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1. Full Text Metabolic and evolutionary origin of actin-binding polyketides from diverse organisms
by Ueoka, Reiko and Uria, Agustinus R and Reiter, Silke and Mori, Tetsushi and Karbaum, Petra and Peters, Eike E and Helfrich, Eric J N and Morinaka, Brandon I and Gugger, Muriel and Takeyama, Haruko and Matsunaga, Shigeki and Piel, Jörn
Nature Chemical Biology, ISSN 1552-4450, 09/2015, Volume 11, Issue 9, pp. 705 - 712
Actin-targeting macrolides comprise a large, structurally diverse group of cytotoxins isolated from remarkably dissimilar micro- and macroorganisms. In spite... 
BACTERIAL SYMBIONT | GENE-CLUSTER | CYTOTOXIC MACROLIDES | NATURAL-PRODUCT DISCOVERY | CYANOBACTERIA | BIOCHEMISTRY & MOLECULAR BIOLOGY | SYNTHASES | IN-SITU HYBRIDIZATION | SPONGE THEONELLA-SWINHOEI | IDENTIFICATION | ANTIFUNGAL MACROLIDE | Cyanobacteria - genetics | Deltaproteobacteria - metabolism | Multigene Family | Peptides | Actins - metabolism | Bacterial Proteins - chemistry | Cyanobacteria - metabolism | Molecular Sequence Data | Polyketides - chemistry | Small Molecule Libraries - metabolism | Polyketides - metabolism | Polyketide Synthases - metabolism | Macrolides - chemistry | Pyrans - chemistry | Pyrans - metabolism | Base Sequence | Actins - chemistry | Symbiosis | Gene Expression | Bacterial Proteins - genetics | Macrolides - metabolism | Biological Evolution | Small Molecule Libraries - chemistry | Polyketide Synthases - chemistry | Animals | Deltaproteobacteria - genetics | Theonella - microbiology | Protein Binding | Bacterial Proteins - metabolism | Polyketide Synthases - genetics | Enzymes | Bacteria | Biosynthesis | Metabolism | Polyketide Synthases/metabolism | Actins/metabolism | Macrolides/chemistry | Polyketide Synthases/chemistry | Life Sciences | Cyanobacteria/metabolism | Deltaproteobacteria/genetics | Bacterial Proteins/chemistry | Macrolides/metabolism | Actins/chemistry | Polyketide Synthases/genetics | Deltaproteobacteria/metabolism | Small Molecule Libraries/metabolism | Theonella/microbiology | Cyanobacteria/genetics | Pyrans/metabolism | Small Molecule Libraries/chemistry | Microbiology and Parasitology | Bacterial Proteins/metabolism | Polyketides/chemistry | Polyketides/metabolism | Bacterial Proteins/genetics | Pyrans/chemistry
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2. Full Text Fungal secondary metabolism - from biochemistry to genomics
by Turner, Geoffrey and Bennett, Joan W and Keller, Nancy P
Nature Reviews Microbiology, ISSN 1740-1526, 12/2005, Volume 3, Issue 12, pp. 937 - 947
Much of natural product chemistry concerns a group of compounds known as secondary metabolites. These low-molecular-weight metabolites often have potent... 
ASPERGILLUS-PARASITICUS DEFICIENT | BIOSYNTHETIC GENE-CLUSTER | AFLATOXIN BIOSYNTHESIS | MICROBIOLOGY | TRANSCRIPTION FACTOR | REGULATORY GENE | GIBBERELLA-FUJIKUROI | FILAMENTOUS FUNGI | PEPTIDE SYNTHETASE | FUSARIUM-SPOROTRICHIOIDES | PLANT-PATHOGENIC FUNGUS | Aflatoxins - metabolism | Penicillins - biosynthesis | Molecular Weight | Terpenes - metabolism | Genome, Fungal | Ergot Alkaloids - metabolism | Epigenesis, Genetic | Genomics | Genes, Fungal | Macrolides - metabolism | Fungi - metabolism
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3. Full Text Structural basis for the interaction of antibiotics with the peptidyl transferase centre in eubacteria
by Harms, Jörg and Schlünzen, Frank and Tocilj, Ante and Bashan, Anat and Albrecht, Renate and Zarivach, Raz and Yonath, Ada and Franceschi, François
Nature, ISSN 0028-0836, 10/2001, Volume 413, Issue 6858, pp. 814 - 821
Ribosomes, the site of protein synthesis, are a major target for natural and synthetic antibiotics. Detailed knowledge of antibiotic binding sites is central... 
