Enea Sancho-Vaello

@uab.cat

Tenure-track lecturer at Department of Biochemistry and Molecular Biology
Universitata Autònoma de Barcelona

Enea Sancho-Vaello


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https://researchid.co/enea_sv

RESEARCH, TEACHING, or OTHER INTERESTS

Biochemistry, Genetics and Molecular Biology, Molecular Biology, Structural Biology
23

Scopus Publications

884

Scholar Citations

18

Scholar h-index

20

Scholar i10-index

Scopus Publications

  • Structure of a barrel-stave pore formed by magainin-2 reveals anion selectivity and zipper-mediated assembly
    Enea Sancho-Vaello, Harun Kücükyildiz, David Gil-Carton, Xevi Biarnés, Kornelius Zeth
    Scientific Reports, 2025
    Antimicrobial peptides (AMPs) are ubiquitous weapons of all higher organisms to suppress antimicrobial growth. Despite intensive research, the killing mechanism of these peptides after interaction with the bacterial cell wall and cytoplasm is not well understood. To investigate this mechanism at a molecular level, we chose a well-studied AMP, Magainin-2 (Mag-2), for biophysical and structural studies. Circular dichroism experiments showed that the folding propensity of Mag-2 is strongly altered towards fully folded molecules in the presence of detergent. To study the pore-forming properties of Mag-2 in membranes, we crystallized the wild-type peptide in the presence of the membrane-mimicking dodecylphosphocholine detergent and obtained crystals diffracting to atomic resolution. Mag-2 structure shows an antiparallel arrangement of monomers, which is stabilised by a phenylalanine zipper motif spanning the hydrophobic interaction surface of this dimer. Trimerization of dimers leads to the formation of a hexameric peptide channel complex with a positively charged pore and a hydrophobic membrane-exposed belt. Using molecular dynamics simulations, a spontaneous flow of ions through this channel was observed, demonstrating anion-selectivity induced by the electrostatic potential characteristics of Mag-2. This first atomic-resolution structure of wild-type Mag-2 showing oligomerization will allow the rational design of improved Mag-2 peptide channels.
  • Targeting MarA N-terminal domain dynamics to prevent DNA binding
    Marina Corbella, Cátia Moreira, Roberto Bello‐Madruga, Marc Torrent Burgas, Shina C. L. Kamerlin, Jessica M. A. Blair, Enea Sancho‐Vaello
    Protein Science, 2025
    Efflux is one of the mechanisms employed by Gram‐negative bacteria to become resistant to routinely used antibiotics. The inhibition of efflux by targeting their regulators is a promising strategy to re‐sensitize bacterial pathogens to antibiotics. AcrAB–TolC is the main resistance‐nodulation‐division efflux pump in Enterobacteriaceae. MarA is an AraC/XylS family global regulator that regulates more than 40 genes related to the antimicrobial resistance phenotype, including acrAB. The aim of this work was to understand the role of the N‐terminal helix of MarA in the mechanism of DNA binding. An N‐terminal deletion of MarA showed that the N‐terminal helix is critical for recognition of the functional marboxes. By engineering two double cysteine variants of MarA that form a disulfide bond between the N‐terminal helix and the hydrophobic core of one of the helices in direct DNA contact, and combining in vitro electrophoretic mobility assays, in vivo measurements of acrAB transcription using a GFP reporter system, and molecular dynamic simulations, it was shown that the immobilization of the N‐terminal helix of MarA prevents binding to DNA. This inhibited conformation seems to be universal for the monomeric members of the AraC/XylS family, as suggested by additional molecular dynamics simulations of the two‐domain protein Rob. These results point to the N‐terminal helix of the AraC/XylS family monomeric regulators as a promising target for the development of inhibitors.
  • Use of pure recombinant human enzymes to assess the disease-causing potential of missense mutations in urea cycle disorders, applied to N-acetylglutamate synthase deficiency
    Nadine Gougeard, Enea Sancho‐Vaello, M. Leonor Fernández‐Murga, Borja Martínez‐Sinisterra, Badr Loukili‐Hassani, Johannes Häberle, Clara Marco‐Marín, Vicente Rubio
    Journal of Inherited Metabolic Disease, 2024
