D. Otzen

D. Otzen, J. Buchner, M. Ramirez-Alvarado, 2017, Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis.

SAXS models of TGFBIp reveal a trimeric structure and show that the overall shape is not affected by the Arg124His mutation.

J. Enghild, D. Otzen, J. S. Pedersen, 2011, Journal of molecular biology.

Detection of Pathogenic Biofilms with Bacterial Amyloid Targeting Fluorescent Probe, CDy11.

D. Otzen, Young‐Tae Chang, P. Nielsen, 2016, Journal of the American Chemical Society.

The impact of α-synuclein aggregates on blood-brain barrier integrity in the presence of neurovascular unit cells

D. Otzen, H. Bardania, D. Morshedi, 2022, bioRxiv.

The Compact and Biologically Relevant Structure of Inter-α-inhibitor Is Maintained by the Chondroitin Sulfate Chain and Divalent Cations*

J. Enghild, D. Otzen, C. Scavenius, 2016, The Journal of Biological Chemistry.

Microfluidics and the quantification of biomolecular interactions.

Alexander K. Buell, D. Otzen, A. Buell, 2021, Current opinion in structural biology.

The diversity of FtsY-lipid interactions.

J. Enghild, D. Otzen, K. Nielsen, 2010, Biopolymers.

Characterization of exogenous αSN response genes and their relation to Parkinson’s disease using network analyses

D. Otzen, D. Morshedi, F. Afzali, 2022, Frontiers in Pharmacology.

The role of membrane properties in Mistic folding and dimerisation.

D. Otzen, K. Nielsen, R. V. Basaiawmoit, 2011, Protein engineering, design & selection : PEDS.

Nanosilver Mitigates Biofilm Formation via FapC Amyloidosis Inhibition.

D. Otzen, C. Landersdorfer, I. Hussain, 2020, Small.

Cooperative folding of a polytopic α-helical membrane protein involves a compact N-terminal nucleus and nonnative loops

Nicholas P. Schafer, N. Schafer, D. Otzen, 2015, Proceedings of the National Academy of Sciences.

Bacterial amphiphiles as amyloid inducers: Effect of Rhamnolipid and Lipopolysaccharide on FapC fibrillation.

D. Otzen, J. S. Pedersen, S. Shojaosadati, 2019, Biochimica et biophysica acta. Proteins and proteomics.

How Glycosaminoglycans Promote Fibrillation of Salmon Calcitonin*

J. Enghild, D. Otzen, J. S. Pedersen, 2016, The Journal of Biological Chemistry.

Stabilizing vitamin D3 using the molten globule state of α-lactalbumin.

D. Otzen, J. Pedersen, H. V. Sørensen, 2018, Journal of dairy science.

Amyloid formation of α-synuclein based on the solubility- and supersaturation-dependent mechanism.

D. Otzen, Y. Kawata, Y. Goto, 2020, Langmuir : the ACS journal of surfaces and colloids.

Interaction of membrane vesicles with the Pseudomonas functional amyloid protein FapC facilitates amyloid formation.

D. Otzen, H. Mohammad-Beigi, G. Christiansen, 2022, BBA advances.

Human Fibrinogen Inhibits Amyloid Assembly of Most Phenol-Soluble Modulins from Staphylococcus aureus

D. Otzen, K. Strømgaard, R. Meyer, 2021, ACS omega.

How glycosaminoglycans promote fibrillation of salmon calcitonin.

J. Enghild, D. Otzen, J. S. Pedersen, 2017, The Journal of Biological Chemistry.

Using Liprotides to Deliver Cholesterol to the Plasma Membrane

D. Otzen, J. Nylandsted, Janni Nielsen, 2018, The Journal of Membrane Biology.

Amyloid formation in surfactants and alcohols: membrane mimetics or structural switchers?

D. Otzen, 2010, Current protein & peptide science.

Surfactant protein SP-B strongly modifies surface collapse of phospholipid vesicles: insights from a quartz crystal microbalance with dissipation.

D. Otzen, J. Pérez-Gil, D. Sutherland, 2009, Biophysical journal.

Phenol-Soluble Modulins Modulate Persister Cell Formation in Staphylococcus aureus

D. Otzen, M. Vestergaard, H. Ingmer, 2020, Frontiers in Microbiology.

FapA is an intrinsically disordered chaperone for Pseudomonas functional amyloid FapC.

D. Otzen, Amit Kumar, Fisentzos Stylianou, 2022, Journal of molecular biology.

A penetratin-derived peptide reduces the membrane permeabilization and cell toxicity of α-synuclein oligomers

D. Otzen, A. Saboury, K. Strømgaard, 2022, The Journal of biological chemistry.

The changing face of SDS denaturation: Complexes of Thermomyces lanuginosus lipase with SDS at pH 4.0, 6.0 and 8.0.

D. Otzen, C. L. Oliveira, J. S. Pedersen, 2022, Journal of colloid and interface science.

Unfolding and partial refolding of a cellulase from the SDS-denatured state: From β-sheet to α-helix and back.

J. Enghild, D. Otzen, J. S. Pedersen, 2019, Biochimica et biophysica acta. General subjects.

Myoglobin and α-Lactalbumin Form Smaller Complexes with the Biosurfactant Rhamnolipid Than with SDS.

D. Otzen, J. S. Pedersen, G. R. Deen, 2017, Biophysical journal.

Journal Pre-proof A penetratin-derived peptide reduces the membrane permeabilization and cell toxicity of α-synuclein oligomers

D. Otzen, A. Saboury, K. Strømgaard, 2022 .

A Triple Role for a Bilayer: Using Nanoliposomes to Cross and Protect Cellular Membranes

D. Otzen, H. Mohammad-Beigi, D. Morshedi, 2021, The Journal of Membrane Biology.

Drug repurposing screens identify compounds that inhibit α-synuclein oligomers' membrane disruption and block antibody interactions

D. Otzen, Madhu Nagaraj, A. K. Somavarapu, 2022, bioRxiv.

Cys-labelling kinetics of membrane protein GlpG: a role for specific SDS binding and micelle changes?

Nicholas P. Schafer, N. Schafer, D. Otzen, 2021, Biophysical journal.

Phospholipid Ether Linkages Significantly Modulate the Membrane Affinity of the Antimicrobial Peptide Novicidin

D. Otzen, V. Balakrishnan, S. Nielsen, 2015, The Journal of Membrane Biology.

UvA-DARE (Digital Academic Repository) Membrane Structure of Aquaporin Observed with Combined Experimental and Theoretical Sum Frequency Generation Spectroscopy

M. Bonn, D. Otzen, J. Pfaendtner, 2021 .

Adsorption of Azo Dyes by a Novel Bio-Nanocomposite Based on Whey Protein Nanofibrils and Montmorillonite: Equilibrium Isotherm and Kinetic Modeling

D. Otzen, D. Morshedi, Shabboo RahimiAqdam, 2021 .

Adsorption of Azo Dyes by a Novel Bio-Nanocomposite Based on Whey Protein Nanofibrils and Nano-clay: Equilibrium Isotherm and Kinetic Modeling

D. Otzen, Niyaz Mohammad Mahmoodi, D. Morshedi, 2020, bioRxiv.

A complete picture of protein unfolding and refolding in surfactants†

D. Otzen, Jeppe Lyngsø, T. Zinn, 2019, Chemical science.

A Semester-Long Learning Path Teaching Computational Skills via Molecular Graphics in PyMOL

D. Otzen, E. Andersen, S. Thirup, 2022, The Biophysicist.

Structural Basis for Dityrosine-Mediated Inhibition of α-Synuclein Fibrillization

E. Marklund, D. Otzen, M. Tiwari, 2022, Journal of the American Chemical Society.

Inhibitory effects of fluorinated benzenesulfonamides on insulin fibrillation.

