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Journal of Molecular Biology|April 23, 2022
Allosteric Regulation of the Soluble Epoxide Hydrolase by Nitro Fatty Acids: a Combined Experimental and Computational ApproachQiongju Qiu, Giancarlo Abis, Florence Mattingly-Peck, et al.
Nature Structural & Molecular Biology|March 9, 2004
Structural analysis of cooperative RNA binding by the La motif and central RRM domain of human La proteinCaterina Alfano, Domenico Sanfelice, Jeff Babon, et al.
Structure (London, England : 1993)|July 5, 2003
Structure of the C-terminal domain of human La protein reveals a novel RNA recognition motif coupled to a helical nuclear retention elementAmanda Jacks, Jeff Babon, Geoff Kelly, et al.
Biomolecular NMR Assignments|April 22, 2015
(1)H, (15)N and (13)C chemical shift assignments of the La motif and RRM1 from human LARP6Luigi Martino, Nicholas J H Salisbury, Paul Brown, et al.
Scientific Reports|January 23, 2023
Metabolic rewiring in MYC-driven medulloblastoma by BET-bromodomain inhibitionVittoria Graziani, Aida Rodriguez Garcia, Lourdes Sainero Alcolado, et al.
Redox Biology|September 12, 2021
A thiol redox sensor in soluble epoxide hydrolase enables oxidative activation by intra-protein disulfide bond formationRebecca L Charles, Giancarlo Abis, Beatriz F Fernandez, et al.
Biochemistry|April 6, 2006
Structure of the eukaryotic initiation factor (eIF) 5 reveals a fold common to several translation factorsMaria R Conte, Geoff Kelly, Jeff Babon, et al.
Acta Crystallographica. Section D, Structural Biology|June 16, 2016
A crystallographic study of human NONO (p54(nrb)): overcoming pathological problems with purification, data collection and noncrystallographic symmetryGavin J Knott, Santosh Panjikar, Andrea Thorn, et al.
The FEBS Journal|August 4, 2009
The interaction of the Escherichia coli protein SlyD with nickel ions illuminates the mechanism of regulation of its peptidyl-prolyl isomerase activityLuigi Martino, Yangzi He, Katherine L D Hands-Taylor, et al.
RNA (New York, N.Y.)|November 14, 2012
The association of a La module with the PABP-interacting motif PAM2 is a recurrent evolutionary process that led to the neofunctionalization of La-related proteinsRémy Merret, Luigi Martino, Cécile Bousquet-Antonelli, et al.
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