M
Matthew J. Lazzara
Researcher at University of Virginia
Publications - 63
Citations - 2067
Matthew J. Lazzara is an academic researcher from University of Virginia. The author has contributed to research in topics: Phosphorylation & Receptor tyrosine kinase. The author has an hindex of 23, co-authored 54 publications receiving 1783 citations. Previous affiliations of Matthew J. Lazzara include Massachusetts Institute of Technology & Millipore Corporation.
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Structural determinants of glomerular permeability.
TL;DR: There is good evidence for a role of charge in restricting the transmural movement ofalbumin and an effect of albumin that has received little attention, namely, its tendency to increase the sieving coefficients of test macromolecules via steric interactions.
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Reactivation of ERK Signaling Causes Resistance to EGFR Kinase Inhibitors
Dalia Ercan,Chunxiao Xu,Masahiko Yanagita,Calixte S. Monast,Christine A. Pratilas,Joan Montero,Mohit Butaney,Takeshi Shimamura,Lynette M. Sholl,Elena Ivanova,Madhavi Tadi,Andrew H. Rogers,Claire E. Repellin,Marzia Capelletti,Ophélia Maertens,Eva M. Goetz,Anthony Letai,Levi A. Garraway,Matthew J. Lazzara,Neal Rosen,Nathanael S. Gray,Kwok-Kin Wong,Pasi A. Jänne +22 more
TL;DR: It is shown, in multiple complementary models, that resistance to WZ4002 develops through aberrant activation of extracellular signal-regulated kinase (ERK) signaling caused by either an amplification of mitogen-activated protein kinase 1 (MAPK1) or by downregulation of negative regulators of ERK signaling.
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Erk1/2 blockade prevents epithelial-mesenchymal transition in lung cancer cells and promotes their sensitivity to egfr inhibition
TL;DR: It is demonstrated that extracellular signal-regulated kinase (ERK) 1/2 (mitogen-activated protein kinase 3/1, MAPK3/1) signaling plays a key role in directing the mesenchymal character of NSCLC cells and that blocking ERK signaling is sufficient to heighten therapeutic responses to EGF receptor (EGFR) inhibitors.
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Cell signaling regulation by protein phosphorylation: a multivariate, heterogeneous, and context-dependent process.
TL;DR: The study of signaling regulation by protein phosphorylation is complicated by the sheer scope of the kinome and phosphoproteome, dependence of signaling protein functionality on cellular localization, and the complex multivariate relationships that exist between proteinosphorylation dynamics and the cellular phenotypes they control.
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Motor Protein Myo1c Is a Podocyte Protein That Facilitates the Transport of Slit Diaphragm Protein Neph1 to the Podocyte Membrane
Ehtesham Arif,Mark C. Wagner,Duncan B. Johnstone,Hetty N. Wong,Britta George,P. A. Pruthi,Matthew J. Lazzara,Deepak Nihalani +7 more
TL;DR: A novel Myo1c-dependent molecular mechanism is identified that mediates the dynamic organization of Neph1 and nephrin at the slit diaphragm and is critical for podocyte function.