D. Otzen, B. Schiøtt, D. Matulis, 2022, International journal of biological macromolecules.

Glycolipid Biosurfactants Activate, Dimerize, and Stabilize Thermomyces lanuginosus Lipase in a pH-Dependent Fashion.

D. Otzen, J. S. Pedersen, K. K. Andersen, 2017, Biochemistry.

The anionic biosurfactant rhamnolipid does not denature industrial enzymes

D. Otzen, A. Madsen, A. Møller, 2015, Front. Microbiol..

Global study of myoglobin-surfactant interactions.

D. Otzen, P. Westh, K. K. Andersen, 2008, Langmuir : the ACS journal of surfaces and colloids.

Enzymatic Characterisation of Novamyl®, a Thermostable α‐Amylase

D. Otzen, T. Schäfer, C. Christophersen, 1998 .

The Antimicrobial Mechanism of Action of Epsilon-Poly-l-Lysine

D. Otzen, R. Meyer, T. Mygind, 2014, Applied and Environmental Microbiology.

Biosurfactants and surfactants interacting with membranes and proteins: Same but different?

D. Otzen, 2017, Biochimica et biophysica acta. Biomembranes.

Weak and Saturable Protein–Surfactant Interactions in the Denaturation of Apo-α-Lactalbumin by Acidic and Lactonic Sophorolipid

D. Otzen, S. Roelants, K. K. Andersen, 2016, Front. Microbiol..

Promoting protein self-association in non-glycosylated Thermomyces lanuginosus lipase based on crystal lattice contacts.

D. Otzen, J. Vind, J. S. Pedersen, 2015, Biochimica et biophysica acta.

Denaturation of α-lactalbumin and myoglobin by the anionic biosurfactant rhamnolipid.

D. Otzen, K. K. Andersen, 2014, Biochimica et biophysica acta.

Low‐Resolution Structures of OmpA⋅DDM Protein–Detergent Complexes

M. Glasius, D. Otzen, J. S. Pedersen, 2014, Chembiochem : a European journal of chemical biology.

Folding of outer membrane protein A in the anionic biosurfactant rhamnolipid

D. Otzen, K. K. Andersen, 2014, FEBS letters.

pH regulation of the kinetic stability of the lipase from Thermomyces lanuginosus.

D. Otzen, P. Westh, P. Sehgal, 2013, Biochemistry.

Protein-surfactant interactions: a tale of many states.

Daniel Otzen, D. Otzen, 2011, Biochimica et biophysica acta.

The role of decorated SDS micelles in sub-CMC protein denaturation and association.

D. Otzen, C. L. Oliveira, J. S. Pedersen, 2009, Journal of molecular biology.

Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism

Michele Vendruscolo, Sara Linse, Christopher M Dobson, 2013, Proceedings of the National Academy of Sciences.

Hydrogen exchange in chymotrypsin inhibitor 2 probed by mutagenesis.

A. Fersht, B. Davis, L. Itzhaki, 1997, Journal of molecular biology.

Interactions between anionic mixed micelles and α-cyclodextrin and their inclusion complexes: conductivity, NMR and fluorescence study

D. Otzen, P. Sehgal, R. Wimmer, 2006 .

Structural basis for cyclodextrins' suppression of human growth hormone aggregation

D. Otzen, F. Aachmann, R. Wimmer, 2002, Protein science : a publication of the Protein Society.

Quantitative Use of Paramagnetic Relaxation Enhancements for Determining Orientations and Insertion Depths of Peptides in Micelles

D. Otzen, R. Wimmer, Magnus Franzmann, 2009, Chembiochem : a European journal of chemical biology.

Interactions and influence of α-cyclodextrin on the aggregation and interfacial properties of mixtures of nonionic and zwitterionic surfactants

H. Doe, D. Otzen, P. Sehgal, 2009 .

Influence of β‐Cyclodextrin on the Mixed Micellization Process of Sodium Dodecyl Sulfate and Sodium Lauroyl Sarcosine and Formation of Inclusion Complexes

H. Doe, D. Otzen, P. Sehgal, 2008 .

Interactions of γ-Cyclodextrin with the Mixed Micelles of Anionic Surfactants and Their Inclusion Complexes Formation

H. Doe, D. Otzen, P. Sehgal, 2008 .

11th International Cyclodextrin Symposuim, Reykjavik. Iceland

D. Otzen, F. Aachmann, R. Wimmer, 2002 .

Interaction and Stability of Mixed Micelle and Monolayer of Nonionic and Cationic Surfactant Mixtures

H. Doe, D. Otzen, P. Sehgal, 2009 .

Protein unfolding in detergents: effect of micelle structure, ionic strength, pH, and temperature.

D. Otzen, 2002, Biophysical journal.

Half a century of amyloids: past, present and future.

D. Eisenberg, C. Dobson, R. Riek, 2020, Chemical Society reviews.

Designed protein tetramer zipped together with a hydrophobic Alzheimer homology: a structural clue to amyloid assembly.

D. Otzen, M. Oliveberg, O. Kristensen, 2000, Proceedings of the National Academy of Sciences of the United States of America.

Modulation of fibrillation of hIAPP core fragments by chemical modification of the peptide backbone.

D. Otzen, F. Besenbacher, M. Dong, 2012, Biochimica et biophysica acta.

Quantitating denaturation by formic acid: imperfect repeats are essential to the stability of the functional amyloid protein FapC

D. Otzen, J. Nowak, S. A. Frank, 2020, The Journal of Biological Chemistry.

Interactions between misfolded protein oligomers and membranes: A central topic in neurodegenerative diseases?

D. Otzen, Nikolai Lorenzen, M. Andreasen, 2015, Biochimica et biophysica acta.

Conservation of the Amyloid Interactome Across Diverse Fibrillar Structures

J. Enghild, D. Otzen, N. Nielsen, 2019, Scientific Reports.

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.

D. Otzen, J. Nielsen, T. Skrydstrup, 2015, Biochimica et biophysica acta.

Cyclodextrin-scaffolded alamethicin with remarkably efficient membrane permeabilizing properties and membrane current conductance.

D. Otzen, N. Nielsen, T. Skrydstrup, 2012, The journal of physical chemistry. B.

Mutation in transforming growth factor beta induced protein associated with granular corneal dystrophy type 1 reduces the proteolytic susceptibility through local structural stabilization.

J. Enghild, D. Otzen, N. Nielsen, 2013, Biochimica et biophysica acta.

Aggregation and fibrillation of bovine serum albumin.

D. Otzen, N. Holm, P. Sehgal, 2007, Biochimica et biophysica acta.

Formulation and anti-neurotoxic activity of baicalein-incorporating neutral nanoliposome.

D. Otzen, A. Saboury, A. Shabani, 2018, Colloids and surfaces. B, Biointerfaces.

Effect of protein-surfactant interactions on aggregation of β-lactoglobulin.

D. Otzen, H. Bertelsen, P. Wejse, 2011, Biochimica et biophysica acta.

Molecular dynamics study of ACBP denaturation in alkyl sulfates demonstrates possible pathways of unfolding through fused surfactant clusters.

Nicholas P. Schafer, N. Schafer, D. Otzen, 2019, Protein engineering, design & selection : PEDS.

How chain length and charge affect surfactant denaturation of acyl coenzyme A binding protein (ACBP).

D. Otzen, K. K. Andersen, 2009, The journal of physical chemistry. B.

Thermodynamics and mechanism of cutinase stabilization by trehalose

D. Otzen, R. Baptista, J. Cabral, 2008, Biopolymers.

Changes in structures of milk proteins upon photo-oxidation.

