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index medicus (23) 23
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x-ray diffraction (5) 5
amino acid sequence (4) 4
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electrochemistry (4) 4
electronic-structure (4) 4
enzyme (4) 4
enzymkatalyse (4) 4
glycosyltransferases - metabolism (4) 4
inorganic chemistry (4) 4
mycobacteria (4) 4
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protein multimerization (4) 4
spectroelectrochemistry (4) 4
substrate specificity (4) 4
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chemical sciences (3) 3
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cyanide (3) 3
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iron (3) 3
lactose (3) 3
magnetic-properties (3) 3
microbiology (3) 3
molecular sequence data (3) 3
molecular structure (3) 3
or physical chemistry (3) 3
oxidation-reduction (3) 3
phosphatidylinositol mannosides (3) 3
ruthenium complexes (3) 3
sequence homology, amino acid (3) 3
sigma-acetylide complexes (3) 3
theoretical and (3) 3
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tuberculosis (3) 3
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11 medical and health sciences (2) 2
[ chim.inor ] chemical sciences/inorganic chemistry (2) 2
[ chim.theo ] chemical sciences/theoretical and/or physical chemistry (2) 2
[ sdv.bbm ] life sciences [q-bio]/biochemistry, molecular biology (2) 2
alkene (2) 2
alkynyl (2) 2
antitubercular agents - chemistry (2) 2
article (2) 2
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1. Full Text The conformational plasticity of glycosyltransferases
by Albesa-Jové, David and Guerin, Marcelo E
Current Opinion in Structural Biology, ISSN 0959-440X, 10/2016, Volume 40, pp. 23 - 32
Glycosyltransferases (GTs) catalyze the transfer of a sugar moiety from nucleotide-sugar or lipid-phospho-sugar donors to a broad range of acceptor substrates,... 
GLYCOGEN-SYNTHASE | RETAINING GLYCOSYLTRANSFERASE | MEMBRANE TRANSLOCATION | ENZYMATIC GLYCOSYL TRANSFER | STRUCTURAL BASIS | CELLULOSE BIOSYNTHESIS | MECHANISTIC INSIGHTS | BIOCHEMISTRY & MOLECULAR BIOLOGY | B GLYCOSYLTRANSFERASES | CRYSTAL-STRUCTURES | MANNOSYLTRANSFERASE PIMA | CELL BIOLOGY | Protein Conformation | Glycosyltransferases - metabolism | Biocatalysis | Glycosyltransferases - chemistry | Humans | Transferases | Catalysis
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2. Full Text Structural Basis of Chitin Oligosaccharide Deacetylation
by Andrés, Eduardo and Albesa‐Jové, David and Biarnés, Xevi and Moerschbacher, Bruno M and Guerin, Marcelo E and Planas, Antoni
Angewandte Chemie International Edition, ISSN 1433-7851, 07/2014, Volume 53, Issue 27, pp. 6882 - 6887
Cell signaling and other biological activities of chitooligosaccharides (COSs) seem to be dependent not only on the degree of polymerization, but markedly on... 
enzyme catalysis | binding modes | structure elucidation | enzyme–substrate complexes | bioorganic chemistry | enzyme-substrate complexes | DEUTEROMYCETE | COLLETOTRICHUM-LINDEMUTHIANUM | MECHANISM | CHITOSAN | CASCADE | POLYSACCHARIDE DEACETYLASE | CHEMISTRY, MULTIDISCIPLINARY | VIBRIO-CHOLERAE | PDAA | BACILLUS-SUBTILIS | ENZYMES | Catalytic Domain | Biocatalysis | Substrate Specificity | Chitin - chemistry | Chitinases - metabolism | Oligosaccharides - metabolism | Disaccharides - chemistry | Acetylglucosamine - chemistry | Acetylglucosamine - metabolism | Vibrio cholerae - enzymology | Trisaccharides - chemistry | Oligosaccharides - chemistry | Molecular Docking Simulation | Acetylation | Kinetics | Binding Sites | Chitinases - chemistry | Enzymes | Crystals | Polymerization | Chitin | Cholera toxin | Catalysis | Structure | Crystal structure | Binding | Chitosan | Biological | Degree of polymerization | Three dimensional | Vibrio
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3. Full Text TssA forms a gp6‐like ring attached to the type VI secretion sheath
by Planamente, Sara and Salih, Osman and Manoli, Eleni and Albesa‐Jové, David and Freemont, Paul S and Filloux, Alain
The EMBO Journal, ISSN 0261-4189, 08/2016, Volume 35, Issue 15, pp. 1613 - 1627
The type VI secretion system (T6SS) is a supra‐molecular bacterial complex that resembles phage tails. It is a killing machine which fires toxins into target... 
