| Year |
Citation |
Score |
| 2024 |
Olsen WP, Courtade G, Peña-Díaz S, Nagaraj M, Sønderby TV, Mulder FAA, Malle MG, Otzen DE. CsgA gatekeeper residues control nucleation but not stability of functional amyloid. Protein Science : a Publication of the Protein Society. 33: e5178. PMID 39302107 DOI: 10.1002/pro.5178 |
0.354 |
|
| 2024 |
Žvirblis M, Sakalauskas A, Janvand SHA, Dudutienė V, Žiaunys M, Sniečkutė R, Otzen DE, Smirnovas V, Matulis D. Structure-Activity Relationship of Fluorinated Benzenesulfonamides as Inhibitors of Amyloid-β Aggregation. Chemistry (Weinheim An Der Bergstrasse, Germany). e202402330. PMID 39109590 DOI: 10.1002/chem.202402330 |
0.334 |
|
| 2024 |
Nielsen J, Lauritsen J, Pedersen JN, Nowak JS, Bendtsen MK, Kleijwegt G, Lusser K, Pitarch LC, Moreno JV, Schneider MM, Krainer G, Goksøyr L, Khalifé P, Kaalund SS, Aznar S, ... ... Otzen DE, et al. Molecular properties and diagnostic potential of monoclonal antibodies targeting cytotoxic α-synuclein oligomers. Npj Parkinson's Disease. 10: 139. PMID 39075088 DOI: 10.1038/s41531-024-00747-6 |
0.341 |
|
| 2024 |
Adam L, Kumar R, Arroyo-Garcia LE, Molenkamp WH, Nowak JS, Klute H, Farzadfard A, Alkenayeh R, Nielsen J, Biverstål H, Otzen DE, Johansson J, Abelein A. Specific inhibition of α-synuclein oligomer generation and toxicity by the chaperone domain Bri2 BRICHOS. Protein Science : a Publication of the Protein Society. 33: e5091. PMID 38980078 DOI: 10.1002/pro.5091 |
0.371 |
|
| 2024 |
Santos J, Cuellar J, Pallarès I, Byrd EJ, Lends A, Moro F, Abdul-Shukkoor MB, Pujols J, Velasco-Carneros L, Sobott F, Otzen DE, Calabrese AN, Muga A, Pedersen JS, Loquet A, et al. A Targetable N-Terminal Motif Orchestrates α-Synuclein Oligomer-to-Fibril Conversion. Journal of the American Chemical Society. 146: 12702-12711. PMID 38683963 DOI: 10.1021/jacs.4c02262 |
0.385 |
|
| 2024 |
Aliakbari F, Marzookian K, Parsafar S, Hourfar H, Nayeri Z, Fattahi A, Raeiji M, Boroujeni NN, Otzen DE, Morshedi D. The impact of hUC MSC-derived exosome-nanoliposome hybrids on α-synuclein fibrillation and neurotoxicity. Science Advances. 10: eadl3406. PMID 38569030 DOI: 10.1126/sciadv.adl3406 |
0.346 |
|
| 2023 |
Otzen DE. Antibodies and α-synuclein: What to target against Parkinson's Disease? Biochimica Et Biophysica Acta. Proteins and Proteomics. 140943. PMID 37783321 DOI: 10.1016/j.bbapap.2023.140943 |
0.326 |
|
| 2023 |
Roeters SJ, Strunge K, Pedersen KB, Golbek TW, Bregnhøj M, Zhang Y, Wang Y, Dong M, Nielsen J, Otzen DE, Schiøtt B, Weidner T. Elevated concentrations cause upright alpha-synuclein conformation at lipid interfaces. Nature Communications. 14: 5731. PMID 37723164 DOI: 10.1038/s41467-023-39843-1 |
0.358 |
|
| 2023 |
Andersen CB, Lausdahl AK, Nielsen J, Clausen MP, Mulder FAA, Otzen DE, Arnspang EC. 4-Oxo-2-nonenal-Induced α-Synuclein Oligomers Interact with Membranes in the Cell, Leading to Mitochondrial Fragmentation. Biochemistry. 62: 2417-2425. PMID 37487228 DOI: 10.1021/acs.biochem.3c00114 |
0.696 |
|
| 2023 |
Østergaard Rasmussen H, Nielsen J, de Poli A, Otzen D, Skov Pedersen J. Tau Fibrillation Induced by Heparin or a Lysophospholipid Show Different Initial Oligomer Formation. Journal of Molecular Biology. 168194. PMID 37437877 DOI: 10.1016/j.jmb.2023.168194 |
0.336 |
|
| 2023 |
Sønderby TV, Louros NN, Khodaparast L, Khodaparast L, Madsen DJ, Olsen WP, Moonen N, Nagaraj M, Sereikaite V, Strømgaard K, Rousseau F, Schymkowitz J, Otzen DE. Sequence-targeted Peptides Divert Functional Bacterial Amyloid Towards Destabilized Aggregates and Reduce Biofilm Formation. Journal of Molecular Biology. 168039. PMID 37330291 DOI: 10.1016/j.jmb.2023.168039 |
0.302 |
|
| 2023 |
Somavarapu AK, Kleijwegt G, Nagaraj M, Alam P, Nielsen J, Otzen DE. Drug repurposing screens identify compounds that inhibit α-synuclein oligomers' membrane disruption and block antibody interactions. Chemical Science. 14: 3030-3047. PMID 36937574 DOI: 10.1039/d2sc05534a |
0.376 |
|
| 2022 |
Najarzadeh Z, Mohammad-Beigi H, Pedersen JN, Christiansen G, Pedersen JS, Nielsen J, Otzen DE. Interaction of membrane vesicles with the functional amyloid protein FapC facilitates amyloid formation. Bba Advances. 2: 100055. PMID 37082589 DOI: 10.1016/j.bbadva.2022.100055 |
0.404 |
|
| 2022 |
Hadi Ali Janvand S, Ladefoged LK, Zubrienė A, Sakalauskas A, Christiansen G, Dudutienė V, Schiøtt B, Matulis D, Smirnovas V, Otzen DE. Inhibitory effects of fluorinated benzenesulfonamides on insulin fibrillation. International Journal of Biological Macromolecules. 227: 590-600. PMID 36529223 DOI: 10.1016/j.ijbiomac.2022.12.105 |
0.35 |
|
| 2022 |
Pirhaghi M, Frank SA, Alam P, Nielsen J, Sereikaite V, Gupta A, Strømgaard K, Andreasen M, Sharma D, Saboury AA, Otzen DE. A penetratin-derived peptide reduces the membrane permeabilization and cell toxicity of α-synuclein oligomers: A penetratin-derived peptide against α-synuclein oligomers. The Journal of Biological Chemistry. 102688. PMID 36370848 DOI: 10.1016/j.jbc.2022.102688 |
0.33 |
|
| 2022 |
Rasmussen HØ, Kumar A, Shin B, Stylianou F, Sewell L, Xu Y, Otzen DE, Skov Pedersen J, Matthews SJ. FapA is an intrinsically disordered chaperone for Pseudomonas functional amyloid FapC. Journal of Molecular Biology. 167878. PMID 36368411 DOI: 10.1016/j.jmb.2022.167878 |
0.351 |
|
| 2022 |
Grønnemose AL, Østerlund EC, Otzen DE, Jørgensen TJD. EGCG has Dual and Opposing Effects on the N-terminal Region of Self-associating α-synuclein Oligomers. Journal of Molecular Biology. 434: 167855. PMID 36240861 DOI: 10.1016/j.jmb.2022.167855 |
0.315 |
|
| 2022 |
Otzen DE. Functional amyloid in a lipid-like environment: a merry dance of many steps. Essays in Biochemistry. PMID 36205438 DOI: 10.1042/EBC20220062 |
