D. Maes

发表

Degenerate interfaces in antigen-antibody complexes.

L. Wyns, K. Decanniere, T. Transue, 2001, Journal of molecular biology.

The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima: A comparative thermostability structural analysis of ten different TIM structures

L. Wyns, J. Martial, D. Maes, 1999, Proteins.

Aspartate transcarbamylase from the hyperthermophilic archaeon Pyrococcus abyssi: thermostability and 1.8A resolution crystal structure of the catalytic subunit complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate.

Raymond Cunin, Dominique Maes, D. Maes, 2003, Journal of molecular biology.

Intricate Interactions within the ccd Plasmid Addiction System*

Lode Wyns, Joris Messens, Remy Loris, 2002, The Journal of Biological Chemistry.

Conserved water molecules in a large family of microbial ribonucleases

K. Decanniere, T. Transue, D. Maes, 1999, Proteins.

Bio-chemical Process Monitoring with Terahertz Sensor

D. Maes, S. Muyldermans, G. He, 2017 .

Confocal Depolarized Dynamic Light Scattering: a Novel Technique for the Characterization of Nanoparticles in Complex Fluids

D. Maes, P. Vekilov, M. Potenza, 2015 .

Characterization of the diffusive dynamics of particles with time-dependent asymmetric microscopy intensity profiles.

D. Maes, P. Vekilov, M. Vorontsova, 2016, Soft matter.

Do protein crystals nucleate within dense liquid clusters?

D. Maes, M. Giglio, P. Vekilov, 2015, Acta crystallographica. Section F, Structural biology communications.

The Ability of Bifidobacteria To Degrade Arabinoxylan Oligosaccharide Constituents and Derived Oligosaccharides Is Strain Dependent

D. Maes, L. De Vuyst, S. Weckx, 2013, Applied and Environmental Microbiology.

The unexpected structure of the designed protein Octarellin V.1 forms a challenge for protein structure prediction tools.

J. Martial, D. Maes, J. Meiler, 2016, Journal of structural biology.

Study on the mixing and migration behavior of micron-size particles in acoustofluidics

D. Maes, W. Malsche, W. De Malsche, 2019, Chemical Engineering Journal.

Structure of the crystalline complex of cytidylic acid (2'-CMP) with ribonuclease at 1.6 A resolution. Conservation of solvent sites in RNase-A high-resolution structures.

Lode Wyns, Rex A. Palmer, Ingrid Zegers, 1993, Acta crystallographica. Section D, Biological crystallography.

YtrASa, a GntR-Family Transcription Factor, Represses Two Genetic Loci Encoding Membrane Proteins in Sulfolobus acidocaldarius

D. Maes, F. van Nieuwerburgh, L. Tilleman, 2019, Front. Microbiol..

Biophysical and Structural Properties of DNA·diC14-amidine Complexes

D. Maes, J. Ruysschaert, J. Backmann, 2000, The Journal of Biological Chemistry.

H NMR study of the solution structure of Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus.

L. Wyns, D. Maes, R. Loris, 1996, Journal of molecular biology.

F/YGG-motif is an intrinsically disordered nucleic-acid binding motif

D. Maes, P. Tompa, Joris Van Lindt, 2022, RNA biology.

A generic approach to study the kinetics of liquid–liquid phase separation under near-native conditions

D. Maes, P. Tompa, R. Pancsa, 2019, Communications Biology.

A comparative structural study on the steroids [1,2,5]oxadiazolo[3′,4′:3,4]-5α-pregn-16-en-20-one oxime (HS998), [1,2,5]oxadiazolo[3′,4′:3,4]-5α-pregn-16-en-20-one (HS974), and [1,2,5]oxadiazolo[3′,4′:3,4]-5β-pregn-16-en-20-one (HS973) by NMR, molecular modeling, and X-ray investigations

L. Wyns, D. Maes, J. Martins, 1995, Steroids.

A New Paradigm of Crystallization Arising from Non-standard Nucleation Pathways

G. Nicolis, D. Maes, C. Kirschhock, 2009 .

The kinetics of the arginine deiminase pathway in the meat starter culture Lactobacillus sakei CTC 494 are pH-dependent.

D. Maes, L. Vuyst, F. Leroy, 2011, Food microbiology.

Crystallization of ornithine acetyltransferase from yeast by counter-diffusion and preliminary X-ray study.

