Protease resistance of ex vivo amyloid fibrils implies the proteolytic selection of disease-associated fibril morphologies-Reference-Cited by-同舟云学术

Protease resistance of ex vivo amyloid fibrils implies the proteolytic selection of disease-associated fibril morphologies

Published:2021-08-02 Issue:4 Volume:28 Page:243-251
ISSN:1350-6129
Container-title:Amyloid
language:en
Short-container-title:Amyloid

Author:

Schönfelder Jonathan¹,Pfeiffer Peter Benedikt¹,Pradhan Tejaswini²,Bijzet Johan³^ORCID,Hazenberg Bouke P. C.³^ORCID,Schönland Stefan O.⁴^ORCID,Hegenbart Ute⁴^ORCID,Reif Bernd²,Haupt Christian¹,Fändrich Marcus¹^ORCID

Affiliation:

1. Institute of Protein Biochemistry, Ulm University, Ulm, Germany

2. Bayerisches NMR Zentrum at the Department Chemie, Technische Universität München, Garching, Germany

3. Department of Rheumatology & Clinical Immunology, AA21, University Medical Center Groningen, University of Groningen, Groningen, The Netherlands

4. Department of Internal Medicine V (Hematology, Oncology and Rheumatology), Amyloidosis Center, University Hospital Heidelberg, Heidelberg, Germany

Funder

Deutsche Forschungsgemeinschaft

Research Unit FOR 2969

Publisher

Informa UK Limited

Subject

Internal Medicine

Link

https://www.tandfonline.com/doi/pdf/10.1080/13506129.2021.1960501

Reference52 articles.

1. Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade

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3. On the structural definition of amyloid fibrils and other polypeptide aggregates

4. [1] Staining methods for identification of amyloid in tissue

5. Amyloid nomenclature 2020: update and recommendations by the International Society of Amyloidosis (ISA) nomenclature committee

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