ANGSTROM RESOLUTION | CHLORAMPHENICOL | MULTIDISCIPLINARY SCIENCES | 23S RIBOSOMAL-RNA | ESCHERICHIA-COLI | DOMAIN-II | BINDING-SITE | MUTATIONS | CONFORMATION | ERYTHROMYCIN RESISTANCE | SUBUNIT | Bacteria - metabolism | Peptidyl Transferases - metabolism | Models, Molecular | Molecular Sequence Data | Ribosomes - metabolism | Anti-Bacterial Agents - metabolism | Crystallography, X-Ray | Magnesium - metabolism | Structure-Activity Relationship | Macrolides - metabolism | Ribosomal Proteins - metabolism | Base Sequence | Protein Conformation | RNA, Ribosomal, 23S - metabolism | Binding Sites | RNA, Bacterial - metabolism | Chloramphenicol - metabolism | Proteins | Bacteria | Antibiotics | Peptides
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4. Full Text H₂S: A Universal Defense Against Antibiotics in Bacteria
by Konstantin Shatalin and Elena Shatalina and Alexander Mironov and Evgeny Nudler
Science, ISSN 0036-8075, 11/2011, Volume 334, Issue 6058, pp. 986 - 990
Many prokaryotic species generate hydrogen sulfide (H₂S) in their natural environments. However, the biochemistry and physiological role of this gas in... 
Enzymes | Cell growth | Antibiotics | Cell walls | Protein synthesis | Macrolides | DNA | REPORTS | Bacteria | Lactams | Oxides | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | NITRIC-OXIDE | HYDROGEN-PEROXIDE | DEATH | IRON | DAMAGE | SULFIDE | Hydrogen Sulfide - metabolism | Cystathionine beta-Synthase - antagonists & inhibitors | Oxidative Stress | Antioxidants - metabolism | Escherichia coli - drug effects | Pseudomonas aeruginosa - growth & development | Bacteria - drug effects | Drug Resistance, Bacterial | Molecular Sequence Data | Cystathionine gamma-Lyase - metabolism | DNA Breaks, Double-Stranded | Bacteria - growth & development | Pseudomonas aeruginosa - metabolism | Drug Resistance, Multiple, Bacterial | Escherichia coli - metabolism | Bacillus anthracis - growth & development | Bacillus anthracis - drug effects | Cystathionine gamma-Lyase - genetics | Escherichia coli - growth & development | Cystathionine beta-Synthase - genetics | Bacillus anthracis - metabolism | Staphylococcus aureus - metabolism | Amino Acid Sequence | Bacteria - metabolism | Hydrogen Sulfide - pharmacology | Sulfurtransferases - genetics | Cystathionine beta-Synthase - metabolism | Pseudomonas aeruginosa - drug effects | Cystathionine gamma-Lyase - antagonists & inhibitors | Sulfurtransferases - antagonists & inhibitors | Anti-Bacterial Agents - pharmacology | Nitric Oxide - metabolism | Staphylococcus aureus - drug effects | Staphylococcus aureus - growth & development | Sulfurtransferases - metabolism | Gases | E coli | Prokaryotes
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5. Full Text Autophagy‐based unconventional secretory pathway for extracellular delivery of IL‐1β
by Dupont, Nicolas and Jiang, Shanya and Pilli, Manohar and Ornatowski, Wojciech and Bhattacharya, Dhruva and Deretic, Vojo
The EMBO Journal, ISSN 0261-4189, 11/2011, Volume 30, Issue 23, pp. 4701 - 4711
Autophagy controls the quality and quantity of the eukaryotic cytoplasm while performing two evolutionarily highly conserved functions: cell‐autonomous... 
