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1.
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11 p, 1.1 MB |
Divergent soil P accrual in ectomycorrhizal and arbuscular mycorrhizal trees : insights from a common garden experiment in subtropical China
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Pingping, Lian (Fujian Normal University. School of Geographical Science) ;
Xu, Linglin (Fujian Normal University. Institute of Geography) ;
Yang, Liuming (Fujian Normal University. School of Geographical Science) ;
Yue, Kai (Fujian Normal University. School of Geographical Science) ;
Peñuelas, Josep (Centre de Recerca Ecològica i d'Aplicacions Forestals)
Tree species establish mycorrhizal associations with both ectomycorrhizal (EM) and arbuscular mycorrhizal fungi (AM), which play crucial roles in facilitating plant phosphorus (P) acquisition. However, little attention has been given to the effects of EM and AM species on soil P dynamics and the underlying mechanisms in subtropical forests, where P availability is typically low. [...]
2024 -  10.3389/fpls.2024.1333505
Frontiers in plant science, Vol. 15 (2024) , art. 1333505
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2.
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31 p, 986.9 KB |
Engineering aldo-keto reductase 1B10 to mimic the distinct 1B15 topology and specificity towards inhibitors and substrates, including retinoids and steroids
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Giménez-Dejoz, Joan (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Weber, Susanne (Research Unit Molecular Endocrinology and Metabolism, Helmholtz Zentrum München) ;
Fernández-Pardo, Álvaro (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Möller, Gabriele (Research Unit Molecular Endocrinology and Metabolism, Helmholtz Zentrum München) ;
Adamski, Jerzy (Research Unit Molecular Endocrinology and Metabolism, Helmholtz Zentrum München) ;
Porté, Sergio (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Parés i Casasampera, Xavier (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Farrés, Jaume (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
The aldo-keto reductase (AKR)superfamily comprises NAD(P)H-dependent enzymes that catalyze the reduction of a variety of carbonyl compounds. AKRs are classified in families and subfamilies. Humans exhibit three members of the AKR1B subfamily: AKR1B1 (aldose reductase, participates in diabetes complications), AKR1B10 (overexpressed in several cancer types), and the recently described AKR1B15. [...]
2019 - 10.1016/j.cbi.2019.04.030
Chemico-Biological Interactions, Vol. 307 (2019) , p. 186-194
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3.
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34 p, 1.3 MB |
Inhibitors of aldehyde dehydrogenases of the 1A subfamily as putative anticancer agents : Kinetic characterization and effect on human cancer cells
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Jiménez, Rafael (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Pequerul, Raquel (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Amor Minguez, Adrián (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Lorenzo Rivera, Julia (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Metwally, Kamel (Zagazig University. Department of Medicinal Chemistry) ;
Avilés, Francesc X (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Parés i Casasampera, Xavier (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Farrés, Jaume (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Aldehyde dehydrogenases (ALDHs) are enzymes catalyzing the NAD(P)+-dependent oxidation of aldehydes to their corresponding carboxylic acids. High ALDH activity has been related to some important features of cancer stem cells. [...]
2019 - 10.1016/j.cbi.2019.04.004
Chemico-Biological Interactions, Vol. 306 (2019) , p. 123-130
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4.
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56 p, 850.1 KB |
Molecular identification of aminoglycoside-modifying enzymes in clinical isolates of Escherichia coli resistant to amoxicillin/clavulanic acid isolated in Spain
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Fernández-Martínez, Marta (Hospital Universitario Marqués de Valdecilla (Santander, Cantabria)) ;
Miró, Elisenda (Institut d'Investigació Biomèdica Sant Pau) ;
Ortega, Adriana (Centro Nacional de Microbiología (Espanya)) ;
Bou, German (Complejo Hospitalario Universitario de A Coruña) ;
González, Juan José (Hospital Universitari Vall d'Hebron) ;
Oliver, Antonio (Hospital Universitari Son Espases (Palma de Mallorca, Balears)) ;
Pascual Hernández, Álvaro (Hospital Universitario Virgen Macarena (Sevilla, Andalusia)) ;
Cercenado, Emilia (Hospital General Universitario Gregorio Marañón) ;
Oteo-Iglesias, Jesús (Centro de Investigación Biomédica en Red de Enfermedades Respiratorias) ;
Martínez-Martínez, Luis (Hospital Universitario Marqués de Valdecilla (Santander, Cantabria)) ;
Navarro Risueño, Ferran (Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia)
The activity of eight aminoglycosides (amikacin, apramycin, arbekacin, gentamicin, kanamycin, neomycin, netilmicin and tobramycin) against a collection of 257 amoxicillin/clavulanic acid (AMC)-resistant Escherichia coli isolates was determined by microdilution. [...]