    N‐acetylglutamate synthase (NAGS) makes acetylglutamate, the essential activator of the first, regulatory enzyme of the urea cycle, carbamoyl phosphate synthetase 1 (CPS1). NAGS deficiency (NAGSD) and CPS1 deficiency (CPS1D) present identical phenotypes. However, they must be distinguished, because NAGSD is cured by substitutive therapy with the N‐acetyl‐L‐glutamate analogue N‐carbamyl‐L‐glutamate, while curative therapy of CPS1D requires liver transplantation. Since their differentiation is done genetically, it is important to ascertain the disease‐causing potential of CPS1 and NAGS genetic variants. With this goal, we previously carried out site‐directed mutagenesis studies with pure recombinant human CPS1. We could not do the same with human NAGS (HuNAGS) because of enzyme instability, leading to our prior utilization of a bacterial NAGS as an imperfect surrogate of HuNAGS. We now use genuine HuNAGS, stabilized as a chimera of its conserved domain (cHuNAGS) with the maltose binding protein (MBP), and produced in Escherichia coli. MBP‐cHuNAGS linker cleavage allowed assessment of the enzymatic properties and thermal stability of cHuNAGS, either wild‐type or hosting each one of 23 nonsynonymous single‐base changes found in NAGSD patients. For all but one change, disease causation was accounted by the enzymatic alterations identified, including, depending on the variant, loss of arginine activation, increased KmGlutamate, active site inactivation, decreased thermal stability, and protein misfolding. Our present approach outperforms experimental in vitro use of bacterial NAGS or in silico utilization of prediction servers (including AlphaMissense), illustrating with HuNAGS the value for UCDs of using recombinant enzymes for assessing disease‐causation and molecular pathogenesis, and for therapeutic guidance.
  • The role of bacterial transport systems in the removal of host antimicrobial peptides in Gram-negative bacteria
    Jessica M A Blair, Kornelius Zeth, Vassiliy N Bavro, Enea Sancho-Vaello
    FEMS Microbiology Reviews, 2022
    Antibiotic resistance is a global issue that threatens our progress in healthcare and life expectancy. In recent years, antimicrobial peptides (AMPs) have been considered as promising alternatives to the classic antibiotics. AMPs are potentially superior due to their lower rate of resistance development, since they primarily target the bacterial membrane (‘Achilles' heel’ of the bacteria). However, bacteria have developed mechanisms of AMP resistance, including the removal of AMPs to the extracellular space by efflux pumps such as the MtrCDE or AcrAB–TolC systems, and the internalization of AMPs to the cytoplasm by the Sap transporter, followed by proteolytic digestion. In this review, we focus on AMP transport as a resistance mechanism compiling all the experimental evidence for the involvement of efflux in AMP resistance in Gram-negative bacteria and combine this information with the analysis of the structures of the efflux systems involved. Finally, we expose some open questions with the aim of arousing the interest of the scientific community towards the AMPs—efflux pumps interactions. All the collected information broadens our understanding of AMP removal by efflux pumps and gives some clues to assist the rational design of AMP-derivatives as inhibitors of the efflux pumps.
  • Structural plasticity of ll-37 indicates elaborate functional adaptation mechanisms to bacterial target structures
    Kornelius Zeth, Enea Sancho-Vaello
    International Journal of Molecular Sciences, 2021
    The human cathelicidin LL-37 is a multifunctional peptide of the human innate immune system. Among the various functions of LL-37, its antimicrobial activity is important in controlling the microorganisms of the human body. The target molecules of LL-37 in bacteria include membrane lipids, lipopolysaccharides (LPS), lipoteichoic acid (LTA), proteins, DNA and RNA. In this mini-review, we summarize the entity of LL-37 structural data determined over the last 15 years and specifically discuss features implicated in the interactions with lipid-like molecules. For this purpose, we discuss partial and full-length structures of LL-37 determined in the presence of membrane-mimicking detergents. This constantly growing structural database is now composed of monomers, dimers, tetramers, and fiber-like structures. The diversity of these structures underlines an unexpected plasticity and