TssA | type VI secretion system | gp6 | T6SS | bacteriophage baseplate | Bacteriophage baseplate | Gp6 | Type VI secretion system | SYSTEM | TARGET-CELLS | BIOCHEMISTRY & MOLECULAR BIOLOGY | COMPLEXES | ELECTRON-MICROSCOPY | PHAGE | CELL BIOLOGY | EFFECTORS | BACTERIOPHAGE-T4 BASEPLATE | PSEUDOMONAS-AERUGINOSA | PROTEIN SECRETION | TAIL STRUCTURE | Sequence Homology, Amino Acid | Microscopy, Electron, Transmission | Pseudomonas aeruginosa - chemistry | Type VI Secretion Systems - metabolism | Models, Biological | Protein Multimerization | Bacterial Proteins - chemistry | Models, Molecular | Protein Binding | Bacterial Proteins - metabolism | Protein Conformation | Type VI Secretion Systems - chemistry | Proteins | Molecular biology | Microbiology, Virology & Host Pathogen Interaction | Structural Biology
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4. Full Text Type VI Secretion System in Pseudomonas aeruginosa SECRETION AND MULTIMERIZATION OF VgrG PROTEINS
by Hachani, Abderrahman and Lossi, Nadine S and Hamilton, Alexander and Jones, Cerith and Bleves, Sophie and Albesa-Jove, David and Filloux, Alain
The Journal of Biological Chemistry, ISSN 0021-9258, 04/2011, Volume 286, Issue 14, pp. 12317 - 12327
Pseudomonas aeruginosa is a Gram-negative bacterium causing chronic infections in cystic fibrosis patients. Such infections are associated with an active type... 
BACTERIA | BACTERIOPHAGE-T4 | GENES | DISEASE | TARGETS | INFECTION | APPARATUS | STRAIN | PREDICTION | PATHOGENS | BIOCHEMISTRY & MOLECULAR BIOLOGY | Pseudomonas aeruginosa - genetics | Pseudomonas aeruginosa - metabolism | Electrophoresis, Polyacrylamide Gel | Protein Multimerization | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | Computational Biology | Bacterial Proteins - metabolism | Immunoblotting | Virulence Factors | Life Sciences | Biochemistry, Molecular Biology | Membrane Trafficking | Protein Export | Protein Secretion | Microbiology | Hcp | Bacteria | Pseudomonas aeruginosa | Gene Knockout | Bacteriophage | Type VI Secretion System | VgrG
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5. Full Text Enzyme dynamics visualized by SAXS
by Albesa-Jové, David and Guerin, Marceo E
Acta Crystallographica Section A Foundations and Advances, ISSN 2053-2733, 08/2016, Volume 72, Issue a1, pp. s13 - s13
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6. Full Text Structure-function relationships of membrane-associated GT-B glycosyltransferases
by Albesa-Jové, David and Giganti, David and Jackson, Mary and Alzari, Pedro M and Guerin, Marcelo E
Glycobiology, ISSN 0959-6658, 02/2014, Volume 24, Issue 2, pp. 108 - 124
Membrane-associated GT-B glycosyltransferases (GTs) comprise a large family of enzymes that catalyze the transfer of a sugar moiety from nucleotide-sugar... 
X-ray crystallography | membrane protein | structural biology | glycosyltransferase | carbohydrate-modifying enzyme | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | NEISSERIA-MENINGITIDIS | N-ACETYLGLUCOSAMINE TRANSFERASE | RETAINING GLYCOSYLTRANSFERASES | BETA-GLUCOSYLTRANSFERASE | LUMINOUS MARINE BACTERIUM | ACHOLEPLASMA-LAIDLAWII | 1,2-DIACYLGLYCEROL 3-GLUCOSYLTRANSFERASE | ALPHA/BETA-GALACTOSIDE ALPHA-2,3-SIALYLTRANSFERASE | Animals | Membrane Proteins - chemistry | Glycosyltransferases - physiology | Membrane Proteins - physiology | Glycosyltransferases - chemistry | Humans | Models, Molecular | Protein Conformation | Structure-Activity Relationship | Catalysis | Protein Folding | Review
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7. Full Text Secondary structure reshuffling modulates glycosyltransferase function at the membrane
by Giganti, David and Giganti, David and Albesa-Jové, David and Urresti, Saioa and Rodrigo-Unzueta, Ane and Martínez, Mariano A and Comino, Natalia and Barilone, Nathalie and Bellinzoni, Marco and Chenal, Alexandre and Guerin, Marcelo E and Alzari, Pedro M
Nature chemical biology, ISSN 1552-4450, 01/2015, Volume 11, Issue 1, pp. 16 - 18
Secondary structure refolding is a key event in biology as it modulates the conformation of many proteins in the cell, generating functional or aberrant... 