0.424 |
|
| 2022 |
Sønderby TV, Zou Y, Wang P, Wang C, Otzen DE. Molecular-level insights into the surface-induced assembly of Functional Bacterial Amyloid. Biophysical Journal. PMID 35982614 DOI: 10.1016/j.bpj.2022.08.013 |
0.304 |
|
| 2022 |
Sønderby TV, Najarzadeh Z, Otzen DE. Functional Bacterial Amyloids: Understanding Fibrillation, Regulating Biofilm Fibril Formation and Organizing Surface Assemblies. Molecules (Basel, Switzerland). 27. PMID 35807329 DOI: 10.3390/molecules27134080 |
0.374 |
|
| 2022 |
Sahin C, Østerlund EC, Österlund N, Costeira-Paulo J, Pedersen JN, Christiansen G, Nielsen J, Grønnemose AL, Amstrup SK, Tiwari MK, Rao RSP, Bjerrum MJ, Ilag LL, Davies MJ, Marklund EG, ... ... Otzen DE, et al. Structural Basis for Dityrosine-Mediated Inhibition of α-Synuclein Fibrillization. Journal of the American Chemical Society. PMID 35749730 DOI: 10.1021/jacs.2c03607 |
0.341 |
|
| 2022 |
Farzadfard A, König A, Petersen SV, Nielsen J, Vasili E, Dominguez-Meijide A, Buell AK, Outeiro TF, Otzen DE. Glycation modulates alpha-synuclein fibrillization kinetics: a sweet spot for inhibition. The Journal of Biological Chemistry. 101848. PMID 35314196 DOI: 10.1016/j.jbc.2022.101848 |
0.406 |
|
| 2022 |
Reimer L, Haikal C, Gram H, Theologidis V, Kovacs G, Ruesink H, Baun A, Nielsen J, Otzen DE, Li JY, Jensen PH. Low dose DMSO treatment induces oligomerization and accelerates aggregation of α-synuclein. Scientific Reports. 12: 3737. PMID 35260646 DOI: 10.1038/s41598-022-07706-2 |
0.37 |
|
| 2022 |
Farzadfard A, Pedersen JN, Meisl G, Somavarapu AK, Alam P, Goksøyr L, Nielsen MA, Sander AF, Knowles TPJ, Pedersen JS, Otzen DE. The C-terminal tail of α-synuclein protects against aggregate replication but is critical for oligomerization. Communications Biology. 5: 123. PMID 35145226 DOI: 10.1038/s42003-022-03059-8 |
0.473 |
|
| 2022 |
Nagaraj M, Najarzadeh Z, Pansieri J, Biverstål H, Musteikyte G, Smirnovas V, Matthews S, Emanuelsson C, Johansson J, Buxbaum JN, Morozova-Roche L, Otzen DE. Chaperones mainly suppress primary nucleation during formation of functional amyloid required for bacterial biofilm formation. Chemical Science. 13: 536-553. PMID 35126986 DOI: 10.1039/d1sc05790a |
0.341 |
|
| 2022 |
Rasmussen HØ, Otzen DE, Pedersen JS. Induction, inhibition, and incorporation: Different roles for anionic and zwitterionic lysolipids in the fibrillation of the functional amyloid FapC. The Journal of Biological Chemistry. 101569. PMID 35007533 DOI: 10.1016/j.jbc.2022.101569 |
0.365 |
|
| 2021 |
Otzen DE, Dueholm MS, Najarzadeh Z, Knowles TPJ, Ruggeri FS. In situ Sub-Cellular Identification of Functional Amyloids in Bacteria and Archaea by Infrared Nanospectroscopy. Small Methods. 5: e2001002. PMID 34927901 DOI: 10.1002/smtd.202001002 |
0.304 |
|
| 2021 |
Haikal C, Ortigosa-Pascual L, Najarzadeh Z, Bernfur K, Svanbergsson A, Otzen DE, Linse S, Li JY. The Bacterial Amyloids Phenol Soluble Modulins from Catalyze Alpha-Synuclein Aggregation. International Journal of Molecular Sciences. 22. PMID 34769023 DOI: 10.3390/ijms222111594 |
0.361 |
|
| 2021 |
Sønderby TV, Rasmussen HØ, Frank SA, Skov Pedersen J, Otzen DE. Folding steps in the fibrillation of functional amyloid: denaturant sensitivity reveals common features in nucleation and elongation. Journal of Molecular Biology. 167337. PMID 34748745 DOI: 10.1016/j.jmb.2021.167337 |
0.371 |
|
| 2021 |
Andersen C, Grønnemose AL, Pedersen JN, Nowak JS, Christiansen G, Nielsen J, Mulder FAA, Otzen DE, Jørgensen TJD. Lipid Peroxidation Products HNE and ONE Promote and Stabilize Alpha-Synuclein Oligomers by Chemical Modifications. Biochemistry. PMID 34730940 DOI: 10.1021/acs.biochem.1c00478 |
0.697 |
|
| 2021 |
Najarzadeh Z, Nielsen J, Farzadfard A, Sereikaite V, Strømgaard K, Meyer RL, Otzen DE. Human Fibrinogen Inhibits Amyloid Assembly of Most Phenol-Soluble Modulins from . Acs Omega. 6: 21960-21970. PMID 34497891 DOI: 10.1021/acsomega.1c02333 |
0.344 |
|
| 2021 |
Otzen DE, Pedersen JN, Somavarapu AK, Clement A, Ji M, Petersen EH, Pedersen JS, Schafer NP. Cys-labelling kinetics of membrane protein GlpG: a role for specific SDS binding and micelle changes? Biophysical Journal. PMID 34370995 DOI: 10.1016/j.bpj.2021.08.001 |
0.351 |
|
| 2021 |
Najarzadeh Z, Zaman M, Sereikaite V, Strømgaard K, Andreasen M, Otzen DE. Heparin promotes fibrillation of most phenol soluble modulin virulence peptides from S. aureus. The Journal of Biological Chemistry. 100953. PMID 34270957 DOI: 10.1016/j.jbc.2021.100953 |
0.352 |
|
| 2021 |
Christensen LFB, Alijanvand SH, Burdukiewicz M, Herbst FA, Kjeldal H, Dueholm MS, Otzen DE. Identification of amyloidogenic proteins in the microbiomes of a rat Parkinson's disease model and wild-type rats. Protein Science : a Publication of the Protein Society. PMID 34075639 DOI: 10.1002/pro.4137 |
0.362 |
|
| 2021 |
Andersen CB, Yoshimura Y, Nielsen J, Otzen DE, Mulder FAA. How epigallocatechin gallate binds and assembles oligomeric forms of human alpha-synuclein. The Journal of Biological Chemistry. 100788. PMID 34019875 DOI: 10.1016/j.jbc.2021.100788 |
0.707 |
|
| 2021 |
Mortensen HG, Otzen DE, Pedersen JS. Ubiquitin forms conventional decorated micelle structures with sodium dodecyl sulfate at saturation. Journal of Colloid and Interface Science. 596: 233-244. PMID 33845230 DOI: 10.1016/j.jcis.2021.03.110 |
0.306 |
|
| 2021 |
Rasmussen HØ, Otzen DE, Pedersen JS. A multimethod approach for analyzing FapC fibrillation and determining mass per length. Biophysical Journal. 120: 2262-2275. PMID 33812849 DOI: 10.1016/j.bpj.2021.03.031 |
0.329 |
|
| 2021 |