highlights the conformational and oligomeric adaptability of LL-37 necessary to target different molecular scaffolds. The recent co-crystal structures of LL-37 in complex with detergents are particularly useful to understand how these molecules mimic lipids and LPS to induce oligomerization and fibrillation. Defined detergent binding sites provide deep insights into a new class of peptide scaffolds, widening our view on the fascinating world of the LL-37 structural factotum. Together, the new structures in their evolutionary context allow for the assignment of functionally conserved residues in oligomerization and target interactions. Conserved phenylalanine and arginine residues primarily mediate those interactions with lipids and LPS. The interactions with macromolecules such as proteins or DNA remain largely unexplored and open a field for future studies aimed at structures of LL-37 complexes. These complexes will then allow for the structure-based rational design of LL-37-derived peptides with improved antibiotic properties.
  • Auxiliary active site mutations enhance the glycosynthase activity of a GH18 chitinase for polymerization of chitooligosaccharides
    Cristina Alsina, Enea Sancho-Vaello, Almudena Aranda-Martínez, Magda Faijes, Antoni Planas
    Carbohydrate Polymers, 2021
    Depolymerization of chitin results in chitooligosaccharides (COS) that induce immunostimulatory effects and disease protective responses and have many potential applications in agriculture and medicine. Isolation of bioactive COS with degree of polymerization (DP) larger than six from chitin hydrolyzates is hampered by their water insolubility. Enzymatic synthesis by exploiting the transglycosylation activity of GH18 chitinases offers a potential strategy to access oligomers in the range of bioactive DPs. We engineered SpChiD chitinase as a glycosynthase by mutation of the assisting residue of the catalytic triad in the substrate-assisted mechanism for polymerization of an oxazoline substrate (DP5ox). The insoluble polymer containing DP10 was partially hydrolyzed due to the significant residual hydrolase activity of the mutant enzyme. Combined mutations that strongly reduce the hydrolytic activity, in which the original catalytic triad only retains the essential acid/base residue, together with neighboring mutations in the -1/+1 subsites region, render glycosynthase-like chitinases able to produce chitin oligomers with DP10 as major product in good yields.
  • The structure of the antimicrobial human cathelicidin LL-37 shows oligomerization and channel formation in the presence of membrane mimics
    Enea Sancho-Vaello, David Gil-Carton, Patrice François, Eve-Julie Bonetti, Mohamed Kreir, Karunakar Reddy Pothula, Ulrich Kleinekathöfer, Kornelius Zeth
    Scientific Reports, 2020
    The human cathelicidin LL-37 serves a critical role in the innate immune system defending bacterial infections. LL-37 can interact with molecules of the cell wall and perforate cytoplasmic membranes resulting in bacterial cell death. To test the interactions of LL-37 and bacterial cell wall components we crystallized LL-37 in the presence of detergents and obtained the structure of a narrow tetrameric channel with a strongly charged core. The formation of a tetramer was further studied by cross-linking in the presence of detergents and lipids. Using planar lipid membranes a small but defined conductivity of this channel could be demonstrated. Molecular dynamic simulations underline the stability of this channel in membranes and demonstrate pathways for the passage of water molecules. Time lapse studies of E. coli cells treated with LL-37 show membrane discontinuities in the outer membrane followed by cell wall damage and cell death. Collectively, our results open a venue to the understanding of a novel AMP killing mechanism and allows the rational design of LL-37 derivatives with enhanced bactericidal activity.
  • Structure and function of the Ts2631 endolysin of Thermus scotoductus phage vB_Tsc2631 with unique N-terminal extension used for peptidoglycan binding
    Magdalena Plotka, Enea Sancho-Vaello, Sebastian Dorawa, Anna-Karina Kaczorowska, Lukasz P. Kozlowski, Tadeusz Kaczorowski, Kornelius Zeth
    Scientific Reports, 2019
