Articles

Search Articles

Advanced search
Help

Catalogue

Articles

Databases

X
Search Filters
Format Format
Subjects Subjects
Subjects Subjects
X
Sort by Item Count (A-Z)
Filter by Count
organic chemistry (110) 110
chemistry (109) 109
metallurgy (107) 107
peptides (107) 107
physics (89) 89
investigating or analysing materials by determining theirchemical or physical properties (88) 88
measuring (88) 88
testing (88) 88
index medicus (75) 75
biochemistry (56) 56
microbiology (53) 53
proteins (49) 49
beer (48) 48
enzymology (48) 48
mutation or genetic engineering (48) 48
spirits (48) 48
vinegar (48) 48
wine (48) 48
compositions thereof (47) 47
culture media (47) 47
microorganisms or enzymes (47) 47
propagating, preserving or maintaining microorganisms (47) 47
models, molecular (36) 36
biochemistry & molecular biology (35) 35
animals (32) 32
crystallography, x-ray (32) 32
humans (30) 30
crystal structure (29) 29
multidisciplinary sciences (28) 28
crystal-structure (27) 27
protein binding (27) 27
binding sites (26) 26
article (24) 24
research (23) 23
structure (21) 21
amino acid sequence (20) 20
crystals (20) 20
binding (19) 19
biophysics (19) 19
receptors (19) 19
molecular sequence data (18) 18
protein structure, tertiary (18) 18
crystallography (17) 17
ligands (17) 17
mutation (17) 17
nanobody (17) 17
protein conformation (17) 17
single-domain antibodies - chemistry (17) 17
analysis (16) 16
physiological aspects (16) 16
protein (15) 15
antibodies (14) 14
crystallization (14) 14
single-domain antibodies - metabolism (13) 13
membrane proteins (12) 12
biological sciences (11) 11
nanobodies (11) 11
camelids, new world (10) 10
cell biology (10) 10
escherichia-coli (10) 10
protein structure, secondary (10) 10
single-domain antibodies - immunology (10) 10
activation (9) 9
mechanism (9) 9
protein multimerization (9) 9
structural biology (9) 9
bacteria (8) 8
camelids, new world - immunology (8) 8
complex (8) 8
kinetics (8) 8
membranes (8) 8
pharmacology (8) 8
science (8) 8
sequence homology, amino acid (8) 8
affinity (7) 7
biology (7) 7
escherichia coli (7) 7
escherichia coli proteins - chemistry (7) 7
g proteins (7) 7
human necessities (7) 7
hygiene (7) 7
identification (7) 7
medical or veterinary science (7) 7
molecular biology (7) 7
preparations for medical, dental, or toilet purposes (7) 7
protein structure (7) 7
recognition (7) 7
viral antibodies (7) 7
x-ray crystallography (7) 7
biochemical research methods (6) 6
dimerization (6) 6
e coli (6) 6
electron microscopy (6) 6
escherichia coli - genetics (6) 6
glycoproteins (6) 6
lipids (6) 6
model (6) 6
nuclear magnetic resonance, biomolecular (6) 6
protein stability (6) 6
protein structure, quaternary (6) 6
more...
Language Language
Language Language
X
Sort by Item Count (A-Z)
Filter by Count
English (277) 277
French (37) 37
German (19) 19
Portuguese (6) 6
Danish (5) 5
Chinese (3) 3
Croatian (3) 3
Hungarian (3) 3
Polish (3) 3
Spanish (3) 3
Japanese (2) 2
more...
Publication Date Publication Date
Click on a bar to filter by decade
Slide to change publication date range


1. Full Text The role of roughage provision on the absorption and disposition of the mycotoxin deoxynivalenol and its acetylated derivatives in calves: from field observations to toxicokinetics
by Valgaeren, Bonnie and Théron, Léonard and Croubels, Siska and Devreese, Mathias and De Baere, Siegrid and Van Pamel, Els and Daeseleire, Els and De Boevre, Marthe and De Saeger, Sarah and Vidal, Arnau and Di Mavungu, José Diana and Fruhmann, Philipp and Adam, Gerhard and Callebaut, Alfons and Bayrou, Calixte and Frisée, Vincent and Rao, Anne-Sophie and Knapp, Emilie and Sartelet, Arnaud and Pardon, Bart and Deprez, Piet and Antonissen, Gunther
Archives of Toxicology, ISSN 0340-5761, 02/2019, Volume 93, Issue 2, pp. 293 - 310
A clinical case in Belgium demonstrated that feeding a feed concentrate containing considerable levels of deoxynivalenol (DON, 1.13mg/kg feed) induced severe... 