Noji M, Samejima T, Yamaguchi K, So M, Yuzu K, Chatani E, Akazawa-Ogawa Y, Hagihara Y, Kawata Y, Ikenaka K, Mochizuki H, Kardos J, Otzen DE, Bellotti V, Buchner J, et al. Breakdown of supersaturation barrier links protein folding to amyloid formation. Communications Biology. 4: 120. PMID 33500517 DOI: 10.1038/s42003-020-01641-6 |
0.35 |
|
| 2020 |
Larsen K, Bæk R, Sahin C, Kjær L, Christiansen G, Nielsen J, Farajzadeh L, Otzen DE. Molecular characteristics of porcine alpha-synuclein splicing variants. Biochimie. PMID 33152422 DOI: 10.1016/j.biochi.2020.10.019 |
0.305 |
|
| 2020 |
Eskandari H, Ghanadian M, Noleto-Dias C, Lomax C, Tawfike A, Christiansen G, Sutherland DS, Ward JL, Mohammad-Beigi H, Otzen DE. Inhibitors of α-Synuclein fibrillation and oligomer toxicity in Rosa damascena: the all-pervading powers of flavonoids and phenolic glycosides. Acs Chemical Neuroscience. PMID 32886481 DOI: 10.1021/acschemneuro.0c00528 |
0.309 |
|
| 2020 |
Jensen GV, Pedersen JN, Otzen DE, Pedersen JS. Multi-Step Unfolding and Rearrangement of α-Lactalbumin by SDS Revealed by Stopped-Flow SAXS. Frontiers in Molecular Biosciences. 7: 125. PMID 32754613 DOI: 10.3389/fmolb.2020.00125 |
0.312 |
|
| 2020 |
Christensen LFB, Nowak JS, Sønderby TV, Frank SA, Otzen DE. Quantitating denaturation by formic acid: Imperfect repeats are essential to the stability of the functional amyloid protein FapC. The Journal of Biological Chemistry. PMID 32719003 DOI: 10.1074/jbc.RA120.013396 |
0.34 |
|
| 2020 |
van Gils JHM, van Dijk E, Peduzzo A, Hofmann A, Vettore N, Schützmann MP, Groth G, Mouhib H, Otzen DE, Buell AK, Abeln S. The hydrophobic effect characterises the thermodynamic signature of amyloid fibril growth. Plos Computational Biology. 16: e1007767. PMID 32365068 DOI: 10.1371/Journal.Pcbi.1007767 |
0.373 |
|
| 2020 |
Adão R, Cruz PF, Vaz DC, Fonseca F, Pedersen JN, Ferreira-da-Silva F, Brito RMM, Ramos CHI, Otzen D, Keller S, Bastos M. DIBMA nanodiscs keep α-synuclein folded. Biochimica Et Biophysica Acta. Biomembranes. 1862: 183314. PMID 32304757 DOI: 10.1016/j.bbamem.2020.183314 |
0.386 |
|
| 2020 |
Sawada M, Yamaguchi K, Hirano M, Noji M, So M, Otzen DE, Kawata Y, Goto Y. Amyloid formation of α-synuclein based on the solubility- and supersaturation-dependent mechanism. Langmuir : the Acs Journal of Surfaces and Colloids. PMID 32271585 DOI: 10.1021/acs.langmuir.0c00426 |
0.389 |
|
| 2020 |
Marvian AT, Aliakbari F, Mohammad-Beigi H, Ahmadi ZA, Mehrpooyan S, Lermyte F, Nasouti M, Collingwood JF, Otzen DE, Morshedi D. The status of the terminal regions of α-synuclein in different forms of aggregates during fibrillization. International Journal of Biological Macromolecules. 155: 543-550. PMID 32240735 DOI: 10.1016/j.ijbiomac.2020.03.238 |
0.384 |
|
| 2020 |
Nagaraj M, Ahmed M, Lyngsø J, Vad BS, Bøggild A, Fillipsen A, Pedersen JS, Otzen DE, Akbey Ü. Predicted Loop Regions Promote Aggregation: A Study of Amyloidogenic Domains in the Functional Amyloid FapC. Journal of Molecular Biology. PMID 32084414 DOI: 10.1016/j.jmb.2020.01.044 |
0.395 |
|
| 2020 |
Alijanvand SH, Christensen MH, Christiansen G, Harikandei KB, Salehi P, Schiøtt B, Moosavi-Movahedi AA, Otzen DE. Novel noscapine derivatives stabilize the native state of insulin against fibrillation. International Journal of Biological Macromolecules. PMID 31923504 DOI: 10.1016/J.Ijbiomac.2020.01.061 |
0.303 |
|
| 2019 |
Poghosyan AH, Schafer NP, Lyngsø J, Shahinyan AA, Pedersen JS, Otzen DE. Molecular dynamics study of ACBP denaturation in alkyl sulfates demonstrates possible pathways of unfolding through fused surfactant clusters. Protein Engineering, Design & Selection : Peds. PMID 31788684 DOI: 10.1093/protein/gzz037 |
0.312 |
|
| 2019 |
Najarzadeh Z, Mohammad-Beigi H, Nedergaard Pedersen J, Christiansen G, Sønderby TV, Shojaosadati SA, Morshedi D, Strømgaard K, Meisl G, Sutherland D, Skov Pedersen J, Otzen DE. Plant Polyphenols Inhibit Functional Amyloid and Biofilm Formation in Strains by Directing Monomers to Off-Pathway Oligomers. Biomolecules. 9. PMID 31717821 DOI: 10.3390/biom9110659 |
0.372 |
|
| 2019 |
Christensen LFB, Schafer N, Wolf-Perez A, Madsen DJ, Otzen DE. Bacterial Amyloids: Biogenesis and Biomaterials. Advances in Experimental Medicine and Biology. 1174: 113-159. PMID 31713198 DOI: 10.1007/978-981-13-9791-2_4 |
0.345 |
|
| 2019 |
van Diggelen F, Frank SA, Somavarapu AK, Scavenius C, Apetri MM, Nielsen J, Tepper AWJW, Enghild JJ, Otzen DE. The interactome of stabilized α-synuclein oligomers and neuronal proteins. The Febs Journal. PMID 31686426 DOI: 10.1111/febs.15124 |
0.31 |
|
| 2019 |
Rasmussen HØ, Enghild JJ, Otzen DE, Pedersen JS. Unfolding and partial refolding of a cellulase from the SDS-denatured state: From β-sheet to α-helix and back. Biochimica Et Biophysica Acta. General Subjects. 129434. PMID 31525408 DOI: 10.1016/j.bbagen.2019.129434 |
0.341 |
|
| 2019 |
Christensen LFB, Jensen KF, Nielsen J, Vad BS, Christiansen G, Otzen DE. Reducing the Amyloidogenicity of Functional Amyloid Protein FapC Increases Its Ability To Inhibit α-Synuclein Fibrillation. Acs Omega. 4: 4029-4039. PMID 31459612 DOI: 10.1021/acsomega.8b03590 |
0.391 |
|
| 2019 |
Najarzadeh Z, Pedersen JN, Christiansen G, Shojaosadati SA, Pedersen JS, Otzen DE. Bacterial amphiphiles as amyloid inducers: Effect of Rhamnolipid and Lipopolysaccharide on FapC fibrillation. Biochimica Et Biophysica Acta. Proteins and Proteomics. 140263. PMID 31421227 DOI: 10.1016/j.bbapap.2019.140263 |
0.366 |
|
| 2019 |
Alam P, Bousset L, Melki R, Otzen DE. Alpha-synuclein oligomers and fibrils: a spectrum of species, a spectrum of toxicities. Journal of Neurochemistry. PMID 31254394 DOI: 10.1111/jnc.14808 |
0.306 |
|
| 2019 |
