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1. Full Text Small-Molecule structure correctors target abnormal protein structure and function: Structure corrector rescue of apolipoprotein E4-associated neuropathology
by Mahley, Robert W and Huang, Yadong
Journal of Medicinal Chemistry, ISSN 0022-2623, 11/2012, Volume 55, Issue 21, pp. 8997 - 9008
An attractive strategy to treat proteinopathies (diseases caused by malformed or misfolded proteins) is to restore protein function by inducing proper... 
INCREASED TAU PHOSPHORYLATION | IN-VITRO | CHEMISTRY, MEDICINAL | E4 DOMAIN INTERACTION | TRAUMATIC BRAIN-INJURY | APOE GENOTYPE | ALZHEIMERS-DISEASE | MUTANT P53 | PHARMACOLOGICAL CHAPERONE | E EPSILON 4 | PARKINSONS-DISEASE | Proteostasis Deficiencies - metabolism | Apolipoprotein E4 - genetics | Apolipoprotein E4 - metabolism | Humans | Alzheimer Disease - drug therapy | Endoplasmic Reticulum - metabolism | Models, Molecular | Lipid Metabolism | Structure-Activity Relationship | Brain Injuries - metabolism | Molecular Targeted Therapy | Protein Transport | Animals | Protein Folding - drug effects | Alzheimer Disease - metabolism | Golgi Apparatus - metabolism | Protein Conformation | Neurons - metabolism | Proteostasis Deficiencies - drug therapy | Apolipoprotein E4 - chemistry | Index Medicus | cholesterol transport | lysosomal storage diseases | neurotoxicity | Alzheimer’s disease | neurotoxic fragments | cystic fibrosis | apoE | ER stress | mitochondrial dysfunction | proteinopathies | p53
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2. Full Text Crystal Structure of a Complex between the Catalytic and Regulatory (RIα) Subunits of PKA
by Choel Kim and Nguyen-Huu Xuong and Susan S. Taylor
Science, ISSN 0036-8075, 2/2005, Volume 307, Issue 5710, pp. 690 - 696
The 2.0-angstrom structure of the cyclic adenosine monophosphate (cAMP)-dependent protein kinase (PKA) catalytic subunit bound to a deletion mutant of a... 
Phosphates | Proteins | Solvents | Docks | Phosphorylation | Active sites | Drug regulation | Biochemistry | Research Articles | Binding sites | Crystal structure | PHOSPHORYLASE-KINASE | AMIDE H/H-2 EXCHANGE | MECHANISM | CAMP-BINDING DOMAINS | MULTIDISCIPLINARY SCIENCES | RESOLUTION | SITES | DEPENDENT PROTEIN-KINASE | MONOPHOSPHATE | CLASSIFICATION | MOLECULAR-BASIS | Cyclic AMP-Dependent Protein Kinases - metabolism | Protein Structure, Tertiary | Catalytic Domain | Protein Structure, Secondary | Crystallization | Cyclic AMP-Dependent Protein Kinases - chemistry | Models, Molecular | Tryptophan - chemistry | Crystallography, X-Ray | Hydrogen Bonding | Cyclic AMP-Dependent Protein Kinase RIalpha Subunit | Protein Structure, Quaternary | Hydrophobic and Hydrophilic Interactions | Protein Binding | Protein Conformation | Cyclic AMP-Dependent Protein Kinases - antagonists & inhibitors | Enzyme Activation | Binding Sites | Cyclic AMP - metabolism | Tyrosine - chemistry | Research | Structure | Cells | Crystals | Enzymes | Mutation | Catalysts
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3. Full Text Metallo‐β‐lactamase structure and function
by Palzkill, Timothy
Annals of the New York Academy of Sciences, ISSN 0077-8923, 01/2013, Volume 1277, Issue 1, pp. 91 - 104
β‐Lactam antibiotics are the most commonly used antibacterial agents and growing resistance to these drugs is a concern. Metallo‐β‐lactamases are a diverse set... 
