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[PMID]:28060484
[Au] Autor:Abugrain ME; Brumsted CJ; Osborn AR; Philmus B; Mahmud T
[Ad] Endereço:Department of Pharmaceutical Sciences, Oregon State University , Corvallis, Oregon 97333, United States.
[Ti] Título:A Highly Promiscuous ß-Ketoacyl-ACP Synthase (KAS) III-like Protein Is Involved in Pactamycin Biosynthesis.
[So] Source:ACS Chem Biol;12(2):362-366, 2017 Feb 17.
[Is] ISSN:1554-8937
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:ß-Ketoacyl-acyl carrier protein (ß-Ketoacyl-ACP) synthase (KAS) III catalyzes the first step in fatty acid biosynthesis, involving a Claisen condensation of the acetyl-CoA starter unit with the first extender unit, malonyl-ACP, to form acetoacetyl-ACP. KAS III-like proteins have also been reported to catalyze acyltransferase reactions using coenzyme A esters or discrete ACP-bound substrates. Here, we report the in vivo and in vitro characterizations of a KAS III-like protein (PtmR), which directly transfers a 6-methylsalicylyl moiety from an iterative type I polyketide synthase to an aminocyclopentitol unit in pactamycin biosynthesis. PtmR is highly promiscuous, recognizing a wide array of S-acyl-N-acetylcysteamines as substrates to produce a suite of pactamycin derivatives with diverse alkyl and aromatic features. The results suggest that KAS III-like proteins may be used as versatile tools for modifications of complex natural products.
[Mh] Termos MeSH primário: 3-Oxoacil-(Proteína de Transporte de Acila) Sintase/metabolismo
Pactamicina/biossíntese
[Mh] Termos MeSH secundário: Catálise
Coenzima A/metabolismo
Estrutura Molecular
Pactamicina/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
23668-11-3 (Pactamycin); EC 2.3.1.180 (3-ketoacyl-acyl carrier protein synthase III); EC 2.3.1.41 (3-Oxoacyl-(Acyl-Carrier-Protein) Synthase); SAA04E81UX (Coenzyme A)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170713
[Lr] Data última revisão:
170713
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170107
[St] Status:MEDLINE
[do] DOI:10.1021/acschembio.6b01043


  2 / 181 MEDLINE  
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[PMID]:27858985
[Au] Autor:Thoduka SG; Zaleski PA; Dabrowska Z; Równicki M; Strózecka J; Górska A; Olejniczak M; Trylska J
[Ad] Endereço:Centre of New Technologies, University of Warsaw, Warsaw, 02-097, Poland.
[Ti] Título:Analysis of ribosomal inter-subunit sites as targets for complementary oligonucleotides.
[So] Source:Biopolymers;107(4), 2017 Apr.
[Is] ISSN:1097-0282
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The bacterial ribosome has many functional ribosomal RNA (rRNA) sites. We have computationally analyzed the rRNA regions involved in the interactions between the 30S and 50S subunits. Various properties of rRNA such as solvent accessibility, opening energy, hydrogen bonding pattern, van der Waals energy, thermodynamic stability were determined. Based on these properties we selected rRNA targets for hybridization with complementary 2'-O-methyl oligoribonucleotides (2'-OMe RNAs). Further, the inhibition efficiencies of the designed ribosome-interfering 2'-OMe RNAs were tested using a ß-galactosidase assay in a translation system based on the E. coli extract. Several of the oligonucleotides displayed IC values below 1 µM, which were in a similar range as those determined for known ribosome inhibitors, tetracycline and pactamycin. The calculated opening and van der Waals stacking energies of the rRNA targets correlated best with the inhibitory efficiencies of 2'-OMe RNAs. Moreover, the binding affinities of several oligonucleotides to both 70S ribosomes and isolated 30S and 50S subunits were measured using a double-filter retention assay. Further, we applied heat-shock chemical transformation to introduce 2'-OMe RNAs to E. coli cells and verify inhibition of bacterial growth. We observed high correlation between IC in the cell-free extract and bacterial growth inhibition. Overall, the results suggest that the computational analysis of potential rRNA targets within the conformationally dynamic regions of inter-subunit bridges can help design efficient antisense oligomers to probe the ribosome function.
[Mh] Termos MeSH primário: Oligonucleotídeos/metabolismo
RNA Ribossômico/metabolismo
[Mh] Termos MeSH secundário: Sequência de Bases
Sítios de Ligação
Projeto Auxiliado por Computador
Escherichia coli/efeitos dos fármacos
Escherichia coli/genética
Escherichia coli/metabolismo
Conformação de Ácido Nucleico
Oligonucleotídeos/química
Pactamicina/química
Pactamicina/metabolismo
Pactamicina/farmacologia
Ligação Proteica
Biossíntese de Proteínas/efeitos dos fármacos
Estrutura Terciária de Proteína
RNA Ribossômico/antagonistas & inibidores
RNA Ribossômico/química
Subunidades Ribossômicas Maiores de Bactérias/química
Subunidades Ribossômicas Maiores de Bactérias/metabolismo
Subunidades Ribossômicas Menores de Bactérias/química
Subunidades Ribossômicas Menores de Bactérias/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Oligonucleotides); 0 (RNA, Ribosomal); 23668-11-3 (Pactamycin)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170207
[Lr] Data última revisão:
170207
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161119
[St] Status:MEDLINE
[do] DOI:10.1002/bip.23004