L. B. Larsen, D. Otzen, T. Dalsgaard, 2007, Journal of agricultural and food chemistry.

In vitro and in silico assessment of the developability of a designed monoclonal antibody library

M. Vendruscolo, D. Otzen, L. De Maria, 2019, mAbs.

Electrochemical analysis of the fibrillation of Parkinson's disease α-synuclein.

E. Ferapontova, D. Otzen, Paula Lopes, 2014, The Analyst.

Alpha-Lactalbumin is unfolded by all classes of surfactants but by different mechanisms.

D. Otzen, P. Westh, P. Sehgal, 2009, Journal of colloid and interface science.

Folding of circular and permuted chymotrypsin inhibitor 2: retention of the folding nucleus.

A. Fersht, D. Otzen, D E Otzen, 1998, Biochemistry.

The Major Birch Allergen, Bet v 1, Shows Affinity for a Broad Spectrum of Physiological Ligands*

D. Otzen, J. Mogensen, M. Spangfort, 2002, The Journal of Biological Chemistry.

The major allergen from birch tree pollen, Bet v 1, binds and permeabilizes membranes.

J. Enghild, D. Otzen, J. Mogensen, 2007, Biochemistry.

Liprotides kill cancer cells by disrupting the plasma membrane

D. Otzen, T. L. Boye, J. Nylandsted, 2017, Scientific Reports.

The neural chaperone proSAAS blocks α-synuclein fibrillation and neurotoxicity

I. Lindberg, D. Otzen, N. Maidment, 2016, Proceedings of the National Academy of Sciences.

Attractive interactions of PEO-containing block copolymer micelles in salt solutions

D. Otzen, J. S. Pedersen, K. K. Andersen, 2008 .

Mapping out the multistage fibrillation of glucagon

D. Otzen, G. Christiansen, S. Nielsen, 2012, The FEBS journal.

α‐synuclein oligomers and fibrils: a spectrum of species, a spectrum of toxicities

P. Alam, D. Otzen, R. Melki, 2019, Journal of neurochemistry.

The role of stable α-synuclein oligomers in the molecular events underlying amyloid formation.

Alexander K. Buell, C. Dobson, J. Enghild, 2014, Journal of the American Chemical Society.

Dendrimers destabilize proteins in a generation‐dependent manner involving electrostatic interactions

D. Otzen, L. Giehm, P. Heegaard, 2008, Biopolymers.

Widespread Abundance of Functional Bacterial Amyloid in Mycolata and Other Gram-Positive Bacteria

J. Enghild, P. Højrup, D. Otzen, 2009, Applied and Environmental Microbiology.

Accelerated Amyloid Beta Pathogenesis by Bacterial Amyloid FapC

R. Mezzenga, D. Otzen, Sijie Lin, 2020, Advanced science.

Modulation of cutinase stability and structure by phospholipid detergents.

D. Otzen, P. Sehgal, S. Pedersen, 2007, Biochimica et biophysica acta.

C subunit of the ATP synthase is an amyloidogenic calcium dependent channel-forming peptide with possible implications in mitochondrial permeability transition

D. Otzen, Z. Leonenko, B. Lee, 2021, Scientific Reports.

A SAXS study of glucagon fibrillation.

Jesper Søndergaard Pedersen, Daniel Otzen, Jan Skov Pedersen, 2009, Journal of molecular biology.

Analysis of protein-protein interactions by mutagenesis: direct versus indirect effects.

A. Fersht, D. Otzen, D E Otzen, 1999, Protein engineering.

Functional Amyloids.

R. Riek, D. Otzen, 2019, Cold Spring Harbor perspectives in biology.

We find them here, we find them there: Functional bacterial amyloid

D. Otzen, P. Nielsen, Per Halkjær Nielsen, 2008, Cellular and Molecular Life Sciences.

Functional amyloid in Pseudomonas

J. Enghild, D. Otzen, J. Nielsen, 2010, Molecular microbiology.

Reduction in the amount of 8‐hydroxy‐2'‐deoxyguanosine in the DNA of SV40‐transformed human fibroblasts as compared with normal cells in culture

J. Barciszewski, B. Clark, D. Otzen, 1993, FEBS letters.

Detection of proteolytic signatures for Parkinson's disease

J. Enghild, D. Otzen, M. Larsen, 2016 .

Polarized α-synuclein trafficking and transcytosis across brain endothelial cells via Rab7-decorated carriers

D. Otzen, M. Nielsen, P. Jensen, 2022, Fluids and Barriers of the CNS.

Liprotides made of α-lactalbumin and cis fatty acids form core-shell and multi-layer structures with a common membrane-targeting mechanism.

D. Otzen, C. L. Oliveira, J. S. Pedersen, 2016, Biochimica et biophysica acta.

Protein–fatty acid complexes: biochemistry, biophysics and function

S. Thiel, D. Otzen, C. Brinkmann, 2013, The FEBS journal.

A Multi-Method Approach for Analyzing FapC Fibrillation and Determining Mass per Length.

D. Otzen, J. S. Pedersen, H. Rasmussen, 2021, Biophysical journal.

Imperfect repeats in the functional amyloid protein FapC reduce the tendency to fragment during fibrillation

J. Enghild, D. Otzen, G. Christiansen, 2019, Protein science : a publication of the Protein Society.

Reducing the Amyloidogenicity of Functional Amyloid Protein FapC Increases Its Ability To Inhibit α-Synuclein Fibrillation

D. Otzen, G. Christiansen, B. Vad, 2019, ACS omega.

Epigallocatechin Gallate Remodels Overexpressed Functional Amyloids in Pseudomonas aeruginosa and Increases Biofilm Susceptibility to Antibiotic Treatment*

D. Otzen, P. Nielsen, R. Meyer, 2016, The Journal of Biological Chemistry.

Expression of Fap amyloids in Pseudomonas aeruginosa, P. fluorescens, and P. putida results in aggregation and increased biofilm formation

D. Otzen, M. Overgaard, A. Stensballe, 2013, MicrobiologyOpen.

Amyloid adhesins are abundant in natural biofilms.

D. Otzen, J. Nielsen, R. Wetzel, 2007, Environmental microbiology.

Interaction of a potyviral VPg with anionic phospholipid vesicles.

D. Otzen, K. Rantalainen, N. Kalkkinen, 2009, Virology.

The changing face of glucagon fibrillation: structural polymorphism and conformational imprinting.

Jesper Søndergaard Pedersen, Gunna Christiansen, Daniel Erik Otzen, 2006, Journal of molecular biology.

Two conformationally distinct α-synuclein oligomers share common epitopes and the ability to impair long-term potentiation

D. Otzen, G. Rammes, G. Christiansen, 2019, PloS one.

Evolutionary Insight into the Functional Amyloids of the Pseudomonads

D. Otzen, P. Nielsen, M. Dueholm, 2013, PloS one.

Novel noscapine derivatives stabilize the native state of insulin against fibrillation.

D. Otzen, A. Moosavi-Movahedi, B. Schiøtt, 2020, International journal of biological macromolecules.

Conformational plasticity in folding of the split β-α-β protein S6: evidence for burst-phase disruption of the native state

Daniel E. Otzen, D. Otzen, M. Oliveberg, 2002 .

Breakdown of supersaturation barrier links protein folding to amyloid formation

D. Otzen, J. Buchner, J. Kardos, 2021, Communications biology.

MIRRAGGE – Minimum Information Required for Reproducible AGGregation Experiments

Alexandra Silva, Daniel E. Otzen, Oxana V. Galzitskaya, 2020, Frontiers in Molecular Neuroscience.

The hydrophobic effect characterises the thermodynamic signature of amyloid fibril growth

Juami Hermine Mariama van Gils, Erik van Dijk, Alessia Peduzzo, 2019, PLoS Comput. Biol..

