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Items: 47


Proteasome-targeted nanobodies alleviate pathology and functional decline in an α-synuclein-based Parkinson's disease model.

Chatterjee D, Bhatt M, Butler D, De Genst E, Dobson CM, Messer A, Kordower JH.

NPJ Parkinsons Dis. 2018 Aug 22;4:25. doi: 10.1038/s41531-018-0062-4. eCollection 2018.


Exploring the role of post-translational modifications in regulating α-synuclein interactions by studying the effects of phosphorylation on nanobody binding.

El Turk F, De Genst E, Guilliams T, Fauvet B, Hejjaoui M, Di Trani J, Chiki A, Mittermaier A, Vendruscolo M, Lashuel HA, Dobson CM.

Protein Sci. 2018 Jul;27(7):1262-1274. doi: 10.1002/pro.3412.


Application of Lysine-specific Labeling to Detect Transient Interactions Present During Human Lysozyme Amyloid Fibril Formation.

Ahn M, Waudby CA, Bernardo-Gancedo A, De Genst E, Dhulesia A, Salvatella X, Christodoulou J, Dobson CM, Kumita JR.

Sci Rep. 2017 Nov 3;7(1):15018. doi: 10.1038/s41598-017-14739-5.


Immunization with α-synuclein/Grp94 reshapes peripheral immunity and suppresses microgliosis in a chronic Parkinsonism model.

Villadiego J, Labrador-Garrido A, Franco JM, Leal-Lasarte M, De Genst EJ, Dobson CM, Pozo D, Toledo-Aral JJ, Roodveldt C.

Glia. 2018 Jan;66(1):191-205. doi: 10.1002/glia.23237. Epub 2017 Oct 11.


Sequential Release of Proteins from Structured Multishell Microcapsules.

Shimanovich U, Michaels TCT, De Genst E, Matak-Vinkovic D, Dobson CM, Knowles TPJ.

Biomacromolecules. 2017 Oct 9;18(10):3052-3059. doi: 10.1021/acs.biomac.7b00351. Epub 2017 Sep 7.


Silk micrococoons for protein stabilisation and molecular encapsulation.

Shimanovich U, Ruggeri FS, De Genst E, Adamcik J, Barros TP, Porter D, Müller T, Mezzenga R, Dobson CM, Vollrath F, Holland C, Knowles TPJ.

Nat Commun. 2017 Jul 19;8:15902. doi: 10.1038/ncomms15902.


Nanobodies raised against monomeric ɑ-synuclein inhibit fibril formation and destabilize toxic oligomeric species.

Iljina M, Hong L, Horrocks MH, Ludtmann MH, Choi ML, Hughes CD, Ruggeri FS, Guilliams T, Buell AK, Lee JE, Gandhi S, Lee SF, Bryant CE, Vendruscolo M, Knowles TPJ, Dobson CM, De Genst E, Klenerman D.

BMC Biol. 2017 Jul 3;15(1):57. doi: 10.1186/s12915-017-0390-6.


Phage display and kinetic selection of antibodies that specifically inhibit amyloid self-replication.

Munke A, Persson J, Weiffert T, De Genst E, Meisl G, Arosio P, Carnerup A, Dobson CM, Vendruscolo M, Knowles TPJ, Linse S.

Proc Natl Acad Sci U S A. 2017 Jun 20;114(25):6444-6449. doi: 10.1073/pnas.1700407114. Epub 2017 Jun 5.


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

Ahn M, Hagan CL, Bernardo-Gancedo A, De Genst E, Newby FN, Christodoulou J, Dhulesia A, Dumoulin M, Robinson CV, Dobson CM, Kumita JR.

Biophys J. 2016 Dec 6;111(11):2358-2367. doi: 10.1016/j.bpj.2016.10.028.


From Compact to String-The Role of Secondary and Tertiary Structure in Charge-Induced Unzipping of Gas-Phase Proteins.

Warnke S, Hoffmann W, Seo J, De Genst E, von Helden G, Pagel K.

J Am Soc Mass Spectrom. 2017 Apr;28(4):638-646. doi: 10.1007/s13361-016-1551-5. Epub 2016 Dec 5.


Protein Aggregate-Ligand Binding Assays Based on Microfluidic Diffusional Separation.

Zhang Y, Buell AK, Müller T, De Genst E, Benesch J, Dobson CM, Knowles TP.

Chembiochem. 2016 Oct 17;17(20):1920-1924. doi: 10.1002/cbic.201600384. Epub 2016 Aug 24.


