M. Dumoulin

发表

Single‐domain antibody fragments with high conformational stability

L. Wyns, S. Muyldermans, K. Conrath, 2002, Protein science : a publication of the Protein Society.

Identification of a universal VHH framework to graft non-canonical antigen-binding loops of camel single-domain antibodies.

L. Wyns, S. Muyldermans, E. Pardon, 2005, Journal of molecular biology.

Structure and properties of a complex of α-synuclein and a single-domain camelid antibody.

C. Dobson, L. Wyns, E. Pardon, 2010, Journal of molecular biology.

Disulfide Bonds Reduce the Toxicity of the Amyloid Fibrils Formed by an Extracellular Protein**

C. Dobson, X. Salvatella, Anne Dhulesia, 2011, Angewandte Chemie.

A non-internalised CD38-binding radiolabelled single-domain antibody fragment to monitor and treat multiple myeloma

F. Baron, N. Devoogdt, M. Dumoulin, 2021, Journal of Hematology & Oncology.

The Role of Active Site Flexible Loops in Catalysis and of Zinc in Conformational Stability of Bacillus cereus 569/H/9 β-Lactamase*

G. Roberts, A. I. Karsisiotis, C. Damblon, 2016, The Journal of Biological Chemistry.

Textural Properties of Pressure-Induced Gels of Food Proteins Obtained under Different Temperatures including Subzero

R. Hayashi, M. Dumoulin, S. Ozawa, 1997 .

Radiotheranostic Agents in Hematological Malignancies

N. Withofs, A. Karlström, N. Devoogdt, 2022, Frontiers in Immunology.

Contribution of the carbohydrate moiety to conformational stability of the carboxypeptidase Y high pressure study.

R. Hayashi, H. Ueno, C. Balny, 1999, European journal of biochemistry.

Development of nanobodies as theranostic agents against CMY-2-like class C β-lactamases

M. Galleni, M. Vandevenne, A. Vanderplasschen, 2022, bioRxiv.

The Significance of the Location of Mutations for the Native-State Dynamics of Human Lysozyme

Francisco N. Newby, C. Dobson, C. Robinson, 2016, Biophysical journal.

Activation of innate immunity by lysozyme fibrils is critically dependent on cross-β sheet structure

J. Ruysschaert, C. Bryant, C. Lonez, 2013, Cellular and Molecular Life Sciences.

Impact of the PEG length and PEGylation site on the structural, thermodynamic, thermal, and proteolytic stability of mono‐PEGylated alpha‐1 antitrypsin

R. Vanbever, M. Dumoulin, Xiao Liu, 2022, Protein science : a publication of the Protein Society.

Comparative study of mature and zymogen mite cysteine protease stability and pH unfolding.

M. Galleni, A. Matagne, M. Dumoulin, 2010, Biochimica et biophysica acta.

Normal and aberrant biological self-assembly: Insights from studies of human lysozyme and its amyloidogenic variants.

C. Dobson, M. Dumoulin, J. Kumita, 2006, Accounts of chemical research.

Protein Engineering Strategies for Improved Pharmacokinetics

R. Vanbever, M. Dumoulin, Francisco Morales-Yánez, 2021, Advanced Functional Materials.

The Bacillus licheniformis BlaP β‐lactamase as a model protein scaffold to study the insertion of protein fragments

J. Frère, J. François, M. Galleni, 2007, Protein science : a publication of the Protein Society.

High Pressure, a Unique Tool for Food Texturization.

R. Hayashi, M. Dumoulin, 1998 .

Modeling Parkinson’s Disease With the Alpha-Synuclein Protein

R. Moratalla, M. Dumoulin, Patricia García-Sanz, 2020, Frontiers in Pharmacology.

The disulphide mapping, folding and characterisation of recombinant Ber e 1, an allergenic protein, and SFA8, two sulphur-rich 2S plant albumins.

M. J. Parker, K. Bailey, M. Alcocer, 2002, Journal of molecular biology.

Camelid single-domain antibody fragments: Uses and prospects to investigate protein misfolding and aggregation, and to treat diseases associated with these phenomena.