van Diggelen F, Hrle D, Apetri M, Christiansen G, Rammes G, Tepper A, Otzen DE. Two conformationally distinct α-synuclein oligomers share common epitopes and the ability to impair long-term potentiation. Plos One. 14: e0213663. PMID 30901378 DOI: 10.1371/journal.pone.0213663 |
0.322 |
|
| 2019 |
Juhl DW, Risør MW, Scavenius C, Rasmussen CB, Otzen D, Nielsen NC, Enghild JJ. Conservation of the Amyloid Interactome Across Diverse Fibrillar Structures. Scientific Reports. 9: 3863. PMID 30846764 DOI: 10.1038/s41598-019-40483-z |
0.38 |
|
| 2019 |
Mohammad-Beigi H, Hosseini A, Adeli M, Ejtehadi MR, Christiansen G, Sahin C, Tu Z, Tavakol M, Dilmaghani-Marand A, Nabipour I, Farzadfar F, Otzen DE, Mahmoudi M, Hajipour MJ. Mechanistic Understanding of the Interactions between Nano-Objects with Different Surface Properties and α-Synuclein. Acs Nano. PMID 30810027 DOI: 10.1021/acsnano.8b08983 |
0.325 |
|
| 2019 |
Mohammad-Beigi H, Aliakbari F, Sahin C, Lomax C, Tawfike A, Schafer NP, Amiri-Nowdijeh A, Eskandari H, Møller IM, Hosseini-Mazinani M, Christiansen G, Ward JL, Morshedi D, Otzen DE. Oleuropein derivatives from olive fruit extracts reduce α-synuclein fibrillation and oligomer toxicity. The Journal of Biological Chemistry. PMID 30655291 DOI: 10.1074/jbc.RA118.005723 |
0.332 |
|
| 2019 |
Rasmussen CB, Christiansen G, Vad BS, Lynggaard C, Enghild JJ, Andreasen M, Otzen D. Imperfect repeats in the functional amyloid protein FapC reduce the tendency to fragment during fibrillation. Protein Science : a Publication of the Protein Society. 28: 633-642. PMID 30592554 DOI: 10.1002/pro.3566 |
0.339 |
|
| 2018 |
Pedersen JN, Jiang Z, Christiansen G, Lee JC, Pedersen JS, Otzen DE. Lysophospholipids induce fibrillation of the repeat domain of Pmel17 through intermediate core-shell structures. Biochimica Et Biophysica Acta. Proteins and Proteomics. PMID 30471451 DOI: 10.1016/j.bbapap.2018.11.007 |
0.433 |
|
| 2018 |
Kurnik M, Sahin C, Andersen CB, Lorenzen N, Giehm L, Mohammad-Beigi H, Jessen CM, Pedersen JS, Christiansen G, Petersen SV, Staal R, Krishnamurthy G, Pitts K, Reinhart PH, Mulder FAA, ... ... Otzen DE, et al. Potent α-Synuclein Aggregation Inhibitors, Identified by High-Throughput Screening, Mainly Target the Monomeric State. Cell Chemical Biology. PMID 30197194 DOI: 10.1016/J.Chembiol.2018.08.005 |
0.681 |
|
| 2018 |
Sahin C, Kjær L, Christensen MS, Nedergaard Pedersen J, Christiansen G, Pérez AW, Moller IM, Enghild J, Pedersen JS, Larsen K, Otzen DE. α-synuclein from animal species show low fibrillation propensity and low oligomer membrane disruption. Biochemistry. PMID 30067901 DOI: 10.1021/acs.biochem.8b00627 |
0.385 |
|
| 2018 |
Bleem A, Christiansen G, Madsen DJ, Maric H, Strømgaard K, Bryers JD, Daggett V, Meyer RL, Otzen DE. Protein Engineering Reveals Mechanisms of Functional Amyloid Formation in Pseudomonas aeruginosa Biofilms. Journal of Molecular Biology. PMID 29964047 DOI: 10.1016/J.Jmb.2018.06.043 |
0.333 |
|
| 2018 |
Aliakbari F, Mohammad-Beigi H, Rezaei-Ghaleh N, Becker S, Dehghani Esmatabad F, Eslampanah Seyedi HA, Bardania H, Tayaranian Marvian A, Collingwood JF, Christiansen G, Zweckstetter M, Otzen DE, Morshedi D. The potential of zwitterionic nanoliposomes against neurotoxic alpha-synuclein aggregates in Parkinson's Disease. Nanoscale. PMID 29725687 DOI: 10.1039/c8nr00632f |
0.414 |
|
| 2018 |
Andersen KK, Vad BS, Kjaer L, Tolker-Nielsen T, Christiansen G, Otzen DE. Pseudomonas aeruginosa rhamnolipid induces fibrillation of human α-synuclein and modulates its effect on biofilm formation. Febs Letters. PMID 29572816 DOI: 10.1002/1873-3468.13038 |
0.408 |
|
| 2018 |
Nedergaard Pedersen J, Skov Pedersen J, Otzen DE. Liprotides assist in folding of outer membrane proteins. Protein Science : a Publication of the Protein Society. 27: 451-462. PMID 29094406 DOI: 10.1002/pro.3337 |
0.351 |
|
| 2017 |
Risør MW, Juhl DW, Bjerring M, Mathiesen J, Enghild JJ, Nielsen NC, Otzen DE. Critical Influence of Cosolutes and Surfaces on the Assembly of Serpin-Derived Amyloid Fibrils. Biophysical Journal. 113: 580-596. PMID 28793213 DOI: 10.1016/j.bpj.2017.06.030 |
0.34 |
|
| 2017 |
Malmos KG, Stenvang M, Sahin C, Christiansen G, Otzen D. The Changing Face of Aging: Highly Sulfated Glycosaminoglycans Induce Amyloid Formation in a Lattice Corneal Dystrophy Model Protein. Journal of Molecular Biology. PMID 28739480 DOI: 10.1016/j.jmb.2017.07.014 |
0.336 |
|
| 2017 |
Madsen JK, Kaspersen JD, Andersen CB, Nedergaard Pedersen J, Andersen KK, Pedersen JS, Otzen DE. Glycolipid biosurfactants activate, dimerize and stabilize T. lanuginosus lipase in a pH-dependent fashion. Biochemistry. PMID 28726390 DOI: 10.1021/acs.biochem.7b00420 |
0.637 |
|
| 2017 |
Gade Malmos K, Blancas-Mejia LM, Weber B, Buchner J, Ramirez-Alvarado M, Naiki H, Otzen D. ThT 101: a primer on the use of thioflavin T to investigate amyloid formation. Amyloid : the International Journal of Experimental and Clinical Investigation : the Official Journal of the International Society of Amyloidosis. 1-16. PMID 28393556 DOI: 10.1080/13506129.2017.1304905 |
0.322 |
|
| 2017 |
Otzen DE. Biosurfactants and surfactants interacting with membranes and proteins: Same but different? Biochimica Et Biophysica Acta. Biomembranes. 1859: 639-649. PMID 27693345 DOI: 10.1016/j.bbamem.2016.09.024 |
0.342 |
|
| 2016 |
Andersen KK, Vad B, Omer S, Otzen DE. Concatemers of Outer Membrane Protein A Take Detours in the Folding Landscape. Biochemistry. PMID 27973779 DOI: 10.1021/acs.biochem.6b01153 |
0.357 |
|
| 2016 |
Sahin C, Lorenzen N, Lemminger L, Christiansen G, Møller IM, Vesterager LB, Pedersen LØ, Fog K, Kallunki P, Otzen DE. Antibodies against the C-terminus of α-synuclein modulate its fibrillation. Biophysical Chemistry. PMID 27863716 DOI: 10.1016/j.bpc.2016.11.002 |