IL‐1 | autophagy | HMGB1 | unconventional secretion | inflammasome | Unconventional secretion | Inflammasome | IL-1 | Autophagy | IMMUNITY | ACTIVATION | ACID | PHOSPHORYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | NALP3 INFLAMMASOME | CELL-DEATH | CELL BIOLOGY | INSULIN | GRASP PROTEIN | CONTRIBUTES | rab GTP-Binding Proteins - metabolism | Inflammasomes - metabolism | Microtubule-Associated Proteins - metabolism | Cells, Cultured | Autophagy - physiology | Protein Transport - drug effects | Autophagy - drug effects | Macrophages - metabolism | Secretory Pathway - drug effects | Secretory Pathway - physiology | Animals | Carrier Proteins - metabolism | Autophagy-Related Protein 5 | Protein Processing, Post-Translational - drug effects | Interleukin-1beta - metabolism | HMGB1 Protein - metabolism | Macrolides - pharmacology | Membrane Proteins - metabolism | Mice | Nigericin - pharmacology | Interleukin-18 - metabolism | Luminescent Proteins - metabolism
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6. Full Text Azithromycin distinctively modulates classical activation of human monocytes in vitro
by Vrančić, M and Banjanac, M and Nujić, K and Bosnar, M and Murati, T and Munić, V and Stupin Polančec, D and Belamarić, D and Parnham, MJ and Eraković Haber, V
British Journal of Pharmacology, ISSN 0007-1188, 03/2012, Volume 165, Issue 5, pp. 1348 - 1360
BACKGROUND AND PURPOSE Azithromycin has been reported to modify activation of macrophages towards the M2 phenotype. Here, we have sought to identify the... 
dexamethasone | roflumilast | human macrophage | lysosome affecting agent | classical activation | azithromycin | human monocyte | SB203580 | anti‐inflammatory drug | TLR4 signalling | anti-inflammatory drug | IMMUNOMODULATORY MEDICATIONS | DENDRITIC CELLS | J774 MACROPHAGES | TUMOR-NECROSIS-FACTOR | TOLL-LIKE RECEPTORS | LIPOPOLYSACCHARIDE | STIMULATED MACROPHAGES | PHARMACOLOGY & PHARMACY | MACROLIDE ANTIBIOTICS | NF-KAPPA-B | EXPRESSION | Tumor Necrosis Factor-alpha - metabolism | Gene Expression - drug effects | Humans | Lysosomes - genetics | Tumor Necrosis Factor-alpha - genetics | Monocytes - metabolism | NF-kappa B - metabolism | Chemokine CCL22 - metabolism | Antigens, CD - genetics | Antigens, CD - metabolism | STAT1 Transcription Factor - metabolism | Lysosomes - metabolism | Interleukin-10 - metabolism | Chemokine CCL2 - metabolism | Interleukin-6 - metabolism | Lysosomes - drug effects | Interleukin-6 - genetics | Anti-Inflammatory Agents - pharmacology | Cells, Cultured | Receptors, Cell Surface - metabolism | Toll-Like Receptor 4 - genetics | Chemokine CCL2 - genetics | Transcription Factors - genetics | Down-Regulation - drug effects | STAT1 Transcription Factor - genetics | Toll-Like Receptor 4 - metabolism | Antigens, Differentiation, Myelomonocytic - genetics | Azithromycin - pharmacology | Monocytes - drug effects | Transcription Factors - metabolism | Chemokine CCL22 - genetics | Macrophages - metabolism | NF-kappa B - genetics | Signal Transduction - drug effects | Antigens, Differentiation, Myelomonocytic - metabolism | Interleukin-10 - genetics | Chemokines, CC - genetics | Lipopolysaccharides - pharmacology | Macrophages - drug effects | Macrophage Activation - drug effects | Interferon-gamma - pharmacology | Chemokines, CC - metabolism | Receptors, Cell Surface - genetics | Research Papers
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7. Full Text Glia re‐sealed particles freshly prepared from adult rat brain are competent for exocytotic release of glutamate
by Stigliani, Sara and Zappettini, Simona and Raiteri, Luca and Passalacqua, Mario and Melloni, Edon and Venturi, Consuelo and Tacchetti, Carlo and Diaspro, Alberto and Usai, Cesare and Bonanno, Giambattista
Journal of Neurochemistry, ISSN 0022-3042, 02/2006, Volume 96, Issue 3, pp. 656 - 668
Glial subcellular re‐sealed particles (referred to as gliosomes here) were purified from rat cerebral cortex and investigated for their ability to release... 
