Johannes S. Schlondorff, Ph.D.

Affiliations: 
2001 Weill Cornell Medical College, New York, NY, United States 
Area:
Cell Biology, Molecular Biology
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"Johannes Schlondorff"

Parents

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Carl P. Blobel grad student 2001 Weill Cornell Medical College
 (Regulation of ectodomain shedding: Insights from studying tumor necrosis factor alpha convertase (TACE) and TRANCE shedding.)
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Publications

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Feng D, Kumar M, Muntel J, et al. (2020) Phosphorylation of ACTN4 Leads to Podocyte Vulnerability and Proteinuric Glomerulosclerosis. Journal of the American Society of Nephrology : Jasn
Subramanian B, Chun J, Perez-Gill C, et al. (2020) FSGS-Causing INF2 Mutation Impairs Cleaved INF2 N-Fragment Functions in Podocytes. Journal of the American Society of Nephrology : Jasn
Stotter BR, Talbot BE, Capen DE, et al. (2020) Cosmc-dependent mucin-type O-linked glycosylation is essential for podocyte function. American Journal of Physiology. Renal Physiology
Dvela-Levitt M, Kost-Alimova M, Emani M, et al. (2019) Small Molecule Targets TMED9 and Promotes Lysosomal Degradation to Reverse Proteinopathy. Cell. 178: 521-535.e23
Talbot BE, Vandorpe DH, Stotter BR, et al. (2019) Transmembrane insertases and N-glycosylation critically determine synthesis, trafficking and activity of the nonselective cation channel TRPC6. The Journal of Biological Chemistry
Subramanian B, Sun H, Yan P, et al. (2016) Mice with mutant Inf2 show impaired podocyte and slit diaphragm integrity in response to protamine-induced kidney injury. Kidney International
Olabisi OA, Zhang JY, VerPlank L, et al. (2015) APOL1 kidney disease risk variants cause cytotoxicity by depleting cellular potassium and inducing stress-activated protein kinases. Proceedings of the National Academy of Sciences of the United States of America
Barua M, Shieh E, Schlondorff J, et al. (2014) Exome sequencing and in vitro studies identified podocalyxin as a candidate gene for focal and segmental glomerulosclerosis. Kidney International. 85: 124-33
Sun H, Schlondorff J, Higgs HN, et al. (2013) Inverted formin 2 regulates actin dynamics by antagonizing Rho/diaphanous-related formin signaling. Journal of the American Society of Nephrology : Jasn. 24: 917-29
Sun H, Schlondorff JS, Brown EJ, et al. (2011) Rho activation of mDia formins is modulated by an interaction with inverted formin 2 (INF2). Proceedings of the National Academy of Sciences of the United States of America. 108: 2933-8
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