0.398 |
|
| 2016 |
Stenvang M, Dueholm MS, Vad BS, Seviour TW, Zeng G, Geifman-Shochat S, Søndergaard MT, Christiansen G, Meyer RL, Kjelleberg S, Nielsen PH, Otzen DE. Epigallocatechin Gallate Remodels overexpressed Functional Amyloids in Pseudomonas aeruginosa and Increases Biofilm Susceptibility to Antibiotic Treatment. The Journal of Biological Chemistry. PMID 27784787 DOI: 10.1074/jbc.M116.739953 |
0.314 |
|
| 2016 |
Jarvela TS, Lam HA, Helwig M, Lorenzen N, Otzen DE, McLean PJ, Maidment NT, Lindberg I. The neural chaperone proSAAS blocks α-synuclein fibrillation and neurotoxicity. Proceedings of the National Academy of Sciences of the United States of America. PMID 27457957 DOI: 10.1073/Pnas.1601091113 |
0.39 |
|
| 2016 |
Christensen LF, Malmos KG, Christiansen G, Otzen DE. A complex dance: the importance of glycosaminoglycans and zinc in the aggregation of human prolactin. Biochemistry. PMID 27305175 DOI: 10.1021/acs.biochem.6b00153 |
0.346 |
|
| 2016 |
Malmos KG, Bjerring M, Jessen CM, Nielsen EH, Poulsen ET, Christiansen G, Vosegaard T, Skrydstrup T, Enghild JJ, Pedersen JS, Otzen DE. How Glycosaminoglycans Promote Fibrillation of Salmon Calcitonin. The Journal of Biological Chemistry. PMID 27281819 DOI: 10.1074/Jbc.M116.715466 |
0.323 |
|
| 2016 |
Pantusa M, Vad B, Lillelund O, Kjær L, Otzen D, Bartucci R. Alpha-synuclein and familial variants affect the chain order and the thermotropic phase behavior of anionic lipid vesicles. Biochimica Et Biophysica Acta. 1864: 1206-1214. PMID 27177693 DOI: 10.1016/j.bbapap.2016.05.003 |
0.346 |
|
| 2016 |
Stenvang M, Christiansen G, Otzen DE. Epigallocatechin Gallate Remodels Fibrils of Lattice Corneal Dystrophy Protein, Facilitating Proteolytic Degradation and Preventing Formation of Membrane-Permeabilizing Species. Biochemistry. 55: 2344-57. PMID 27042751 DOI: 10.1021/acs.biochem.6b00063 |
0.403 |
|
| 2016 |
Tian P, Lindorff-Larsen K, Boomsma W, Jensen MH, Otzen DE. A Monte Carlo Study of the Early Steps of Functional Amyloid Formation. Plos One. 11: e0146096. PMID 26745180 DOI: 10.1371/Journal.Pone.0146096 |
0.323 |
|
| 2016 |
Paslawski W, Lorenzen N, Otzen DE. Formation and Characterization of α-Synuclein Oligomers. Methods in Molecular Biology (Clifton, N.J.). 1345: 133-50. PMID 26453210 DOI: 10.1007/978-1-4939-2978-8_9 |
0.331 |
|
| 2015 |
Estrela N, Franquelim HG, Lopes C, Tavares E, Macedo JA, Christiansen G, Otzen DE, Melo EP. Sucrose prevents protein fibrillation through compaction of the tertiary structure but hardly affects the secondary structure. Proteins. 83: 2039-51. PMID 26344410 DOI: 10.1002/prot.24921 |
0.322 |
|
| 2015 |
Kulminskaya NV, Yoshimura Y, Runager K, Sørensen CS, Bjerring M, Andreasen M, Otzen DE, Enghild JJ, Nielsen NC, Mulder FA. Near-complete (1)H, (13)C, (15)N resonance assignments of dimethylsulfoxide-denatured TGFBIp FAS1-4 A546T. Biomolecular Nmr Assignments. PMID 26275916 DOI: 10.1007/S12104-015-9630-2 |
0.58 |
|
| 2015 |
Paslawski W, Lillelund OK, Kristensen JV, Schafer NP, Baker RP, Urban S, Otzen DE. Cooperative folding of a polytopic α-helical membrane protein involves a compact N-terminal nucleus and nonnative loops. Proceedings of the National Academy of Sciences of the United States of America. 112: 7978-83. PMID 26056273 DOI: 10.1073/pnas.1424751112 |
0.302 |
|
| 2015 |
Christoffersen HF, Hansen SK, Vad BS, Nielsen EH, Nielsen JT, Vosegaard T, Skrydstrup T, Otzen DE. The natural, peptaibolic peptide SPF-5506-A4 adopts a β-bend spiral structure, shows low hemolytic activity and targets membranes through formation of large pores. Biochimica Et Biophysica Acta. 1854: 882-9. PMID 25796141 DOI: 10.1016/J.Bbapap.2015.03.003 |
0.329 |
|
| 2015 |
Otzen D. Protein aggregation: close encounters of the greasy kind. Nature Chemical Biology. 11: 176-7. PMID 25689332 DOI: 10.1038/nchembio.1759 |
0.314 |
|
| 2015 |
Andreasen M, Lorenzen N, Otzen D. Interactions between misfolded protein oligomers and membranes: A central topic in neurodegenerative diseases? Biochimica Et Biophysica Acta. 1848: 1897-907. PMID 25666871 DOI: 10.1016/j.bbamem.2015.01.018 |
0.36 |
|
| 2015 |
Lorenzen N, Otzen DE. Oligomers of α-synuclein: picking the culprit in the line-up. Essays in Biochemistry. 56: 137-48. PMID 25131592 DOI: 10.1042/bse0560137 |
0.43 |
|
| 2015 |
Paslawski W, Lillelund OK, Kristensen JV, Schafer NP, Baker RP, Urban S, Otzen DE. Cooperative folding of a polytopic α-helical membrane protein involves a compact N-terminal nucleus and nonnative loops Proceedings of the National Academy of Sciences of the United States of America. 112: 7978-7983. DOI: 10.1073/pnas.1424751112 |
0.307 |
|
| 2014 |
Andersen KK, Otzen DE. Denaturation of α-lactalbumin and myoglobin by the anionic biosurfactant rhamnolipid. Biochimica Et Biophysica Acta. 1844: 2338-2345. PMID 25450503 DOI: 10.1016/j.bbapap.2014.10.005 |
0.356 |
|
| 2014 |
Paslawski W, Andreasen M, Nielsen SB, Lorenzen N, Thomsen K, Kaspersen JD, Pedersen JS, Otzen DE. High stability and cooperative unfolding of α-synuclein oligomers. Biochemistry. 53: 6252-63. PMID 25216651 DOI: 10.1021/bi5007833 |
0.415 |
|
| 2014 |
Neumann J, Klein N, Otzen DE, Schneider D. Folding energetics and oligomerization of polytopic α-helical transmembrane proteins. Archives of Biochemistry and Biophysics. 564: 281-96. PMID 25057769 DOI: 10.1016/j.abb.2014.07.017 |
0.325 |
|
| 2014 |
Lorenzen N, Nielsen SB, Yoshimura Y, Vad BS, Andersen CB, Betzer C, Kaspersen JD, Christiansen G, Pedersen JS, Jensen PH, Mulder FA, Otzen DE. How epigallocatechin gallate can inhibit α-synuclein oligomer toxicity in vitro. The Journal of Biological Chemistry. 289: 21299-310. PMID 24907278 DOI: 10.1074/Jbc.M114.554667 |