M. Crabeel, L. Wyns, J. Martial, 2006, Acta crystallographica. Section F, Structural biology and crystallization communications.

The Effect of Controlled Mixing on ROY Polymorphism

D. Maes, Q. Galand, W. De Malsche, 2022, Crystals.

ArticleThe Effect of Controlled Mixing on ROY PolymorphismMargot Van Nerom 1

D. Maes, Q. Galand, W. De Malsche, 2022 .

Vrije Universiteit Brussel Growth and Separation of Crystals and Protein Aggregates in Acoustofluidics

D. Maes, W. Malsche, K. Pauwels, 2018 .

In Vitro Kinetic Analysis of Fermentation of Prebiotic Inulin-Type Fructans by Bifidobacterium Species Reveals Four Different Phenotypes

G. Falony, D. Maes, L. De Vuyst, 2008, Applied and Environmental Microbiology.

High-throughput amplicon sequencing to assess the impact of processing factors on the development of microbial communities during spontaneous meat fermentation.

D. Maes, F. Leroy, L. De Vuyst, 2021, International journal of food microbiology.

Sourdoughs as a function of their species diversity and process conditions, a meta-analysis

D. Maes, L. Vuyst, S. V. Kerrebroeck, 2017 .

Lactic acid bacteria community dynamics and metabolite production of rye sourdough fermentations share characteristics of wheat and spelt sourdough fermentations.

P. Vandamme, D. Maes, L. De Vuyst, 2010, Food microbiology.

Aspartate transcarbamylase from the hyperthermophilic archaeon Pyrococcus abyssi

D. Maes, S. Van Boxstael, R. Cunin, 2005, The FEBS journal.

Tri-n-butyltin 2,6-difluorobenzoate, a Unique Macrocyclic Tetramer Containing a 16-membered Sn4c4o8 Ring, and Other Related-compounds

L. Wyns, D. Maes, B. Mahieu,, 1994 .

A Structure of the Complex between Concanavalin A and Methyl-3,6-di-O-(α-D-mannopyranosyl)-α-D-mannopyranoside Reveals Two Binding Modes*

L. Wyns, D. Maes, R. Loris, 1996, The Journal of Biological Chemistry.

Fluxes for Unraveling Complex Binding Mechanisms.

D. Maes, D. Swinney, G. Vauquelin, 2020, Trends in pharmacological sciences.

Purine and pyrimidine-specific repression of the Escherichia coli carAB operon are functionally and structurally coupled.

D. Gigot, D. Maes, D. Charlier, 2004, Journal of molecular biology.

A generic approach to study the kinetics of liquid–liquid phase separation under near-native conditions

D. Maes, P. Tompa, R. Pancsa, 2021, Communications biology.

1H NMR study of the interaction of N,N′,N″‐triacetyl chitotriose with Ac‐AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus

L. Wyns, D. Maes, J. Martins, 1995, FEBS letters.

Ss‐LrpB, a novel Lrp‐like regulator of Sulfolobus solfataricus P2, binds cooperatively to three conserved targets in its own control region

Daniel Charlier, Dominique Maes, Eveline Peeters, 2004, Molecular microbiology.

Observing classical nucleation theory at work by monitoring phase transitions with molecular precision

D. Maes, A. V. Van Driessche, J. Lutsko, 2014, Nature Communications.

Size and Shape Analysis of Sedimentary Grains by Automated Dynamic Image Analysis

D. Maes, L. Deriemaeker, R. Finsy, 2006 .

Dissection of the structural and functional role of a conserved hydration site in RNase T1

D. Maes, J. Steyaert, R. Loris, 2008, Protein science : a publication of the Protein Society.

Triose-phosphate Isomerase (TIM) of the Psychrophilic BacteriumVibrio marinus

Lode Wyns, Dominique Maes, Joseph A. Martial, 1998, The Journal of Biological Chemistry.

Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus. Kinetic and structural properties.

L. Wyns, J. Martial, D. Maes, 1998, The Journal of biological chemistry.

Ss-LrpB from Sulfolobus solfataricus Condenses about 100 Base Pairs of Its Own Operator DNA into Globular Nucleoprotein Complexes*

D. Maes, D. Charlier, R. Willaert, 2006, Journal of Biological Chemistry.

Ligand binding specificity of RutR, a member of the TetR family of transcription regulators in Escherichia coli

V. Rubio, D. Maes, D. Charlier, 2015, FEBS open bio.

Influence of Centrifugation and Shaking on the Self-Assembly of Lysozyme Fibrils

D. Maes, W. De Malsche, S. Stroobants, 2022, Biomolecules.

Recent advances in the understanding of two-step nucleation of protein crystals.