CATALYSIS | MYCOBACTERIA | DOMAIN | CONSTANTS | PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | MANNOSYLTRANSFERASE PIMA | Mutagenesis, Site-Directed | Humans | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | Models, Molecular | Crystallography, X-Ray | Mannosyltransferases - genetics | Mannosyltransferases - chemistry | Mannosyltransferases - isolation & purification | Protein Structure, Secondary - genetics | Cell Membrane - enzymology | Glycosyltransferases - metabolism | Animals | Cell Membrane - metabolism | Phospholipids - metabolism | Bacterial Proteins - isolation & purification | Life Sciences | Glycosyltransferases/metabolism | Biochemistry, Molecular Biology | Cell Membrane/enzymology/metabolism | Bacterial Proteins/chemistry/genetics | isolation & purification
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8. Full Text Structure-function relationships underlying the dual N-acetylmuramic and N-acetylglucosamine specificities of the bacterial peptidoglycan deacetylase PdaC
by Grifoll-Romero, Laia and Sainz-Polo, María Angela and Albesa-Jové, David and Guerin, Marcelo E and Biarnés, Xevi and Planas, Antoni
Journal of Biological Chemistry, ISSN 0021-9258, 11/2019, p. jbc.RA119.009510
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9. Full Text Structural Snapshots of α‐1,3‐Galactosyltransferase with Native Substrates: Insight into the Catalytic Mechanism of Retaining Glycosyltransferases
by Albesa‐Jové, David and Sainz‐Polo, M. Ángela and Marina, Alberto and Guerin, Marcelo E
Angewandte Chemie International Edition, ISSN 1433-7851, 11/2017, Volume 56, Issue 47, pp. 14853 - 14857
Glycosyltransferases (GTs) are a key family of enzymes that catalyze the synthesis of glycosidic bonds in all living organisms. The reaction involves the... 
reaction mechanisms | glycosyltransferases | enzyme catalysis | enzymes | structural biology | Galactosyltransferases - chemistry | Catalytic Domain | Glycosyltransferases - metabolism | Animals | Lactose - metabolism | Cations, Divalent | Cattle | Substrate Specificity | Crystallography, X-Ray | Protein Conformation | Catalysis | Galactosyltransferases - metabolism | CHEMISTRY, MULTIDISCIPLINARY
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10. Full Text Synthesis, Crystal Structures, Linear and Nonlinear Optical Properties, and Theoretical Studies of (p‐R‐Phenyl)‐, (p‐R‐Phenylethynyl)‐, and (E)‐[2‐(p‐R‐Phenyl)ethenyl]dimesitylboranes and Related Compounds
by Yuan, Zheng and Entwistle, Christopher D and Collings, Jonathan C and Albesa‐Jové, David and Batsanov, Andrei S and Howard, Judith A. K and Taylor, Nicholas J and Kaiser, Hanns Martin and Kaufmann, Dieter E and Poon, Suk‐Yue and Wong, Wai‐Yeung and Jardin, Christophe and Fathallah, Sofiane and Boucekkine, Abdou and Halet, Jean‐François and Marder, Todd B
Chemistry – A European Journal, ISSN 0947-6539, 03/2006, Volume 12, Issue 10, pp. 2758 - 2771
The (p‐R‐phenyl)dimesitylboranes (R=Me2N, MeO, MeS, Br, I), (p‐R‐phenylethynyl)dimesitylboranes (R=Me2N, MeO, MeS, H),... 
boranes | nonlinear optics | X‐ray diffraction | semiempirical calculations | synthetic methods | X-ray diffraction | Boranes | Semiempirical calculations | Synthetic methods | Nonlinear optics | ELECTRON | SINGLE-PHOTON | AMORPHOUS MOLECULAR MATERIALS | CHEMISTRY, MULTIDISCIPLINARY | 2-PHOTON-EXCITED FLUORESCENCE | TRIVALENT BORON | 5,5'-BIS(DIMESITYLBORYL)-2,2'-BITHIOPHENE | PI-A COMPOUNDS | 3-COORDINATE ORGANOBORON COMPOUNDS | DERIVATIVES | ACCEPTOR | or physical chemistry | Inorganic chemistry | Chemical Sciences | Theoretical and
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11. Full Text Structural insights into the molecular organization of the S‐layer from Clostridium difficile
by Fagan, Robert P and Albesa‐Jové, David and Qazi, Omar and Svergun, Dmitri I and Brown, Katherine A and Fairweather, Neil F
Molecular Microbiology, ISSN 0950-382X, 03/2009, Volume 71, Issue 5, pp. 1308 - 1322
Summary Clostridium difficile expresses a surface layer (S‐layer) which coats the surface of the bacterium and acts as an adhesin facilitating interaction of... 
