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1. Full Text Molecular pathways: Fatty acid synthase
by Jones, Suzanne F and Infante, Jeffrey R
Clinical Cancer Research, ISSN 1078-0432, 12/2015, Volume 21, Issue 24, pp. 5434 - 5438
Therapies that target tumor metabolism represent a new horizon in anticancer therapies. In particular, cancer cells are dependent on the generation of lipids,... 
CELL LUNG-CANCER | TARGET | OVEREXPRESSION | INHIBITION | THERAPY | METABOLISM | ONCOLOGY | PROSTATE-CANCER | EXPRESSION | CARCINOMA | CAVEOLIN-1 | Fatty Acid Synthases - antagonists & inhibitors | Neoplasms - metabolism | Animals | Fatty Acid Synthases - metabolism | Signal Transduction - drug effects | Humans | Translational Medical Research | Lipid Metabolism - drug effects | Antineoplastic Agents - pharmacology | Antineoplastic Agents - therapeutic use | Molecular Targeted Therapy | Neoplasms - drug therapy
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2. Full Text Polyketide Synthase Modules Redefined
by Keatinge‐Clay, Adrian T
Angewandte Chemie International Edition, ISSN 1433-7851, 04/2017, Volume 56, Issue 17, pp. 4658 - 4660
Modular redefinition : A long‐standing paradigm in modular polyketide synthase enzymology, namely the definition of a module, has been challenged by Abe and... 
assembly lines | evolution-guided engineering | polyketides | enzymology | modules | ACYL CARRIER PROTEIN | SUBSTRATE-SPECIFICITY | BIOSYNTHESIS | DOCKING DOMAINS | CHEMISTRY, MULTIDISCIPLINARY | KETOSYNTHASE DOMAINS | Bacteria - metabolism | Bacteria - chemistry | Biocatalysis | Fatty Acid Synthases - metabolism | Acyl Carrier Protein - metabolism | Humans | Computational Biology | Substrate Specificity | Acyltransferases - metabolism | Bacteria - genetics | Polyketides - metabolism | Polyketide Synthases - chemistry | Polyketide Synthases - metabolism | Animals | Protein Engineering | Protein Domains | Bacteria - enzymology | Polyketide Synthases - genetics | Evolution, Molecular | Assembly lines | Polyketide synthase | Enzymology | Workers
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3. Full Text Structure of a modular polyketide synthase
by Dutta, Somnath and Whicher, Jonathan R and Hansen, Douglas A and Hale, Wendi A and Chemler, Joseph A and Congdon, Grady R and Narayan, Alison R. H and Håkansson, Kristina and Sherman, David H and Smith, Janet L and Skiniotis, Georgios
Nature, ISSN 0028-0836, 2014, Volume 510, Issue 7506, pp. 512 - 517
Polyketide natural products constitute a broad class of compounds with diverse structural features and biological activities. Their biosynthetic machinery,... 
ACYL CARRIER PROTEIN | SUBSTRATE-SPECIFICITY | 6-DEOXYERYTHRONOLIDE B SYNTHASE | PARTICLE ELECTRON CRYOMICROSCOPY | NEAR-ATOMIC-RESOLUTION | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | DOCKING DOMAINS | ITERATIVE CHAIN ELONGATION | FATTY-ACID SYNTHASE | CRYO-EM STRUCTURE | Cryoelectron Microscopy | Catalytic Domain | Polyketide Synthases - chemistry | Polyketide Synthases - metabolism | Biocatalysis | Polyketide Synthases - ultrastructure | Models, Molecular | Streptomyces - enzymology | Macrolides - metabolism | Fatty Acid Synthases - chemistry | Proteins | Physiological aspects | Polyketides | Structure | Observations | Enzymes | Fourier transforms | Polypeptides | Microscopy | Chemical bonds | Carbon | Crystal structure | Index Medicus
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4. Full Text Structure–function relationship in the CYP74 family: Conversion of divinyl ether synthases into allene oxide synthases by site-directed mutagenesis
by Toporkova, Yana Y and Ermilova, Valeria S and Gorina, Svetlana S and Mukhtarova, Lucia S and Osipova, Elena V and Gogolev, Yuri V and Grechkin, Alexander N
FEBS Letters, ISSN 0014-5793, 08/2013, Volume 587, Issue 16, pp. 2552 - 2558
Non-classical P450s of CYP74 family control several enzymatic conversions of fatty acid hydroperoxides to bioactive oxylipins in plants, some invertebrates and... 
