Calisto / Manuela M. Pereira

    Frontiers in Chemistry, Vol

    2021  Volume 9

    Abstract: Several energy-transducing microbial enzymes have their peripheral subunits connected to the membrane through an integral membrane protein, that interacts with quinones but does not have redox cofactors, the so-called NrfD-like subunit. The periplasmic ... ...

    Abstract Several energy-transducing microbial enzymes have their peripheral subunits connected to the membrane through an integral membrane protein, that interacts with quinones but does not have redox cofactors, the so-called NrfD-like subunit. The periplasmic nitrite reductase (NrfABCD) was the first complex recognized to have a membrane subunit with these characteristics and consequently provided the family's name: NrfD. Sequence analyses indicate that NrfD homologs are present in many diverse enzymes, such as polysulfide reductase (PsrABC), respiratory alternative complex III (ACIII), dimethyl sulfoxide (DMSO) reductase (DmsABC), tetrathionate reductase (TtrABC), sulfur reductase complex (SreABC), sulfite dehydrogenase (SoeABC), quinone reductase complex (QrcABCD), nine-heme cytochrome complex (NhcABCD), group-2 [NiFe] hydrogenase (Hyd-2), dissimilatory sulfite-reductase complex (DsrMKJOP), arsenate reductase (ArrC) and multiheme cytochrome c sulfite reductase (MccACD). The molecular structure of ACIII subunit C (ActC) and Psr subunit C (PsrC), NrfD-like subunits, revealed the existence of ion-conducting pathways. We performed thorough primary structural analyses and built structural models of the NrfD-like subunits. We observed that all these subunits are constituted by two structural repeats composed of four-helix bundles, possibly harboring ion-conducting pathways and containing a quinone/quinol binding site. NrfD-like subunits may be the ion-pumping module of several enzymes. Our data impact on the discussion of functional implications of the NrfD-like subunit-containing complexes, namely in their ability to transduce energy.
    Keywords NrfD-like ; membrane protein ; ion translocation ; quinine/quinol binding site ; CISM family ; energy transduction ; Chemistry ; QD1-999
    Language English
    Publishing date 2021-04-01T00:00:00Z
    Publisher Frontiers Media S.A.
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

    Full text online

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  9. Article ; Online: The protein family of pyruvate:quinone oxidoreductases: Amino acid sequence conservation and taxonomic distribution

    Sousa, Filipe M. / Fernandes, Barbara / Pereira, Manuela M.

    BBA - Bioenergetics. 2023 Apr., v. 1864, no. 2 p.148958-

    2023  

    Abstract: Pyruvate:quinone oxidoreductases (PQOs) catalyse the oxidative decarboxylation of pyruvate to acetate and concomitant reduction of quinone to quinol with the release of CO₂. They are thiamine pyrophosphate (TPP) and flavin-adenine dinucleotide (FAD) ... ...

    Abstract Pyruvate:quinone oxidoreductases (PQOs) catalyse the oxidative decarboxylation of pyruvate to acetate and concomitant reduction of quinone to quinol with the release of CO₂. They are thiamine pyrophosphate (TPP) and flavin-adenine dinucleotide (FAD) containing enzymes, which interact with the membrane in a monotopic way. PQOs are considered as part of alternatives to most recognized pyruvate catabolizing pathways, and little is known about their taxonomic distribution and structural/functional relationship. In this bioinformatics work we tackled these gaps in PQO knowledge. We used the KEGG database to identify PQO coding genes, performed a multiple sequence analysis which allowed us to study the amino acid conservation on these enzymes, and looked at their possible cellular function. We observed that PQOS are enzymes exclusively present in prokaryotes with most of the sequences identified in bacteria. Regarding the amino acid sequence conservation, we found that 75 amino acid residues (out of 570, on average) have a conservation over 90 %, and that the most conserved regions in the protein are observed around the TPP and FAD binding sites. We systematized the presence of conserved features involved in Mg²⁺, TPP and FAD binding, as well as residues directly linked to the catalytic mechanism. We also established the presence of a new motif named "HEH lock", possibly involved in the dimerization process. The results here obtained for the PQO protein family contribute to a better understanding of the biochemistry of these respiratory enzymes.
    Keywords acetates ; amino acid sequences ; amino acids ; bioinformatics ; carbon dioxide ; databases ; decarboxylation ; dimerization ; energy metabolism ; flavin-adenine dinucleotide ; germplasm conservation ; oxidoreductases ; prokaryotic cells ; pyruvic acid ; quinones ; sequence analysis ; thiamin ; Respiratory chain ; Monotopic quinone reductases ; Flavoproteins ; Thiamine pyrophosphate ; Taxonomic profile ; Amino-acid residue conservation ; Pyruvate metabolism
    Language English
    Dates of publication 2023-04
    Publishing place Elsevier B.V.
    Document type Article ; Online
    Note Use and reproduction
    ZDB-ID 282711-6
    ISSN 0005-2728 ; 0304-4173
    ISSN 0005-2728 ; 0304-4173
    DOI 10.1016/j.bbabio.2023.148958
    Database NAL-Catalogue (AGRICOLA)

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  10. Article: Improving γ-Oryzanol and γ-Aminobutyric Acid Contents in Rice Beverage

    Castanho, Ana / Pereira, Cristiana / Lageiro, Manuela / Oliveira, Jorge C / Cunha, Luís M / Brites, Carla

    Foods (Basel, Switzerland)

    2023  Volume 12, Issue 7

    Abstract: Rice is an important source of γ-oryzanol (GO) and γ-aminobutyric acid (GABA), which are bioactive compounds that may benefit blood lipid and pressure control. Both GO and GABA can be improved by germination and fermentation. Fermentation ... ...

    Abstract Rice is an important source of γ-oryzanol (GO) and γ-aminobutyric acid (GABA), which are bioactive compounds that may benefit blood lipid and pressure control. Both GO and GABA can be improved by germination and fermentation. Fermentation with
    Language English
    Publishing date 2023-03-31
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2704223-6
    ISSN 2304-8158
    ISSN 2304-8158
    DOI 10.3390/foods12071476
    Database MEDical Literature Analysis and Retrieval System OnLINE

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