Identification of amyloidogenic proteins in the microbiomes of a rat Parkinson's disease model and wild‐type rats

D. Otzen, M. Dueholm, Florian-Alexander Herbst, 2021, Protein science : a publication of the Protein Society.

Functional amyloids in the microbiomes of a rat Parkinson’s disease model and wild-type rats

D. Otzen, M. Dueholm, Florian-Alexander Herbst, 2021, bioRxiv.

Glucagon fibril polymorphism reflects differences in protofilament backbone structure.

Daniel Erik Otzen, Louise C Serpell, J. Enghild, 2010, Journal of molecular biology.

Curli Functional Amyloid Systems Are Phylogenetically Widespread and Display Large Diversity in Operon and Protein Structure

D. Otzen, P. Nielsen, M. Dueholm, 2012, PloS one.

Unique identification of supramolecular structures in amyloid fibrils by solid-state NMR spectroscopy.

D. Otzen, N. Nielsen, M. Bjerring, 2009, Angewandte Chemie.

Amyloid—a state in many guises: Survival of the fittest fibril fold

D. Otzen, J. S. Pedersen, 2007, Protein science : a publication of the Protein Society.

Bidirectional protein–protein interactions control liquid–liquid phase separation of PSD-95 and its interaction partners

Christian Parsbæk Pedersen, D. Otzen, K. Teilum, 2021, bioRxiv.

The Effect of Osmolytes on Protein Fibrillation

Daniel E. Otzen, Francesca Macchi, D. Otzen, 2012, International journal of molecular sciences.

In-Silico Evidence for a Two Receptor Based Strategy of SARS-CoV-2

G. Ruocco, D. Otzen, Lorenzo Di Rienzo, 2020, Frontiers in Molecular Biosciences.

Amyloid structure – one but not the same: the many levels of fibrillar polymorphism

D. Otzen, J. S. Pedersen, C. B. Andersen, 2010, The FEBS journal.

Structural changes in the transition state of protein folding: alternative interpretations of curved chevron plots.

M. Proctor, D. Otzen, M. Oliveberg, 1999, Biochemistry.

The optimal docking strength for reversibly tethered kinases

D. Otzen, M. Dyla, Nicolás S. González Foutel, 2022, bioRxiv.

The Tubular Sheaths Encasing Methanosaeta thermophila Filaments Are Functional Amyloids*

D. Otzen, K. Finster, P. Nielsen, 2015, The Journal of Biological Chemistry.

Aggregation of S6 in a quasi-native state by sub-micellar SDS.

H. Doe, D. Otzen, P. Sehgal, 2008, Biochimica et biophysica acta.

Sulfates dramatically stabilize a salt-dependent type of glucagon fibrils.

D. Otzen, J. Flink, J. S. Pedersen, 2006, Biophysical journal.

Mechanistic Understanding of the Interactions between Nano-Objects with Different Surface Properties and α-Synuclein.

F. Farzadfar, D. Otzen, M. Mahmoudi, 2019, ACS nano.

Pardaxin permeabilizes vesicles more efficiently by pore formation than by disruption.

Niels Chr Nielsen, D. Otzen, N. Nielsen, 2010, Biophysical journal.

Nature and consequences of GroEL-protein interactions.

A. Fersht, L. Itzhaki, D. Otzen, 1995, Biochemistry.

Salt-induced detour through compact regions of the protein folding landscape.

D. Otzen, M. Oliveberg, Daniel E. Otzen, 1999, Proceedings of the National Academy of Sciences of the United States of America.

How Epigallocatechin Gallate Can Inhibit α-Synuclein Oligomer Toxicity in Vitro♦

D. Otzen, F. Mulder, J. S. Pedersen, 2014, The Journal of Biological Chemistry.

The transcriptional regulator GalR self-assembles to form highly regular tubular structures

Nicholas P. Schafer, N. Schafer, D. Otzen, 2016, Scientific Reports.

The Neuroendocrine Protein 7B2 Suppresses the Aggregation of Neurodegenerative Disease-related Proteins

I. Lindberg, D. Otzen, Nikolai Lorenzen, 2012, The Journal of Biological Chemistry.

Low-resolution structure of a vesicle disrupting α-synuclein oligomer that accumulates during fibrillation

Dmitri I Svergun, Bente Vestergaard, D. Svergun, 2011, Proceedings of the National Academy of Sciences.

The N‐terminus of α‐synuclein is essential for both monomeric and oligomeric interactions with membranes

D. Otzen, Nikolai Lorenzen, S. Nielsen, 2014, FEBS letters.

A Complex Dance: The Importance of Glycosaminoglycans and Zinc in the Aggregation of Human Prolactin.

D. Otzen, G. Christiansen, Line Friis Bakmann Christensen, 2016, Biochemistry.

Quartz crystal microbalance studies of multilayer glucagon fibrillation at the solid-liquid interface.

D. Otzen, F. Besenbacher, M. Dong, 2007, Biophysical journal.

Molecular characteristics of porcine alpha-synuclein splicing variants.

D. Otzen, K. Larsen, G. Christiansen, 2020, Biochimie.

Crystallographic analysis reveals a unique lidocaine binding site on human serum albumin.

Poul Nissen, Daniel Otzen, D. Otzen, 2010, Journal of structural biology.

The status of the terminal regions of α-synuclein in different forms of aggregates during fibrillization.

D. Otzen, J. Collingwood, Frederik Lermyte, 2020, International journal of biological macromolecules.

The structural architecture of an α-synuclein toxic oligomer

D. Otzen, A. Muga, S. Ventura, 2023, bioRxiv.

Formation and Characterization of α-Synuclein Oligomers.

D. Otzen, Nikolai Lorenzen, Wojciech Paslawski, 2016, Methods in molecular biology.

Protein aggregation: close encounters of the greasy kind.

D. Otzen, 2015, Nature chemical biology.

High stability and cooperative unfolding of α-synuclein oligomers.

D. Otzen, J. S. Pedersen, Nikolai Lorenzen, 2014, Biochemistry.

Oligomers of α-synuclein: picking the culprit in the line-up.

D. Otzen, Nikolai Lorenzen, 2014, Essays in biochemistry.

Co-existence of two different α-synuclein oligomers with different core structures determined by hydrogen/deuterium exchange mass spectrometry.

D. Otzen, T. Jørgensen, K. Thomsen, 2014, Angewandte Chemie.

Sequential pH-driven dimerization and stabilization of the N-terminal domain enables rapid spider silk formation

Jerker Widengren, Qing Meng, Hans Jörnvall, 2014, Nature Communications.

Functional Amyloids in Bacteria

D. Otzen, M. Chapman, P. Nielsen, 2013 .

Structural background of cyclodextrin-protein interactions.

D. Otzen, F. Aachmann, R. Wimmer, 2003, Protein engineering.

In vitro association of fragments of a beta-sheet membrane protein.

D. Otzen, K. Nielsen, D. Debnath, 2010, Biophysical chemistry.

Stability and Folding of Endoglucanase I (CEL7B) from Humicoia Insolens

D. Otzen, M. Schülein, 2001 .

Amyloid formation in surfactants and alcohols: membrane mimetics or structural switchers?

D. Otzen, 2010, Current protein & peptide science.

A semi high-throughput method for real-time monitoring of curli producing Salmonella biofilms on air-solid interfaces

D. Otzen, K. Melican, Ferdinand X. Choong, 2021, Biofilm.

A monomer-trimer model supports intermittent glucagon fibril growth

M. Jensen, D. Otzen, L. Oddershede, 2015, Scientific Reports.

Glucagon stop-go kinetics supports a monomer-trimer fibrillation model

M. Jensen, D. Otzen, L. Oddershede, 2014, 1410.4853.

Role of Charge and Hydrophobicity in Liprotide Formation: A Molecular Dynamics Study with Experimental Constraints

Pim W. J. M. Frederix, D. Otzen, S. Marrink, 2018, Chembiochem : a European journal of chemical biology.

