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AMP-activated Protein Kinase / / edited by Mario D. Cordero, Benoit Viollet
| AMP-activated Protein Kinase / / edited by Mario D. Cordero, Benoit Viollet |
| Edizione | [1st ed. 2016.] |
| Pubbl/distr/stampa | Cham : , : Springer International Publishing : , : Imprint : Springer, , 2016 |
| Descrizione fisica | 1 online resource (X, 523 p. 55 illus., 42 illus. in color.) |
| Disciplina | 572.792 |
| Collana | Experientia Supplementum |
| Soggetto topico |
Human physiology
Clinical biochemistry Metabolism - Disorders Human Physiology Medical Biochemistry Metabolic Diseases |
| Formato | Materiale a stampa  |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto | Part I: AMPK in health -- Structure and Regulation of AMPK -- AMPK Regulation of Carbohydrate Metabolism -- AMPK Regulation of Lipid Metabolism -- AMPK Regulation of Protein Metabolism -- AMPK Regulation of cell growth, apoptosis, autophagy and bioenergetics -- AMPK Regulation of immunology -- AMPK and Stem Cells -- Part II: AMPK in the diseases -- AMPK in metabolic diseases -- AMPK in neurodegenerative diseases -- AMPK in cardiovascular diseases -- AMPK in cancer -- AMPK in aging -- AMPK in musculoskeletal diseases and pain -- AMPK in pathogens -- Part III: Pharmacology of AMPK -- Metformin, new drugs and AMPK -- Small molecules and AMPK -- Nutraceutical compounds and AMPK -- Part IV: Methods of study in AMPK -- Animal models -- In vitro study methods. |
| Record Nr. | UNINA-9910149489103321 |
| Cham : , : Springer International Publishing : , : Imprint : Springer, , 2016 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
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DNA Methyltransferases - Role and Function / / edited by Albert Jeltsch, Renata Z. Jurkowska
| DNA Methyltransferases - Role and Function / / edited by Albert Jeltsch, Renata Z. Jurkowska |
| Edizione | [2nd ed. 2022.] |
| Pubbl/distr/stampa | Cham : , : Springer International Publishing : , : Imprint : Springer, , 2022 |
| Descrizione fisica | 1 online resource (562 pages) |
| Disciplina |
572.86
572.792 |
| Collana | Advances in Experimental Medicine and Biology |
| Soggetto topico |
Cytology
Epigenetics Medical genetics Enzymology Cell Biology Medical Genetics |
| ISBN | 3-031-11454-X |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto | Chapter 1. Mechanisms and biological roles of DNA methyltransferases and DNA methylation – from past achievements to future challenges -- Chapter 2.Bacterial DNA Methylation and Methylomes -- Chapter 3. ChapterDomain Structure of the Dnmt1, Dnmt3a, and Dnmt3b DNA Methyltransferases -- Chapter 4. Enzymology of Mammalian DNA Methyltransferases -- Chapter 5. Genetic Studies on Mammalian DNA Methyltransferase -- Chapter 6. Structure and Mechanism of Plant DNA Methyltransferases -- Chapter 7. DNA Methylation in Honey Bees and the Unresolved Questions in Insect Methylomics -- Chapter 8. N6-Methyladenine: A Conserved and Dynamic DNA Mark -- Chapter 9. Pathways of DNA Demethylation -- Chapter 10. Structure and Function of TET Enzymes -- Chapter 11.Proteins That Read DNA Methylation -- Chapter 12. Recent advances on DNA base flipping – a general mechanism for writing, reading, and erasing DNA modifications.-Chapter 13. The Role of DNA Methylation in Cancer -- Chapter 14. DNMTs and DNA damage -- Chapter 15. Role of DNMTs in brain -- Chapter 16. Current and Emerging Technologies for the Analysis of the Genome-Wide and Locus-Specific DNA Methylation Patterns.-Chapter 17. Inhibitors of DNA methylation -- Chapter 18. Rewriting DNA Methylation Signatures at Will: The Curable Genome Within Reach? -- Chapter 19. DNA Labeling Using DNA Methyltransferases. |