Individual aggregates of amyloid beta induce temporary calcium influx through the cell membrane of neuronal cells.

Drews A, Flint J, Shivji N, Jönsson P, Wirthensohn D, De Genst E, Vincke C, Muyldermans S, Dobson C, Klenerman D.

Sci Rep. 2016 Aug 24;6:31910. doi: 10.1038/srep31910.


Structural Effects of Two Camelid Nanobodies Directed to Distinct C-Terminal Epitopes on α-Synuclein.

El-Turk F, Newby FN, De Genst E, Guilliams T, Sprules T, Mittermaier A, Dobson CM, Vendruscolo M.

Biochemistry. 2016 Jun 7;55(22):3116-22. doi: 10.1021/acs.biochem.6b00149. Epub 2016 May 26.


Microfluidic Diffusion Analysis of the Sizes and Interactions of Proteins under Native Solution Conditions.

Arosio P, Müller T, Rajah L, Yates EV, Aprile FA, Zhang Y, Cohen SI, White DA, Herling TW, De Genst EJ, Linse S, Vendruscolo M, Dobson CM, Knowles TP.

ACS Nano. 2016 Jan 26;10(1):333-41. doi: 10.1021/acsnano.5b04713. Epub 2015 Dec 23.


Chaperome screening leads to identification of Grp94/Gp96 and FKBP4/52 as modulators of the α-synuclein-elicited immune response.

Labrador-Garrido A, Cejudo-Guillén M, Daturpalli S, Leal MM, Klippstein R, De Genst EJ, Villadiego J, Toledo-Aral JJ, Dobson CM, Jackson SE, Pozo D, Roodveldt C.

FASEB J. 2016 Feb;30(2):564-77. doi: 10.1096/fj.15-275131. Epub 2015 Oct 6.


Latent analysis of unmodified biomolecules and their complexes in solution with attomole detection sensitivity.

Yates EV, Müller T, Rajah L, De Genst EJ, Arosio P, Linse S, Vendruscolo M, Dobson CM, Knowles TP.

Nat Chem. 2015 Oct;7(10):802-9. doi: 10.1038/nchem.2344. Epub 2015 Sep 14.


Development of a high affinity Affibody-derived protein against amyloid β-peptide for future Alzheimer's disease therapy.

De Genst E, Muyldermans S.

Biotechnol J. 2015 Sep;10(11):1668-9. doi: 10.1002/biot.201500405. Epub 2015 Sep 10. No abstract available.


Chaperoned amyloid proteins for immune manipulation: α-Synuclein/Hsp70 shifts immunity toward a modulatory phenotype.

Labrador-Garrido A, Cejudo-Guillén M, Klippstein R, De Genst EJ, Tomas-Gallardo L, Leal MM, Villadiego J, Toledo-Aral JJ, Dobson CM, Pozo D, Roodveldt C.

Immun Inflamm Dis. 2014 Dec;2(4):226-38. doi: 10.1002/iid3.39. Epub 2014 Dec 5.


Structure of a single-chain Fv bound to the 17 N-terminal residues of huntingtin provides insights into pathogenic amyloid formation and suppression.

De Genst E, Chirgadze DY, Klein FA, Butler DC, Matak-Vinković D, Trottier Y, Huston JS, Messer A, Dobson CM.

J Mol Biol. 2015 Jun 19;427(12):2166-78. doi: 10.1016/j.jmb.2015.03.021. Epub 2015 Apr 8.


Structural characterization of toxic oligomers that are kinetically trapped during α-synuclein fibril formation.

Chen SW, Drakulic S, Deas E, Ouberai M, Aprile FA, Arranz R, Ness S, Roodveldt C, Guilliams T, De-Genst EJ, Klenerman D, Wood NW, Knowles TP, Alfonso C, Rivas G, Abramov AY, Valpuesta JM, Dobson CM, Cremades N.

Proc Natl Acad Sci U S A. 2015 Apr 21;112(16):E1994-2003. doi: 10.1073/pnas.1421204112. Epub 2015 Apr 8.


Differential nuclear localization of complexes may underlie in vivo intrabody efficacy in Huntington's disease.

Butler DC, Snyder-Keller A, De Genst E, Messer A.

Protein Eng Des Sel. 2014 Oct;27(10):359-63. doi: 10.1093/protein/gzu041.


Antibodies and protein misfolding: From structural research tools to therapeutic strategies.

De Genst E, Messer A, Dobson CM.