carbapenem | antibiotic resistance | β‐lactamase | zinc metallo‐enzyme | Carbapenem | Zinc metallo-enzyme | β-lactamase | Antibiotic resistance | ACTIVE-SITE | zinc metallo-enzyme | CRYSTAL-STRUCTURE | ANTIBIOTIC-RESISTANCE | SITE-DIRECTED MUTAGENESIS | BACTEROIDES-FRAGILIS | PSEUDOMONAS-AERUGINOSA | PENICILLIN-BINDING PROTEINS | PHARMACOLOGY & PHARMACY | beta-lactamase | BACILLUS-CEREUS | STANDARD NUMBERING SCHEME | BACTERIAL-CELL WALL | beta-Lactamases - chemistry | Catalytic Domain | beta-Lactamases - classification | Mutagenesis | Metalloendopeptidases - chemistry | Protein Binding | Substrate Specificity | Metalloendopeptidases - metabolism | Catalysis | Metalloendopeptidases - classification | beta-Lactamases - metabolism | Drugs | Enzymes | Inhibitors | Genes | Blocking | Bacteria | Antiinfectives and antibacterials | Zinc
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4. Full Text Crystal structures of murine angiogenin‐2 and ‐3 – probing ‘structure – function’ relationships amongst angiogenin homologues
by Iyer, Shalini and Holloway, Daniel E and Acharya, K. Ravi
The FEBS Journal, ISSN 1742-464X, 01/2013, Volume 280, Issue 1, pp. 302 - 318
Angiogenin (Ang) is a potent inducer of neovascularization. Point mutations in human Ang have been linked to cancer progression and two neurodegenerative... 
crystal structure | angiogenin | enzyme mechanism | metal‐ion binding | ribonuclease A | metal-ion binding | PROTEIN | VARIANTS | RECOGNITION | ACTIVE-SITE | BIOCHEMISTRY & MOLECULAR BIOLOGY | TUMOR | IDENTIFICATION | REFINEMENT | TARGETING SIGNAL | PLACENTAL RIBONUCLEASE INHIBITOR | BINDING | Amino Acid Sequence | Catalytic Domain | Protein Structure, Secondary | Ribonucleases - chemistry | Humans | Models, Molecular | Molecular Sequence Data | Crystallography, X-Ray | RNA Cleavage | Nuclear Localization Signals | Ribonuclease, Pancreatic - chemistry | Zinc - chemistry | Hydrogen Bonding | Sulfates - chemistry | Protein Binding | Protein Interaction Domains and Motifs | Structural Homology, Protein | RNA, Transfer - chemistry | Nervous system diseases | Parkinson's disease | Crystals | Development and progression | Ribonuclease | Sulfates | Structure | Investigations | Mutagenesis | Neurodegeneration | Crystal structure | Cancer | Original
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5. Full Text Lignin Biosynthesis and Structure
by Ruben Vanholme and Brecht Demedts and Kris Morreel and John Ralph and Wout Boerjan and Great Lakes Bioenergy Research Center (GLBRC)
Plant Physiology, ISSN 0032-0889, 7/2010, Volume 153, Issue 3, pp. 895 - 905
Lignin | Transcription factors | Cell walls | Genes | Biosynthesis | Update on Lignin Biosynthesis and Structure | Plants | Polymers | Monomers | Alcohols | Plant cells | DOMAIN TRANSCRIPTION FACTOR | ARABIDOPSIS-THALIANA | SECONDARY METABOLISM | O-METHYLTRANSFERASE ACTIVITY | CINNAMYL-ALCOHOL-DEHYDROGENASE | PHENYLPROPANOID METABOLISM | CELL-WALL FORMATION | DOWN-REGULATION | FERULATE 5-HYDROXYLASE | CAD-DEFICIENT | PLANT SCIENCES | Lignin - chemistry | Lignin - biosynthesis | Biological Transport | Metabolic Networks and Pathways | Gene Expression Regulation, Plant | Evolution, Molecular | Research | Properties | Phytochemistry
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6. Full Text Spliceosome structure and function
by Will, Cindy L and Lührmann, Reinhard
Cold Spring Harbor Perspectives in Biology, ISSN 1943-0264, 07/2011, Volume 3, Issue 7, pp. 1 - 2
Pre-mRNA splicing is catalyzed by the spliceosome, a multimegadalton ribonucleoprotein (RNP) complex comprised of five snRNPs and numerous proteins. Intricate... 