    To escape from hosts after completing their life cycle, bacteriophages often use endolysins, which degrade bacterial peptidoglycan. While mesophilic phages have been extensively studied, their thermophilic counterparts are not well characterized. Here, we present a detailed analysis of the structure and function of Ts2631 endolysin from thermophilic phage vB_Tsc2631, which is a zinc-dependent amidase. The active site of Ts2631 consists of His30, Tyr58, His131 and Cys139, which are involved in Zn2+ coordination and catalysis. We found that the active site residues are necessary for lysis yet not crucial for peptidoglycan binding. To elucidate residues involved in the enzyme interaction with peptidoglycan, we tested single-residue substitution variants and identified Tyr60 and Lys70 as essential residues. Moreover, substitution of Cys80, abrogating disulfide bridge formation, inactivates Ts2631, as do substitutions of His31, Thr32 and Asn85 residues. The endolysin contains a positively charged N-terminal extension of 20 residues that can protrude from the remainder of the enzyme and is crucial for peptidoglycan binding. We show that the deletion of 20 residues from the N-terminus abolished the bacteriolytic activity of the enzyme. Because Ts2631 exhibits intrinsic antibacterial activity and unusual thermal stability, it is perfectly suited as a scaffold for the development of antimicrobial agents.
  • Metal Positions and Translocation Pathways of the Dodecameric Ferritin-like Protein Dps
    Kornelius Zeth, Enea Sancho-Vaello, Mitsuhiro Okuda
    Inorganic Chemistry, 2019
    Iron storage in biology is carried out by cage-shaped proteins of the ferritin superfamily, one of which is the dodecameric protein Dps. In Dps, four distinct steps lead to the formation of metal nanoparticles: attraction of ion-aquo complexes to the protein matrix, passage of these complexes through translocation pores, oxidation of these complexes at ferroxidase centers, and, ultimately, nanoparticle formation. In this study, we investigated Dps from Listeria innocua to structurally characterize these steps for Co2+, Zn2+, and La3+ ions. The structures reveal that differences in their ion coordination chemistry determine alternative metal ion-binding sites on the areas of the surface surrounding the translocation pore that captures nine La3+, three Co2+, or three Zn2+ ions as aquo clusters and passes them on for translocation. Inside these pores, ion-selective conformational changes at key residues occur before a gating residue to actively move ions through the constriction zone. Ions upstream of the Asp130 gate residue are typically hydrated, while ions downstream directly interact with the protein matrix. Inside the cavity, ions move along negatively charged residues to the ferroxidase center, where seven main residues adapt to the three different ions by dynamically changing their conformations. In total, we observed more than 20 metal-binding sites per Dps monomer, which clearly highlights the metal-binding capacity of this protein family. Collectively, our results provide a detailed structural description of the preparative steps for amino acid-assisted biomineralization in Dps proteins, demonstrating unexpected protein matrix plasticity.
  • Expression and specificity of a chitin deacetylase from the nematophagous fungus Pochonia chlamydosporia potentially involved in pathogenicity
    Almudena Aranda-Martinez, Laia Grifoll-Romero, Hugo Aragunde, Enea Sancho-Vaello, Xevi Biarnés, Luis Vicente Lopez-Llorca, Antoni Planas
    Scientific Reports, 2018
    Chitin deacetylases (CDAs) act on chitin polymers and low molecular weight oligomers producing chitosans and chitosan oligosaccharides. Structurally-defined, partially deacetylated chitooligosaccharides produced by enzymatic methods are of current interest as bioactive molecules for a variety of applications. Among Pochonia chlamydosporia (Pc) annotated CDAs, gene pc_2566 was predicted to encode for an extracellular CE4 deacetylase with two CBM18 chitin binding modules. Chitosan formation during nematode egg infection by this nematophagous fungus suggests a role for their CDAs in pathogenicity. The P. chlamydosporia CDA catalytic domain (PcCDA) was expressed in E. coli BL21, recovered from inclusion bodies, and purified by affinity chromatography. It displays deacetylase activity on chitooligosaccharides with a degree of polymerization (DP) larger than 3, generating mono- and di-deacetylated products with a pattern different from those of closely related fungal CDAs. This is the first report of a CDA from a nematophagous fungus. On a DP5 substrate, PcCDA gave a single mono-deacetylated product in the penultimate position from the non-reducing end (ADAAA) which was then transformed into a di-deacetylated product (ADDAA). This novel deacetylation pattern expands our toolbox of specific CDAs for biotechnological applications, and will provide further insights into the determinants of substrate specificity in this family of enzymes.
