Journal of the American Society of Nephrology

Journal: Journal of the American Society of Nephrology

Abbreviation

J Am Soc Nephrol

Publisher

American Society of Nephrology

ISSN

1046-6673
1533-3450

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Publications 1 - 6 of 6

The role of the renal ammonia transporter Rhcg in metabolic responses to dietary protein
Bounoure, Lisa; Ruffoni, Davide; Müller, Ralph; et al. (2014)
Journal of the American Society of Nephrology
Mutation in the Monocarboxylate Transporter 12 Gene Affects Guanidinoacetate Excretion but Does Not Cause Glucosuria
Dhayat, Nasser; Simonin, Alexandre; Anderegg, Manuel; et al. (2016)
Journal of the American Society of Nephrology
Pretransplant Kinetics of Anti-HLA Antibodies in Patients on the Waiting List for Kidney Transplantation
Togninalli, Matteo; Yoneoka, Daisuke; Kolios, Antonios G. A.; et al. (2019)
Journal of the American Society of Nephrology
Membranoproliferative Glomerulonephritis Type II (Dense Deposit Disease)
Appel, Gerald B.; Cook, H. Terence; Hageman, Gregory; et al. (2005)
Journal of the American Society of Nephrology
Phosphoproteomic Analysis Reveals Regulatory Mechanisms at the Kidney Filtration Barrier
Rinschen, Markus M.; Wu, Xiongwu; König, Tim; et al. (2014)
Journal of the American Society of Nephrology
Diseases of the kidney filtration barrier are a leading cause of ESRD. Most disorders affect the podocytes, polarized cells with a limited capacity for self-renewal that require tightly controlled signaling to maintain their integrity, viability, and function. Here, we provide an atlas of in vivo phosphorylated, glomerulus-expressed proteins, including podocyte-specific gene products, identified in an unbiased tandem mass spectrometry–based approach. We discovered 2449 phosphorylated proteins corresponding to 4079 identified high-confidence phosphorylated residues and performed a systematic bioinformatics analysis of this dataset. We discovered 146 phosphorylation sites on proteins abundantly expressed in podocytes. The prohibitin homology domain of the slit diaphragm protein podocin contained one such site, threonine 234 (T234), located within a phosphorylation motif that is mutated in human genetic forms of proteinuria. The T234 site resides at the interface of podocin dimers. Free energy calculation through molecular dynamic simulations revealed a role for T234 in regulating podocin dimerization. We show that phosphorylation critically regulates formation of high molecular weight complexes and that this may represent a general principle for the assembly of proteins containing prohibitin homology domains.
New approaches to the treatment of dense deposit disease
Smith, Richard J.H.; Alexander, Jessy; Barlow, Paul N.; et al. (2007)
Journal of the American Society of Nephrology

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