Publication Beamlines Strategic Pillar
González, Javier M.; Marti-Arbona, Ricardo; Chen, Julian C.-H.; Broom-Peltz, Brian; Unkefer, Clifford J. et al. (2018). Conformational changes on substrate binding revealed by structures of Methylobacterium extorquens malate dehydrogenase. Acta Crystallographica Section F:Structural Biology Communications 74(10) , 610-616. 10.1107/s2053230x18011809. [PDB: 5ujk] CMCF-ID Health
Gonzalez, J.M. (2017). Malate dehydrogenase from Methylobacterium extorquens, complexed with NAD. Protein Data Bank: 5ujk. CMCF-ID Agriculture
Gonzalez, J.M. (2016). Crystal structure of Enolase from Synechococcus elongatus, complex with phosphoenolpyruvate. Protein Data Bank: 5j04. CMCF-ID Agriculture
Gonzalez-Lopez de Turiso, Felix; Sun, Daqing; Rew, Yosup; Bartberger, Michael D.; Beck, Hilary P. et al. (2013). Rational Design and Binding Mode Duality of MDM2–p53 Inhibitors. Journal of Medicinal Chemistry 56(10) , 4053-4070. 10.1021/jm400293z. [PDB: 4jwr] CMCF-ID Health
Goode; Angela E. (2012). Correlation of electron and x-ray spectroscopies in nanoscale systems. Supervisor: Ryan, Mary; Porter, Alexandra; McComb, David. London, UK: Imperial College London. http://hdl.handle.net/10044/1/14421. SM
Goode, Angela E.; Perkins, James M.; Sandison, Ann; Karunakaran, Chithra; Cheng, Huikai et al. (2012). Chemical speciation of nanoparticles surrounding metal-on-metal hips. Chemical Communications 48(67) , 8335. 10.1039/c2cc33016d. SM
Good, Jacob; Duchesne, Paul N.; Zhang, Peng; Koshut, William; Zhou, Meng et al. (2017). On the functional role of the cerium oxide support in the Au38(SR)24/CeO2 catalyst for CO oxidation. Catalysis Today 280, 239-245. 10.1016/j.cattod.2016.04.016. CLS-APS
Gordon, Lyle Matthew (2014). Buried Organic-Inorganic Interfaces in Biological Minerals. Illinois, USA: Northwestern University. . SGM
Gordon, Lyle M.; Cohen, Michael J.; MacRenaris, Keith W.; Pasteris, Jill D.; Seda, Takele et al. (2015). Amorphous intergranular phases control the properties of rodent tooth enamel. Science 347(6223) , 746-750. 10.1126/science.1258950. SGM
Gorelik, A.; Gebai, A.; Illes, K.; Piomelli, D.; Nagar, B. et al. (2018). Caenorhabditis elegans N-acylethanolamine-hydrolyzing acid amidase (NAAA) ortholog. Protein Data Bank: 6dy3. CMCF-ID Health
Gorelik, A.; Gebai, A.; Illes, K.; Piomelli, D.; Nagar, B. et al. (2018). Guinea pig N-acylethanolamine-hydrolyzing acid amidase (NAAA) covalently bound to beta-lactam inhibitor ARN726. Protein Data Bank: 6dy2. CMCF-ID Health
Gorelik, A.; Gebai, A.; Illes, K.; Piomelli, D.; Nagar, B. et al. (2018). Rabbit N-acylethanolamine-hydrolyzing acid amidase (NAAA) with fatty acid (myristate), in presence of Triton X-100. Protein Data Bank: 6dy1. CMCF-ID Health
Gorelik, A.; Gebai, A.; Illes, K.; Piomelli, D.; Nagar, B. et al. (2018). Rabbit N-acylethanolamine-hydrolyzing acid amidase (NAAA) covalently bound to beta-lactam inhibitor ARN726, in presence of Triton X-100. Protein Data Bank: 6dy0. CMCF-ID Health
Gorelik, A.; Gebai, A.; Illes, K.; Piomelli, D.; Nagar, B. et al. (2018). Rabbit N-acylethanolamine-hydrolyzing acid amidase (NAAA) in complex with non-covalent benzothiazole-piperazine inhibitor ARN19702, in presence of Triton X-100. Protein Data Bank: 6dxz. CMCF-ID Health
Gorelik, A.; Gebai, A.; Illes, K.; Piomelli, D.; Nagar, B. et al. (2018). Murine N-acylethanolamine-hydrolyzing acid amidase (NAAA). Protein Data Bank: 6dxy. CMCF-ID Health