Biodegradation | Toxicokinetics | 3- and 15-Acetyldeoxynivalenol | Deoxynivalenol | Calf | Mycotoxin | CATTLE | BIOAVAILABILITY | VEAL CALVES | CARRY-OVER | 3-and 15-Acetyldeoxynivalenol | TRICHOTHECENES | METABOLISM | FUSARIUM MYCOTOXINS | TOXIN-CONTAMINATED WHEAT | TOXICOLOGY | FEED | FOOD | Rumen | Liver diseases | Cattle | Urine | Intravenous administration | Toxicity | Liver | Corn | Calves | Maize | Bioavailability | Derivatives | Contamination | Crossovers | Straw | Veal | Absorption | Metabolites | Developmental stages | Farms | Intestine | Intestinal absorption | Feeds
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
2. Full Text Activation and allosteric modulation of a muscarinic acetylcholine receptor
by Kruse, Andrew C and Ring, Aaron M and Manglik, Aashish and Hu, Jianxin and Hu, Kelly and Eitel, Katrin and Hübner, Harald and Pardon, Els and Valant, Celine and Sexton, Patrick M and Christopoulos, Arthur and Felder, Christian C and Gmeiner, Peter and Steyaert, Jan and Weis, William I and Garcia, K. Christopher and Wess, Jürgen and Kobilka, Brian K and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Nature, ISSN 0028-0836, 2013, Volume 504, Issue 7478, pp. 101 - 106
Despite recent advances in crystallography and the availability of G-protein-coupled receptor (GPCR) structures, little is known about the mechanism of their... 
LIGANDS | PROTEIN-COUPLED RECEPTOR | STRUCTURAL BASIS | NANOBODY | CRYSTAL-STRUCTURE | AMINO-ACIDS | MULTIDISCIPLINARY SCIENCES | BINDING-SITE | IDENTIFICATION | SITE-DIRECTED MUTAGENESIS | BETA-ADRENERGIC RECEPTOR | Protein Structure, Tertiary | Allosteric Regulation | Humans | Isoxazoles - metabolism | Models, Molecular | Cytoplasm - metabolism | Receptors, Muscarinic - metabolism | Isoxazoles - chemistry | Quaternary Ammonium Compounds - chemistry | Receptors, Muscarinic - chemistry | Quaternary Ammonium Compounds - metabolism | Protein Binding | Binding Sites | Physiological aspects | Rhodopsin | G proteins | Research | Muscarinic receptors | Protein binding | Proteins | Yeast | Mutagenesis | Rodents | Ligands | Crystallography | Binding sites | Metabolic disorders
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
3. Full Text Crystal structure of a SLC11 (NRAMP) transporter reveals the basis for transition-metal ion transport
by Ehrnstorfer, Ines A and Geertsma, Eric R and Pardon, Els and Steyaert, Jan and Dutzler, Raimund
Nature Structural and Molecular Biology, ISSN 1545-9993, 11/2014, Volume 21, Issue 11, pp. 990 - 996
Members of the SLC11 (NRAMP) family transport iron and other transition-metal ions across cellular membranes. These membrane proteins are present in all... 
NEUROTRANSMITTER TRANSPORTERS | MECHANISM | DMT1 | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | FAMILY | CELL BIOLOGY | NATURAL-RESISTANCE | IRON TRANSPORT | MNTH | BIOPHYSICS | RESIDUES | SELECTIVITY | Amino Acid Transport Systems - chemistry | Transcription Factors - chemistry | Humans | Bacterial Proteins - chemistry | Molecular Sequence Data | Substrate Specificity | Crystallography, X-Ray | Recombinant Proteins | Escherichia coli - metabolism | Staphylococcus - metabolism | Conserved Sequence | Cation Transport Proteins - genetics | Ion Transport | Binding Sites | Amino Acid Sequence | Gene Expression | Iron - chemistry | Bacterial Proteins - genetics | Models, Molecular | Manganese - chemistry | Transcription Factors - genetics | Staphylococcus - chemistry | Cations, Divalent | Escherichia coli - genetics | Amino Acid Transport Systems - genetics | Protein Binding | Protein Conformation | Structural Homology, Protein | Cation Transport Proteins - chemistry | Cadmium - chemistry | Protein research | Transition metals | Crystals | Ion transport | Physiological aspects | Research | Structure | Membrane proteins | Proteins | Ions | Membranes | Metals | Crystal structure
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
4. Full Text A general protocol for the generation of Nanobodies for structural biology
by Pardon, Els and Laeremans, Toon and Triest, Sarah and Rasmussen, Søren G F and Wohlkönig, Alexandre and Ruf, Armin and Muyldermans, Serge and Hol, Wim G J and Kobilka, Brian K and Steyaert, Jan
Nature Protocols, ISSN 1754-2189, 2014, Volume 9, Issue 3, pp. 674 - 693
There is growing interest in using antibodies as auxiliary tools to crystallize proteins. Here we describe a general protocol for the generation of Nanobodies... 