Dynamic content exchange between liprotides.

D. Otzen, S. A. Frank, Henriette S. Frislev, 2018, Biophysical chemistry.

Tailoring thermal treatment to form liprotide complexes between oleic acid and different proteins.

D. Otzen, J. Pedersen, H. V. Sørensen, 2017, Biochimica et biophysica acta. Proteins and proteomics.

The Use of Liprotides To Stabilize and Transport Hydrophobic Molecules.

D. Otzen, J. Pedersen, J. Pedersen, 2015, Biochemistry.

Generic Structures of Cytotoxic Liprotides: Nano‐Sized Complexes with Oleic Acid Cores and Shells of Disordered Proteins

D. Otzen, E. Permyakov, S. Permyakov, 2014, Chembiochem : a European journal of chemical biology.

Using micellar mole fractions to assess membrane protein stability in mixed micelles.

D. Otzen, J. Mogensen, P. Sehgal, 2005, Biochimica et biophysica acta.

Amyloid fibril inhibition, acceleration, or fragmentation; Are nano-based approaches advance in the right direction?

Daniel E. Otzen, Mohammad Javad Hajipour, Iraj Nabipour, 2020 .

Proteolytic activation of proteose peptone component 3 by release of a C-terminal peptide with antibacterial properties.

D. Otzen, E. Sørensen, S. Nielsen, 2012, Journal of dairy science.

PP3 forms stable tetrameric structures through hydrophobic interactions via the C‐terminal amphipathic helix and undergoes reversible thermal dissociation and denaturation

D. Otzen, E. Sørensen, S. Nielsen, 2012, The FEBS journal.

Synergistic behavior of sodiumdodecylsulfate and 1,2-diheptanoyl-sn- glycero-3-phosphocholine in an aqueous medium: interfacial and bulk behavior

H. Doe, D. Otzen, P. Sehgal, 2005 .

Interactions between folding factors and bacterial outer membrane proteins

D. Otzen, J. Mogensen, 2005, Molecular microbiology.

Fibrillation of the major curli subunit CsgA under a wide range of conditions implies a robust design of aggregation.

D. Otzen, P. Nissen, P. Nielsen, 2011, Biochemistry.

Functional Bacterial Amyloids in Biofilms

D. Otzen, J. Nielsen, P. Nielsen, 2011 .

Size-Selective Phagocytic Clearance of Fibrillar α-Synuclein through Conformational Activation of Complement Receptor 4

B. Vestergaard, D. Otzen, S. Paludan, 2020, The Journal of Immunology.

Early stages of amyloid fibril formation studied by liquid-state NMR: the peptide hormone glucagon.

D. Otzen, Kasper Jahn, N. Nielsen, 2008, Biophysical journal.

How epigallocatechin gallate binds and assembles oligomeric forms of human alpha-synuclein

D. Otzen, F. Mulder, Camilla B. Andersen, 2021, The Journal of biological chemistry.

α-Synucleins from Animal Species Show Low Fibrillation Propensities and Weak Oligomer Membrane Disruption.

J. Enghild, D. Otzen, J. S. Pedersen, 2018, Biochemistry.

Corneal Dystrophy Mutations Drive Pathogenesis by Targeting TGFBIp Stability and Solubility in a Latent Amyloid-forming Domain.

Nicholas P. Schafer, N. Schafer, D. Otzen, 2018, Journal of molecular biology.

Functional amyloid

D. Otzen, 2010, Prion.

Kinetic partitioning between aggregation and vesicle permeabilization by modified ADan.

D. Otzen, G. Christiansen, B. Vad, 2009, Biochimica et biophysica acta.

Effect of glycosylation on the extracellular domain of the Ag43 bacterial autotransporter: enhanced stability and reduced cellular aggregation.

D. Otzen, A. Stensballe, U. Westergaard, 2008, The Biochemical journal.

Branching in amyloid fibril growth.

V. Martorana, D. Otzen, T. Ban, 2009, Biophysical journal.

Stabilization of the ribosomal protein S6 by trehalose is counterbalanced by the formation of a putative off-pathway species.

D. Otzen, Luyang Chen, G. Cabrita, 2005, Journal of molecular biology.

Modeling proteasome dynamics in Parkinson's disease

Kim Sneppen, Simone Pigolotti, Ludvig Lizana, 2009, Physical biology.

Modeling Protaesome dynamics in Parkinson Disease

M. Jensen, K. Sneppen, D. Otzen, 2009 .

Ubiquitin forms conventional decorated micelle structures with sodium dodecyl sulfate at saturation.

D. Otzen, J. S. Pedersen, H. Mortensen, 2021, Journal of colloid and interface science.

Assembling good amyloid: some structures at last.

D. Otzen, 2011, Structure.

Conformational plasticity in folding of the split beta-alpha-beta protein S6: evidence for burst-phase disruption of the native state.

D. Otzen, M. Oliveberg, Mikael Oliveberg, 2002, Journal of molecular biology.

A comparative study of the unfolding of the endoglucanase Cel45 from Humicola insolens in denaturant and surfactant

L. Christiansen, D. Otzen, M. Schülein, 1999, Protein science : a publication of the Protein Society.

Peak Force Infrared - Kelvin Probe Force Microscopy.

Xiaoji G. Xu, D. Otzen, G. Zeng, 2020, Angewandte Chemie.

Driving forces in amyloidosis: How does a light chain make a heavy heart?

D. Otzen, 2021, The Journal of biological chemistry.

Proteomic changes in response to chromium(VI) toxicity in Pseudomonas aeruginosa.

D. Otzen, A. Stensballe, G. Dönmez, 2010, Bioresource technology.

Conformational pathway of the polypeptide chain of chymotrypsin inhibitor-2 growing from its N terminus in vitro. Parallels with the protein folding pathway.

A. Fersht, D. Otzen, J. Neira, 1995, Journal of molecular biology.

Flexibility of the Thrombin-activatable Fibrinolysis Inhibitor Pro-domain Enables Productive Binding of Protein Substrates*

J. Enghild, D. Otzen, F. Avilés, 2010, The Journal of Biological Chemistry.

Near-complete 1H, 13C, 15N resonance assignments of dimethylsulfoxide-denatured TGFBIp FAS1-4 A546T

J. Enghild, D. Otzen, F. Mulder, 2015, Biomolecular NMR Assignments.

A thermodynamic analysis of fibrillar polymorphism.

D. Otzen, P. Nissen, P. Westh, 2010, Biophysical chemistry.

Glucagon amyloid-like fibril morphology is selected via morphology-dependent growth inhibition.

D. Otzen, C. Rischel, G. Christiansen, 2007, Biochemistry.

The Use of Surfactants to Solubilise a Glucagon Analogue

D. Otzen, L. Giehm, J. K. Madsen, 2018, Pharmaceutical Research.

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*

J. Enghild, D. Otzen, N. Nielsen, 2012, The Journal of Biological Chemistry.

Role of elongation and secondary pathways in S6 amyloid fibril growth.

C. Dobson, D. Otzen, T. Knowles, 2012, Biophysical journal.

Hydrogen exchange mass spectrometry as an analytical tool for the analysis of amyloid fibrillogenesis.

J. Enghild, D. Otzen, C. Scavenius, 2011, International journal of mass spectrometry.

The role of protonation in protein fibrillation

Peter Westh, D. Otzen, P. Westh, 2010, FEBS letters.