D. Maes, P. Vekilov, M. Vorontsova, 2015, Faraday discussions.

Crystal structure determination and refinement at 2.3-A resolution of the lentil lectin.

R. Pickersgill, L. Wyns, D. Maes, 1993, Biochemistry.

Thiol pegylation facilitates purification of chymopapain leading to diffraction studies at 1.4 Å resolution

L. Wyns, D. Maes, M. Azarkan, 1996 .

Overexpression, purification, crystallization and preliminary X-ray diffraction analysis of the C-terminal domain of Ss-LrpB, a transcription regulator from Sulfolobus solfataricus.

D. Maes, D. Charlier, I. Zegers, 2005, Acta crystallographica. Section F, Structural biology and crystallization communications.

Mutational analysis of Escherichia coli PepA, a multifunctional DNA-binding aminopeptidase.

D. Gigot, N. Glansdorff, D. Maes, 2000, Journal of molecular biology.

What can Mesoscopic Level IN SITU Observations Teach us About Kinetics and Thermodynamics of Protein Crystallization

D. Maes, A. V. Driessche, M. Sleutel, 2012 .

C9orf72-linked arginine-rich dipeptide repeats aggravate pathological phase separation of G3BP1

D. Maes, P. Tompa, R. Pancsa, 2023, bioRxiv.

The structures of rnase a complexed with 3′‐CMP and d(CpA): Active site conformation and conserved water molecules

L. Wyns, D. Maes, I. Zegers, 1994, Protein science : a publication of the Protein Society.

Competition in drug binding and … the race to equilibrium

D. Maes, G. Vauquelin, 2022, Fundamental & clinical pharmacology.

Induced fit versus conformational selection: From rate constants to fluxes… and back to rate constants

D. Maes, G. Vauquelin, 2021, Pharmacology research & perspectives.

Does Solution Viscosity Scale the Rate of Aggregation of Folded Proteins?

Dominique Maes, Weichun Pan, D. Maes, 2012, The journal of physical chemistry letters.

The molecular structure of [1,2,5]oxadiazolo[3′,4′ : 3,4]-5α-pregn-16-en-20-one (HS974). Crystal structure and NMR investigations

L. Wyns, D. Maes, R. Palmer, 1992 .

Mesoscopic Impurities Expose a Nucleation-Limited Regime of Crystal Growth.

D. Maes, A. V. Van Driessche, J. Lutsko, 2015, Physical review letters.

Structure of (20R)-5α-pregnano[3,4-c][1,2,5]oxadiazol-20-ol (HS1011)

L. Wyns, D. Maes, R. Palmer, 1992 .

The structure of 20 oximo-5α-pregnano-16-eno[3,4-C]-1′,2′,5′-oxadiazole (HS976)

D. Maes, R. Palmer, D. Lisgarten, 1993 .

Structure of (20R)-5α-Pregnano(3,4-c)(1,2,5)oxadiazol-20-ol ( HS1011)

L. Wyns, D. Maes, R. Palmer, 1992 .

Protein crystallisation under microgravity conditions: What did we learn on TIM crystallisation from the Soyuz missions?

C. Weerdt, J. Martial, K. Decanniere, 2007 .

SizeandShapeAnalysisof SedimentaryGrainsbyAutomated Dynamic ImageAnalysis

D. Maes, L. Deriemaeker, R. Finsy, 2006 .

The protein–DNA contacts in RutR·carAB operator complexes

D. Maes, D. Charlier, Indra Bervoets, 2010, Nucleic acids research.

Insights into the architecture and stoichiometry of Escherichia coli PepA•DNA complexes involved in transcriptional control and site-specific DNA recombination by atomic force microscopy

D. Maes, D. Charlier, J. Massant, 2009, Nucleic acids research.

Crystal Growth Cessation Revisited: The Physical Basis of Step Pinning

D. Maes, A. V. Driessche, N. González-Segredo, 2014 .

An Unconventional Mode of Protein Crystal Growth: Case Study Xylanase

D. Maes, A. V. Driessche, M. Sleutel, 2012 .

Structures of chromium(III) cyclam complexes. 2. Structure of trans‐dibromo(1,4,8,11‐tetraazacyclotetradecane)chromium(III) bromide

R. W. Janes, D. Maes, R. Palmer, 1990 .

Structural study of the type II 3-dehydroquinate dehydratase from Actinobacillus pleuropneumoniae.