HEAVY-CHAIN ANTIBODIES | CRYSTALLIZATION | COMPLEX | FRAGMENTS | TERMINAL DOMAIN | PROTEIN-COUPLED RECEPTOR | CRYSTAL-STRUCTURE | BIOCHEMICAL RESEARCH METHODS | SINGLE-DOMAIN ANTIBODIES | MEMBRANE-PROTEINS | BINDING | Biotechnology - methods | Animals | Camelus | Cell Surface Display Techniques | Cloning, Molecular | Models, Molecular | Protein Conformation | DNA Primers - genetics | Single-Domain Antibodies - biosynthesis | Crystallization - methods | Usage | Physiological aspects | Research | B cells | Crystallography | Protein binding | Antigenic determinants | Nanobody | Structural Biology | Protein conformation | Crystallization chaperones
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
5. Full Text Structure of a prokaryotic fumarate transporter reveals the architecture of the SLC26 family
by Geertsma, Eric R and Chang, Yung-Ning and Shaik, Farooque R and Neldner, Yvonne and Pardon, Els and Steyaert, Jan and Dutzler, Raimund
Nature Structural and Molecular Biology, ISSN 1545-9993, 10/2015, Volume 22, Issue 10, pp. 803 - 808
The SLC26 family of membrane proteins combines a variety of functions within a conserved molecular scaffold. Its members, besides coupled anion transporters... 
ANION TRANSPORTERS | BIOCHEMISTRY & MOLECULAR BIOLOGY | STOICHIOMETRY | IDENTIFICATION | SELECTIVITY FILTER | CELL BIOLOGY | POLYAMINE-ORGANOCATION SUPERFAMILY | BIOPHYSICS | MOTOR PROTEIN | PRESTIN | BICARBONATE TRANSPORTER | MEMBRANE-PROTEINS | STAS DOMAIN | Multigene Family - genetics | Electrophoresis, Polyacrylamide Gel | Escherichia coli | Fluorescence | Models, Molecular | Molecular Sequence Data | Crystallography, X-Ray | DNA Primers - genetics | Open Reading Frames - genetics | Anion Transport Proteins - metabolism | Sequence Analysis, DNA | Anion Transport Proteins - chemistry | Deinococcus - genetics | Base Sequence | Cloning, Molecular | Polymerase Chain Reaction | Fumarates - metabolism | Protein Conformation | Chromatography, Gel | Selenomethionine | Physiological aspects | Research | Structure | Membrane proteins | Proteins | Membranes | Molecular biology | Crystal structure
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
6. Full Text Allosteric nanobodies reveal the dynamic range and diverse mechanisms of G-protein-coupled receptor activation
by Staus, Dean P and Strachan, Ryan T and Manglik, Aashish and Pani, Biswaranjan and Kahsai, Alem W and Kim, Tae Hun and Wingler, Laura M and Ahn, Seungkirl and Chatterjee, Arnab and Masoudi, Ali and Kruse, Andrew C and Pardon, Els and Steyaert, Jan and Weis, William I and Prosser, R. Scott and Kobilka, Brian K and Costa, Tommaso and Lefkowitz, Robert J and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Nature, ISSN 0028-0836, 07/2016, Volume 535, Issue 7612, pp. 448 - 452
G-protein-coupled receptors (GPCRs) modulate many physiological processes by transducing a variety of extracellular cues into intracellular responses. Ligand... 