exocytosis | gliosomes | glutamate release | SNARE proteins | Glutamate release | Exocytosis | Gliosomes | NEURONAL-ACTIVITY | SYNAPTIC VESICLES | HIPPOCAMPAL ASTROCYTES | BIOCHEMISTRY & MOLECULAR BIOLOGY | PLASMALEMMAL VESICLES | SYNAPTOSOMES | CALCIUM WAVES | NEUROSCIENCES | AMINO-ACIDS | CULTURED ASTROCYTES | H+-ATPASE | IN-SITU | Disks Large Homolog 4 Protein | L-Lactate Dehydrogenase - metabolism | Propionates - metabolism | Neuroglia - ultrastructure | Microscopy, Electron, Transmission - methods | Microtubule-Associated Proteins - metabolism | Vesicular Transport Proteins - metabolism | Male | Intracellular Signaling Peptides and Proteins - metabolism | Synaptosomes - metabolism | Glial Fibrillary Acidic Protein - metabolism | Cerebral Cortex - cytology | Exocytosis - physiology | Dose-Response Relationship, Drug | Tubulin - metabolism | Tritium - metabolism | Time Factors | Macrolides - pharmacology | Membrane Proteins - metabolism | Ionophores - pharmacology | Calcium - pharmacology | Myelin Basic Protein - metabolism | Vesicular Glutamate Transport Protein 1 - metabolism | Fluorescent Antibody Technique - methods | Cells, Cultured | Enzyme Inhibitors - pharmacology | Rats | S100 Proteins - metabolism | D-Aspartic Acid - metabolism | Microscopy, Confocal - methods | Rats, Sprague-Dawley | Synaptosomes - ultrastructure | Animals | Ionomycin - pharmacology | Neuroglia - metabolism | Glutamic Acid - metabolism | Synaptosomal-Associated Protein 25 - metabolism | CD11b Antigen - metabolism | Vesicle-Associated Membrane Protein 2 - metabolism | Proteins | Brain | Amino acids | Neurotransmitters | Neurons | Rodents
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8. Full Text PKC regulates a farnesyl-electrostatic switch on K-Ras that promotes its association with Bcl-XL on mitochondria and induces apoptosis
by Bivona, Trever G and Quatela, Steven E and Bodemann, Brian O and Ahearn, Ian M and Soskis, Michael J and Mor, Adam and Miura, John and Wiener, Heidi H and Wright, Latasha and Saba, Shahryar G and Yim, Duke and Fein, Adam and Pérez De Castro, Ignacio and Li, Chi and Thompson, Craig B and Cox, Adrienne D and Philips, Mark R
Molecular Cell, ISSN 1097-2765, 02/2006, Volume 21, Issue 4, pp. 481 - 493
K-Ras associates with the plasma membrane (PM) through farnesylation that functions in conjunction with an adjacent polybasic sequence. We show that... 