Biochim Biophys Acta. 2014 Nov;1844(11):1907-1919. doi: 10.1016/j.bbapap.2014.08.016. Epub 2014 Sep 4. Review.


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

De Genst E, Chan PH, Pardon E, Hsu SD, Kumita JR, Christodoulou J, Menzer L, Chirgadze DY, Robinson CV, Muyldermans S, Matagne A, Wyns L, Dobson CM, Dumoulin M.

J Phys Chem B. 2013 Oct 24;117(42):13245-13258. doi: 10.1021/jp403425z. Epub 2013 Sep 24.


Nanobodies raised against monomeric α-synuclein distinguish between fibrils at different maturation stages.

Guilliams T, El-Turk F, Buell AK, O'Day EM, Aprile FA, Esbjörner EK, Vendruscolo M, Cremades N, Pardon E, Wyns L, Welland ME, Steyaert J, Christodoulou J, Dobson CM, De Genst E.

J Mol Biol. 2013 Jul 24;425(14):2397-411. doi: 10.1016/j.jmb.2013.01.040. Epub 2013 Apr 1.


Analysis of the native structure, stability and aggregation of biotinylated human lysozyme.

Ahn M, De Genst E, Kaminski Schierle GS, Erdelyi M, Kaminski CF, Dobson CM, Kumita JR.

PLoS One. 2012;7(11):e50192. doi: 10.1371/journal.pone.0050192. Epub 2012 Nov 16.


A rationally designed six-residue swap generates comparability in the aggregation behavior of α-synuclein and β-synuclein.

Roodveldt C, Andersson A, De Genst EJ, Labrador-Garrido A, Buell AK, Dobson CM, Tartaglia GG, Vendruscolo M.

Biochemistry. 2012 Nov 6;51(44):8771-8. doi: 10.1021/bi300558q. Epub 2012 Oct 22.


Nanobodies as structural probes of protein misfolding and fibril formation.

De Genst E, Dobson CM.

Methods Mol Biol. 2012;911:533-58. doi: 10.1007/978-1-61779-968-6_34. Review.


Observation of spatial propagation of amyloid assembly from single nuclei.

Knowles TP, White DA, Abate AR, Agresti JJ, Cohen SI, Sperling RA, De Genst EJ, Dobson CM, Weitz DA.

Proc Natl Acad Sci U S A. 2011 Sep 6;108(36):14746-51. doi: 10.1073/pnas.1105555108. Epub 2011 Aug 26.


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

De Genst EJ, Guilliams T, Wellens J, O'Day EM, Waudby CA, Meehan S, Dumoulin M, Hsu ST, Cremades N, Verschueren KH, Pardon E, Wyns L, Steyaert J, Christodoulou J, Dobson CM.

J Mol Biol. 2010 Sep 17;402(2):326-43. doi: 10.1016/j.jmb.2010.07.001. Epub 2010 Jul 8.


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.

Hagan CL, Johnson RJ, Dhulesia A, Dumoulin M, Dumont J, De Genst E, Christodoulou J, Robinson CV, Dobson CM, Kumita JR.

Protein Eng Des Sel. 2010 Jul;23(7):499-506. doi: 10.1093/protein/gzq023. Epub 2010 Apr 9.


(1)H, (13)C and (15)N assignments of a camelid nanobody directed against human alpha-synuclein.

Vuchelen A, O'Day E, De Genst E, Pardon E, Wyns L, Dumoulin M, Dobson CM, Christodoulou J, Hsu ST.

Biomol NMR Assign. 2009 Dec;3(2):231-3. doi: 10.1007/s12104-009-9182-4.


Camelid immunoglobulins and nanobody technology.

Muyldermans S, Baral TN, Retamozzo VC, De Baetselier P, De Genst E, Kinne J, Leonhardt H, Magez S, Nguyen VK, Revets H, Rothbauer U, Stijlemans B, Tillib S, Wernery U, Wyns L, Hassanzadeh-Ghassabeh G, Saerens D.

Vet Immunol Immunopathol. 2009 Mar 15;128(1-3):178-83. doi: 10.1016/j.vetimm.2008.10.299. Epub 2008 Oct 17.


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

Chan PH, Pardon E, Menzer L, De Genst E, Kumita JR, Christodoulou J, Saerens D, Brans A, Bouillenne F, Archer DB, Robinson CV, Muyldermans S, Matagne A, Redfield C, Wyns L, Dobson CM, Dumoulin M.

