Identification of Transthyretin Variants by Sequential Proteomic and Genomic Analysis | Zendy

H. Robert Bergen | Zendy; Steven R. Zeldenrust | Zendy; Malinda L. Butz | Zendy; Denise S. Snow | Zendy; P. James B. Dyck | Zendy; Christopher J. Klein | Zendy; John F. O’Brien | Zendy; Stephen N. Thibodeau | Zendy; David C. Muddiman | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

Identification of Transthyretin Variants by Sequential Proteomic and Genomic Analysis

Author(s) -

H. Robert Bergen,

Steven R. Zeldenrust,

Malinda L. Butz,

Denise S. Snow,

P. James B. Dyck,

Christopher J. Klein,

John F. O’Brien,

Stephen N. Thibodeau,

David C. Muddiman

Publication year - 2004

Publication title -

clinical chemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.705

H-Index - 218

eISSN - 1530-8561

pISSN - 0009-9147

DOI - 10.1373/clinchem.2004.033266

Subject(s) - transthyretin , amyloidosis , sequence analysis , chemistry , electrospray ionization , mass spectrometry , tandem mass spectrometry , microbiology and biotechnology , dna , biology , medicine , biochemistry , chromatography

Transthyretin-associated hereditary amyloidosis (ATTR) is an inherited disease in which variants in the primary structure of transthyretin (TTR; prealbumin) lead to the extracellular polymerization of insoluble protein fibrils, causing organ failure and ultimately death when major organs are involved. We have developed an integrated approach to molecular diagnosis with initial analysis of intact plasma TTR by electrospray ionization mass spectrometry (MS) and referral of positive samples for DNA sequence analysis and real-time PCR to confirm the common Gly6Ser polymorphism.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research