| Record Nr. | UNINA-9910629285803321 |
| Cham : , : Springer International Publishing : , : Imprint : Springer, , 2022 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
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Next Generation Kinase Inhibitors : Moving Beyond the ATP Binding/Catalytic Sites / / edited by Paul Shapiro
| Next Generation Kinase Inhibitors : Moving Beyond the ATP Binding/Catalytic Sites / / edited by Paul Shapiro |
| Edizione | [1st ed. 2020.] |
| Pubbl/distr/stampa | Cham : , : Springer International Publishing : , : Imprint : Springer, , 2020 |
| Descrizione fisica | 1 online resource (XII, 217 p. 59 illus., 56 illus. in color.) |
| Disciplina | 572.792 |
| Soggetto topico |
Cancer - Research
Cancer Research Proteïnes quinases |
| Soggetto genere / forma | Llibres electrònics |
| ISBN | 3-030-48283-9 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto | Chapter 1: Introduction to Kinases, Cellular Signaling, and Kinase Inhibitors -- Chapter 2: Overview of Current Type I/II Kinase Inhibitors -- Chapter 3: Avoiding or Co-opting ATP Inhibition: Type III, IV, V, and VI Kinase Inhibitors -- Chapter 4: Structural Features Regulating Kinase Interactions with Regulatory and Substrate Proteins -- Chapter 5: Developing Kinase Inhibitors using Computer-Aided Drug Design Approaches -- Chapter 6: A Toolbox of Structural Biology and Enzyme Kinetics Reveals the Case for ERK Docking Site Inhibition -- Chapter 7: Novel Stabilized Peptide Inhibitors of Protein Kinases -- Chapter 8: Novel peptide-based inhibitors of protein kinases -- Index. |
| Record Nr. | UNINA-9910416107703321 |
| Cham : , : Springer International Publishing : , : Imprint : Springer, , 2020 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Proteinkinase Inhibitors / / edited by Stefan Laufer
| Proteinkinase Inhibitors / / edited by Stefan Laufer |
| Edizione | [1st ed. 2021.] |
| Pubbl/distr/stampa | Cham : , : Springer International Publishing : , : Imprint : Springer, , 2021 |
| Descrizione fisica | 1 online resource (259 pages) : illustrations |
| Disciplina | 572.792 |
| Collana | Topics in Medicinal Chemistry |
| Soggetto topico |
Medicinal chemistry
Proteins Bioorganic chemistry Pharmaceutical chemistry Medicinal Chemistry Protein Biochemistry Bioorganic Chemistry Pharmaceutics |
| ISBN | 3-030-68180-7 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto | ProteinKinase-Inhibitors: A Story of Success -- Function, Structure and Topology of Proteinkinases -- Molecular Modelling -- Case study on Receptor Tyrosine Kinases EGFR, VEGFR, PDGFR -- Achieving high level of selectivity for kinase inhibitors -- Inhibitors of c-Jun N-terminal kinase 3 -- Exploiting kinase inhibitors for cancer treatment - An Overview of Clinical Results and Outlook -- Covalent Janus Kinase 3 Inhibitors. |
| Record Nr. | UNINA-9910483133403321 |
| Cham : , : Springer International Publishing : , : Imprint : Springer, , 2021 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Springer handbook of enzymes . Supplement, Volume S9 Class 2-3.2 transferases, hydrolases : EC 2-3.2 / / Dietmar Schomburg, Ida Schomburg (eds.); co-edited by Antje Chang
| Springer handbook of enzymes . Supplement, Volume S9 Class 2-3.2 transferases, hydrolases : EC 2-3.2 / / Dietmar Schomburg, Ida Schomburg (eds.); co-edited by Antje Chang |
| Edizione | [2nd ed.] |
| Pubbl/distr/stampa | Berlin ; ; Heidleberg, : Springer-Verlag, 2013 |
| Descrizione fisica | 1 online resource (698 p.) |
| Disciplina |
572.7
572.792 572/.792 |
| Altri autori (Persone) |
SchomburgD (Dietmar)
SchomburgIda <1954-> ChangAntje |
| Collana | Springer Handbook of Enzymes |