LOCALIZATION | PROTEIN-KINASE-C | CYCLIC-AMP | CAAX MOTIF | H-RAS | BIOCHEMISTRY & MOLECULAR BIOLOGY | RHO GTPASES | TUMOR-SUPPRESSOR | ENDOPLASMIC-RETICULUM | GOLGI | PLASMA-MEMBRANE | CELL BIOLOGY | Neoplasms - metabolism | T-Lymphocytes - physiology | Bryostatins | Myristoylated Alanine-Rich C Kinase Substrate | Humans | Molecular Sequence Data | Intracellular Signaling Peptides and Proteins - metabolism | Mitochondria - ultrastructure | Recombinant Fusion Proteins - metabolism | Antineoplastic Agents - metabolism | Protein Isoforms - metabolism | Protein Isoforms - chemistry | Protein Kinase C - metabolism | Cell Membrane - metabolism | Membrane Proteins - metabolism | Amino Acid Sequence | Cell Line | Mitochondria - metabolism | Macrolides - metabolism | Static Electricity | Serine - metabolism | Animals | Mice, Nude | Recombinant Fusion Proteins - genetics | Signal Transduction - physiology | Mice | Apoptosis - physiology | Genes, ras | Neoplasms - pathology | bcl-X Protein - metabolism | Intracellular Membranes - metabolism | Protein Isoforms - genetics | Proteins | Medical colleges | Mitochondrial DNA | Protein kinases | Apoptosis
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9. Full Text Structures of the Escherichia coli ribosome with antibiotics bound near the peptidyl transferase center explain spectra of drug action
by Jack A. Dunkle and Liqun Xiong and Alexander S. Mankin and Jamie H. D. Cate
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 10/2010, Volume 107, Issue 40, pp. 17152 - 17157
Differences between the structures of bacterial, archaeal, and eukaryotic ribosomes account for the selective action of antibiotics. Even minor variations in... 
Ketolides | Antibiotics | Macrolides | Drug interactions | Ribosomes | Bacteria | Nucleotides | Electron density | Genetic mutation | Binding sites | Ribosome structure | Chloramphenicol | Telithromycin | Erythromycin | Clindamycin | PROTEIN | BACTERIAL RIBOSOME | RNA GENE | MULTIDISCIPLINARY SCIENCES | telithromycin | RESISTANCE MUTATIONS | CONFERRING RESISTANCE | erythromycin | DOMAIN-II | BINDING-SITE | chloramphenicol | MACROLIDE ANTIBIOTICS | ribosome structure | clindamycin | PLEUROMUTILINS | Haloarcula marismortui - genetics | Haloarcula marismortui - metabolism | Chloramphenicol - chemistry | Erythromycin - metabolism | Molecular Sequence Data | Ribosomes - metabolism | Deinococcus - metabolism | Deinococcus - genetics | Haloarcula marismortui - chemistry | X-Ray Diffraction | Anti-Bacterial Agents - chemistry | Base Sequence | Escherichia coli - metabolism | Ketolides - metabolism | Deinococcus - chemistry | Molecular Structure | Clindamycin - chemistry | Peptidyl Transferases - metabolism | Clindamycin - metabolism | Peptidyl Transferases - chemistry | Ribosomes - chemistry | Anti-Bacterial Agents - metabolism | Escherichia coli - chemistry | RNA, Ribosomal, 23S - chemistry | Erythromycin - chemistry | Escherichia coli - genetics | Ketolides - chemistry | RNA, Ribosomal, 23S - metabolism | Chloramphenicol - metabolism | Escherichia coli | Crystals | Genetic aspects | Research | Properties | Structure | Observations | Peptidyl transferases | Drugs | lincosamides | Pathogens | rRNA | rRNA 23S | Data processing | Ribosomal subunits | Ionizing radiation | Peptidyltransferase | Crystal structure | Tunnels | Biological Sciences
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10. Full Text p62/SQSTM1 and ALFY interact to facilitate the formation of p62 bodies/ALIS and their degradation by autophagy
by Clausen, Terje Høyvarde and Lamark, Trond and Isakson, Pauline and Finley, Kim D and Larsen, Kenneth Bowitz and Brech, Andreas and Øvervatn, Aud and Stenmark, Harald and Bjørkøy, Geir and Simonsen, Anne and Johansen, Terje
Autophagy, ISSN 1554-8627, 04/2010, Volume 6, Issue 3, pp. 330 - 344
Accumulation of ubiquitinated proteins in cytoplasmic and/or nuclear inclusions is a hallmark of several diseases associated with premature cell death.... 
