Binding of TCA to the Prion Protein: Mechanism, Implication for Therapy, and Application as Probe for Complex Formation of Bio-macromolecules-Reference-Cited by-同舟云学术

Binding of TCA to the Prion Protein: Mechanism, Implication for Therapy, and Application as Probe for Complex Formation of Bio-macromolecules

Published:2009-10-01 Issue:2 Volume:27 Page:163-170
ISSN:0739-1102
Container-title:Journal of Biomolecular Structure and Dynamics
language:en
Short-container-title:Journal of Biomolecular Structure and Dynamics

Author:

Mangels Christian¹,Frank Andreas O.¹,Ziegler Jan¹,Klingenstein Ralph²,Schweimer Kristian¹,Willbold Dieter³,Korth Carsten²,Rösch Paul¹,Schwarzinger Stephan¹

Affiliation:

1. a Department of Biopolymers , University of Bayreuth Universitätsstrasse 30 , 95440 , Bayreuth , Germany

2. b Institute of Neuropathology, Heinrich-Heine-University , Moorenstr. 5, 40225 , Düsseldorf , Germany

3. c Institute for Physical Biology Heinrich-Heine-University Düsseldorf and Institute of Neuroscience and Biophysics 2 at the Research Centre, Jülich , 52425 , Jülich , Germany

Publisher

Informa UK Limited

Subject

Molecular Biology,General Medicine,Structural Biology

Link

https://www.tandfonline.com/doi/pdf/10.1080/07391102.2009.10507306

Reference43 articles.

1. Nobel Lecture: Prions

2. The cellular prion protein binds copper in vivo

3. Structure of the recombinant full-length hamster prion protein PrP(29-231): The N terminus is highly flexible

4. NMR structure of the mouse prion protein domain PrP(121–231)

5. NMR characterization of the full-length recombinant murine prion protein, m PrP(23-231)

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