GROUP-II INTRON | SMALL NUCLEAR-RNA | CRYSTAL-STRUCTURE | DEXD/H-BOX ATPASE | ELECTRON-MICROSCOPY | SPLICING SIGNAL INTERACTIONS | TRI-SNRNP | U2 SNRNA | CATALYTIC STEPS | PRE-MESSENGER-RNA | CELL BIOLOGY | Protein Structure, Tertiary | Spliceosomes - chemistry | Catalytic Domain | Humans | Spliceosomes - physiology | Ribonucleoproteins - physiology | Models, Molecular | Crystallography, X-Ray | Spliceosomes - ultrastructure | RNA Splicing - physiology | Ribonucleoproteins, Small Nuclear - physiology | Nuclear Magnetic Resonance, Biomolecular | RNA Precursors - metabolism | Models, Genetic | Protein Processing, Post-Translational | Ribonucleoproteins, Small Nuclear - chemistry | Ribonucleoproteins - chemistry | Nucleic Acid Conformation | Concepts | 052
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7. Full Text Actin Structure and Function
by Dominguez, Roberto and Holmes, Kenneth C
Annual Review of Biophysics, ISSN 1936-122X, 6/2011, Volume 40, Issue 1, pp. 169 - 186
Actin is the most abundant protein in most eukaryotic cells. It is highly conserved and participates in more protein-protein interactions than any known... 
X-ray crystallography | electron microscopy | fiber diffraction | actin-binding-proteins | F-ACTIN | FILAMENT ELONGATION | I COMPLEX | CRYSTAL-STRUCTURE | ARP2/3 COMPLEX | DYNAMIC INSTABILITY | ELECTRON CRYOMICROSCOPY | BIOPHYSICS | BINDING PROTEINS | FORMIN HOMOLOGY-2 DOMAIN | WH2 DOMAIN | Models, Chemical | Models, Biological | Computer Simulation | Actins - chemistry | Actins - ultrastructure | Models, Molecular | Protein Binding | Protein Conformation | Structure-Activity Relationship | Actins - physiology | Binding Sites | Physiological aspects | Eukaryotes | Research | Actin | Protein-protein interactions
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8. Full Text A novel β‐xylosidase structure from Geobacillus thermoglucosidasius: the first crystal structure of a glycoside hydrolase family GH52 enzyme reveals unpredicted similarity to other glycoside hydrolase folds
by Espina, Giannina and Eley, Kirstin and Pompidor, Guillaume and Schneider, Thomas R and Crennell, Susan J and Danson, Michael J
Acta Crystallographica Section D, ISSN 1399-0047, 05/2014, Volume 70, Issue 5, pp. 1366 - 1374
Geobacillus thermoglucosidasius is a thermophilic bacterium that is able to ferment both C6 and C5 sugars to produce ethanol. During growth on hemicellulose... 
β‐xylosidase | GH family 52 | Geobacillus thermoglucosidasius | fold conservation | retaining mechanism | thermophile | β-xylosidase | CRYSTALLOGRAPHY | BIOPHYSICS | BIOCHEMISTRY & MOLECULAR BIOLOGY | BIOCHEMICAL RESEARCH METHODS | Catalytic Domain | Disaccharides - metabolism | Escherichia coli - genetics | Xylosidases - metabolism | Cloning, Molecular | Xylosidases - chemistry | Xylosidases - genetics | Models, Molecular | Crystallography, X-Ray | Protein Conformation | Geobacillus - enzymology | Disaccharides - chemistry | Enzymes | Addition polymerization | Similarity | Glycosides | Ethyl alcohol | Biomass | Crystal structure | Recombinant
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9. Full Text Structure of a yeast activated spliceosome at 3.5 Å resolution
by Yan, Chuangye and Wan, Ruixue and Bai, Rui and Huang, Gaoxingyu and Shi, Yigong
Science, ISSN 0036-8075, 08/2016, Volume 353, Issue 6302, pp. 904 - 912
Pre-messenger RNA (pre-mRNA) splicing is carried out by the spliceosome, which undergoes an intricate assembly and activation process. Here, we report an... 
RNA Precursors - chemistry | Spliceosomes - chemistry | Catalytic Domain | Exons | Introns | RNA-Binding Proteins - chemistry | RNA Splicing Factors - chemistry | Saccharomyces cerevisiae - chemistry | Cryoelectron Microscopy | RNA Splicing | RNA, Small Nuclear - chemistry | Ribonucleoprotein, U5 Small Nuclear - chemistry | Saccharomyces cerevisiae Proteins - chemistry | Genetic aspects | Spliceosomes | Brewer's yeast | Methods | RNA splicing | Proteins | Eukaryotes | Yeast | Catalysis | Microscopy | Ribonucleic acid--RNA
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