2015 - 10.1016/j.ijantimicag.2015.03.008
International Journal of Antimicrobial Agents, Vol. 46, Issue 2 (August 2015) , p. 157-163
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5.
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18 p, 2.0 MB |
Establishing In-House Cutoffs of CSF Alzheimer's Disease Biomarkers for the AT(N) Stratification of the Alzheimer Center Barcelona Cohort
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Orellana, Adelina (Universitat Internacional de Catalunya. Ace Alzheimer Center Barcelona) ;
0000-0003-0125-5403 García-gonzález, Pablo (Universitat Internacional de Catalunya. Ace Alzheimer Center Barcelona) ;
Valero, Sergi (Centro de Investigación Biomédica en Red sobre Enfermedades Neurodegenerativas) ;
Montrreal, Laura (Universitat Internacional de Catalunya. Ace Alzheimer Center Barcelona) ;
De Rojas, Itziar (Centro de Investigación Biomédica en Red sobre Enfermedades Neurodegenerativas) ;
Hernández, Isabel (Centro de Investigación Biomédica en Red sobre Enfermedades Neurodegenerativas) ;
Rosende-roca, Maitee (Universitat Internacional de Catalunya. Ace Alzheimer Center Barcelona) ;
Vargas, Liliana (Universitat Internacional de Catalunya. Ace Alzheimer Center Barcelona) ;
Tartari, Juan Pablo (Universitat Internacional de Catalunya. Ace Alzheimer Center Barcelona) ;
Esteban de Antonio, Ester (Universitat Internacional de Catalunya. Ace Alzheimer Center Barcelona) ;
Bojaryn, Urszula (Universitat Internacional de Catalunya. Ace Alzheimer Center Barcelona) ;
Narvaiza, Leire (Universitat Internacional de Catalunya. Ace Alzheimer Center Barcelona) ;
Alarcón-Martín, Emilio (Universitat Internacional de Catalunya. Ace Alzheimer Center Barcelona) ;
Alegret, Montserrat (Centro de Investigación Biomédica en Red sobre Enfermedades Neurodegenerativas) ;
Alcolea, Daniel (Institut d'Investigació Biomèdica Sant Pau) ;
Lleó, Alberto (Institut d'Investigació Biomèdica Sant Pau) ;
Tárraga, Lluís (Centro de Investigación Biomédica en Red sobre Enfermedades Neurodegenerativas) ;
Pytel, Vanesa (Universitat Internacional de Catalunya. Ace Alzheimer Center Barcelona) ;
Cano, Amanda (Centro de Investigación Biomédica en Red sobre Enfermedades Neurodegenerativas) ;
Marquié, Marta. (Centro de Investigación Biomédica en Red sobre Enfermedades Neurodegenerativas) ;
Boada, Mercè (Centro de Investigación Biomédica en Red sobre Enfermedades Neurodegenerativas) ;
Ruiz, Agustín (Centro de Investigación Biomédica en Red sobre Enfermedades Neurodegenerativas) ;
Universitat Autònoma de Barcelona
Background: Clinical diagnosis of Alzheimer's disease (AD) increasingly incorporates CSF biomarkers. However, due to the intrinsic variability of the immunodetection techniques used to measure these biomarkers, establishing in-house cutoffs defining the positivity/negativity of CSF biomarkers is recommended. [...]
2022 - 10.3390/ijms23136891
International journal of molecular sciences, Vol. 23 Núm. 13 (july 2022) , p. 6891
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14 p, 7.3 MB |
Distal Mutations Shape Substrate-Binding Sites during Evolution of a Metallo-Oxidase into a Laccase
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Brissos, Vânia (Universidade Nova de Lisboa) ;
Borges, Patrícia T. (Universidade Nova de Lisboa) ;
Núñez-Franco, Reyes (Zymvol Biomodeling) ;
Lucas, Maria Fátima (Zymvol Biomodeling) ;
Frazão, Carlos (Universidade Nova de Lisboa) ;
Monza, Emanuele (Zymvol Biomodeling) ;
Masgrau, Laura (Universitat Autònoma de Barcelona. Departament de Química) ;
Cordeiro, Tiago N. (Universidade Nova de Lisboa) ;
Martins, Lígia O. (Universidade Nova de Lisboa)
Laccases are in increasing demand as innovative solutions in the biorefinery fields. Here, we combine mutagenesis with structural, kinetic, and in silico analyses to characterize the molecular features that cause the evolution of a hyperthermostable metallo-oxidase from the multicopper oxidase family into a laccase (k 273 s -1 for a bulky aromatic substrate). [...]
