Literature DB >> 19708985

Beta2-microglobulin.

Tilman B Drüeke1, Ziad A Massy.   

Abstract

Among the uremic toxins in the "middle molecule" range, beta2-microglobulin (beta2-M) is certainly one of the most frequently studied compounds. Its serum level increases with the progression of chronic kidney disease, to reach very high concentrations in patients with end-stage kidney disease. It is the major protein component of dialysis-related amyloidosis, a dramatic complication which results from high extracellular concentration and posttranslational modification of beta2-M and a number of other promoters of amyloid fibril formation and deposition in osteo-articular tissues. Effective removal of beta2-M can be achieved with highly effective hemodialysis and hemodiafiltration techniques but predialysis session serum levels cannot be normalized. The prevalence and severity of beta2-M amyloidosis appear to have decreased in the last 20 years, although its occurrence may simply be delayed.

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Year:  2009        PMID: 19708985     DOI: 10.1111/j.1525-139X.2009.00584.x

Source DB:  PubMed          Journal:  Semin Dial        ISSN: 0894-0959            Impact factor:   3.455


  33 in total

1.  Proteomic analyses of human plasma: Venus versus Mars.

Authors:  Christopher C Silliman; Monika Dzieciatkowska; Ernest E Moore; Marguerite R Kelher; Anirban Banerjee; Xiayuan Liang; Kevin J Land; Kirk C Hansen
Journal:  Transfusion       Date:  2011-08-31       Impact factor: 3.157

2.  Genome-wide association study identified the human leukocyte antigen region as a novel locus for plasma beta-2 microglobulin.

Authors:  Adrienne Tin; Brad C Astor; Eric Boerwinkle; Ron C Hoogeveen; Josef Coresh; Wen Hong Linda Kao
Journal:  Hum Genet       Date:  2013-02-16       Impact factor: 4.132

3.  Top-down study of β2-microglobulin deamidation.

Authors:  Xiaojuan Li; Xiang Yu; Catherine E Costello; Cheng Lin; Peter B O'Connor
Journal:  Anal Chem       Date:  2012-06-29       Impact factor: 6.986

4.  Epigallocatechin-3-gallate Inhibits Cu(II)-Induced β-2-Microglobulin Amyloid Formation by Binding to the Edge of Its β-Sheets.

Authors:  Tyler M Marcinko; Thomas Drews; Tianying Liu; Richard W Vachet
Journal:  Biochemistry       Date:  2020-03-03       Impact factor: 3.162

5.  Small molecule-mediated inhibition of β-2-microglobulin-based amyloid fibril formation.

Authors:  Tyler M Marcinko; Jia Dong; Raquel LeBlanc; Kate V Daborowski; Richard W Vachet
Journal:  J Biol Chem       Date:  2017-05-03       Impact factor: 5.157

6.  Hydrazone bond-oriented molecularly imprinted nanocomposites for the selective separation of protein via the well-defined recognition sites.

Authors:  Le Sheng; Yulong Jin; Huiqing Hou; Yanyan Huang; Rui Zhao
Journal:  Mikrochim Acta       Date:  2022-06-08       Impact factor: 5.833

Review 7.  Colostrogenesis: Role and Mechanism of the Bovine Fc Receptor of the Neonate (FcRn).

Authors:  Craig R Baumrucker; Ann L Macrina; Rupert M Bruckmaier
Journal:  J Mammary Gland Biol Neoplasia       Date:  2022-01-26       Impact factor: 2.673

8.  Structural Heterogeneity in the Preamyloid Oligomers of β-2-Microglobulin.

Authors:  Tyler M Marcinko; Chungwen Liang; Sergey Savinov; Jianhen Chen; Richard W Vachet
Journal:  J Mol Biol       Date:  2019-11-09       Impact factor: 5.469

9.  Using Covalent Labeling and Mass Spectrometry To Study Protein Binding Sites of Amyloid Inhibiting Molecules.

Authors:  Tianying Liu; Tyler M Marcinko; Patrick A Kiefer; Richard W Vachet
Journal:  Anal Chem       Date:  2017-10-26       Impact factor: 6.986

Review 10.  Pathophysiology and treatment of systemic amyloidosis.

Authors:  Julian D Gillmore; Philip N Hawkins
Journal:  Nat Rev Nephrol       Date:  2013-08-27       Impact factor: 28.314

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