EFFICACY | MULTIDISCIPLINARY SCIENCES | STATE | TERNARY COMPLEX MODEL | BINDING | BETA-ADRENERGIC RECEPTOR | CONFORMATIONS | Allosteric Regulation - drug effects | Drug Partial Agonism | Allosteric Site - drug effects | Humans | Protein Conformation - drug effects | Models, Molecular | Crystallography, X-Ray | Receptors, Adrenergic, beta-2 - metabolism | Adrenergic beta-2 Receptor Agonists - pharmacology | Receptors, Adrenergic, beta-2 - chemistry | Single-Domain Antibodies - pharmacology | Isoproterenol - pharmacology | Protein Stability - drug effects | Nuclear Magnetic Resonance, Biomolecular | Ligands | Physiological aspects | G proteins | Analysis | Protein binding | Proteins | Spectrum analysis | Binding sites | Cells
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
7. Full Text Structures of β-klotho reveal a â € zip code'-like mechanism for endocrine FGF signalling
by Lee, Sangwon and Choi, Jungyuen and Mohanty, Jyotidarsini and Sousa, Leiliane P and Tome, Francisco and Pardon, Els and Steyaert, Jan and Lemmon, Mark A and Lax, Irit and Schlessinger, Joseph and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Nature, ISSN 0028-0836, 01/2018, Volume 553, Issue 7689, pp. 501 - 505
Canonical fibroblast growth factors (FGFs) activate FGF receptors (FGFRs) through paracrine or autocrine mechanisms in a process that requires cooperation with... 
RECEPTOR | FIBROBLAST | BINDING | MULTIDISCIPLINARY SCIENCES | Signal Transduction | Humans | Models, Molecular | Substrate Specificity | Crystallography, X-Ray | Fibroblast Growth Factors - chemistry | Fibroblast Growth Factors - metabolism | Extracellular Space - metabolism | Membrane Proteins - chemistry | Receptors, Fibroblast Growth Factor - metabolism | HEK293 Cells | Glycoside Hydrolases - chemistry | Protein Binding | Protein Domains | Ligands | Membrane Proteins - metabolism | Glycoside Hydrolases - metabolism | Binding Sites | Fibroblast growth factor | Fibroblast growth factor 23 | Paracrine signalling | Amino acids | Intracellular signalling | Hormones | Tissues | Cell surface | Experiments | Proteins | Receptors | Fibroblasts | Catalysis | Autocrine signalling | Lipogenesis | Growth factors | Sugar | Crystal structure | Heparan sulfate | Enzymes | Proteoglycans | Energy expenditure | Metabolism | Insulin | Chemical compounds | Biological activity | Klotho protein | Heparan sulfate proteoglycans | Receptor mechanisms | Cooperativity | Sulfate | Fibroblast growth factor receptors
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
8. Full Text Structure and flexibility of the endosomal Vps34 complex reveals the basis of its function on membranes
by Rostislavleva, Ksenia and Soler, Nicolas and Ohashi, Yohei and Zhang, Lufei and Pardon, Els and Burke, John E and Masson, Glenn R and Johnson, Chris and Steyaert, Jan and Ktistakis, Nicholas T and Williams, Roger L
Science, ISSN 0036-8075, 10/2015, Volume 350, Issue 6257, pp. 140 - 140
Phosphatidylinositol 3-kinase Vps34 complexes regulate intracellular membrane trafficking in endocytic sorting, cytokinesis, and autophagy. We present the 4.4... 
ACTIVATION | DOMAIN | BECLIN 1 | PROTEIN-KINASE | MULTIDISCIPLINARY SCIENCES | AUTOPHAGY | INHIBITOR | VPS15 | PHOSPHOINOSITIDE 3-KINASE | BINDING | Protein Structure, Tertiary | Protein Structure, Secondary | Protein Multimerization | Crystallography, X-Ray | Class III Phosphatidylinositol 3-Kinases - ultrastructure | Cell Membrane - chemistry | Cell Membrane - enzymology | Vacuolar Sorting Protein VPS15 - chemistry | Vacuolar Sorting Protein VPS15 - ultrastructure | Endosomes - chemistry | Saccharomyces cerevisiae - enzymology | Class III Phosphatidylinositol 3-Kinases - chemistry | Endosomes - enzymology | Proteins | Enzymes | Lipids | Membranes | Kinases | Flexibility | Assembly | Sorting | Crystal structure
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
9. Full Text Structures of P-glycoprotein reveal its conformational flexibility and an epitope on the nucleotide-binding domain
by Andrew B. Ward and Paul Szewczyk and Vinciane Grimard and Chang-Wook Lee and Lorena Martinez and Rupak Doshi and Alexandra Caya and Mark Villaluz and Els Pardon and Cristina Cregger and Douglas J. Swartz and Pierre Guy Falson and Ina L. Urbatsch and Cedric Govaerts and Jan Steyaert and Geoffrey Chang
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 8/2013, Volume 110, Issue 33, pp. 13386 - 13391
P-glycoprotein (P-gp) is one of the best-known mediators of drug efflux-based multidrug resistance in many cancers. This validated therapeutic target is a... 