CYP74 family | Cytochrome P450 | Site-directed mutagenesis | Divinyl ether synthase | Allene oxide synthase | DES (CYP74B16) | HPL | allene oxide synthase | 9-hydroperoxy-10,12-octadecadienoic acid | NtDES | Nicotiana tabacum | LuDES | 13-HPOT | immobilized metal affinity chromatography | Linum usitatissimum | 9-HPOD | 13-hydroperoxy-9,11,15-octadecatrienoic acid | SRS | hydroperoxide lyase | methyl | 10 | 11 | 12 | IHCD | 13 | 15 | IMAC | divinyl ether synthase | AOS | DES (CYP74D3) | trimethylsilyl | DES | wild type | TMS | substrate recognition site | I-helix central domain | CYTOCHROME-P450 | OXYLIPINS | HYDROPEROXIDE LYASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | LEAVES | FATTY-ACIDS | CELL BIOLOGY | BIOPHYSICS | PATHWAY | BIOSYNTHESIS | ENZYMES | Amino Acid Sequence | Gas Chromatography-Mass Spectrometry | Intramolecular Oxidoreductases - chemistry | Mutagenesis, Site-Directed | Computational Biology | Molecular Sequence Data | Recombinant Proteins - chemistry | Structure-Activity Relationship | Flax - enzymology | Sequence Homology, Amino Acid | Point Mutation | Cytochrome P-450 Enzyme System - chemistry | Plant Proteins - chemistry | Protein Conformation | Tobacco - enzymology | Gene mutations | Enzymes | Index Medicus
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5. Full Text UCP2-induced fatty acid synthase promotes NLRP3 inflammasome activation during sepsis
by Moon, Jong-Seok and Lee, Seonmin and Park, Mi-Ae and Siempos, Ilias I and Haslip, Maria and Lee, Patty J and Yun, Mijin and Kim, Chun K and Howrylak, Judie and Ryter, Stefan W and Nakahira, Kiichi and Choi, Augustine M. K
Journal of Clinical Investigation, ISSN 0021-9738, 02/2015, Volume 125, Issue 2, pp. 665 - 680
Cellular lipid metabolism has been linked to immune responses; however, the precise mechanisms by which de novo fatty acid synthesis can regulate inflammatory... 
MEDICINE, RESEARCH & EXPERIMENTAL | OXIDATIVE STRESS | GLUCOSE-METABOLISM | ATP-CITRATE LYASE | UCP2 | SEPTIC SHOCK | CELL-GROWTH | CRITICALLY-ILL PATIENTS | INTENSIVE INSULIN THERAPY | CANCER | MITOCHONDRIAL UNCOUPLING PROTEINS | Fatty Acid Synthase, Type I - genetics | Fatty Acid Synthase, Type I - biosynthesis | Lipids - genetics | Inflammasomes - metabolism | NLR Family, Pyrin Domain-Containing 3 Protein | Humans | Ion Channels - genetics | Caspase 1 - metabolism | Mitochondrial Proteins - genetics | Interleukin-1beta - genetics | Lipids - biosynthesis | Sepsis - pathology | Interleukin-1beta - metabolism | Mitochondrial Proteins - metabolism | Sepsis - metabolism | Macrophages - pathology | Down-Regulation - genetics | Inflammasomes - genetics | Sepsis - genetics | Mice, Knockout | Carrier Proteins - genetics | Enzyme Induction - genetics | Macrophages - metabolism | Animals | Carrier Proteins - metabolism | Sepsis - chemically induced | Ion Channels - metabolism | Caspase 1 - genetics | Sepsis - therapy | Mice | Uncoupling Protein 2 | Interleukin-18 - genetics | Interleukin-18 - metabolism | Cellular proteins | Immune response | Synthesis | Sepsis | Development and progression | Lipids | Genetic aspects | Properties | Enzymes | Cytokines | Pathogenesis | Mortality | Glucose | Metabolism | Gene expression | Fatty acids | Proteins | Studies | Metabolites | Consent | Rodents
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6. Full Text The mitochondrial H+-ATP synthase and the lipogenic switch
: New core components of metabolic reprogramming in induced pluripotent stem (iPS) cells
by Vazquez-Martin, Alejandro and Corominas-Faja, Bruna and Cufi, Sílvia and Vellon, Luciano and Oliveras-Ferraros, Cristina and Menendez, Octavio J and Joven, Jorge and Lupu, Ruth and Menendez, Javier A
Cell Cycle, ISSN 1538-4101, 01/2013, Volume 12, Issue 2, pp. 207 - 218
Induced pluripotent stem (iPS) cells share some basic properties, such as self-renewal and pluripotency, with cancer cells, and they also appear to share... 
