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The Journal of biological chemistry, ISSN 1083-351X, 2017, Volume 292, Issue 31, pp. 12764 - 12771
Eukaryotic cells contain hundreds of metalloproteins that are supported by intracellular systems coordinating the uptake and distribution of metal cofactors.... 
metalloprotein | HUMAN BOLA2 | HEME-BIOSYNTHESIS | DEOXYHYPUSINE HYDROXYLASE | BolA2 | BIOCHEMISTRY & MOLECULAR BIOLOGY | glutaredoxin | SACCHAROMYCES-CEREVISIAE | iron metabolism | molecular chaperone | PHP4 FUNCTION | FERRITIN DEGRADATION | poly C-binding protein | IN-VIVO | GENE-EXPRESSION | iron | iron-sulfur protein | SULFUR CLUSTER | MONOTHIOL GLUTAREDOXIN | Molecular Chaperones - metabolism | Humans | Protein Multimerization | Iron-Sulfur Proteins - chemistry | Molecular Chaperones - chemistry | Nuclear Receptor Coactivators - chemistry | Autophagy | Apoferritins - metabolism | Ferritins - metabolism | Cation Transport Proteins - metabolism | Apoenzymes - metabolism | Carrier Proteins - chemistry | Dimerization | Nuclear Receptor Coactivators - metabolism | Erythroid Precursor Cells - cytology | RNA-Binding Proteins - chemistry | Heterogeneous-Nuclear Ribonucleoproteins - metabolism | Models, Molecular | Apoferritins - chemistry | Iron - metabolism | Protein Transport | Animals | Carrier Proteins - metabolism | Proteins - metabolism | Models, Biological | Heterogeneous-Nuclear Ribonucleoproteins - chemistry | Apoenzymes - chemistry | Erythroid Precursor Cells - metabolism | Cytosol - metabolism | Iron-Sulfur Proteins - metabolism | Proteins - chemistry | Cation Transport Proteins - chemistry | Ferritins - chemistry | RNA-Binding Proteins - metabolism | iron–sulfur protein | Minireviews
Journal Article
Chemistry – A European Journal, ISSN 0947-6539, 07/2015, Volume 21, Issue 29, pp. 10306 - 10309
Multifunctional silica nanoparticles decorated with fluorescent and sulfonamide carbonic anhydrase (CA) inhibitors were prepared and investigated as... 
carbonic anhydrase | inhibitors | nanoparticles | sulfonamide | multivalency | Nanoparticles | Inhibitors | Multivalency | Sulfonamide | Carbonic anhydrase | THERAPEUTIC APPLICATIONS | CHEMISTRY, MULTIDISCIPLINARY | Nanoparticles - chemistry | Carbonic Anhydrase Inhibitors - chemistry | Humans | Cytosol - drug effects | Carbonic Anhydrase II - metabolism | Isoenzymes - chemistry | Structure-Activity Relationship | Carbonic Anhydrase I - metabolism | Antigens, Neoplasm - chemistry | Carbonic Anhydrase II - antagonists & inhibitors | Carbonic Anhydrases - metabolism | Dose-Response Relationship, Drug | Cytosol - enzymology | Neoplasms - chemistry | Isoenzymes - metabolism | Enzyme Inhibitors - chemistry | Antigens, Neoplasm - metabolism | Antineoplastic Agents - pharmacology | Molecular Structure | Silicon Dioxide - chemistry | Enzyme Inhibitors - pharmacology | Neoplasms - enzymology | Carbonic Anhydrase I - chemistry | Carbonic Anhydrase Inhibitors - pharmacology | Antineoplastic Agents - chemistry | Cytosol - chemistry | Neoplasms - drug therapy | Carbonic Anhydrase I - antagonists & inhibitors | Cell Line, Tumor | Isoenzymes - antagonists & inhibitors | Carbonic Anhydrase II - chemistry | Enzyme inhibitors | Isoenzymes | Sulfonamides | Silica | Enzymes | Binding | Fluorescence | Inhibition | Clustering | Silicon dioxide | Material chemistry | Chemical Sciences
Journal Article
FEBS Letters, ISSN 0014-5793, 12/2016, Volume 590, Issue 24, pp. 4531 - 4540
Iron–sulfur (Fe–S) clusters are ubiquitously conserved and play essential cellular roles. The mechanism of Fe–S cluster biogenesis involves multiple proteins... 
[2Fe‐2S] cluster transfer | iron–sulfur cluster | Nfu | glutaredoxin | IscU | [2Fe-2S] cluster transfer | HUMAN NFU | iron-sulfur cluster | BIOCHEMISTRY & MOLECULAR BIOLOGY | PROTEIN BIOGENESIS | MATURATION | SACCHAROMYCES-CEREVISIAE | 4FE-4S CLUSTER | CELL BIOLOGY | MONOTHIOL GLUTAREDOXINS | BIOPHYSICS | BIOSYNTHESIS | 2FE-2S CLUSTER | SCAFFOLD PROTEIN | Apoproteins - chemistry | Humans | Bacterial Proteins - chemistry | Iron-Sulfur Proteins - genetics | Iron-Sulfur Proteins - chemistry | Oxidoreductases - chemistry | Saccharomyces cerevisiae - metabolism | Biological Transport | Escherichia coli - metabolism | Carrier Proteins - chemistry | Thermotoga maritima - chemistry | Thermotoga maritima - metabolism | Apoproteins - metabolism | Sulfur - chemistry | Recombinant Proteins - metabolism | Sulfur - metabolism | Gene Expression | Oxidoreductases - metabolism | Oxidoreductases - genetics | Iron - chemistry | Bacterial Proteins - genetics | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Saccharomyces cerevisiae Proteins - genetics | Iron - metabolism | Saccharomyces cerevisiae - chemistry | Cytosol - chemistry | Carrier Proteins - genetics | Carrier Proteins - metabolism | Escherichia coli - genetics | Saccharomyces cerevisiae Proteins - metabolism | Apoproteins - genetics | Bacterial Proteins - metabolism | Cytosol - metabolism | Iron-Sulfur Proteins - metabolism | Kinetics | Saccharomyces cerevisiae Proteins - chemistry
Journal Article
Angewandte Chemie International Edition, ISSN 1433-7851, 09/2016, Volume 55, Issue 38, pp. 11377 - 11381
Journal Article
Journal Article