  • Structural remodeling and oligomerization of human cathelicidin on membranes suggest fibril-like structures as active species
    Enea Sancho-Vaello, Patrice François, Eve-Julie Bonetti, Hauke Lilie, Sebastian Finger, Fernando Gil-Ortiz, David Gil-Carton, Kornelius Zeth
    Scientific Reports, 2017
  • The human antimicrobial peptides dermcidin and LL-37 show novel distinct pathways in membrane interactions
    Kornelius Zeth, Enea Sancho-Vaello
    Frontiers in Chemistry, 2017
  • Structural basis of phosphatidyl-myo-inositol mannosides biosynthesis in mycobacteria
    Enea Sancho-Vaello, David Albesa-Jové, Ane Rodrigo-Unzueta, Marcelo E. Guerin
    Biochimica Et Biophysica Acta Molecular and Cell Biology of Lipids, 2017
  • The antibacterial prodrug activator Rv2466c is a mycothiol-dependent reductase in the oxidative stress response of Mycobacterium tuberculosis
    Leonardo Astolfi Rosado, Khadija Wahni, Giulia Degiacomi, Brandán Pedre, David Young, Alfonso G. de la Rubia, Francesca Boldrin, Edo Martens, Laura Marcos-Pascual, Enea Sancho-Vaello, David Albesa-Jové, Roberta Provvedi, Charlotte Martin, Vadim Makarov, Wim Versées, Guido Verniest, Marcelo E. Guerin, Luis M. Mateos, Riccardo Manganelli, Joris Messens
    Journal of Biological Chemistry, 2017
  • Structural Snapshots and Loop Dynamics along the Catalytic Cycle of Glycosyltransferase GpgS
    David Albesa-Jové, Javier Romero-García, Enea Sancho-Vaello, F.-Xabier Contreras, Ane Rodrigo-Unzueta, Natalia Comino, Ana Carreras-González, Pedro Arrasate, Saioa Urresti, Xevi Biarnés, Antoni Planas, Marcelo E. Guerin
    Structure, 2017
  • Understanding N-Acetyl-L-Glutamate Synthase Deficiency: Mutational Spectrum, Impact of Clinical Mutations on Enzyme Functionality, and Structural Considerations
    Enea Sancho-Vaello, Clara Marco-Marín, Nadine Gougeard, Leonor Fernández-Murga, Véronique Rüfenacht, Merima Mustedanagic, Vicente Rubio, Johannes Häberle
    Human Mutation, 2016
  • Structural basis for selective recognition of acyl chains by the membrane-associated acyltransferase PatA
    David Albesa-Jové, Zuzana Svetlíková, Montse Tersa, Enea Sancho-Vaello, Ana Carreras-González, Pascal Bonnet, Pedro Arrasate, Ander Eguskiza, Shiva K. Angala, Javier O. Cifuente, Jana Korduláková, Mary Jackson, Katarína Mikušová, Marcelo E. Guerin
    Nature Communications, 2016
  • A Native Ternary Complex Trapped in a Crystal Reveals the Catalytic Mechanism of a Retaining Glycosyltransferase
    David Albesa‐Jové, Fernanda Mendoza, Ane Rodrigo‐Unzueta, Fernando Gomollón‐Bel, Javier O. Cifuente, Saioa Urresti, Natalia Comino, Hansel Gómez, Javier Romero‐García, José M. Lluch, Enea Sancho‐Vaello, Xevi Biarnés, Antoni Planas, Pedro Merino, Laura Masgrau, Marcelo E. Guerin
    Angewandte Chemie International Edition, 2015
  • Antimicrobial peptides: Has their time arrived?
    Enea Sancho-Vaello, Kornelius Zeth
    Future Microbiology, 2015
  • Acidic pH and divalent cation sensing by PhoQ are dispensable for systemic salmonellae virulence
    Kevin G Hicks, Scott P Delbecq, Enea Sancho-Vaello, Marie-Pierre Blanc, Katja K Dove, Lynne R Prost, Margaret E Daley, Kornelius Zeth, Rachel E Klevit, Samuel I Miller
    Elife, 2015
  • Functional dissection of N-Acetylglutamate synthase (ArgA) of pseudomonas aeruginosa and restoration of its ancestral n-acetylglutamate kinase activity
    Enea Sancho-Vaello, María L. Fernández-Murga, Vicente Rubio
    Journal of Bacteriology, 2012
  • Mechanism of arginine regulation of acetylglutamate synthase, the first enzyme of arginine synthesis
    Enea Sancho-Vaello, María L. Fernández-Murga, Vicente Rubio
    FEBS Letters, 2009
  • Site-directed mutagenesis studies of acetylglutamate synthase delineate the site for the arginine inhibitor
    Enea Sancho-Vaello, M. Leonor Fernández-Murga, Vicente Rubio
    FEBS Letters, 2008