0.707 |
|
| 2014 |
Paslawski W, Mysling S, Thomsen K, Jørgensen TJ, Otzen DE. Co-existence of two different α-synuclein oligomers with different core structures determined by hydrogen/deuterium exchange mass spectrometry. Angewandte Chemie (International Ed. in English). 53: 7560-3. PMID 24740651 DOI: 10.1002/anie.201400491 |
0.322 |
|
| 2014 |
Andersen KK, Otzen DE. Folding of outer membrane protein A in the anionic biosurfactant rhamnolipid. Febs Letters. 588: 1955-60. PMID 24735722 DOI: 10.1016/j.febslet.2014.04.004 |
0.3 |
|
| 2014 |
Lorenzen N, Nielsen SB, Buell AK, Kaspersen JD, Arosio P, Vad BS, Paslawski W, Christiansen G, Valnickova-Hansen Z, Andreasen M, Enghild JJ, Pedersen JS, Dobson CM, Knowles TPJ, Otzen DE. The role of stable α-synuclein oligomers in the molecular events underlying amyloid formation Journal of the American Chemical Society. 136: 3859-3868. PMID 24527756 DOI: 10.1021/Ja411577T |
0.419 |
|
| 2014 |
Lopes P, Dyrnesli H, Lorenzen N, Otzen D, Ferapontova EE. Electrochemical analysis of the fibrillation of Parkinson's disease α-synuclein. The Analyst. 139: 749-56. PMID 24343298 DOI: 10.1039/c3an01616a |
0.366 |
|
| 2013 |
Lorenzen N, Lemminger L, Pedersen JN, Nielsen SB, Otzen DE. The N-terminus of α-synuclein is essential for both monomeric and oligomeric interactions with membranes. Febs Letters. 588: 497-502. PMID 24374342 DOI: 10.1016/j.febslet.2013.12.015 |
0.36 |
|
| 2013 |
Nielsen SB, Macchi F, Raccosta S, Langkilde AE, Giehm L, Kyrsting A, Svane AS, Manno M, Christiansen G, Nielsen NC, Oddershede L, Vestergaard B, Otzen DE. Wildtype and A30P mutant alpha-synuclein form different fibril structures. Plos One. 8: e67713. PMID 23861789 DOI: 10.1371/journal.pone.0067713 |
0.327 |
|
| 2013 |
Abelein A, Kaspersen JD, Nielsen SB, Jensen GV, Christiansen G, Pedersen JS, Danielsson J, Otzen DE, Gräslund A. Formation of dynamic soluble surfactant-induced amyloid β peptide aggregation intermediates. The Journal of Biological Chemistry. 288: 23518-28. PMID 23775077 DOI: 10.1074/jbc.M113.470450 |
0.363 |
|
| 2013 |
Cohen SI, Linse S, Luheshi LM, Hellstrand E, White DA, Rajah L, Otzen DE, Vendruscolo M, Dobson CM, Knowles TP. Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism. Proceedings of the National Academy of Sciences of the United States of America. 110: 9758-63. PMID 23703910 DOI: 10.1073/Pnas.1218402110 |
0.355 |
|
| 2013 |
Deva T, Lorenzen N, Vad BS, Petersen SV, Thørgersen I, Enghild JJ, Kristensen T, Otzen DE. Off-pathway aggregation can inhibit fibrillation at high protein concentrations Biochimica Et Biophysica Acta - Proteins and Proteomics. 1834: 677-687. PMID 23313095 DOI: 10.1016/j.bbapap.2012.12.020 |
0.351 |
|
| 2013 |
Helwig M, Hoshino A, Berridge C, Lee SN, Lorenzen N, Otzen DE, Eriksen JL, Lindberg I. The neuroendocrine protein 7B2 suppresses the aggregation of neurodegenerative disease-related proteins. The Journal of Biological Chemistry. 288: 1114-24. PMID 23172224 DOI: 10.1074/Jbc.M112.417071 |
0.336 |
|
| 2012 |
Otzen DE, Andersen KK. Folding of outer membrane proteins. Archives of Biochemistry and Biophysics. 531: 34-43. PMID 23131493 DOI: 10.1016/j.abb.2012.10.008 |
0.312 |
|
| 2012 |
Oeemig JS, Lynggaard C, Knudsen DH, Hansen FT, Nørgaard KD, Schneider T, Vad BS, Sandvang DH, Nielsen LA, Neve S, Kristensen HH, Sahl HG, Otzen DE, Wimmer R. Eurocin, a new fungal defensin: structure, lipid binding, and its mode of action. The Journal of Biological Chemistry. 287: 42361-72. PMID 23093408 DOI: 10.1074/Jbc.M112.382028 |
0.304 |
|
| 2012 |
Andersen KK, Wang H, Otzen DE. A kinetic analysis of the folding and unfolding of OmpA in urea and guanidinium chloride: single and parallel pathways. Biochemistry. 51: 8371-83. PMID 22992178 DOI: 10.1021/bi300974y |
0.306 |
|
| 2012 |
Wang H, Andersen KK, Vad BS, Otzen DE. OmpA can form folded and unfolded oligomers. Biochimica Et Biophysica Acta. 1834: 127-36. PMID 22982243 DOI: 10.1016/j.bbapap.2012.09.002 |
0.384 |
|
| 2012 |
Andreasen M, Nielsen SB, Runager K, Christiansen G, Nielsen NC, Enghild JJ, Otzen DE. Polymorphic fibrillation of the destabilized fourth fasciclin-1 domain mutant A546T of the Transforming growth factor-β-induced protein (TGFBIp) occurs through multiple pathways with different oligomeric intermediates. The Journal of Biological Chemistry. 287: 34730-42. PMID 22893702 DOI: 10.1074/jbc.M112.379552 |
0.357 |
|
| 2012 |
Kalashnyk N, Nielsen JT, Nielsen EH, Skrydstrup T, Otzen DE, Lægsgaard E, Wang C, Besenbacher F, Nielsen NC, Linderoth TR. Scanning tunneling microscopy reveals single-molecule insights into the self-assembly of amyloid fibrils. Acs Nano. 6: 6882-9. PMID 22779709 DOI: 10.1021/Nn301708D |
0.308 |
|
| 2012 |
Calcutta A, Jessen CM, Behrens MA, Oliveira CL, Renart ML, González-Ros JM, Otzen DE, Pedersen JS, Malmendal A, Nielsen NC. Mapping of unfolding states of integral helical membrane proteins by GPS-NMR and scattering techniques: TFE-induced unfolding of KcsA in DDM surfactant. Biochimica Et Biophysica Acta. 1818: 2290-301. PMID 22525601 DOI: 10.1016/j.bbamem.2012.04.005 |
0.311 |
|
| 2012 |
Macchi F, Eisenkolb M, Kiefer H, Otzen DE. The effect of osmolytes on protein fibrillation. International Journal of Molecular Sciences. 13: 3801-19. PMID 22489184 DOI: 10.3390/ijms13033801 |
0.342 |
|
| 2012 |
Nielsen SB, Yde P, Giehm L, Sundbye S, Christiansen G, Mathiesen J, Jensen MH, Jensen PH, Otzen DE. Multiple roles of heparin in the aggregation of p25α. Journal of Molecular Biology. 421: 601-15. PMID 22326478 DOI: 10.1016/J.Jmb.2012.01.050 |
0.416 |
|
| 2011 |
