Description

Human protein diversity arises as a result of alternative splicing, single nucleotide polymorphisms (SNPs) and posttranslational modifications. Because of these processes, each protein can exists as multiple variants in vivo.

Human protein diversity arises as a result of alternative splicing, single nucleotide polymorphisms (SNPs) and posttranslational modifications. Because of these processes, each protein can exists as multiple variants in vivo. Tailored strategies are needed to study these protein variants and understand their role in health and disease. In this work we utilized quantitative mass spectrometric immunoassays to determine the protein variants concentration of beta-2-microglobulin, cystatin C, retinol binding protein, and transthyretin, in a population of 500 healthy individuals.

Reuse Permissions
  • application/pdf

    Download count: 0

    Details

    Contributors
    Date Created
    • 2014-06-23
    Resource Type
  • Text
  • Collections this item is in
    Identifier

    Citation and reuse

    Cite this item

    This is a suggested citation. Consult the appropriate style guide for specific citation guidelines.

    Trenchevska, Olgica, Phillips, David A., Nelson, Randall W., & Nedelkov, Dobrin (2014). Delineation of Concentration Ranges and Longitudinal Changes of Human Plasma Protein Variants. PLOS ONE, 9(6). http://dx.doi.org/10.1371/journal.pone.0100713

    Machine-readable links