Biochemistry. 2008 Oct 21;47(42):11041-54. doi: 10.1021/bi8005797. Epub 2008 Sep 25.


Wnt3a binds to several sFRPs in the nanomolar range.

Wawrzak D, Métioui M, Willems E, Hendrickx M, de Genst E, Leyns L.

Biochem Biophys Res Commun. 2007 Jun 15;357(4):1119-23. Epub 2007 Apr 19.


Molecular basis for the preferential cleft recognition by dromedary heavy-chain antibodies.

De Genst E, Silence K, Decanniere K, Conrath K, Loris R, Kinne J, Muyldermans S, Wyns L.

Proc Natl Acad Sci U S A. 2006 Mar 21;103(12):4586-91. Epub 2006 Mar 13.


Variations in antigen-antibody association kinetics as a function of pH and salt concentration: a QSAR and molecular modeling study.

Dejaegere A, Choulier L, Lafont V, De Genst E, Altschuh D.

Biochemistry. 2005 Nov 8;44(44):14409-18.


Antibody repertoire development in camelids.

De Genst E, Saerens D, Muyldermans S, Conrath K.

Dev Comp Immunol. 2006;30(1-2):187-98. Review.


Molecular basis of gyrase poisoning by the addiction toxin CcdB.

Dao-Thi MH, Van Melderen L, De Genst E, Afif H, Buts L, Wyns L, Loris R.

J Mol Biol. 2005 May 20;348(5):1091-102. Epub 2005 Apr 7.


Strong in vivo maturation compensates for structurally restricted H3 loops in antibody repertoires.

De Genst E, Silence K, Ghahroudi MA, Decanniere K, Loris R, Kinne J, Wyns L, Muyldermans S.

J Biol Chem. 2005 Apr 8;280(14):14114-21. Epub 2005 Jan 19.


Receptor binding studies disclose a novel class of high-affinity inhibitors of the Escherichia coli FimH adhesin.

Bouckaert J, Berglund J, Schembri M, De Genst E, Cools L, Wuhrer M, Hung CS, Pinkner J, Slättegård R, Zavialov A, Choudhury D, Langermann S, Hultgren SJ, Wyns L, Klemm P, Oscarson S, Knight SD, De Greve H.

Mol Microbiol. 2005 Jan;55(2):441-55.


Chemical basis for the affinity maturation of a camel single domain antibody.

De Genst E, Handelberg F, Van Meirhaeghe A, Vynck S, Loris R, Wyns L, Muyldermans S.

J Biol Chem. 2004 Dec 17;279(51):53593-601. Epub 2004 Sep 21.


Crystallization of CcdB in complex with a GyrA fragment.

Dao-Thi MH, Van Melderen L, De Genst E, Buts L, Ranquin A, Wyns L, Loris R.

Acta Crystallogr D Biol Crystallogr. 2004 Jun;60(Pt 6):1132-4. Epub 2004 May 21.


The fimbrial adhesin F17-G of enterotoxigenic Escherichia coli has an immunoglobulin-like lectin domain that binds N-acetylglucosamine.

Buts L, Bouckaert J, De Genst E, Loris R, Oscarson S, Lahmann M, Messens J, Brosens E, Wyns L, De Greve H.

Mol Microbiol. 2003 Aug;49(3):705-15.


Solving the phase problem for carbohydrate-binding proteins using selenium derivatives of their ligands: a case study involving the bacterial F17-G adhesin.

Buts L, Loris R, De Genst E, Oscarson S, Lahmann M, Messens J, Brosens E, Wyns L, De Greve H, Bouckaert J.

Acta Crystallogr D Biol Crystallogr. 2003 Jun;59(Pt 6):1012-5. Epub 2003 May 23.


Kinetic and affinity predictions of a protein-protein interaction using multivariate experimental design.

De Genst E, Areskoug D, Decanniere K, Muyldermans S, Andersson K.

J Biol Chem. 2002 Aug 16;277(33):29897-907. Epub 2002 Jun 4.


Camel single-domain antibody inhibits enzyme by mimicking carbohydrate substrate.

Transue TR, De Genst E, Ghahroudi MA, Wyns L, Muyldermans S.

Proteins. 1998 Sep 1;32(4):515-22.


Potent enzyme inhibitors derived from dromedary heavy-chain antibodies.

Lauwereys M, Arbabi Ghahroudi M, Desmyter A, Kinne J, Hölzer W, De Genst E, Wyns L, Muyldermans S.

EMBO J. 1998 Jul 1;17(13):3512-20.

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