ATP binding cassette transporters | Proteins | Hydrolysis | Molecules | Crystals | Adenosine triphosphatases | Cell membranes | Biochemistry | Epitopes | Crystal structure | Nanobody-transporter complex | ABC transporter | Membrane protein structure | nanobody-transporter complex | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | TRANSITION-STATE | membrane protein structure | CHEMOTHERAPY | ABC TRANSPORTER MSBA | RESISTANCE | CASSETTE TRANSPORTER | INHIBITORS | MOLECULAR-BASIS | RESIDUES | CYCLE | Epitope Mapping | Animals | Single-Domain Antibodies - chemistry | Models, Molecular | Protein Conformation | ATP-Binding Cassette, Sub-Family B, Member 1 - chemistry | Mice | Drug Delivery Systems - methods | Physiological aspects | Glycoproteins | Research | Drug resistance | Structure | Health aspects | Protein binding | Biological Sciences
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
10. Full Text Allosteric coupling from G protein to the agonist-binding pocket in GPCRs
by Devree, Brian T and Mahoney, Jacob P and Vélez-Ruiz, Gisselle A and Rasmussen, Soren G. F and Kuszak, Adam J and Edwald, Elin and Fung, Juan-Jose and Manglik, Aashish and Masureel, Matthieu and Du, Yang and Matt, Rachel A and Pardon, Els and Steyaert, Jan and Kobilka, Brian K and Sunahara, Roger K
Nature, ISSN 0028-0836, 07/2016, Volume 535, Issue 7610, pp. 182 - 186
G-protein-coupled receptors (GPCRs) remain the primary conduit by which cells detect environmental stimuli and communicate with each other(1). Upon activation... 
ACTIVATION | AFFINITY | BETA-ADRENERGIC-RECEPTOR | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | ANTAGONIST BINDING | TERNARY COMPLEX MODEL | NEUROTENSIN RECEPTOR | ADENYLATE-CYCLASE | GUANINE-NUCLEOTIDES | MUSCARINIC ACETYLCHOLINE-RECEPTOR | Allosteric Regulation - drug effects | GTP-Binding Protein alpha Subunits, Gs - metabolism | Single-Chain Antibodies - pharmacology | GTP-Binding Protein alpha Subunits, Gs - pharmacology | Allosteric Site - drug effects | Humans | Protein Conformation - drug effects | Adrenergic beta-2 Receptor Agonists - metabolism | Models, Molecular | Receptors, Adrenergic, beta-2 - immunology | Receptors, Adrenergic, beta-2 - metabolism | Receptors, Adrenergic, beta-2 - chemistry | Guanine - metabolism | Guanine - pharmacology | Protein Binding - drug effects | Adrenergic beta-2 Receptor Antagonists - metabolism | Ligands | Kinetics | Single-Chain Antibodies - immunology | G proteins | Observations | Health aspects | Protein-protein interactions | Proteins | Cellular biology | Binding sites | Cells | nucleotide-free | receptor conformation | GPCR
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
11. Full Text An intrabody based on a llama single-domain antibody targeting the N-terminal α-helical multimerization domain of HIV-1 Rev prevents viral production
by Vercruysse, Thomas and Pardon, Els and Vanstreels, Els and Steyaert, Jan and Daelemans, Dirk
Journal of Biological Chemistry, ISSN 0021-9258, 07/2010, Volume 285, Issue 28, pp. 21768 - 21780
The human immunodeficiency virus, type 1 (HIV-1)-encoded Rev protein is essential for the expression of late viral mRNAs. Rev forms a large organized... 
PFIZER MONKEY VIRUS | PROTEIN | VIRUS TYPE-1 REPLICATION | MESSENGER-RNA | TRANS-ACTIVATOR | BIOCHEMISTRY & MOLECULAR BIOLOGY | IN-VIVO | NUCLEAR EXPORT SIGNAL | GENE-EXPRESSION | FUNCTIONAL-ANALYSIS | STRUCTURAL MODEL | Anti-HIV Agents - pharmacology | Protein Structure, Tertiary | Amino Acid Sequence | HIV-1 - metabolism | Protein Structure, Secondary | Antibodies - chemistry | Humans | Molecular Sequence Data | Protein Interaction Mapping | Camelids, New World | Gene Products, rev - metabolism | Animals | Gene Products, rev - chemistry | Fluorescence Resonance Energy Transfer | HIV Infections - drug therapy | Active Transport, Cell Nucleus | HeLa Cells | Lysine - chemistry | Dimerization | Tyrosine - chemistry | Nanobody | RNA Transport | Single-domain Antibody | Microbiology | RNA | HIV | Rev Multimerization | Fluorescence Resonance Energy Transfer (FRET) | RNA-binding Protein | Protein-Protein Interactions
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights