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Daniel E. Otzen

Daniel E. Otzen

D-Index & Metrics

Chemistry

D-Index
87
Citations
27043
World Ranking
2415
National Ranking
20

Overview

Daniel E. Otzen is affiliated with Aarhus University in Denmark. Their research encompasses extensive work in the fields of Biochemistry, Genetics and Molecular Biology, and Medicine, with a focus on Molecular Biology, Physiology, Neurology, Cell Biology, and Cellular and Molecular Neuroscience.

Their main research topics include:

  • Alzheimer's disease research and treatments
  • Parkinson's Disease Mechanisms and Treatments
  • Protein Structure and Dynamics
  • Lipid Membrane Structure and Behavior
  • Bacterial biofilms and quorum sensing
  • Enzyme Structure and Function
  • Cellular transport and secretion

Frequent co-authors in their scientific collaborations are:

  • Janni Nielsen
  • Jan Skov Pedersen
  • Jannik Nedergaard Pedersen
  • Jan Stanislaw Nowak
  • Dina Morshedi

Daniel E. Otzen has contributed to numerous scientific papers. Selected recent publications include:

  • Half a century of amyloids: past, present and future, 2020, Chemical Society Reviews
  • Adsorption of azo dyes by a novel bio-nanocomposite based on whey protein nanofibrils and nano-clay: Equilibrium isotherm and kinetic modeling, 2021, Journal of Colloid and Interface Science
  • Accelerated Amyloid Beta Pathogenesis by Bacterial Amyloid FapC, 2020, Advanced Science
  • Multiple system atrophy-associated oligodendroglial protein p25α stimulates formation of novel α-synuclein strain with enhanced neurodegenerative potential, 2021, Acta Neuropathologica
  • Breakdown of supersaturation barrier links protein folding to amyloid formation, 2021, Communications Biology

Their work is frequently published in venues such as:

  • bioRxiv (Cold Spring Harbor Laboratory)
  • Journal of Biological Chemistry
  • Journal of Molecular Biology
  • International Journal of Biological Macromolecules
  • SSRN Electronic Journal

Best Publications

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

    Samuel I. A. Cohen;Sara Linse;Leila M. Luheshi;Erik Hellstrand

  • Protein drug stability: a formulation challenge

    Sven Frokjaer;Daniel E. Otzen

  • The Structure of the Transition State for Folding of Chymotrypsin Inhibitor 2 Analysed by Protein Engineering Methods: Evidence for a Nucleation-condensation Mechanism for Protein Folding

    Laura S. Itzhaki;Daniel E. Otzen;Alan R. Fersht

  • Protein-surfactant interactions: a tale of many states.

    Daniel Otzen

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

    Pu Chun Ke;Pu Chun Ke;Ruhong Zhou;Ruhong Zhou;Louise C. Serpell;Roland Riek

  • ThT 101: a primer on the use of thioflavin T to investigate amyloid formation

    Kirsten Gade Malmos;Luis M. Blancas-Mejia;Benedikt Weber;Johannes Buchner

  • Functional Amyloids.

    Unknown

  • Functional amyloid in Pseudomonas.

    Morten Simonsen Dueholm;Steen V. Petersen;Mads Sønderkær;Poul Larsen

  • The Antimicrobial Mechanism of Action of Epsilon-Poly-L-Lysine

    Morten Hyldgaard;Tina Mygind;Brian S. Vad;Marcel Stenvang

  • α-synuclein oligomers and fibrils: a spectrum of species, a spectrum of toxicities.

    Parvez Alam;Luc Bousset;Ronald Melki;Daniel E. Otzen

  • Aggregation and fibrillation of bovine serum albumin

    Nikolaj K Holm;Stine K Jespersen;Lise V. Thomassen;Tine Y Wolff

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

    Daniel E. Otzen

  • The major birch allergen, Bet v 1, shows affinity for a broad spectrum of physiological ligands.

    Jesper E. Mogensen;Reinhard Wimmer;Jørgen N. Larsen;Michael D. Spangfort

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

    Nikolai Lorenzen;Søren Bang Nielsen;Alexander K. Buell;Jørn Døvling Kaspersen

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

    Daniel E. Otzen;Laura S. Itzhaki;Nadia F. Elmasry;Sophie E. Jackson

  • STRUCTURE OF THE TRANSITION STATE FOR FOLDING OF A PROTEIN DERIVED FROM EXPERIMENT AND SIMULATION

    Valerie Daggett;Aijun Li;Laura S. Itzhaki;Daniel E. Otzen

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

    Daniel E. Otzen

  • The Changing Face of Glucagon Fibrillation: Structural Polymorphism and Conformational Imprinting

    Jesper Søndergaard Pedersen;Dantcho Dikov;James L. Flink;Hans Aage Hjuler

  • Strategies to increase the reproducibility of protein fibrillization in plate reader assays

    Lise Giehm;Daniel Erik Otzen

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

    Alan R. Fersht;Laura S. Itzhaki;Nadia F. Elmasry;Jacqueline M. Matthews

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

    Lise Giehm;Dmitri I. Svergun;Daniel E. Otzen;Bente Vestergaard

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

    Daniel E. Otzen;Ole Kristensen;Mikael Oliveberg

Frequent Co-Authors

Gunna Christiansen
Gunna Christiansen Aalborg University
Jan Skov Pedersen
Jan Skov Pedersen Aarhus University
Jan J. Enghild
Jan J. Enghild Aarhus University
Per Halkjær Nielsen
Per Halkjær Nielsen Aalborg University
Niels Chr. Nielsen
Niels Chr. Nielsen Aarhus University
Troels Skrydstrup
Troels Skrydstrup Aarhus University
Mingdong Dong
Mingdong Dong Aarhus University
Poul Henning Jensen
Poul Henning Jensen Aarhus University
Flemming Besenbacher
Flemming Besenbacher Aarhus University
Alan R. Fersht
Alan R. Fersht University of Cambridge

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