An additive destabilising effect of compound T60I and V122I substitutions in ATTRv amyloidosis-Reference-Cited by-同舟云学术

An additive destabilising effect of compound T60I and V122I substitutions in ATTRv amyloidosis

Published:2022-10-26 Issue: Volume: Page:1-12
ISSN:1350-6129
Container-title:Amyloid
language:en
Short-container-title:Amyloid

Author:

Prokaeva Tatiana¹^ORCID,Klimtchuk Elena S.¹,Feschenko Polina¹,Spencer Brian¹,Cui Haili¹,Burks Eric J.²,Aslebagh Roshanak³⁴,Muneeruddin Khaja³⁴,Shaffer Scott A.³⁴,Varghese Elizabeth¹,Berk John L.¹^ORCID,Connors Lawreen H.¹²^ORCID

Affiliation:

1. Amyloidosis Center, Boston University School of Medicine, Boston, MA, USA

2. Department of Pathology and Laboratory Medicine, Boston University School of Medicine, Boston, MA, USA

3. Mass Spectrometry Facility, University of Massachusetts Medical School, Shrewsbury, MA, USA

4. Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA, USA

Funder

Wildflower Foundation

Boston University Amyloid Research Fund

Young Family Amyloid Research Fund

Publisher

Informa UK Limited

Subject

Internal Medicine

Link

https://www.tandfonline.com/doi/pdf/10.1080/13506129.2022.2135988

Reference51 articles.

1. Modulation of the Mechanisms Driving Transthyretin Amyloidosis

2. Tabulation of human transthyretin (TTR) variants, 2003

3. Clinical features and survival in senile systemic amyloidosis: comparison to familial transthyretin cardiomyopathy

4. The V122I cardiomyopathy variant of transthyretin increases the velocity of rate-limiting tetramer dissociation, resulting in accelerated amyloidosis

5. Cardiac amyloidosis in African Americans: Comparison of clinical and laboratory features of transthyretin V122I amyloidosis and immunoglobulin light chain amyloidosis

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