RECENT SCHOLAR PUBLICATIONS

  • Structure of a barrel-stave pore formed by magainin-2 reveals anion selectivity and zipper-mediated assembly
    E Sancho-Vaello, H Kücükyildiz, D Gil-Carton, X Biarnés, K Zeth
    Scientific Reports 15 (1), 39830 , 2025
    2025
    Citations: 3
  • Molecular dynamics simulation data for" Structure of a barrel-stave pore formed by maganin-2 reveals anion selectivity and zipper-mediated assembly"
    E Sancho-Vaello, K Harun, D Gil-Cartón, X Biarnés, K Zeth
    Zenodo , 2025
    2025
  • Targeting MarA N‐terminal domain dynamics to prevent DNA binding
    M Corbella, C Moreira, R Bello‐Madruga, M Torrent Burgas, ...
    Protein Science 34 (1), e5258 , 2025
    2025
  • Use of pure recombinant human enzymes to assess the disease‐causing potential of missense mutations in urea cycle disorders, applied to N ‐acetylglutamate …
    N Gougeard, E Sancho‐Vaello, ML Fernández‐Murga, ...
    Journal of Inherited Metabolic Disease 47 (6), 1194-1212 , 2024
    2024
    Citations: 2
  • The N-terminal helix of MarA as a key element in the mechanism of DNA binding
    M Corbella, C Moreira, R Bello-Madruga, M Torrent, SCL Kamerlin, ...
    bioRxiv, 2024.02. 13.580091 , 2024
    2024
  • The role of bacterial transport systems in the removal of host antimicrobial peptides in Gram-negative bacteria
    JMA Blair, K Zeth, VN Bavro, E Sancho-Vaello
    FEMS microbiology reviews 46 (6), fuac032 , 2022
    2022
    Citations: 27
  • Structural plasticity of LL-37 indicates elaborate functional adaptation mechanisms to bacterial target structures
    K Zeth, E Sancho-Vaello
    International Journal of Molecular Sciences 22 (10), 5200 , 2021
    2021
    Citations: 47
  • Auxiliary active site mutations enhance the glycosynthase activity of a GH18 chitinase for polymerization of chitooligosaccharides
    C Alsina, E Sancho-Vaello, A Aranda-Martínez, M Faijes, A Planas
    Carbohydrate Polymers 252, 117121 , 2021
    2021
    Citations: 15
  • The structure of the antimicrobial human cathelicidin LL-37 shows oligomerization and channel formation in the presence of membrane mimics
    E Sancho-Vaello, D Gil-Carton, P François, EJ Bonetti, M Kreir, ...
    Scientific reports 10 (1), 17356 , 2020
    2020
    Citations: 155
  • Metal positions and translocation pathways of the dodecameric ferritin-like protein Dps
    K Zeth, E Sancho-Vaello, M Okuda
    Inorganic chemistry 58 (17), 11351-11363 , 2019
    2019
    Citations: 18
  • Structure and function of the Ts2631 endolysin of Thermus scotoductus phage vB_Tsc2631 with unique N-terminal extension used for peptidoglycan binding