Binding | Proteins | Landes | Calcium | Bioscience | Biology | Cell | Cycle | Cancer | Organogenesis | ALFY | Autophagy | LC3 | p62 | Protein aggregates | SYSTEM | STORAGE | APOPTOSIS | PROTEIN-KINASE-C | DOMAIN | autophagy | UBIQUITIN | protein aggregates | SELECTIVE AUTOPHAGY | DROSOPHILA | CELL BIOLOGY | PROTEASOME | AGGREGATION | RNA, Small Interfering - genetics | Sequestosome-1 Protein | Humans | Autophagy - physiology | Drosophila Proteins - metabolism | Drosophila melanogaster - genetics | Recombinant Fusion Proteins - metabolism | Drosophila melanogaster - metabolism | Multiprotein Complexes - metabolism | Membrane Proteins - metabolism | Drosophila melanogaster - anatomy & histology | Inclusion Bodies - metabolism | Ubiquitinated Proteins - metabolism | Enzyme Inhibitors - metabolism | Membrane Proteins - genetics | Macrolides - metabolism | Transcription Factors - genetics | Protein Folding | Transcription Factors - metabolism | Animals | Adaptor Proteins, Signal Transducing - genetics | Recombinant Fusion Proteins - genetics | Drosophila Proteins - genetics | HeLa Cells | Adaptor Proteins, Signal Transducing - metabolism | RNA, Small Interfering - metabolism
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11. Full Text The natural product carolacton inhibits folate-dependent C1 metabolism by targeting FolD/MTHFD
by Fu, Chengzhang and Sikandar, Asfandyar and Donner, Jannik and Zaburannyi, Nestor and Herrmann, Jennifer and Reck, Michael and Wagner-Döbler, Irene and Koehnke, Jesko and Müller, Rolf
Nature Communications, ISSN 2041-1723, 12/2017, Volume 8, Issue 1, pp. 1529 - 9
The natural product carolacton is a macrolide keto-carboxylic acid produced by the myxobacterium Sorangium cellulosum, and was originally described as an... 
SYSTEM | TETRAHYDROFOLATE | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | PURIFICATION | SEQUENCE | CYCLOHYDROLASE | BIFUNCTIONAL ENZYME | METHYLENETETRAHYDROFOLATE DEHYDROGENASE | ONE-CARBON METABOLISM | Humans | Multienzyme Complexes - metabolism | Crystallography, X-Ray | Antineoplastic Agents - therapeutic use | Biological Products - pharmacology | Myxococcales - metabolism | Multifunctional Enzymes - metabolism | Microbial Sensitivity Tests | Inhibitory Concentration 50 | Macrolides - pharmacology | Antineoplastic Agents - pharmacology | Methylenetetrahydrofolate Dehydrogenase (NADP) - metabolism | Biofilms - drug effects | Enzyme Assays | Mitochondria - metabolism | Neoplasms - drug therapy | Formate-Tetrahydrofolate Ligase - metabolism | Minor Histocompatibility Antigens - metabolism | Cell Line, Tumor | Folic Acid - metabolism | Protein Binding | Aminohydrolases - metabolism | Bacterial Proteins - metabolism | Anti-Bacterial Agents - pharmacology | Neoplasms - pathology | Mitochondria | Natural products | Cell lines | Bacteria | Tumor cell lines | Carboxylic acids | Metabolism | Antibacterial materials | Folic acid | Cancer | Crystal structure
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