Protease resistance of <i>ex vivo</i> amyloid fibrils implies the proteolytic selection of disease-associated fibril morphologies.

Schönfelder, Jonathan; Pfeiffer, Peter Benedikt; Pradhan, Tejaswini; Bijzet, Johan; Hazenberg, Bouke P C; Schönland, Stefan O; Hegenbart, Ute; Reif, Bernd; Haupt, Christian; Fändrich, Marcus

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

Schönfelder, Jonathan; Pfeiffer, Peter Benedikt; Pradhan, Tejaswini; Bijzet, Johan; Hazenberg, Bouke P C; Schönland, Stefan O; Hegenbart, Ute; Reif, Bernd; Haupt, Christian; Fändrich, Marcus.

Afiliação

Schönfelder J; Institute of Protein Biochemistry, Ulm University, Ulm, Germany.
Pfeiffer PB; Institute of Protein Biochemistry, Ulm University, Ulm, Germany.
Pradhan T; Bayerisches NMR Zentrum at the Department Chemie, Technische Universität München, Garching, Germany.
Bijzet J; Department of Rheumatology & Clinical Immunology, AA21, University Medical Center Groningen, University of Groningen, Groningen, The Netherlands.
Hazenberg BPC; Department of Rheumatology & Clinical Immunology, AA21, University Medical Center Groningen, University of Groningen, Groningen, The Netherlands.
Schönland SO; Department of Internal Medicine V (Hematology, Oncology and Rheumatology), Amyloidosis Center, University Hospital Heidelberg, Heidelberg, Germany.
Hegenbart U; Department of Internal Medicine V (Hematology, Oncology and Rheumatology), Amyloidosis Center, University Hospital Heidelberg, Heidelberg, Germany.
Reif B; Bayerisches NMR Zentrum at the Department Chemie, Technische Universität München, Garching, Germany.
Haupt C; Institute of Protein Biochemistry, Ulm University, Ulm, Germany.
Fändrich M; Institute of Protein Biochemistry, Ulm University, Ulm, Germany.

Amyloid ; 28(4): 243-251, 2021 Dec.

Article em En | MEDLINE | ID: mdl-34338090

Assuntos

Amiloide; Amiloidose; Sequência de Aminoácidos; Animais; Humanos; Peptídeo Hidrolases; Proteína Amiloide A Sérica

Palavras-chave

Amyloid structure; prion; protein misfolding; proteolytic stability; immunoglobulin light chain; transthyretin; serum amyloid A

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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Amiloide / Amiloidose Idioma: En Ano de publicação: 2021 Tipo de documento: Article

Texto completo

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PubMed Links

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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Amiloide / Amiloidose Idioma: En Ano de publicação: 2021 Tipo de documento: Article