Pedersen LR, Nielsen SB, Hansted JG, Petersen TE, Otzen DE, Sørensen ES. PP3 forms stable tetrameric structures through hydrophobic interactions via the C-terminal amphipathic helix and undergoes reversible thermal dissociation and denaturation. The Febs Journal. 279: 336-47. PMID 22099394 DOI: 10.1111/j.1742-4658.2011.08428.x |
0.315 |
|
| 2011 |
Dueholm MS, Nielsen SB, Hein KL, Nissen P, Chapman M, Christiansen G, Nielsen PH, Otzen DE. Fibrillation of the major curli subunit CsgA under a wide range of conditions implies a robust design of aggregation. Biochemistry. 50: 8281-90. PMID 21877724 DOI: 10.1021/Bi200967C |
0.358 |
|
| 2011 |
Du XT, Wang L, Wang YJ, Andreasen M, Zhan DW, Feng Y, Li M, Zhao M, Otzen D, Xue D, Yang Y, Liu RT. Aβ1-16 can aggregate and induce the production of reactive oxygen species, nitric oxide, and inflammatory cytokines. Journal of Alzheimer's Disease : Jad. 27: 401-13. PMID 21860093 DOI: 10.3233/JAD-2011-110476 |
0.328 |
|
| 2011 |
Hansted JG, Wejse PL, Bertelsen H, Otzen DE. Effect of protein-surfactant interactions on aggregation of β-lactoglobulin. Biochimica Et Biophysica Acta. 1814: 713-23. PMID 21440683 DOI: 10.1016/j.bbapap.2011.03.011 |
0.395 |
|
| 2011 |
Otzen D. Protein-surfactant interactions: a tale of many states. Biochimica Et Biophysica Acta. 1814: 562-91. PMID 21397738 DOI: 10.1016/j.bbapap.2011.03.003 |
0.327 |
|
| 2011 |
Weber M, Prodöhl A, Dreher C, Becker C, Underhaug J, Svane AS, Malmendal A, Nielsen NC, Otzen D, Schneider D. SDS-facilitated in vitro formation of a transmembrane B-type cytochrome is mediated by changes in local pH. Journal of Molecular Biology. 407: 594-606. PMID 21315727 DOI: 10.1016/j.jmb.2011.02.005 |
0.302 |
|
| 2011 |
Giehm L, Svergun DI, Otzen DE, Vestergaard B. Low-resolution structure of a vesicle disrupting α-synuclein oligomer that accumulates during fibrillation. Proceedings of the National Academy of Sciences of the United States of America. 108: 3246-51. PMID 21300904 DOI: 10.1073/pnas.1013225108 |
0.383 |
|
| 2011 |
Otzen DE. Amyloid formation in surfactants and alcohols: membrane mimetics or structural switchers? Current Protein & Peptide Science. 11: 355-71. PMID 20423296 DOI: 10.2174/138920310791330622 |
0.394 |
|
| 2010 |
Giehm L, Lorenzen N, Otzen DE. Assays for α-synuclein aggregation. Methods (San Diego, Calif.). 53: 295-305. PMID 21163351 DOI: 10.1016/j.ymeth.2010.12.008 |
0.431 |
|
| 2010 |
Debnath DK, Otzen DE. Cell-free synthesis and folding of transmembrane OmpA reveals higher order structures and premature truncations Biophysical Chemistry. 152: 80-88. PMID 20813447 DOI: 10.1016/j.bpc.2010.08.003 |
0.317 |
|
| 2010 |
Giehm L, Degan Fd, Fraser P, Klysner S, Otzen D. An Aβ concatemer with altered aggregation propensities Biochimica Et Biophysica Acta. 1804: 2025-2035. PMID 20619363 DOI: 10.1016/J.Bbapap.2010.06.023 |
0.395 |
|
| 2010 |
Giehm L, Oliveira CL, Christiansen G, Pedersen JS, Otzen DE. SDS-induced fibrillation of alpha-synuclein: an alternative fibrillation pathway. Journal of Molecular Biology. 401: 115-33. PMID 20540950 DOI: 10.1016/j.jmb.2010.05.060 |
0.403 |
|
| 2010 |
Debnath D, Nielsen KL, Otzen DE. In vitro association of fragments of a β-sheet membrane protein Biophysical Chemistry. 148: 112-120. PMID 20356666 DOI: 10.1016/j.bpc.2010.03.004 |
0.307 |
|
| 2010 |
Nielsen SB, Franzmann M, Basaiawmoit RV, Wimmer R, Mikkelsen JD, Otzen DE. beta-Sheet aggregation of kisspeptin-10 is stimulated by heparin but inhibited by amphiphiles. Biopolymers. 93: 678-89. PMID 20301214 DOI: 10.1002/Bip.21434 |
0.391 |
|
| 2010 |
Giehm L, Otzen DE. Strategies to increase the reproducibility of protein fibrillization in plate reader assays. Analytical Biochemistry. 400: 270-81. PMID 20149780 DOI: 10.1016/j.ab.2010.02.001 |
0.341 |
|
| 2010 |
Vad B, Thomsen LA, Bertelsen K, Franzmann M, Pedersen JM, Nielsen SB, Vosegaard T, Valnickova Z, Skrydstrup T, Enghild JJ, Wimmer R, Nielsen NC, Otzen DE. Divorcing folding from function: how acylation affects the membrane-perturbing properties of an antimicrobial peptide. Biochimica Et Biophysica Acta. 1804: 806-20. PMID 20026432 DOI: 10.1016/J.Bbapap.2009.12.006 |
0.314 |
|
| 2010 |
Giehm L, Vestergaard B, Oliveira C, Pedersen JS, Svergun DI, Pitts K, Krishnamurthy G, Staal R, Reinhart P, Otzen DE. Low Resolution Structure of a Membrane-Permeabilizing Oligomer of α-Synuclein: the Basis for a High-Throughput Screening of Compounds against α-Synuclein Aggregation Biophysical Journal. 98: 423a. DOI: 10.1016/J.BPJ.2009.12.2291 |
0.328 |
|
| 2009 |
Rantalainen KI, Christensen PA, Hafrén A, Otzen DE, Kalkkinen N, Mäkinen K. Interaction of a potyviral VPg with anionic phospholipid vesicles. Virology. 395: 114-20. PMID 19800647 DOI: 10.1016/j.virol.2009.09.009 |
0.35 |
|
| 2009 |
Reinau ME, Otzen DE. Stability and structure of the membrane protein transporter Ffh is modulated by substrates and lipids. Archives of Biochemistry and Biophysics. 492: 48-53. PMID 19800309 DOI: 10.1016/j.abb.2009.09.018 |
0.343 |
|
| 2009 |
Andersen KK, Oliveira CL, Larsen KL, Poulsen FM, Callisen TH, Westh P, Pedersen JS, Otzen D. The role of decorated SDS micelles in sub-CMC protein denaturation and association. Journal of Molecular Biology. 391: 207-26. PMID 19523473 DOI: 10.1016/J.Jmb.2009.06.019 |
0.344 |
|
| 2009 |
Sneppen K, Lizana L, Jensen MH, Pigolotti S, Otzen D. Modeling proteasome dynamics in Parkinson's disease. Physical Biology. 6: 036005. PMID 19411740 DOI: 10.1088/1478-3975/6/3/036005 |
0.311 |
|
| 2009 |
Oliveira CL, Behrens MA, Pedersen JS, Erlacher K, Otzen D, Pedersen JS. A SAXS study of glucagon fibrillation. Journal of Molecular Biology. 387: 147-61. PMID 19385046 DOI: 10.1016/J.JMB.2009.01.020 |
0.341 |
|
| 2009 |