| Soggetto topico |
Transferases
Hydrolases |
| ISBN | 3-642-36240-0 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto | 2.1.1.163 demethylmenaquinone methyltransferase -- 2.1.1.164 demethylrebeccamycin-D-glucose Omethyltransferase -- 2.1.1.165 methyl halide transferase -- 2.1.1.166 23S rRNA (uridine2552-2’-O-)-methyltransferase -- 2.1.1.167 27S pre-rRNA (guanosine2922-2’-O)-methyltransferase -- 2.1.1.168 21S rRNA (uridine2791-2’-O)-methyltransferase -- 2.1.1.169 tricetin 3’,4’,5’-O-trimethyltransferase -- 2.1.1.170 16S rRNA (guanine527-N7)-methyltransferase -- 2.1.1.171 16S rRNA (guanine966-N2)-methyltransferase -- 2.1.1.172 16S rRNA (guanine1207-N2)-methyltransferase -- 2.1.1.173 23S rRNA (guanine2445-N2)-methyltransferase -- 2.1.1.174 23S rRNA (guanine1835-N2)-methyltransferase -- 2.1.1.175 tricin synthase -- 2.1.1.176 16S rRNA (cytosine967-C5)-methyltransferase -- 2.1.1.177 23S rRNA (pseudouridine1915-N3)-methyltransferase -- 2.1.1.178 16S rRNA (cytosine1407-C5)-methyltransferase -- 2.1.1.179 16S rRNA (guanine1405-N7)-methyltransferase -- 2.1.1.180 16S rRNA (adenine1408-N1)-methyltransferase -- 2.1.1.181 23S rRNA (adenine1618-N6)-methyltransferase -- 2.1.1.182 16S rRNA (adenine1518-N6/adenine1519-N6)-dimethyltransferase -- 2.1.1.183 18S rRNA (adenine1779-N6/adenine1780-N6)-dimethyltransferase -- 2.1.1.184 23S rRNA (adenine2085-N6)- dimethyltransferase -- 2.1.1.185 23S rRNA (guanosine2251-2’-O-)- methyltransferase -- 2.1.1.186 23S rRNA (cytidine2498-2’-O)-methyltransferase -- 2.1.1.195 cobalt-precorrin-5B (C1)-methyltransferase -- 2.1.1.196 cobalt-precorrin-7 (C15)-methyltransferase[decarboxylating] -- 2.1.1.197 malonyl-CoA O-methyltransferase -- 2.1.1.198 16S rRNA (cytidine1402-2’-O)-methyltransferase -- 2.1.1.199 16S rRNA (cytosine1402-N4)-methyltransferase -- 2.1.2.13 UDP-4-amino-4-deoxy-L-arabinose formyltransferase -- 2.1.3.10 malonyl-S-ACP:biotin-protein carboxyltransferase:- 2.1.3.11 N-succinylornithine carbamoyltransferase -- 2.2.1.9 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase -- 2.3.1.185 tropine acyltransferase -- 2.3.1.186 pseudotropine acyltransferase -- 2.3.1.187 acetyl-S-ACP:malonate ACP transferase -- 2.3.1.188 w-hydroxypalmitate O-feruloyl transferase -- 2.3.1.189 mycothiol synthase -- 2.3.1.190 acetoin dehydrogenase -- 2.3.1.191 UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase -- 2.3.1.192 glycine N-phenylacetyltransferase -- 2.3.2.16 lipid II:glycine glycyltransferase -- 2.3.2.17 N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl- (N6-glycyl)-D-alanyl-D-alaninediphosphoundecaprenyl-Nacetylglucosamine: glycine glycyltransferase -- 2.3.2.18 N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl- (N6-triglycine)-D-alanyl-D-alaninediphosphoundecaprenyl-Nacetylglucosamine: glycine lycyltransferase -- 2.4.1.245 a,a-trehalose synthase -- 2.4.1.247 b-D-galactosyl-(1!4)-L-rhamnose phosphorylase -- 2.4.1.248 cycloisomaltooligosaccharide glucanotransferase -- 2.4.1.249 delphinidin 3’,5’-O-glucosyltransferase -- 2.4.1.250 D-inositol-3-phosphate glycosyltransferase -- 2.4.1.251 GlcA-b-(1!2)-D-Man-a-(1!3)-D-Glc-b- (1!4)-D-Glc-a-1-diphospho-ditrans,octacisundecaprenol 4-b-mannosyltransferase -- 2.4.1.252 GDP-mannose:cellobiosyldiphosphopolyprenol a-mannosyltransferase -- 2.4.1.253 baicalein 7-O-glucuronosyltransferase -- 2.4.2.41 xylogalacturonan b-1,3-xylosyltransferase -- 2.4.2.42 UDP-D-xylose:b-D-glucoside a-1,3-Dxylosyltransferase -- 2.4.2.43 lipid IVA 4-amino-4-deoxy-Larabinosyltransferase -- 2.4.99.12 lipid IVA 3-deoxy-D-manno-octulosonic acid transferase -- 2.4.99.13 (KDO)-lipid IVA 3-deoxy-D-manno-octulosonic acid transferase -- 2.4.99.14 (KDO)2-lipid IVA (2-8) 