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Plos One|December 28, 2020
The plasticity of the pyruvate dehydrogenase complex confers a labile structure that is associated with its catalytic activityJaehyoun Lee, Seunghee Oh, Saikat Bhattacharya, et al.
Nature Structural & Molecular Biology|November 26, 2008
The MSL3 chromodomain directs a key targeting step for dosage compensation of the Drosophila melanogaster X chromosomeTuba H Sural, Shouyong Peng, Bing Li, et al.
Plos One|December 5, 2014
Live imaging provides new insights on dynamic F-actin filopodia and differential endocytosis during myoblast fusion in DrosophilaShruti Haralalka, Claude Shelton, Heather N Cartwright, et al.
The Journal of Biological Chemistry|January 22, 2005
Characterization of the yeast trimeric-SAS acetyltransferase complexWei-Jong Shia, Shigehiro Osada, Laurence Florens, et al.
The Journal of Biological Chemistry|April 4, 2003
Opposite role of yeast ING family members in p53-dependent transcriptional activationAmine Nourani, LeAnn Howe, Marilyn G Pray-Grant, et al.
Molecular Cell|November 4, 2015
Serine and SAM Responsive Complex SESAME Regulates Histone Modification Crosstalk by Sensing Cellular MetabolismShanshan Li, Selene K Swanson, Madelaine Gogol, et al.
Nucleic Acids Research|February 14, 2019
Set1-catalyzed H3K4 trimethylation antagonizes the HIR/Asf1/Rtt106 repressor complex to promote histone gene expression and chronological life spanQianyun Mei, Chen Xu, Madelaine Gogol, et al.
Molecular & Cellular Proteomics : MCP|November 5, 2010
Highly reproducible label free quantitative proteomic analysis of RNA polymerase complexesAmber L Mosley, Mihaela E Sardiu, Samantha G Pattenden, et al.
The Journal of Biological Chemistry|April 14, 2005
Mechanism of transcription factor recruitment by acidic activatorsMonica E Ferreira, Stefan Hermann, Philippe Prochasson, et al.
The Journal of Biological Chemistry|September 4, 2014
Phosphorylation by casein kinase 2 facilitates Psh1 protein-assisted degradation of Cse4 proteinGeetha S Hewawasam, Mark Mattingly, Swaminathan Venkatesh, et al.
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