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Currents in Pharmacy Teaching and Learning, ISSN 1877-1297, 05/2017, Volume 9, Issue 3, pp. 383 - 390
Objective measures for assessing teaching effectiveness and learning outcomes in the pharmacy curriculum are needed for improving quality of instruction and... 
Student evaluations of teaching | Student self-assessment | Learning outcomes | Teaching effectiveness | Study and teaching | Research | Student evaluation of teachers | Pharmacy | Quality management
Journal Article
Antimicrobial Agents and Chemotherapy, ISSN 0066-4804, 07/2012, Volume 56, Issue 7, pp. 3481 - 3491
Journal Article
PLoS Neglected Tropical Diseases, ISSN 1935-2727, 09/2012, Volume 6, Issue 9, p. e1839
Journal Article
Journal of Inorganic Biochemistry, ISSN 0162-0134, 12/2008, Volume 102, Issue 12, p. 2043
Metallo-[beta]-lactamases (MBLs) confer antibiotic resistance to bacteria by hydrolyzing and thus inactivating [beta]-lactam antibiotics. They have raised... 
Drug resistance in microorganisms | Analysis | Caprolactam | Beta lactamases
Journal Article
PLoS ONE, ISSN 1932-6203, 07/2015, Volume 10, Issue 7, p. e0132221
Abnormal alteration of bone morphogenetic protein (BMP) signaling is implicated in many types of diseases including cancer and heterotopic ossifications.... 
FREE-ENERGY CALCULATIONS | POLYPOSIS SYNDROME | POTENT | SPECIFICITY | MULTIDISCIPLINARY SCIENCES | DYNAMICS | KINASE INHIBITOR | CHARMM | BINDING FREE-ENERGIES | DISCOVERY | FIBRODYSPLASIA OSSIFICANS PROGRESSIVA | Activin Receptors, Type I - antagonists & inhibitors | Receptor, Transforming Growth Factor-beta Type I | Receptors, Transforming Growth Factor beta - chemistry | Humans | Substrate Specificity | Crystallography, X-Ray | Pyrimidines - chemistry | Quinolines - pharmacology | Vascular Endothelial Growth Factor Receptor-2 - antagonists & inhibitors | Protein Kinase Inhibitors - chemistry | Pyrazoles - chemistry | Adenosine Triphosphate - metabolism | Drug Design | Protein-Serine-Threonine Kinases - antagonists & inhibitors | Molecular Structure | Binding Sites - drug effects | Pyrazoles - pharmacology | Bone Morphogenetic Protein Receptors, Type I - antagonists & inhibitors | Protein Structure, Tertiary | Quinolines - chemistry | Pyrimidines - pharmacology | Activin Receptors, Type I - genetics | Molecular Dynamics Simulation | Amino Acid Motifs | Point Mutation | Vascular Endothelial Growth Factor Receptor-2 - chemistry | Bone Morphogenetic Protein Receptors, Type I - chemistry | Receptors, Transforming Growth Factor beta - antagonists & inhibitors | Ligands | Protein Conformation | Molecular Docking Simulation | Protein Kinase Inhibitors - pharmacology | Protein-Serine-Threonine Kinases - chemistry | Activin Receptors, Type I - chemistry | Amino Acid Substitution | Vascular endothelial growth factor | Phosphotransferases | Growth factors | Analysis | Health sciences | Molecular dynamics | Selectivity | Kinases | Proteins | Receptors | Energy | Bone morphogenetic proteins | Docking | Protein-tyrosine kinase | Pharmaceutical sciences | Quantitative analysis | Tyrosine | Computer simulation | Test procedures | Pharmacology | Free energy | Diseases | Signaling | Inhibitors | Computation | Pharmacy | Computer applications | Determinants | Bone | Aberration | Binding sites | Cancer
Journal Article
PLoS ONE, ISSN 1932-6203, 2011, Volume 6, Issue 2, p. e14712
Background: The probiotic Escherichia coli strain Nissle 1917 (EcN) has been shown to interfere in a human in vitro model with the invasion of several... 