GRAM-POSITIVE BACTERIA | BIOLOGICAL MACROMOLECULES | SMALL-ANGLE SCATTERING | BIOCHEMISTRY & MOLECULAR BIOLOGY | RESOLUTION | SEQUENCE | MICROBIOLOGY | CELL-SURFACE PROTEINS | WALL POLYMERS | BINDING | ADHERENCE | SOFTWARE | Protein Structure, Tertiary | Amino Acid Sequence | Sequence Alignment | Membrane Glycoproteins - metabolism | Cell Wall - metabolism | Models, Molecular | Molecular Sequence Data | Bacterial Proteins - metabolism | Clostridium difficile - metabolism | Proteins | Biosynthesis | Structure | Analysis | Crystals
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12. Full Text Structural basis of phosphatidyl-myo-inositol mannosides biosynthesis in mycobacteria
by Sancho-Vaello, Enea and Albesa-Jové, David and Rodrigo-Unzueta, Ane and Guerin, Marcelo E
BBA - Molecular and Cell Biology of Lipids, ISSN 1388-1981, 11/2017, Volume 1862, Issue 11, pp. 1355 - 1367
Phosphatidyl- -inositol mannosides (PIMs) are glycolipids of unique chemical structure found in the inner and outer membranes of the cell envelope of all... 
Phosphatidylinositol mannosides | Acyltransferase | Glycosyltransferase | Mycobacteria | Structural biology | Glycolipid | ACYLATION STATE | OUTER-MEMBRANE | ENZYMATIC ACYLATION | BACILLUS-CALMETTE-GUERIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | LIPOARABINOMANNAN BIOSYNTHESIS | SACCHAROMYCES-CEREVISIAE | CELL BIOLOGY | CELL-WALL | BIOPHYSICS | CONFORMATIONAL PLASTICITY | MOLECULAR-BASIS | MANNOSYLTRANSFERASE PIMA | Phosphates | Enzymes | Membrane lipids | Inositol | Physiological aspects | Plant lipids | Acylation
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13. Full Text Regulation of Human Hsc70 ATPase and Chaperone Activities by Apg2: Role of the Acidic Subdomain
by Cabrera, Yovana and Dublang, Leire and Fernández-Higuero, José Angel and Albesa-Jové, David and Lucas, Maria and Viguera, Ana Rosa and Guerin, Marcelo E and Vilar, Jose M.G and Muga, Arturo and Moro, Fernando
Journal of Molecular Biology, ISSN 0022-2836, 01/2019, Volume 431, Issue 2, pp. 444 - 461
Protein aggregate reactivation in metazoans is accomplished by the combined activity of Hsp70, Hsp40 and Hsp110 chaperones. Hsp110s support the refolding of... 
Apg2 | chaperone complex | Hsc70 | Hsp110 | aggregate reactivation | GRPE | PROTEIN | MECHANISM | MOLECULAR CHAPERONES | BIOCHEMISTRY & MOLECULAR BIOLOGY | QUALITY-CONTROL | NUCLEOTIDE EXCHANGE FACTORS | YEAST HSP110 | DNAK | MITOCHONDRIAL HSP70 | BINDING | Heat shock proteins | Biopolymers | Adenosine triphosphatase | Protein binding
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14. Full Text The redox state regulates the conformation of Rv2466c to activate the antitubercular prodrug TP053
by Albesa-Jove, David and Comino, Natalia and Tersa, Montse and Mohorko, Elisabeth and Urresti, Saioa and Dainese, Elisa and Chiarelli, Laurent R and Pasca, Maria Rosalia and Manganelli, Riccardo and Makarov, Vadim and Riccardi, Giovanna and Svergun, Dmitri I and Glockshuber, Rudi and Guerin, Marcelo E
Journal of Biological Chemistry, ISSN 0021-9258, 12/2015, Volume 290, Issue 52, pp. 31077 - 31089
Rv2466c is a key oxidoreductase that mediates the reductive activation of TP053, a thienopyrimidine derivative that kills replicating and non-replicating... 
SYSTEM | PROTEIN-DISULFIDE-ISOMERASE | MECHANISM | THIOREDOXIN | TUBERCULOSIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | HIGH-RESOLUTION | TRANSFERASES | INFLUENZA HEMAGGLUTININ | SCATTERING | DSBA | Protein Structure, Tertiary | Antitubercular Agents - chemistry | Oxidation-Reduction | Protein Multimerization | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | Models, Molecular | Crystallography, X-Ray | Prodrugs - chemistry | Protein Structure, Quaternary | Protein Binding | Mycobacterium tuberculosis - chemistry | Mycobacterium tuberculosis - genetics | enzyme | small-angle x-ray scattering (SAXS) | x-ray crystallography | Mycobacterium tuberculosis | thioredoxin | oxidation-reduction (redox) | Enzymology | conformational change
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