morinlab.bib
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+@article{scheffzekRasRasGAPComplexStructural1997,
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+ title = {The {{Ras-RasGAP}} Complex: Structural Basis for {{GTPase}} Activation and Its Loss in Oncogenic {{Ras}} Mutants},
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+ shorttitle = {The {{Ras-RasGAP}} Complex},
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+ author = {Scheffzek, K. and Ahmadian, M. R. and Kabsch, W. and Wiesmüller, L. and Lautwein, A. and Schmitz, F. and Wittinghofer, A.},
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+ date = {1997-07-18},
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+ journaltitle = {Science (New York, N.Y.)},
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+ shortjournal = {Science},
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+ volume = {277},
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+ number = {5324},
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+ eprint = {9219684},
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+ eprinttype = {pmid},
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+ pages = {333--338},
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+ issn = {0036-8075},
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+ doi = {10.1126/science.277.5324.333},
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+ abstract = {The three-dimensional structure of the complex between human H-Ras bound to guanosine diphosphate and the guanosine triphosphatase (GTPase)-activating domain of the human GTPase-activating protein p120GAP (GAP-334) in the presence of aluminum fluoride was solved at a resolution of 2.5 angstroms. The structure shows the partly hydrophilic and partly hydrophobic nature of the communication between the two molecules, which explains the sensitivity of the interaction toward both salts and lipids. An arginine side chain (arginine-789) of GAP-334 is supplied into the active site of Ras to neutralize developing charges in the transition state. The switch II region of Ras is stabilized by GAP-334, thus allowing glutamine-61 of Ras, mutation of which activates the oncogenic potential, to participate in catalysis. The structural arrangement in the active site is consistent with a mostly associative mechanism of phosphoryl transfer and provides an explanation for the activation of Ras by glycine-12 and glutamine-61 mutations. Glycine-12 in the transition state mimic is within van der Waals distance of both arginine-789 of GAP-334 and glutamine-61 of Ras, and even its mutation to alanine would disturb the arrangements of residues in the transition state.},
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+ langid = {english},
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+ keywords = {Aluminum Compounds,Amino Acid Sequence,Binding Sites,Catalysis,Cell Transformation Neoplastic,Crystallography X-Ray,Enzyme Activation,Fluorides,GTP Phosphohydrolases,GTP-Binding Proteins,GTPase-Activating Proteins,Guanosine Diphosphate,Guanosine Triphosphate,Humans,Models Molecular,Molecular Sequence Data,Mutation,Protein Conformation,Protein Structure Secondary,Proteins,ras GTPase-Activating Proteins,ras Proteins,Signal Transduction}
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+}
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+
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@article{pfeiferPTENLossDefines2013,
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title = {{{PTEN}} Loss Defines a {{PI3K}}/{{AKT}} Pathway-Dependent Germinal Center Subtype of Diffuse Large {{B-cell}} Lymphoma},
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author = {Pfeifer, Matthias and Grau, Michael and Lenze, Dido and Wenzel, Sören-Sebastian and Wolf, Annette and Wollert-Wulf, Brigitte and Dietze, Kerstin and Nogai, Hendrik and Storek, Benjamin and Madle, Hannelore and Dörken, Bernd and Janz, Martin and Dirnhofer, Stephan and Lenz, Peter and Hummel, Michael and Tzankov, Alexandar and Lenz, Georg},