INVASION GENES | IN-VITRO | DIARRHEA | NONPATHOGENIC ESCHERICHIA-COLI | ENTERICA SEROVAR TYPHIMURIUM | GROWTH | BIOLOGY | INFECTION | PPGPP | STRAIN NISSLE-1917 | EXPRESSION | Intestinal Mucosa - metabolism | Epithelial Cells - metabolism | Species Specificity | Salmonella typhimurium - growth & development | Swine - physiology | Bacterial Adhesion - physiology | Escherichia coli Infections - veterinary | Escherichia coli - growth & development | Escherichia coli - physiology | Salmonella typhimurium - physiology | Salmonella typhimurium - genetics | Cells, Cultured | Escherichia coli Infections - microbiology | Swine Diseases - pathology | Epithelial Cells - pathology | Intestinal Mucosa - microbiology | Salmonella Infections, Animal - complications | Animals | Epithelial Cells - microbiology | Salmonella Infections, Animal - microbiology | Antibiosis - physiology | Swine - microbiology | Swine Diseases - microbiology | Gene Expression Regulation, Bacterial | Escherichia coli Infections - complications | Intestinal Mucosa - pathology | Infection | Salmonella | Analysis | Genetic aspects | Research | Virulence (Microbiology) | Health aspects | Pathogens | Cell culture | Environmental regulations | Growth rate | Epithelial cells | Gene regulation | Genes | Virulence | Infections | Gene expression | Adhesion | Mutants | Probiotics | Molecular modelling | Pili | E coli | Intestine | Bacteria | Intracellular
Journal Article
Medicare and Medicaid Research Review, ISSN 2159-0354, 2013, Volume 3, Issue 2, pp. E1 - E12
Journal Article
Journal of Molecular Biology, ISSN 0022-2836, 2007, Volume 366, Issue 1, pp. 316 - 329
Metallo-β-lactamases (MBLs) efficiently hydrolyze and thereby inactivate various β-lactam antibiotics in clinical use. Their potential to evolve into more... 
zinc β-lactamase | molecular dynamics | metallo-β-lactamase | substrate specificity | catalytic efficiency
Journal Article
Antimicrobial Agents & Chemotherapy, ISSN 0066-4804, 07/2012, Volume 56, Issue 7, pp. 3481 - 3491
Metallo- beta -lactamases (MBLs) are enzymes that hydrolyze beta -lactam antibiotics, resulting in bacterial resistance to these drugs. These proteins have... 
Bushes | Enzymes | beta -Lactamase | Databases | Nomenclature | Inosine monophosphate | Mbl protein | Mutation | Drug resistance | Metallo- beta -lactamase | beta -Lactam antibiotics
Journal Article
Protein Science, ISSN 0961-8368, 10/2014, Volume 23, Issue 10, pp. 1451 - 1460
Journal Article
Journal of Molecular Biology, ISSN 0022-2836, 2005, Volume 350, Issue 3, pp. 395 - 401
Metallo-β-lactamases challenge antimicrobial therapies by their ability to hydrolyze and inactivate a broad spectrum of β-lactam antibiotics. The potential of... 
zinc β-lactamase | metallo-β-lactamase | protein design | substrate specificity | catalytic efficiency | Metallo-β-lactamase | Catalytic efficiency | Zinc β-lactamase | Protein design | Substrate specificity
Journal Article
Protein Science, ISSN 0961-8368, 10/2014, Volume 23, Issue 10, p. 1451
In Gram-negative bacteria, resistance to [beta]-lactam antibacterials is largely due to [beta]-lactamases and is a growing public health threat. One of the... 
Enzymes | Bacteriology | Beta
Journal Article
Journal of Chemical Information and Modeling, ISSN 1549-9596, 09/2018, Volume 58, Issue 9, pp. 1902 - 1914
Journal Article