An Aß concatemer with altered aggregation propensities.

P. Fraser, D. Otzen, L. Giehm, 2010, Biochimica et biophysica acta.

Unfolding of beta-sheet proteins in SDS.

D. Otzen, P. Westh, K. K. Andersen, 2007, Biophysical journal.

AFM-based force spectroscopy measurements of mature amyloid fibrils of the peptide glucagon

D. Otzen, F. Besenbacher, M. Dong, 2008, Nanotechnology.

Protein fragments as models for events in protein folding pathways: protein engineering analysis of the association of two complementary fragments of the barley chymotrypsin inhibitor 2 (CI-2).

A. Fersht, D. Otzen, J. Ruiz-Sanz, 1995, Biochemistry.

Mapping of unfolding states of integral helical membrane proteins by GPS-NMR and scattering techniques: TFE-induced unfolding of KcsA in DDM surfactant.

J. González-Ros, D. Otzen, C. L. Oliveira, 2012, Biochimica et biophysica acta.

Unfolding of b -Sheet Proteins in SDS

D. Otzen, P. Westh, K. K. Andersen, 2007 .

Functional bacterial amyloid increases Pseudomonas biofilm hydrophobicity and stiffness

D. Otzen, P. Nielsen, T. Tolker-Nielsen, 2015, Front. Microbiol..

�rotein� in �io�ilici�cation

D. Otzen, 2014 .

The Role of Proteins in Biosilicification

D. Otzen, 2012, Scientifica.

Modulation of S6 fibrillation by unfolding rates and gatekeeper residues.

Jesper Søndergaard Pedersen, Daniel Erik Otzen, D. Otzen, 2004, Journal of molecular biology.

Variant of the Thermomyces lanuginosus lipase with improved kinetic stability: a candidate for enzyme replacement therapy.

D. Otzen, A. Svendsen, K. Borch, 2013, Biophysical chemistry.

Side-chain determinants of beta-sheet stability.

A. Fersht, D. Otzen, 1995, Biochemistry.

Quartz crystal microbalances as tools for probing protein-membrane interactions.

D. Otzen, S. Nielsen, 2013, Methods in molecular biology.

Impact of the antimicrobial peptide Novicidin on membrane structure and integrity.

D. Otzen, S. Nielsen, 2010, Journal of colloid and interface science.

Investigating porcine pancreatic phospholipase A2 action on vesicles and supported planar bilayers using a quartz crystal microbalance with dissipation.

D. Otzen, Tina Kristensen, Pernille H Justesen, 2004, Journal of colloid and interface science.

Alterations in Blood Monocyte Functions in Parkinson's Disease

D. Berg, H. Møller, D. Otzen, 2019, Movement disorders : official journal of the Movement Disorder Society.

Movement of the position of the transition state in protein folding.

A. Fersht, L. Itzhaki, D. Otzen, 1995, Biochemistry.

Chaperones mainly suppress primary nucleation during formation of functional amyloid required for bacterial biofilm formation

C. Emanuelsson, D. Otzen, Jonathan Pansieri, 2021, Chemical science.

Gallic acid loaded onto polyethylenimine-coated human serum albumin nanoparticles (PEI-HSA-GA NPs) stabilizes α-synuclein in the unfolded conformation and inhibits aggregation

D. Otzen, S. Shojaosadati, H. Mohammad-Beigi, 2016 .

Spectroscopic evidence for the existence of an obligate pre‐fibrillar oligomer during glucagon fibrillation

D. Otzen, G. Christiansen, J. S. Pedersen, 2008, FEBS Letters.

Divorcing folding from function: how acylation affects the membrane-perturbing properties of an antimicrobial peptide.

J. Enghild, D. Otzen, N. Nielsen, 2010, Biochimica et biophysica acta.

Folding energetics and oligomerization of polytopic α-helical transmembrane proteins.

D. Otzen, D. Schneider, J. Neumann, 2014, Archives of biochemistry and biophysics.

AFM study of glucagon fibrillation via oligomeric structures resulting in interwoven fibrils

D. Otzen, F. Besenbacher, M. Dong, 2006, Nanotechnology.

p25α Stimulates α-Synuclein Aggregation and Is Co-localized with Aggregated α-Synuclein in α-Synucleinopathies*

Daniel Otzen, P. Højrup, J. Nyengaard, 2005, Journal of Biological Chemistry.

A simple way to measure protein refolding rates in water.

D. Otzen, M. Oliveberg, 2001, Journal of molecular biology.

Quality control system response to stochastic growth of amyloid fibrils

K. Sneppen, D. Otzen, L. Lizana, 2012, FEBS letters.

Coexistence of ribbon and helical fibrils originating from hIAPP20–29 revealed by quantitative nanomechanical atomic force microscopy

D. Otzen, F. Besenbacher, M. Dong, 2013, Proceedings of the National Academy of Sciences.

Liprotides assist in folding of outer membrane proteins

D. Otzen, Jannik Nedergaard Pedersen, Jan Skov Pedersen, 2018, Protein science : a publication of the Protein Society.

The stability of transmembrane helix interactions measured in a biological membrane.

D. Engelman, D. Otzen, D. Schneider, 2006, Journal of molecular biology.

DIBMA nanodiscs keep α-synuclein folded.

D. Otzen, P. Cruz, Daniela C. Vaz, 2020, Biochimica et biophysica acta. Biomembranes.

Surfactants and Alcohols as Inducers of Protein Amyloid: Aggregation Chaperones or Membrane Simulators?

D. Otzen, 2011 .

Extracellular G-quadruplex and Z-DNA protect biofilms from DNase I and forms a DNAzyme with peroxidase activity

D. Otzen, V. Birkedal, R. Meyer, 2023, bioRxiv.

Experimental Approaches to Inducing Amyloid Aggregates

D. Otzen, L. Giehm, 2013 .

Condenser: a statistical aggregation tool for multi-sample quantitative proteomic data from Matrix Science Mascot Distiller™.

Allan Stensballe, Svend Birkelund, Anders Dahl Knudsen, 2014, Journal of proteomics.

Concatemers of Outer Membrane Protein A Take Detours in the Folding Landscape.

D. Otzen, K. K. Andersen, B. Vad, 2016, Biochemistry.

Human Phenotypically Distinct TGFBI Corneal Dystrophies Are Linked to the Stability of the Fourth FAS1 Domain of TGFBIp*

J. Enghild, D. Otzen, N. Nielsen, 2010, The Journal of Biological Chemistry.

Overexpression of human alpha-Synuclein leads to dysregulated microbiome/metabolites with ageing in a rat model of Parkinson disease

D. Otzen, F. Lang, H. Lashuel, 2020, bioRxiv.

Inhibitors of α-Synuclein fibrillation and oligomer toxicity in Rosa damascena: the all-pervading powers of flavonoids and phenolic glycosides.

D. Otzen, J. Ward, Duncan S Sutherland, 2020, ACS chemical neuroscience.

Alpha-synuclein and familial variants affect the chain order and the thermotropic phase behavior of anionic lipid vesicles.

D. Otzen, R. Bartucci, M. Pantusa, 2016, Biochimica et biophysica acta.

The influence of vesicle size and composition on alpha-synuclein structure and stability.

D. Otzen, T. Heimburg, L. Giehm, 2009, Biophysical journal.

Directed evolution of barnase stability using proteolytic selection.

D. Otzen, P. Kristensen, J. S. Pedersen, 2002, Journal of molecular biology.

Conservation of the Amyloid Interactome Across Diverse Fibrillar Structures

J. Enghild, D. Otzen, N. Nielsen, 2019, Scientific Reports.

Single versus parallel pathways of protein folding and fractional formation of structure in the transition state.