Vad BS, Thomsen LA, Nielsen SB, Pedersen JM, Skrydstrup T, Nielsen NC, Valnickova Z, Enghild JJ, Otzen DE. Action Of The Antimicrobial Peptide Novicidin: Divorcing Folding From Function Biophysical Journal. 96: 379a. DOI: 10.1016/J.Bpj.2008.12.2840 |
0.32 |
|
| 2008 |
Nesgaard L, Vad B, Christiansen G, Otzen D. Kinetic partitioning between aggregation and vesicle permeabilization by modified ADan. Biochimica Et Biophysica Acta. 1794: 84-93. PMID 18977466 DOI: 10.1016/j.bbapap.2008.09.021 |
0.395 |
|
| 2008 |
Christensen PA, Pedersen JS, Christiansen G, Otzen DE. Spectroscopic evidence for the existence of an obligate pre-fibrillar oligomer during glucagon fibrillation. Febs Letters. 582: 1341-5. PMID 18358836 DOI: 10.1016/j.febslet.2008.03.017 |
0.31 |
|
| 2008 |
Knudsen SK, Stensballe A, Franzmann M, Westergaard UB, Otzen DE. Effect of glycosylation on the extracellular domain of the Ag43 bacterial autotransporter: enhanced stability and reduced cellular aggregation. The Biochemical Journal. 412: 563-77. PMID 18341480 DOI: 10.1042/BJ20071497 |
0.303 |
|
| 2008 |
Svane AS, Jahn K, Deva T, Malmendal A, Otzen DE, Dittmer J, Nielsen NC. Early stages of amyloid fibril formation studied by liquid-state NMR: the peptide hormone glucagon. Biophysical Journal. 95: 366-77. PMID 18339765 DOI: 10.1529/biophysj.107.122895 |
0.308 |
|
| 2008 |
Otzen DE, Nesgaard LW, Andersen KK, Hansen JH, Christiansen G, Doe H, Sehgal P. Aggregation of S6 in a quasi-native state by sub-micellar SDS. Biochimica Et Biophysica Acta. 1784: 400-14. PMID 18083130 DOI: 10.1016/j.bbapap.2007.11.010 |
0.38 |
|
| 2007 |
Andersen KK, Westh P, Otzen DE. Global study of myoglobin-surfactant interactions. Langmuir : the Acs Journal of Surfaces and Colloids. 24: 399-407. PMID 18069862 DOI: 10.1021/LA702890Y |
0.337 |
|
| 2007 |
Pedersen JS, Otzen DE. Amyloid-a state in many guises: survival of the fittest fibril fold. Protein Science : a Publication of the Protein Society. 17: 2-10. PMID 18042680 DOI: 10.1110/ps.073127808 |
0.316 |
|
| 2007 |
Holm NK, Jespersen SK, Thomassen LV, Wolff TY, Sehgal P, Thomsen LA, Christiansen G, Andersen CB, Knudsen AD, Otzen DE. Aggregation and fibrillation of bovine serum albumin. Biochimica Et Biophysica Acta. 1774: 1128-38. PMID 17689306 DOI: 10.1016/j.bbapap.2007.06.008 |
0.373 |
|
| 2007 |
Heegaard PM, Boas U, Otzen DE. Dendrimer effects on peptide and protein fibrillation. Macromolecular Bioscience. 7: 1047-59. PMID 17595681 DOI: 10.1002/MABI.200700051 |
0.353 |
|
| 2007 |
Pedersen JS, Dikov D, Otzen DE. N- and C-terminal hydrophobic patches are involved in fibrillation of glucagon. Biochemistry. 45: 14503-12. PMID 17128989 DOI: 10.1021/BI061228N |
0.328 |
|
| 2007 |
Pedersen S, Nesgaard L, Baptista RP, Melo EP, Kristensen SR, Otzen DE. pH-dependent aggregation of cutinase is efficiently suppressed by 1,8-ANS. Biopolymers. 83: 619-29. PMID 16964599 DOI: 10.1002/BIP.20598 |
0.34 |
|
| 2006 |
Dong M, Hovgaard MB, Xu S, Otzen DE, Besenbacher F. AFM study of glucagon fibrillation via oligomeric structures resulting in interwoven fibrils. Nanotechnology. 17: 4003-9. PMID 21727528 DOI: 10.1088/0957-4484/17/16/001 |
0.32 |
|
| 2006 |
Otzen DE, Giehm L, Baptista RP, Kristensen SR, Melo EP, Pedersen S. Aggregation as the basis for complex behaviour of cutinase in different denaturants. Biochimica Et Biophysica Acta. 1774: 323-33. PMID 17208524 DOI: 10.1016/J.BBAPAP.2006.11.012 |
0.307 |
|
| 2006 |
Sehgal P, Otzen DE. Thermodynamics of unfolding of an integral membrane protein in mixed micelles. Protein Science : a Publication of the Protein Society. 15: 890-9. PMID 16600971 DOI: 10.1110/ps.052031306 |
0.324 |
|
| 2006 |
Pedersen JS, Flink JM, Dikov D, Otzen DE. Sulfates dramatically stabilize a salt-dependent type of glucagon fibrils. Biophysical Journal. 90: 4181-94. PMID 16533857 DOI: 10.1529/BIOPHYSJ.105.070912 |
0.344 |
|
| 2005 |
Pedersen JS, Dikov D, Flink JL, Hjuler HA, Christiansen G, Otzen DE. The changing face of glucagon fibrillation: structural polymorphism and conformational imprinting. Journal of Molecular Biology. 355: 501-23. PMID 16321400 DOI: 10.1016/J.JMB.2005.09.100 |
0.31 |
|
| 2005 |
Otzen DE, Lundvig DM, Wimmer R, Nielsen LH, Pedersen JR, Jensen PH. p25alpha is flexible but natively folded and binds tubulin with oligomeric stoichiometry. Protein Science : a Publication of the Protein Society. 14: 1396-409. PMID 15883183 DOI: 10.1110/Ps.041285605 |
0.321 |
|
| 2004 |
Otzen DE, Miron S, Akke M, Oliveberg M. Transient aggregation and stable dimerization induced by introducing an Alzheimer sequence into a water-soluble protein. Biochemistry. 43: 12964-12978. PMID 15476390 DOI: 10.1021/Bi048509K |
0.326 |
|
| 2004 |
Pedersen JS, Christensen G, Otzen DE. Modulation of S6 fibrillation by unfolding rates and gatekeeper residues. Journal of Molecular Biology. 341: 575-88. PMID 15276845 DOI: 10.1016/J.JMB.2004.06.020 |
0.338 |
|
| 2003 |
Aachmann FL, Otzen DE, Larsen KL, Wimmer R. Structural background of cyclodextrin-protein interactions. Protein Engineering. 16: 905-12. PMID 14983070 DOI: 10.1093/Protein/Gzg137 |
0.316 |
|
| 2003 |
Otzen DE. Folding of DsbB in mixed micelles: a kinetic analysis of the stability of a bacterial membrane protein. Journal of Molecular Biology. 330: 641-9. PMID 12850136 DOI: 10.1016/S0022-2836(03)00624-7 |
0.307 |
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| 1996 |
de Prat Gay G, Ruiz-Sanz J, Neira JL, Corrales FJ, Otzen DE, Ladurner AG, Fersht AR. Conformational pathway of the polypeptide chain of chymotrypsin inhibitor-2 growing from its N terminus in vitro. Parallels with the protein folding pathway. Journal of Molecular Biology. 254: 968-79. PMID 7500364 DOI: 10.1006/Jmbi.1995.0669 |
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