mitochondria | glycolysis | H | lipogenesis | + | SSEA1 | iPS cells | ATP synthase | acetyl CoA carboxylase | bioenergetics | IF1 | fatty acid synthase | Warburg effect | Mitochondria | Bioenergetics | Glycolysis | IPS cells | Fatty acid synthase | Acetyl CoA carboxylase | Lipogenesis | SOMATIC-CELLS | H+-ATP synthase | ACETYL-COA CARBOXYLASE | COENZYME-A | TUMORIGENICITY | CELL BIOLOGY | BREAST-CANCER CELLS | INHIBITION | SORAPHEN | FATTY-ACID SYNTHASE | ENERGY-METABOLISM | LIPID DROPLETS | Gene Expression Regulation, Enzymologic - drug effects | Cell Dedifferentiation - physiology | Fatty Acid Synthases - metabolism | Metformin - pharmacology | Mitochondria - drug effects | Cell Transformation, Neoplastic - metabolism | Proton-Translocating ATPases - metabolism | Animals | Proteins - metabolism | Fibroblasts | Metabolic Networks and Pathways - physiology | Mice | Lipogenesis - physiology | Acetyl-CoA Carboxylase - metabolism | Induced Pluripotent Stem Cells - metabolism | Extra Views
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7. Full Text Mycocerosic acid synthase exemplifies the architecture of reducing polyketide synthases
by Herbst, Dominik A and Jakob, Roman P and Zähringer, Franziska and Maier, Timm
Nature, ISSN 0028-0836, 03/2016, Volume 531, Issue 7595, pp. 533 - 537
Polyketide synthases (PKSs) are biosynthetic factories that produce natural products with important biological and pharmacological activities(1-3). Their... 
SWISS-MODEL | ORGANIZATION | ITERATION | PROTEIN INTERACTIONS | MODULE | DOMAIN | CRYSTAL-STRUCTURE | BIOSYNTHESIS | MULTIDISCIPLINARY SCIENCES | FLEXIBILITY | SOFTWARE | Protein Structure, Tertiary | Polyketide Synthases - chemistry | Polyketide Synthases - metabolism | Fatty Acid Synthases - metabolism | Oxidation-Reduction | Models, Molecular | Crystallography, X-Ray | Acyltransferases - chemistry | Acyltransferases - metabolism | Mycobacterium smegmatis - enzymology | Virulence Factors | Enzymes | Polyketides | Chemical properties | Structure | Proteins | Bacteria | Biosynthesis | Acids | Crystal structure
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8. Full Text Fatty acid synthase and the lipogenic phenotype in cancer pathogenesis
by Menendez, Javier A and Lupu, Ruth
Nature Reviews Cancer, ISSN 1474-175X, 10/2007, Volume 7, Issue 10, pp. 763 - 777
There is a renewed interest in the ultimate role of fatty acid synthase ( FASN) a key lipogenic enzyme catalysing the terminal steps in the de novo biogenesis... 