D. Maes, S. Gulnik, B. Yu, 2004, Acta crystallographica. Section D, Biological crystallography.

Step Crowding Effects Dampen the Stochasticity of Crystal Growth Kinetics.

D. Maes, A. V. Van Driessche, J. Lutsko, 2016, Physical review letters.

Kinetic Roughening of Glucose Isomerase Crystals

L. Wyns, D. Maes, R. Willaert, 2008 .

Analysis of the DNA-binding sequence specificity of the archaeal transcriptional regulator Ss-LrpB from Sulfolobus solfataricus by systematic mutagenesis and high resolution contact probing

D. Maes, D. Charlier, E. Peeters, 2006, Nucleic acids research.

Retrocopied Genes May Enhance Male Fitness

D. Maes, D. Charlier, E. Peeters, 2005, PLoS Biology.

Kinetic rougheninglike transition with finite nucleation barrier.

J. J. Kozak, G. Nicolis, D. Maes, 2010, The Journal of chemical physics.

Aspidosperma subincanum II. Usefulness of uleine and ribonucleic fragments in the treatment of AIDS patients

D. Maes, R. Maes, 2015 .

Quantification of Intrinsically Disordered Proteins: A Problem Not Fully Appreciated

D. Maes, P. Tompa, K. Pauwels, 2018, Front. Mol. Biosci..

BarR, an Lrp‐type transcription factor in Sulfolobus acidocaldarius, regulates an aminotransferase gene in a β‐alanine responsive manner

D. Maes, R. Bernander, D. Charlier, 2014, Molecular microbiology.

Structure of the Prx6-subfamily 1-Cys peroxiredoxin from Sulfolobus islandicus

D. Maes, I. Van Molle, Karl Jonckheere, 2019, Acta crystallographica. Section F, Structural biology communications.

Structure of chymopapain at 1.7 A resolution.

L. Wyns, D. Maes, Y. Looze, 1996, Biochemistry.

Focusing of Microcrystals and Liquid Condensates in Acoustofluidics

Peter Tompa, Dominique Maes, Anna Bratek-Skicki, 2019, Crystals.

Lys13 Plays a Crucial Role in the Functional Adaptation of the Thermophilic Triose-phosphate Isomerase fromBacillus stearothermophilus to High Temperatures*

L. Wyns, J. Martial, D. Maes, 1999, The Journal of Biological Chemistry.

Competition between induced fit- and conformational selection binding: how different flux-based approaches help clarifying their interplay

D. Maes, G. Vauquelin, 2023, bioRxiv.

Polymorph Selection of ROY by Flow-Driven Crystallization

D. Maes, A. Wit, I. Ziemecka, 2019, Crystals.

Crystallization and preliminary X-ray diffraction analysis of the arginine repressor of the hyperthermophile Thermotoga neapolitana.

D. Maes, D. Charlier, E. Peeters, 2006, Acta crystallographica. Section F, Structural biology and crystallization communications.

Two crystal forms of the lentil lectin diffract to high resolution.

R. Pickersgill, L. Wyns, D. Maes, 1992, Journal of molecular biology.

Kinetics and Thermodynamics of Glucose Isomerase Crystallization

L. Wyns, D. Maes, R. Willaert, 2009 .

Toward a Definition of X-ray Crystal Quality†

G. Nicolis, C. Weerdt, J. Martial, 2008 .

In Vitro Kinetic Analysis of Fermentation of Prebiotic Inulin-Type Fructans by Bifidobacterium Species Reveals Four Different Phenotypes

G. Falony, D. Maes, L. De Vuyst, 2008, Applied and Environmental Microbiology.

Microfluidic Device for High-Throughput Production of Monodisperse Droplets

D. Maes, I. Ziemecka, W. De Malsche, 2020 .

Does Solution Viscosity Scale the Rate of Aggregation of Folded Proteins?

D. Maes, P. Vekilov, Weichun Pan, 2012, The journal of physical chemistry letters.