3-deoxy-D-mannooctulosonic acid transferase -- 2.4.99.15 (KDO)3-lipid IVA (2-4) 3-deoxy-D-mannooctulosonic acid transferase -- 2.5.1.72 quinolinate synthase -- 2.5.1.73 O-phospho-L-seryl-tRNA:Cys-tRNA synthase -- 2.5.1.74 1,4-dihydroxy-2-naphthoate polyprenyltransferase -- 2.5.1.75 tRNA dimethylallyltransferase -- 2.5.1.76 cysteate synthase -- 2.5.1.77 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase -- 2.5.1.78 6,7-dimethyl-8-ribityllumazine synthase -- 2.5.1.79 thermospermine synthase -- 2.5.1.80 7-dimethylallyltryptophan synthase -- 2.5.1.81 geranylfarnesyl diphosphate synthase -- 2.5.1.82 hexaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific] -- 2.5.1.83 hexaprenyl-diphosphate synthase [(2E,6E)- farnesyl-diphosphate specific] -- 2.5.1.84 all-trans-nonaprenyl-diphosphate synthase [geranyl-diphosphate specific] -- 2.5.1.85 all-trans-nonaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific] -- 2.5.1.86 trans,polycis-decaprenyl diphosphate Synthase -- 2.5.1.87 ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific] -- 2.5.1.88 trans,polycis-polyprenyl diphosphate synthase [(2Z,6E)-farnesyl diphosphate specific] -- 2.5.1.89 tritrans,polycis-undecaprenyl-diphosphate synthase [geranylgeranyl-diphosphate specific] -- 2.5.1.93 4-hydroxybenzoate geranyltransferase -- 2.5.1.94 adenosyl-chloride synthase -- 2.6.1.86 2-amino-4-deoxychorismate synthase -- 2.6.1.87 UDP-4-amino-4-deoxy-L-arabinose aminotransferase -- 2.7.1.161 CTP-dependent riboflavin kinase -- 2.7.1.162 N-acetylhexosamine 1-kinase -- 2.7.1.163 hygromycin B 4-O-kinase -- 2.7.1.164 O-phosphoseryl-tRNASec kinase -- 2.7.1.165 glycerate 2-kinase -- 2.7.1.166 3-deoxy-D-manno-octulosonic acid kinase -- 2.7.1.167 D-glycero-b-D-manno-heptose-7-phosphate kinase -- 2.7.1.168 D-glycero-a-D-manno-heptose-7-phosphate kinase -- 2.7.1.169 pantoate kinase -- 2.7.4.25 (d)CMP kinase -- 2.7.7.66 malonate decarboxylase holo-[acyl-carrier protein] synthase -- 2.7.7.67 CDP-archaeol synthase -- 2.7.7.68 2-phospho-L-lactate guanylyltransferase -- 2.7.7.70 D-glycero-b-D-manno-heptose 1-phosphate adenylyltransferase -- 2.7.7.71 D-glycero-a-D-manno-heptose 1-phosphate guanylyltransferase -- 2.7.7.72 CCA tRNA nucleotidyltransferase -- 2.7.8.28 2-phospho-L-lactate transferase -- 2.7.8.29 L-serine-phosphatidylethanolamine phosphatidyltransferase -- 2.7.8.30 undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase -- 2.7.8.31 undecaprenyl-phosphate glucose phosphotransferase -- 2.8.2.35 dermatan 4-sulfotransferase -- 2.8.4.2 arsenate-mycothiol transferase -- 2.9.1.2 O-phospho-L-seryl-tRNASec:L-selenocysteinyltRNA synthase -- 3.1.1.83 monoterpene e-lactone hydrolase -- 3.1.1.84 cocaine esterase -- 3.1.2.28 1,4-dihydroxy-2-naphthoyl-CoA hydrolase -- 3.1.3.78 phosphatidylinositol-4,5-bisphosphate 4-phosphatase -- 3.1.3.80 2,3-bisphosphoglycerate 3-phosphatase -- 3.1.3.81 diacylglycerol diphosphate phosphatase -- 3.1.3.82 -glycero-b-D-manno-heptose 1,7-bisphosphate 7-phosphatase -- 3.1.3.83 D-glycero-a-D-manno-heptose 1,7-bisphosphate 7-phosphatase -- 3.1.4.53 3’,5’-cyclic-AMP phosphodiesterase -- 3.1.7.4 sclareol cyclase -- 3.1.7.5 geranylgeranyl diphosphate diphosphatase -- 3.1.7.6 farnesyl diphosphatase -- 3.1.26.12 ribonuclease E -- 3.1.26.13 retroviral ribonuclease H -- 3.2.1.165 exo-1,4-b-D-glucosaminidase -- 3.2.1.167 baicalin-b-D-glucuronidase -- 3.2.1.168 hesperidin 6-O-a-L-rhamnosyl-b-Dglucosidase -- 3.2.2.27 uracil-DNA glycosylase -- 3.2.2.28 double-stranded uracil-DNA glycosylase -- 3.2.2.29 thymine-DNA glycosylase. |
| Record Nr. | UNINA-9910437616803321 |
| Berlin ; ; Heidleberg, : Springer-Verlag, 2013 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||