M. Dumoulin, J. Dumont, C. Pain, 2015, Biochimie.

Mass and charge distributions of amyloid fibers involved in neurodegenerative diseases: mapping heterogeneity and polymorphism† †Electronic supplementary information (ESI) available: Experimental section and supplementary figures. See DOI: 10.1039/c7sc04542e

P. Dugourd, R. Antoine, S. Chierici, 2018, Chemical science.

The Non-Core Regions of Human Lysozyme Amyloid Fibrils Influence Cytotoxicity

Christopher M. Dobson, Mireille Dumoulin, Xavier Salvatella, 2010, Journal of molecular biology.

DNA-binding and dimerization domains of adenosine 3',5'- cyclic monophosphate-responsive protein CREB reside in the carboxyl-terminal 66 amino acids.

J. Habener, M. Dumoulin, Y. Yun, 1990, Molecular endocrinology.

C. Dobson, D. Lomas, D. Crowther, 2012, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

Rationalising lysozyme amyloidosis: insights from the structure and solution dynamics of T70N lysozyme.

Mireille Dumoulin, Christopher M Dobson, Carol V Robinson, 2005, Journal of molecular biology.

A nanobody binding to non-amyloidogenic regions of the protein human lysozyme enhances partial unfolding but inhibits amyloid fibril formation.

C. Dobson, L. Wyns, S. Muyldermans, 2013, The journal of physical chemistry. B.

Mass and charge distributions of amyloid fibers involved in neurodegenerative diseases: mapping heterogeneity and polymorphism

P. Dugourd, R. Antoine, S. Chierici, 2018 .

Characterization of oligomeric species on the aggregation pathway of human lysozyme.

C. Dobson, A. Fontana, P. P. de Laureto, 2009, Journal of molecular biology.

Local Cooperativity in an Amyloidogenic State of Human Lysozyme Observed at Atomic Resolution

Christopher M. Dobson, Mireille Dumoulin, Xavier Salvatella, 2010, Journal of the American Chemical Society.

Influence of the protein context on the polyglutamine length-dependent elongation of amyloid fibrils.

Alexander K. Buell, C. Jérôme, Anne-Sophie Duwez, 2015, Biochimica et biophysica acta.

Class A β-Lactamases as Versatile Scaffolds to Create Hybrid Enzymes: Applications from Basic Research to Medicine

M. Galleni, A. Matagne, M. Dumoulin, 2013, BioMed research international.

Effects of monopropanediamino-β-cyclodextrin on the denaturation process of the hybrid protein BlaPChBD.

J. Frère, M. Galleni, M. Vandevenne, 2011, Biochimica et biophysica acta.

A camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme

Christopher M. Dobson, Mireille Dumoulin, Lode Wyns, 2003, Nature.

Identification of the core structure of lysozyme amyloid fibrils by proteolysis.

Mireille Dumoulin, Angelo Fontana, Christopher M Dobson, 2006, Journal of molecular biology.

Probing the origins, diagnosis and treatment of amyloid diseases using antibodies.

C. Dobson, M. Dumoulin, 2004, Biochimie.

Separation and determination of alpha‐synuclein monomeric and oligomeric species using two electrophoretic approaches

A. Servais, M. Merville, G. Garraux, 2018, Electrophoresis.

1H, 13C and 15N backbone resonance assignments of the β-lactamase BlaP from Bacillus licheniformis 749/C and two mutational variants

A. Corazza, C. Damblon, M. Dumoulin, 2017, Biomolecular NMR Assignments.

1H, 13C and 15N backbone resonance assignments of the β-lactamase BlaP from Bacillus licheniformis 749/C and two mutational variants

A. Corazza, C. Damblon, M. Dumoulin, 2017, Biomolecular NMR Assignments.

Amyloid-Like Fibril Formation by PolyQ Proteins: A Critical Balance between the PolyQ Length and the Constraints Imposed by the Host Protein

Mireille Dumoulin, André Matagne, Moreno Galleni, 2012, PloS one.

Multimodal imaging Gd-nanoparticles functionalized with Pittsburgh compound B or a nanobody for amyloid plaques targeting.