A. Fersht, L. Itzhaki, D. Otzen, 1994, Proceedings of the National Academy of Sciences of the United States of America.

Structure of the transition state for the folding/unfolding of the barley chymotrypsin inhibitor 2 and its implications for mechanisms of protein folding.

A. Fersht, L. Itzhaki, D. Otzen, 1994, Proceedings of the National Academy of Sciences of the United States of America.

Burst-phase expansion of native protein prior to global unfolding in SDS.

D. Otzen, M. Oliveberg, 2002, Journal of molecular biology.

Multiple roles of heparin in the aggregation of p25α.

M. Jensen, D. Otzen, J. Mathiesen, 2012, Journal of molecular biology.

Sucrose prevents protein fibrillation through compaction of the tertiary structure but hardly affects the secondary structure

Gunna Christiansen, D. Otzen, Eduardo P Melo, 2015, Proteins.

Human Lysozyme Peptidase Resistance Is Perturbed by the Anionic Glycolipid Biosurfactant Rhamnolipid Produced by the Opportunistic Pathogen Pseudomonas aeruginosa.

J. Enghild, D. Otzen, C. Scavenius, 2017, Biochemistry.

Using Liprotides to Deliver Cholesterol to the Plasma Membrane

D. Otzen, J. Nylandsted, Janni Nielsen, 2018, The Journal of Membrane Biology.

p25α is flexible but natively folded and binds tubulin with oligomeric stoichiometry

D. Otzen, P. Jensen, R. Wimmer, 2005, Protein science : a publication of the Protein Society.

Purification and Identification of High Molecular Weight Products Formed During Storage of Neutral Formulation of Human Insulin

D. Otzen, F. Hubálek, Jonatan Andersson, 2015, Pharmaceutical Research.

The Molecular Basis For TGFBIp-Related Corneal Dystrophies

J. Enghild, D. Otzen, M. Andreasen, 2014 .

Topological constraints and modular structure in the folding and functional motions of GlpG, an intramembrane protease

Nicholas P. Schafer, P. Wolynes, K. Lindorff-Larsen, 2016, Proceedings of the National Academy of Sciences.

Folding of DsbB in mixed micelles: a kinetic analysis of the stability of a bacterial membrane protein.

D. Otzen, 2003, Journal of molecular biology.

Mapping the folding pathway of the transmembrane protein DsbB by protein engineering.

D. Otzen, 2011, Protein engineering, design & selection : PEDS.

Misfolding of a bacterial autotransporter

D. Otzen, M. Schmidt, J. Mogensen, 2005, Protein science : a publication of the Protein Society.

Characteristic and cytotoxic activity of different a-Lactalbumin/fatty acids nanocomplex

D. Otzen, H. Salama, M. Foda, 2015 .

Structure of the transition state for folding of a protein derived from experiment and simulation.

A. Fersht, A. Li, V. Daggett, 1996, Journal of molecular biology.

Folding of outer membrane proteins.

D. Otzen, K. K. Andersen, 2013, Archives of biochemistry and biophysics.

Off-pathway aggregation can inhibit fibrillation at high protein concentrations.

Taru Deva, Jan J Enghild, J. Enghild, 2013, Biochimica et biophysica acta.

GFP fusions of Sec-routed extracellular proteins in Staphylococcus aureus reveal surface-associated coagulase in biofilms

D. Otzen, M. Leake, B. Kallipolitis, 2023, Microbial cell.

Folding of circular permutants with decreased contact order: general trend balanced by protein stability.

A. Finkelstein, A. V. Finkelstein, D. Otzen, 2001, Journal of molecular biology.

Scanning tunneling microscopy reveals single-molecule insights into the self-assembly of amyloid fibrils.

E. Lægsgaard, D. Otzen, F. Besenbacher, 2012, ACS nano.

The importance of being capped: Terminal capping of an amyloidogenic peptide affects fibrillation propensity and fibril morphology.

D. Otzen, M. Dong, B. Schiøtt, 2014, Biochemistry.

The rate of isomerisation of peptidyl-proline bonds as a probe for interactions in the physiological denatured state of chymotrypsin inhibitor 2.

A. Fersht, D. Otzen, M. Oliveberg, 1997, Journal of molecular biology.

The length distribution of frangible biofilaments.

Julian C. W. Willis, C. Dobson, M. Jensen, 2015, The Journal of chemical physics.

Stop-and-go kinetics in amyloid fibrillation.

S. Krishna, M. Jensen, D. Otzen, 2009, Physical review. E, Statistical, nonlinear, and soft matter physics.

Predicted Loop Regions Promote Aggregation: A Study of Amyloidogenic Domains in the Functional Amyloid FapC.

D. Otzen, J. S. Pedersen, Mumdooh Ahmed, 2020, Journal of molecular biology.

A kinetic analysis of the folding and unfolding of OmpA in urea and guanidinium chloride: single and parallel pathways.

D. Otzen, K. K. Andersen, Huabing Wang, 2012, Biochemistry.

Aggregation as the basis for complex behaviour of cutinase in different denaturants.

D. Otzen, S. Kristensen, R. Baptista, 2007, Biochimica et biophysica acta.

Heparin promotes fibrillation of most phenol-soluble modulin virulence peptides from Staphylococcus aureus

D. Otzen, K. Strømgaard, M. Andreasen, 2021, The Journal of biological chemistry.

The anti-platelet drug ticlopidine inhibits FapC fibrillation and biofilm production: Highlighting its antibiotic activity.

D. Otzen, A. Saboury, D. Morshedi, 2022, Biochimica et biophysica acta. Proteins and proteomics.

A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis

S. Matthews, C. Robinson, H. Bayley, 2017, Nature Communications.

A Protein Corona Modulates Interactions of α-Synuclein with Nanoparticles and Alters the Rates of the Microscopic Steps of Amyloid Formation.

Alexander K. Buell, J. Enghild, D. Otzen, 2022, ACS nano.

Model process for separation based on unfolding and refolding of chymotrypsin inhibitor 2 in thermoseparating polymer two-phase systems.

D. Otzen, J. Persson, F. Tjerneld, 2000, Journal of chromatography. B, Biomedical sciences and applications.

Sequence-targeted Peptides Divert Functional Bacterial Amyloid Towards Destabilized Aggregates and Reduce Biofilm Formation.

Nikolaos N. Louros, D. Otzen, F. Rousseau, 2023, Journal of molecular biology.

Transient formation of nano‐crystalline structures during fibrillation of an Aβ‐like peptide

D. Otzen, M. Oliveberg, 2004, Protein science : a publication of the Protein Society.

SDS-facilitated in vitro formation of a transmembrane B-type cytochrome is mediated by changes in local pH.

D. Otzen, N. Nielsen, A. Malmendal, 2011, Journal of molecular biology.

Supporting Information: In-Silico evidence for a two receptors based strategy of SARS-CoV-2

G. Ruocco, D. Otzen, Lorenzo Di Rienzo, 2021 .

Multi-Step Unfolding and Rearrangement of α-Lactalbumin by SDS Revealed by Stopped-Flow SAXS

D. Otzen, G. Jensen, J. Pedersen, 2020, Frontiers in Molecular Biosciences.

The Changing Face of Aging: Highly Sulfated Glycosaminoglycans Induce Amyloid Formation in a Lattice Corneal Dystrophy Model Protein.

D. Otzen, G. Christiansen, Cagla Sahin, 2017, Journal of molecular biology.

Cell-free synthesis and folding of transmembrane OmpA reveals higher order structures and premature truncations.

D. Otzen, D. Debnath, 2010, Biophysical chemistry.

Novicidin's membrane permeabilizing activity is driven by membrane partitioning but not by helicity: a biophysical study of the impact of lipid charge and cholesterol.