    M Plotka, E Sancho-Vaello, S Dorawa, AK Kaczorowska, LP Kozlowski, ...
    Scientific reports 9 (1), 1261 , 2019
    2019
    Citations: 42
  • The Human Antimicrobial Peptides Dermcidin and LL-37 Show Novel Distinct Pathways in Membrane
    K Zeth, E Sancho-Vaello
    Antimicrobial and Anticancer Peptides, 120 , 2018
    2018
  • Expression and specificity of a chitin deacetylase from the nematophagous fungus Pochonia chlamydosporia potentially involved in pathogenicity
    A Aranda-Martinez, L Grifoll-Romero, H Aragunde, E Sancho-Vaello, ...
    Scientific reports 8 (1), 2170 , 2018
    2018
    Citations: 35
  • Enginyeria de quitinases de la família GH18 per a l'obtenció de polímers de quitosà amb seqüències definides
    CA Verdú, A Aranda-Martínez, ES Vaello, X Biarnés, MF Simona, ...
    Revista de la Societat Catalana de Química, 32-44 , 2018
    2018
    Citations: 1
  • Structural remodeling and oligomerization of human cathelicidin on membranes suggest fibril-like structures as active species
    E Sancho-Vaello, P François, EJ Bonetti, H Lilie, S Finger, F Gil-Ortiz, ...
    Scientific reports 7 (1), 15371 , 2017
    2017
    Citations: 78
  • The human antimicrobial peptides dermcidin and LL-37 show novel distinct pathways in membrane interactions
    K Zeth, E Sancho-Vaello
    Frontiers in chemistry 5, 86 , 2017
    2017
    Citations: 97
  • Structural basis of phosphatidyl-myo-inositol mannosides biosynthesis in mycobacteria
    E Sancho-Vaello, D Albesa-Jove, A Rodrigo-Unzueta, ME Guerin
    Biochimica et Biophysica Acta (BBA)-Molecular and Cell Biology of Lipids … , 2017
    2017
    Citations: 32
  • The antibacterial prodrug activator Rv2466c is a mycothiol-dependent reductase in the oxidative stress response of Mycobacterium tuberculosis
    LA Rosado, K Wahni, G Degiacomi, B Pedre, D Young, AG De la Rubia, ...
    Journal of Biological Chemistry 292 (32), 13097-13110 , 2017
    2017
    Citations: 33
  • Structural snapshots and loop dynamics along the catalytic cycle of glycosyltransferase GpgS
    D Albesa-Jové, J Romero-García, E Sancho-Vaello, FX Contreras, ...
    Structure 25 (7), 1034-1044. e3 , 2017
    2017
    Citations: 19
  • Understanding N‐acetyl‐L‐glutamate synthase deficiency: mutational spectrum, impact of clinical mutations on enzyme functionality, and structural considerations
    E Sancho‐Vaello, C Marco‐Marín, N Gougeard, L Fernández‐Murga, ...
    Human Mutation 37 (7), 679-694 , 2016
    2016
    Citations: 43