  3 / 181 MEDLINE  
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[PMID]:27305101
[Au] Autor:Abugrain ME; Lu W; Li Y; Serrill JD; Brumsted CJ; Osborn AR; Alani A; Ishmael JE; Kelly JX; Mahmud T
[Ad] Endereço:Department of Pharmaceutical Sciences, Oregon State University, Corvallis, OR, 97331-3507, USA.
[Ti] Título:Interrogating the Tailoring Steps of Pactamycin Biosynthesis and Accessing New Pactamycin Analogues.
[So] Source:Chembiochem;17(17):1585-8, 2016 09 02.
[Is] ISSN:1439-7633
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Pactamycin is a bacteria-derived aminocyclitol antibiotic with a wide-range of biological activity. Its chemical structure and potent biological activities have made it an interesting lead compound for drug discovery and development. Despite its unusual chemical structure, many aspects of its formation in nature remain elusive. Using a combination of genetic inactivation and metabolic analysis, we investigated the tailoring processes of pactamycin biosynthesis in Streptomyces pactum. The results provide insights into the sequence of events during the tailoring steps of pactamycin biosynthesis and explain the unusual production of various pactamycin analogues by S. pactum mutants. We also identified two new pactamycin analogues that have better selectivity indexes than pactamycin against malarial parasites.
[Mh] Termos MeSH primário: Antibióticos Antineoplásicos/biossíntese
Pactamicina/análogos & derivados
Pactamicina/biossíntese
Streptomyces/metabolismo
[Mh] Termos MeSH secundário: Antibióticos Antineoplásicos/química
Conformação Molecular
Pactamicina/química
Streptomyces/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antibiotics, Antineoplastic); 23668-11-3 (Pactamycin)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171101
[Lr] Data última revisão:
171101
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160616
[St] Status:MEDLINE
[do] DOI:10.1002/cbic.201600261


  4 / 181 MEDLINE  
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[PMID]:26741730
[Au] Autor:Gerstner NC; Adams CS; Grigg RD; Tretbar M; Rigoli JW; Schomaker JM
[Ad] Endereço:Department of Chemistry, University of Wisconsin , Madison, Wisconsin 53706, United States.
[Ti] Título:Diastereoselective Synthesis of the Aminocyclitol Core of Jogyamycin via an Allene Aziridination Strategy.
[So] Source:Org Lett;18(2):284-7, 2016 Jan 15.
[Is] ISSN:1523-7052
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Oxidative allene amination provides rapid access to densely functionalized amine-containing stereotriads through highly reactive bicyclic methyleneaziridine intermediates. This strategy has been demonstrated as a viable approach for the construction of the densely functionalized aminocyclitol core of jogyamycin, a natural product with potent antiprotozoal activity. Importantly, the flexibility of oxidative allene amination will enable the syntheses of modified aminocyclitol analogues of the jogyamycin core.
[Mh] Termos MeSH primário: Pactamicina/análogos & derivados
Pactamicina/síntese química
[Mh] Termos MeSH secundário: Alcadienos/química
Aminação
Aminas/química
Estrutura Molecular
Oxirredução
Pactamicina/química
Pactamicina/farmacologia
Estereoisomerismo
Streptomyces/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Alkadienes); 0 (Amines); 0 (jogyamycin); 23668-11-3 (Pactamycin); 4AV0LZ8QKB (propadiene)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160108
[St] Status:MEDLINE
[do] DOI:10.1021/acs.orglett.5b03453


