Unraveling the mechanism of cell death induced by chemical fibrils

[1]  J. Weissman,et al.  Functional genomics platform for pooled screening and generation of mammalian genetic interaction maps , 2014, Nature Protocols.

[2]  Brian K. Shoichet,et al.  Colloidal Drug Formulations Can Explain “Bell-Shaped” Concentration–Response Curves , 2014, ACS chemical biology.

[3]  A. Burlingame,et al.  Global cellular response to chemotherapy-induced apoptosis , 2013, eLife.

[4]  Mathias Jucker,et al.  Self-propagation of pathogenic protein aggregates in neurodegenerative diseases , 2013, Nature.

[5]  F. Brodsky,et al.  Heparan sulfate proteoglycans mediate internalization and propagation of specific proteopathic seeds , 2013, Proceedings of the National Academy of Sciences.

[6]  Martin Kampmann,et al.  Integrated platform for genome-wide screening and construction of high-density genetic interaction maps in mammalian cells , 2013, Proceedings of the National Academy of Sciences.

[7]  Michael T. McManus,et al.  A Systematic Mammalian Genetic Interaction Map Reveals Pathways Underlying Ricin Susceptibility , 2013, Cell.

[8]  Julia E. Seaman,et al.  The DegraBase: A Database of Proteolysis in Healthy and Apoptotic Human Cells* , 2012, Molecular & Cellular Proteomics.

[9]  M. Beal,et al.  Neuroprotection by cyclodextrin in cell and mouse models of Alzheimer disease , 2012, The Journal of experimental medicine.

[10]  Dennis W Wolan,et al.  Fibrils Colocalize Caspase-3 with Procaspase-3 to Foster Maturation* , 2012, The Journal of Biological Chemistry.

[11]  Alma L. Burlingame,et al.  Quantitative profiling of caspase-cleaved substrates reveals different drug-induced and cell-type patterns in apoptosis , 2012, Proceedings of the National Academy of Sciences.

[12]  B. Shoichet,et al.  Colloidal Aggregation Affects the Efficacy of Anticancer Drugs in Cell Culture , 2012, ACS chemical biology.

[13]  Mathias Jucker,et al.  The Amyloid State of Proteins in Human Diseases , 2012, Cell.

[14]  D. Wolan,et al.  Self-assembling small molecules form nanofibrils that bind procaspase-3 to promote activation. , 2011, Journal of the American Chemical Society.

[15]  Dana Pe'er,et al.  Modulatory profiling identifies mechanisms of small molecule-induced cell death , 2011, Proceedings of the National Academy of Sciences.

[16]  Y. Koide,et al.  Rab GTPases Regulating Phagosome Maturation Are Differentially Recruited to Mycobacterial Phagosomes , 2011, Traffic.

[17]  Christian Münch,et al.  Prion-like propagation of mutant superoxide dismutase-1 misfolding in neuronal cells , 2011, Proceedings of the National Academy of Sciences.

[18]  Egil Lien,et al.  NLRP3 inflammasomes are required for atherogenesis and activated by cholesterol crystals , 2010, Nature.

[19]  James A. Wells,et al.  Small-Molecule Activators of a Proenzyme , 2009, Science.

[20]  H. Stenmark.  Rab GTPases as coordinators of vesicle traffic , 2009, Nature Reviews Molecular Cell Biology.

[21]  Michael T. McManus,et al.  Rapid Creation and Quantitative Monitoring of High Coverage shRNA Libraries , 2009, Nature Methods.

[22]  David T. Barkan,et al.  Global Sequencing of Proteolytic Cleavage Sites in Apoptosis by Specific Labeling of Protein N Termini , 2008, Cell.

[23]  K. Moore,et al.  The NALP3 inflammasome is involved in the innate immune response to amyloid-β , 2008, Nature Immunology.

[24]  William A Weiss,et al.  Recognizing and exploiting differences between RNAi and small-molecule inhibitors. , 2007, Nature chemical biology.

[25]  D. Selkoe,et al.  Aβ Oligomers – a decade of discovery , 2007, Journal of neurochemistry.

[26]  Acknowledgments , 2006, Molecular and Cellular Endocrinology.

[27]  O. Bocharova,et al.  Amyloid Fibrils of Mammalian Prion Protein Are Highly Toxic to Cultured Cells and Primary Neurons* , 2006, Journal of Biological Chemistry.

[28]  J. Kelly,et al.  Pathological and functional amyloid formation orchestrated by the secretory pathway. , 2003, Current opinion in structural biology.

[29]  Adrian E. Raftery,et al.  Model-Based Clustering, Discriminant Analysis, and Density Estimation , 2002 .

[30]  B. Deurs,et al.  Rab7: a key to lysosome biogenesis. , 2000, Molecular biology of the cell.

[31]  M. Zerial,et al.  Rabaptin-5 is a direct effector of the small GTPase Rab5 in endocytic membrane fusion , 1995, Cell.

[32]  C. Der,et al.  GTP-binding mutants of rab1 and rab2 are potent inhibitors of vesicular transport from the endoplasmic reticulum to the Golgi complex , 1992, The Journal of cell biology.

[33]  W. A. Hagins,et al.  Liposome-cell interaction: transfer and intracellular release of a trapped fluorescent marker. , 1977, Science.

[34]  Julia E. Seaman,et al.  Global analysis of cellular proteolysis by selective enzymatic labeling of protein N-termini. , 2014, Methods in enzymology.