D. Otzen, V. Balakrishnan, B. Vad, 2013, Biochimica et biophysica acta.

Supporting information Mechanistic Understanding of the Interactions Between Nano- Objects, with Different Surface Properties, and α-Synuclein

F. Farzadfar, D. Otzen, I. Nabipour, 2019 .

Stability and structure of the membrane protein transporter Ffh is modulated by substrates and lipids.

D. Otzen, M. E. Reinau, 2009, Archives of biochemistry and biophysics.

Correspondence between anomalous m‐ and Δ Cp‐values in protein folding

D. Otzen, M. Oliveberg, 2004 .

Tau Fibrillation Induced by Heparin or a Lysophospholipid Show Different Initial Oligomer Formation.

D. Otzen, Janni Nielsen, Jan Skov Pedersen, 2023, Journal of molecular biology.

Induction, inhibition, and incorporation: Different roles for anionic and zwitterionic lysolipids in the fibrillation of the functional amyloid FapC

D. Otzen, J. S. Pedersen, H. Rasmussen, 2022, The Journal of biological chemistry.

The Spectral and Thermodynamic Properties of Staphylococcal Enterotoxin A, E, and Variants Suggest That Structural Modifications Are Important to Control Their Function*

D. Otzen, P. Antonsson, P. Björk, 2000, The Journal of Biological Chemistry.

OmpA can form folded and unfolded oligomers.

D. Otzen, K. K. Andersen, B. Vad, 2013, Biochimica et biophysica acta.

Functional amyloid in a lipid-like environment: a merry dance of many steps.

D. Otzen, 2022, Essays in biochemistry.

Partial volume correction using cortical surfaces

Lasse Riis Østergaard, Simon F. Eskildsen, Per Borghammer, 2010, Medical Imaging.

Alzheimer's Progenitor Amyloid‐β Targets and Dissolves Microbial Amyloids and Impairs Biofilm Function

A. Balaji, D. Otzen, Aleksandr Kakinen, 2023, Advanced science.

Folding steps in the fibrillation of functional amyloid: denaturant sensitivity reveals common features in nucleation and elongation.

D. Otzen, S. A. Frank, T. V. Sønderby, 2021, Journal of molecular biology.

Peroxynitrous acid (ONOOH) modifies the structure of anastellin and influences its capacity to polymerize fibronectin

D. Otzen, P. Hägglund, P. Gourdon, 2020, Redox biology.

Molecular-level insights into the surface-induced assembly of Functional Bacterial Amyloid.

D. Otzen, Pengyu Wang, T. V. Sønderby, 2022, Biophysical journal.

Lactadherin binds to phosphatidylserine-containing vesicles in a two-step mechanism sensitive to vesicle size and composition.

D. Otzen, J. Rasmussen, Kristine Blans, 2012, Biochimica et biophysica acta.

Multiple roles of heparin in the aggregation of p25α.

M. Jensen, D. Otzen, J. Mathiesen, 2012, Journal of molecular biology.

Unique identification of supramolecular structures in amyloid fibrils by solid-state NMR spectroscopy.

D. Otzen, N. Nielsen, M. Bjerring, 2009, Angewandte Chemie.

Soft interactions at nanoparticles alter protein function and conformation in a size dependent manner.

D. Otzen, F. Besenbacher, J. S. Pedersen, 2011, Nano letters.

Amyloid structure – one but not the same: the many levels of fibrillar polymorphism

D. Otzen, J. S. Pedersen, C. B. Andersen, 2010, The FEBS journal.

Elevated concentrations cause upright alpha-synuclein conformation at lipid interfaces

D. Otzen, Mengming Michael Dong, Steven Joop Roeters, 2023, Nature communications.

The length distribution of frangible biofilaments.

Alexander K. Buell, Julian C. W. Willis, C. Dobson, 2015, The Journal of chemical physics.

Trehalose favors a cutinase compact intermediate off-folding pathway.

S. Petersen, D. Otzen, Luyang Chen, 2003, Biochemistry.

A Possible Connection Between Plant Longevity and the Absence of Protein Fibrillation: Basis for Identifying Aggregation Inhibitors in Plants

D. Otzen, J. Ward, H. Mohammad-Beigi, 2019, Front. Plant Sci..

Eurocin, a New Fungal Defensin

H. Kristensen, D. Otzen, H. Sahl, 2012, The Journal of Biological Chemistry.

Sequential pH-driven dimerization and stabilization of the N-terminal domain enables rapid spider silk formation

J. Johansson, H. Jörnvall, D. Otzen, 2014, Nature Communications.

The Spectral and Thermodynamic Properties of Staphylococcal

D. Otzen, P. Antonsson, P. Björk, 2000 .

Liprotides kill cancer cells by disrupting the plasma membrane

D. Otzen, T. L. Boye, Jesper Nylandsted, 2017, Scientific Reports.

The Use of Liprotides To Stabilize and Transport Hydrophobic Molecules.

D. Otzen, J. Pedersen, J. N. Pedersen, 2015, Biochemistry.

Interaction between whey protein nanoparticles and fatty acids

D. Otzen, M. Foda, R. Awad, 2015 .

Transdisciplinary pragmatic melioration for the plastic life cycle: Why the social, natural, and technical sciences should prioritize reducing harm.

D. Otzen, Mogens Hinge, Gauri Pathak, 2023, The Science of the total environment.

Periostin C-Terminal Is Intrinsically Disordered and Interacts with 143 Proteins in an In Vitro Epidermal Model of Atopic Dermatitis

J. Enghild, D. Otzen, N. S. Nielsen, 2023, Biochemistry.

N for AsN – O for StrOcture? A strand–loop–strand motif for prokaryotic O‐glycosylation

D. Otzen, 2012, Molecular microbiology.

Membrane protein folding and stability.

D. Otzen, 2014, Archives of Biochemistry and Biophysics.

Differential adsorption of variants of the Thermomyces lanuginosus lipase on a hydrophobic surface suggests a role for local flexibility.

D. Otzen, 2008, Colloids and Surfaces B: Biointerfaces.

Quartz Crystal Microbalances as Tools for Probing Protein-Membrane Interactions.

D. Otzen, S. Nielsen, 2019, Methods in molecular biology.

Adsorption of a small protein to a methyl-terminated hydrophobic surfaces: effect of protein-folding thermodynamics and kinetics

Daniel E. Otzen, Fredrik Höök, D. Otzen, 2003 .

Occupancy of nonannular lipid binding sites on KcsA greatly increases the stability of the tetrameric protein.

J. González-Ros, J. Encinar, D. Otzen, 2010, Biochemistry.

C subunit of the ATP synthase is an amyloidogenic channel-forming peptide: possible implications in mitochondrial pathogenesis

D. Otzen, Z. Leonenko, B. Lee, 2020, bioRxiv.

Structural factors contributing to the hydrophobic effect: the partly exposed hydrophobic minicore in chymotrypsin inhibitor 2.

A. Fersht, D. Otzen, M. Rheinnecker, 1995, Biochemistry.

Fast Mapping of Global Protein Folding States by Multivariate NMR: A GPS for Proteins

D. Otzen, N. Nielsen, A. Malmendal, 2010, PloS one.

A Targetable N-Terminal Motif Orchestrates α-Synuclein Oligomer-to-Fibril Conversion

D. Otzen, A. Muga, S. Ventura, 2024, bioRxiv.

Thermodynamics of unfolding of an integral membrane protein in mixed micelles

D. Otzen, P. Sehgal, 2006, Protein science : a publication of the Protein Society.

Helping proteins come in from the cold: 5 burning questions about cold-active enzymes

D. Otzen, J. S. Nowak, 2023, BBA advances.