O. Tillement, M. Saraiva, Laurence Heinrich-Balard, 2017, Nanomedicine.

In vitro stability and immunoreactivity of the native and recombinant plant food 2S albumins Ber e 1 and SFA‐8

M. Alcocer, D. Archer, M. Dumoulin, 2003, Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology.

Reduced global cooperativity is a common feature underlying the amyloidogenicity of pathogenic lysozyme mutations.

Mireille Dumoulin, Lode Wyns, Christopher M Dobson, 2005, Journal of molecular biology.

Impact of the native‐state stability of human lysozyme variants on protein secretion by Pichia pastoris

C. Dobson, C. Robinson, M. Alcocer, 2006, The FEBS journal.

The zinc center influences the redox and thermodynamic properties of Escherichia coli thioredoxin 2.

Mireille Dumoulin, Goedele Roos, Joris Messens, 2009, Journal of molecular biology.

Insights on peptide topology in the computational design of protein ligands: the example of lysozyme binding peptides.

Miguel A. Soler, G. Scoles, R. Grandori, 2021, Physical chemistry chemical physics : PCCP.

1H, 13C and 15N assignments of a camelid nanobody directed against human α-synuclein

C. Dobson, L. Wyns, E. Pardon, 2009, Biomolecular NMR assignments.

Stability of recombinant 2 S albumin allergens in vitro.

M. Alcocer, D. Archer, M. Dumoulin, 2001, Biochemical Society transactions.

In vitro aggregating β-lactamase-polyQ chimeras do not induce toxic effects in an in vivo Caenorhabditis elegans model

Roel Van Assche, L. Schoofs, L. Temmerman, 2017, Journal of Negative Results in BioMedicine.

Gd-nanoparticles functionalization with specific peptides for ß-amyloid plaques targeting

O. Tillement, M. Saraiva, Laurence Heinrich-Balard, 2016, Journal of Nanobiotechnology.

Population of nonnative states of lysozyme variants drives amyloid fibril formation.

Alexander K. Buell, C. Dobson, X. Salvatella, 2011, Journal of the American Chemical Society.

Nebulization of PEGylated recombinant human deoxyribonuclease I using vibrating membrane nebulizers: A technical feasibility study.

H. Frijlink, K. Vanvarenberg, R. Vanbever, 2023, European journal of pharmaceutical sciences : official journal of the European Federation for Pharmaceutical Sciences.

Characterisation of the structural, dynamic and aggregation properties of the W64R amyloidogenic variant of human lysozyme.

C. Dobson, P. Charlier, A. Brans, 2021, Biophysical chemistry.

The extracellular chaperone clusterin potently inhibits human lysozyme amyloid formation by interacting with prefibrillar species.

Mireille Dumoulin, Christopher M Dobson, Elise M. Stewart, 2007, Journal of molecular biology.

A non-natural variant of human lysozyme (I59T) mimics the in vitro behaviour of the I56T variant that is responsible for a form of familial amyloidosis.

C. Dobson, C. Robinson, J. Christodoulou, 2010, Protein engineering, design & selection : PEDS.

Engineering a camelid antibody fragment that binds to the active site of human lysozyme and inhibits its conversion into amyloid fibrils.

C. Dobson, L. Wyns, S. Muyldermans, 2008, Biochemistry.

Activation of innate immunity by lysozyme fibrils is critically dependent on cross-β sheet structure

J. Ruysschaert, C. Bryant, C. Lonez, 2013, Cellular and Molecular Life Sciences.

Reflections on professor Sir Christopher M. Dobson (1949–2019)

M. Dumoulin, 2020, Biophysical Reviews.

Combinatorial Design of a Nanobody that Specifically Targets Structured RNAs.

S. Muyldermans, M. Galleni, M. Vandevenne, 2018, Journal of molecular biology.

Familial Amyloidosis Caused by Lysozyme

M. Dumoulin, 2010 .

Structure and Properties of a Complex of alpha-Synuclein and a Single-Domain Camelid Antibody

L. Wyns, E. Pardon, J. Steyaert, 2010 .