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Coordination Chemistry Reviews, ISSN 0010-8545, 2010, Volume 254, Issue 15, pp. 1815 - 1825
Journal Article
Journal of the American Ceramic Society, ISSN 1551-2916, 2018, Volume 102, Issue 5, pp. 2482 - 2505
Journal Article
Applied Surface Science, ISSN 0169-4332, 05/2018, Volume 439, Issue C, pp. 1103 - 1110
Journal Article
Chemistry – A European Journal, ISSN 0947-6539, 04/2017, Volume 23, Issue 24, pp. 5830 - 5841
The synthesis of a class of electron‐rich amino‐functionalized β‐diketiminato (N‐nacnac) ligands is reported, with two synthetic methodologies having been... 
ligand design | coordination chemistry | electron-rich compounds | main group chemistry | nacnac ligands
Journal Article
Scientific Reports, ISSN 2045-2322, 06/2016, Volume 6, Issue 1, p. 29049
... within TiO6 octahedron to form a mass of Ti-O-O coordination bond in the interlayers. The introduction of these Ti-O-O coordination bonds result in lowering the band... 
AQUEOUS PEROXOTITANATE SOLUTION | NANOCOMPOSITES | TEMPERATURE | REDUCTION | MULTIDISCIPLINARY SCIENCES | DIOXIDE | ANATASE | OXYGEN-RICH TIO2 | THIN-FILM | INTERCALATION | TITANATE
Journal Article
03/2016, Volume 6, Issue 34, pp. 2867 - 28611
The mechanism of the adsorption of CO 2 onto various sites of MgAl 2 O 4 (100), in particular with regards to binding coordination, was investigated using density functional theory (DFT) calculations... 
Journal Article
Journal of Organometallic Chemistry, ISSN 0022-328X, 09/2015, Volume 792, Issue C, pp. 177 - 183
Journal Article
PLoS ONE, ISSN 1932-6203, 10/2012, Volume 7, Issue 10, p. e47784
Mutations in the leucine-rich repeat kinase 2 (LRRK2) gene are a common cause of autosomal dominant familial Parkinson's disease (PD). LRRK2 encodes a... 
DISEASE-ASSOCIATED MUTATIONS | KINASE-ACTIVITY | ACTIVATION | PROTEIN-KINASE | MULTIDISCIPLINARY SCIENCES | LINK | GTP-BINDING | DOPAMINERGIC NEURON | PARKINSONS-DISEASE | Phosphorylation | Humans | Male | Phosphoproteins - metabolism | Brain - metabolism | Multiprotein Complexes - metabolism | HEK293 Cells | Aged, 80 and over | Eukaryotic Initiation Factors | Female | Mammals - metabolism | Parkinson Disease - pathology | Protein-Serine-Threonine Kinases - genetics | Rats | Mutation - genetics | Subcellular Fractions - metabolism | Phosphothreonine - metabolism | Leucine-Rich Repeat Serine-Threonine Protein Kinase-2 | Animals | Carrier Proteins - metabolism | Parkinson Disease - enzymology | Brain - pathology | Aged | Mice | Protein Processing, Post-Translational | Adaptor Proteins, Signal Transducing - metabolism | Cell Cycle Proteins | Brain | Usage | Parkinson's disease | Gene mutations | Leucine zipper | Genetic aspects | Research | Complex formation | Toxicity | Parkinsons disease | Leucine | Kinases | Mammalian cells | Proteins | Neurotoxicity | Enzymatic activity | Neurodegeneration | Rodents | Animal tissues | Post-translation | Physiology | Life sciences | LRRK2 protein | Localization | Coordination compounds | Movement disorders | Neurodegenerative diseases | Drosophila | Transgenic mice | Mammals | Substrates | Neurology | Insects | Mutation | Initiation factor eIF-4E | Guanosinetriphosphatase
Journal Article