HUMAN PROSTATE-CANCER | ATP CITRATE LYASE | ACTIVATED PROTEIN-KINASE | ONCOLOGY | HYPOXIA-INDUCIBLE FACTOR-1-ALPHA | APOPTOTIC CELL-DEATH | ACETYL-COA-CARBOXYLASE | ENDOPLASMIC-RETICULUM STRESS | HUMAN BREAST-CANCER | HER2/NEU ERBB-2 ONCOGENE | ELEMENT-BINDING PROTEINS | Fatty Acid Synthases - antagonists & inhibitors | Fatty Acid Synthases - metabolism | Carcinoma in Situ - pathology | Neoplasm Invasiveness | Humans | Multienzyme Complexes - metabolism | Neoplasms - enzymology | Transcription Factors - genetics | AMP-Activated Protein Kinases | Neoplasms - drug therapy | Neoplasm Metastasis | Phenotype | Cell Death - genetics | Lipogenesis - genetics | Neoplasms - genetics | Glucose - metabolism | Antineoplastic Agents - pharmacology | Genes, BRCA1 | Neoplasms - pathology | Nuclear Proteins - genetics | Protein-Serine-Threonine Kinases - metabolism | Sterol Regulatory Element Binding Protein 1 - metabolism | Fatty Acids - biosynthesis | Physiological aspects | Synthesis | Research | Fatty acids | Cancer
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9. Full Text Structure of the human β‐ketoacyl [ACP] synthase from the mitochondrial type II fatty acid synthase
by Christensen, Caspar Elo and Kragelund, Birthe B and von Wettstein‐Knowles, Penny and Henriksen, Anette
Protein Science, ISSN 0961-8368, 02/2007, Volume 16, Issue 2, pp. 261 - 272
Two distinct ways of organizing fatty acid biosynthesis exist: the multifunctional type I fatty acid synthase (FAS) of mammals, fungi, and lower eukaryotes... 
acyl binding | fatty acid synthesis | hexanoyl | X‐ray crystal structure | binding pockets | cerulenin | antibiotics | Hexanoyl | Antibiotics | Acyl binding | X-ray crystal structure | Cerulenin | Binding pockets | Fatty acid synthesis | MECHANISM | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | ACYL-CARRIER PROTEIN | ANTIBIOTIC CERULENIN | SACCHAROMYCES-CEREVISIAE | CONDENSING ENZYMES | STREPTOCOCCUS-PNEUMONIAE | INHIBITION | THIOLACTOMYCIN | Protein Structure, Tertiary | Amino Acid Sequence | Fatty Acid Synthases - metabolism | Protein Structure, Secondary | Humans | Models, Molecular | Molecular Sequence Data | Crystallography, X-Ray | Structure-Activity Relationship | Cerulenin - chemistry | 3-Oxoacyl-(Acyl-Carrier-Protein) Synthase - chemistry | Sequence Homology, Amino Acid | Cerulenin - metabolism | Sequence Alignment | Mitochondrial Proteins - metabolism | Mitochondrial Proteins - chemistry | Protein Binding | Binding Sites | Fatty Acid Synthases - chemistry | 3-Oxoacyl-(Acyl-Carrier-Protein) Synthase - metabolism
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10. Full Text Engineering strategies for rational polyketide synthase design
by Klaus, Maja and Grininger, Martin
Natural Product Reports, ISSN 0265-0568, 10/2018, Volume 35, Issue 1, pp. 17 - 181
Covering: mid 1990s to 2018 Over the last two decades, diverse approaches have been explored to generate new polyketides by engineering polyketide synthases... 
CHEMISTRY, MEDICINAL | 6-DEOXYERYTHRONOLIDE B SYNTHASE | ACYLTRANSFERASE DOMAIN | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | DOCKING DOMAINS | CHEMISTRY, ORGANIC | ACYL-CARRIER PROTEIN | ERYTHROMYCIN DERIVATIVES | NATURAL-PRODUCT BIOSYNTHESIS | ASSEMBLY-LINE | ITERATIVE CHAIN ELONGATION | FATTY-ACID SYNTHASE | Recombinant Proteins - metabolism | Polyketide Synthases - chemistry | Polyketide Synthases - metabolism | Protein Engineering - methods | Protein Domains | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Polyketide Synthases - genetics | Polyketide synthase | Domains | Engineering | Design engineering | Polyketides | Modular engineering
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