2022 - 10.1021/acscatal.2c00336
ACS catalysis, Vol. 12, Issue 9 (April 2022) , p. 5022-5035
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7.
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17 p, 7.9 MB |
Defect-free graphene enhances enzyme delivery to fibroblasts derived from patients with lysosomal storage disorders
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Chen, Yingxian (University of Manchester. Nanomedicine Lab) ;
Taufiq, Tooba (The University of Manchester) ;
Zeng, Niting (University of Manchester. Department of Chemistry) ;
Lozano, Neus (Institut Català de Nanociència i Nanotecnologia) ;
Karakasidi, Angeliki (University of Manchester. Nanomedicine Lab) ;
Church, Heather (Manchester Centre for Genomic Medicine) ;
Jovanovic, Ana (Salford Royal NHS Foundation Trust) ;
Jones, Simon A. (Manchester Centre for Genomic Medicine) ;
Panigrahi, Adyasha (University of Manchester. Department of Chemistry) ;
Larrosa, Igor (University of Manchester. Department of Chemistry) ;
Kostarelos, Kostas (Institut Català de Nanociència i Nanotecnologia) ;
Casiraghi, Cinzia (University of Manchester. Department of Chemistry) ;
Vranic, Sandra (University of Manchester. Nanomedicine Lab)
Enzyme replacement therapy shows remarkable clinical improvement in treating lysosomal storage disorders. However, this therapeutic approach is hampered by limitations in the delivery of the enzyme to cells and tissues. [...]
2023 - 10.1039/d2nr04971f
Nanoscale, Vol. 15, Issue 21 (June 2023) , p. 9348-9364
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37 p, 16.6 MB |
Marine Invertebrates : A Promissory Still Unexplored Source of Inhibitors of Biomedically Relevant Metallo Aminopeptidases Belonging to the M1 and M17 Families
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Pascual Alonso, Isel (University of Havana. Center for Protein Studies) ;
Almeida García, Fabiola (University of Havana. Center for Protein Studies) ;
Valdés Tresanco, Mario Ernesto (University of Calgary. Department of Biological Sciences) ;
Arrebola Sánchez, Yarini (University of Havana. Center for Protein Studies) ;
Ojeda del Sol, Daniel (University of Havana. Center for Protein Studies) ;
Sánchez Ramírez, Belinda (Centro de Inmunología Molecular) ;
Florent, Isabelle (Muséum National d'Histoire Naturelle) ;
Schmitt, Marjorie (Université de Strasbourg) ;
Avilés, Francesc X. (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Universitat Autònoma de Barcelona.
Departament de Bioquímica i de Biologia Molecular
Proteolytic enzymes, also known as peptidases, are critical in all living organisms. Peptidases control the cleavage, activation, turnover, and synthesis of proteins and regulate many biochemical and physiological processes. [...]
2023 - 10.3390/md21050279
Marine drugs, Vol. 21, Issue 5 (April 2023) , art. 279
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29 p, 20.1 MB |
Hydroperoxidation of Docosahexaenoic Acid by Human ALOX12 and pigALOX15-mini-LOX
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Canyelles-Niño, Miquel (Universitat Autònoma de Barcelona. Departament de Química) ;
González-Lafont, Àngels (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Lluch López, Josep Maria (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Human lipoxygenase 12 (hALOX12) catalyzes the conversion of docosahexaenoic acid (DHA) into mainly 14S-hydroperoxy-4Z,7Z,10Z,12E,16Z,19Z-docosahexaenoic acid (14S-H(p)DHA). This hydroperoxidation reaction is followed by an epoxidation and hydrolysis process that finally leads to maresin 1 (MaR1), a potent bioactive specialized pro-resolving mediator (SPM) in chronic inflammation resolution. [...]
2023 - 10.3390/ijms24076064
International journal of molecular sciences, Vol. 24, Issue 7 (April 2023) , art. 6064
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