MOST CITED SCHOLAR PUBLICATIONS

  • The structure of the antimicrobial human cathelicidin LL-37 shows oligomerization and channel formation in the presence of membrane mimics
    E Sancho-Vaello, D Gil-Carton, P François, EJ Bonetti, M Kreir, ...
    Scientific reports 10 (1), 17356 , 2020
    2020
    Citations: 155
  • The human antimicrobial peptides dermcidin and LL-37 show novel distinct pathways in membrane interactions
    K Zeth, E Sancho-Vaello
    Frontiers in chemistry 5, 86 , 2017
    2017
    Citations: 97
  • Structural remodeling and oligomerization of human cathelicidin on membranes suggest fibril-like structures as active species
    E Sancho-Vaello, P François, EJ Bonetti, H Lilie, S Finger, F Gil-Ortiz, ...
    Scientific reports 7 (1), 15371 , 2017
    2017
    Citations: 78
  • A native ternary complex trapped in a crystal reveals the catalytic mechanism of a retaining glycosyltransferase
    D Albesa‐Jové, F Mendoza, A Rodrigo‐Unzueta, F Gomollón‐Bel, ...
    Angewandte Chemie International Edition 54 (34), 9898-9902 , 2015
    2015
    Citations: 52
  • Acidic pH and divalent cation sensing by PhoQ are dispensable for systemic salmonellae virulence
    KG Hicks, SP Delbecq, E Sancho-Vaello, MP Blanc, KK Dove, LR Prost, ...
    Elife 4, e06792 , 2015
    2015
    Citations: 48
  • Structural plasticity of LL-37 indicates elaborate functional adaptation mechanisms to bacterial target structures
    K Zeth, E Sancho-Vaello
    International Journal of Molecular Sciences 22 (10), 5200 , 2021
    2021
    Citations: 47
  • Understanding N‐acetyl‐L‐glutamate synthase deficiency: mutational spectrum, impact of clinical mutations on enzyme functionality, and structural considerations
    E Sancho‐Vaello, C Marco‐Marín, N Gougeard, L Fernández‐Murga, ...
    Human Mutation 37 (7), 679-694 , 2016
    2016
    Citations: 43
  • Structure and function of the Ts2631 endolysin of Thermus scotoductus phage vB_Tsc2631 with unique N-terminal extension used for peptidoglycan binding
    M Plotka, E Sancho-Vaello, S Dorawa, AK Kaczorowska, LP Kozlowski, ...
    Scientific reports 9 (1), 1261 , 2019
    2019
    Citations: 42
  • Structural basis for selective recognition of acyl chains by the membrane-associated acyltransferase PatA
    D Albesa-Jové, Z Svetlíková, M Tersa, E Sancho-Vaello, ...
    Nature communications 7 (1), 10906 , 2016
    2016
    Citations: 39
  • Expression and specificity of a chitin deacetylase from the nematophagous fungus Pochonia chlamydosporia potentially involved in pathogenicity
    A Aranda-Martinez, L Grifoll-Romero, H Aragunde, E Sancho-Vaello, ...
    Scientific reports 8 (1), 2170 , 2018
    2018
    Citations: 35
  • The antibacterial prodrug activator Rv2466c is a mycothiol-dependent reductase in the oxidative stress response of Mycobacterium tuberculosis
    LA Rosado, K Wahni, G Degiacomi, B Pedre, D Young, AG De la Rubia, ...
    Journal of Biological Chemistry 292 (32), 13097-13110 , 2017
    2017
    Citations: 33
  • Structural basis of phosphatidyl-myo-inositol mannosides biosynthesis in mycobacteria
    E Sancho-Vaello, D Albesa-Jove, A Rodrigo-Unzueta, ME Guerin
    Biochimica et Biophysica Acta (BBA)-Molecular and Cell Biology of Lipids … , 2017
    2017
    Citations: 32
  • Mechanism of arginine regulation of acetylglutamate synthase, the first enzyme of arginine synthesis
    E Sancho-Vaello, ML Fernández-Murga, V Rubio
    FEBS letters 583 (1), 202-206 , 2009
    2009
    Citations: 30
  • The role of bacterial transport systems in the removal of host antimicrobial peptides in Gram-negative bacteria
    JMA Blair, K Zeth, VN Bavro, E Sancho-Vaello
    FEMS microbiology reviews 46 (6), fuac032 , 2022
    2022
    Citations: 27
  • Antimicrobial peptides: has their time arrived?
    E Sancho-Vaello, K Zeth
    Future Microbiology 10 (7), 1103-1106 , 2015
    2015
    Citations: 26
  • Site-directed mutagenesis studies of acetylglutamate synthase delineate the site for the arginine inhibitor
    E Sancho-Vaello, ML Fernández-Murga, V Rubio
    FEBS letters 582 (7), 1081-1086 , 2008
    2008
    Citations: 22
  • Structural snapshots and loop dynamics along the catalytic cycle of glycosyltransferase GpgS
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