Kamau Fahie, Ph.D. - Publications

2009 Johns Hopkins University, Baltimore, MD 
lysine ubiquitination and acetylation, using x-ray crystallography, together with biochemical, biophysical and genetic analysis

5 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2012 Chaumorcel M, Lussignol M, Mouna L, Cavignac Y, Fahie K, Cotte-Laffitte J, Geballe A, Brune W, Beau I, Codogno P, Esclatine A. The human cytomegalovirus protein TRS1 inhibits autophagy via its interaction with Beclin 1. Journal of Virology. 86: 2571-84. PMID 22205736 DOI: 10.1128/JVI.05746-11  0.36
2010 Mohan S, Tse CM, Gabelli SB, Sarker R, Cha B, Fahie K, Nadella M, Zachos NC, Tu-Sekine B, Raben D, Amzel LM, Donowitz M. NHE3 activity is dependent on direct phosphoinositide binding at the N terminus of its intracellular cytosolic region. The Journal of Biological Chemistry. 285: 34566-78. PMID 20736165 DOI: 10.1074/jbc.M110.165712  0.36
2009 Fahie K, Hu P, Swatkoski S, Cotter RJ, Zhang Y, Wolberger C. Side chain specificity of ADP-ribosylation by a sirtuin. The Febs Journal. 276: 7159-76. PMID 19895577 DOI: 10.1111/j.1742-4658.2009.07427.x  0.36
2006 Haigis MC, Mostoslavsky R, Haigis KM, Fahie K, Christodoulou DC, Murphy AJ, Valenzuela DM, Yancopoulos GD, Karow M, Blander G, Wolberger C, Prolla TA, Weindruch R, Alt FW, Guarente L. SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie restriction in pancreatic beta cells. Cell. 126: 941-54. PMID 16959573 DOI: 10.1016/j.cell.2006.06.057  0.36
2002 Fahie K, Pitts R, Elkins K, Nelson DJ. Molecular dynamics study of Ca(2+) binding loop variants of silver hake parvalbumin with aspartic acid at the "gateway" position. Journal of Biomolecular Structure & Dynamics. 19: 821-37. PMID 11922838 DOI: 10.1080/07391102.2002.10506787  0.36
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