  5 / 181 MEDLINE  
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[PMID]:26426567
[Au] Autor:Hirayama A; Miyanaga A; Kudo F; Eguchi T
[Ad] Endereço:Department of Chemistry and Materials Science, Tokyo Institute of Technology, 2-12-1 O-okayama, Meguro-ku, Tokyo, 152-8551, Japan.
[Ti] Título:Mechanism-Based Trapping of the Quinonoid Intermediate by Using the K276R Mutant of PLP-Dependent 3-Aminobenzoate Synthase PctV in the Biosynthesis of Pactamycin.
[So] Source:Chembiochem;16(17):2484-90, 2015 Nov.
[Is] ISSN:1439-7633
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Mutational analysis of the pyridoxal 5'-phosphate (PLP)-dependent enzyme PctV was carried out to elucidate the multi-step reaction mechanism for the formation of 3-aminobenzoate (3-ABA) from 3-dehydroshikimate (3-DSA). Introduction of mutation K276R led to the accumulation of a quinonoid intermediate with an absorption maximum at 580 nm after the reaction of pyridoxamine 5'-phosphate (PMP) with 3-DSA. The chemical structure of this intermediate was supported by X-ray crystallographic analysis of the complex formed between the K276R mutant and the quinonoid intermediate. These results clearly show that a quinonoid intermediate is involved in the formation of 3-ABA. They also indicate that Lys276 (in the active site of PctV) plays multiple roles, including acid/base catalysis during the dehydration reaction of the quinonoid intermediate.
[Mh] Termos MeSH primário: Oxirredutases/metabolismo
Pactamicina/biossíntese
[Mh] Termos MeSH secundário: Sítios de Ligação
Biocatálise
Domínio Catalítico
Cristalografia por Raios X
Cinética
Simulação de Dinâmica Molecular
Mutagênese Sítio-Dirigida
Oxirredutases/química
Oxirredutases/genética
Pactamicina/química
Fosfato de Piridoxal/química
Ácido Chiquímico/análogos & derivados
Ácido Chiquímico/química
Ácido Chiquímico/metabolismo
Espectrofotometria Ultravioleta
meta-Aminobenzoatos/química
meta-Aminobenzoatos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (meta-Aminobenzoates); 23668-11-3 (Pactamycin); 27655-56-7 (3-dehydroshikimate); 29MS2WI2NU (Shikimic Acid); 5V5IOJ8338 (Pyridoxal Phosphate); EC 1.- (Oxidoreductases); EC 1.- (benzoate synthase); G2X3B3O37U (3-aminobenzoic acid)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:170103
[Lr] Data última revisão:
170103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151002
[St] Status:MEDLINE
[do] DOI:10.1002/cbic.201500426


  6 / 181 MEDLINE  
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[PMID]:25938491
[Au] Autor:Guha G; Lu W; Li S; Liang X; Kulesz-Martin MF; Mahmud T; Indra AK; Ganguli-Indra G
[Ad] Endereço:Department of Pharmaceutical Sciences, College of Pharmacy, Oregon State University, Corvallis, Oregon, United States of America.
[Ti] Título:Novel Pactamycin Analogs Induce p53 Dependent Cell-Cycle Arrest at S-Phase in Human Head and Neck Squamous Cell Carcinoma (HNSCC) Cells.
[So] Source:PLoS One;10(5):e0125322, 2015.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Pactamycin, although putatively touted as a potent antitumor agent, has never been used as an anticancer drug due to its high cytotoxicity. In this study, we characterized the effects of two novel biosynthetically engineered analogs of pactamycin, de-6MSA-7-demethyl-7-deoxypactamycin (TM-025) and 7-demethyl-7-deoxypactamycin (TM-026), in head and neck squamous cell carcinoma (HNSCC) cell lines SCC25 and SCC104. Both TM-025 and TM-026 exert growth inhibitory effects on HNSCC cells by inhibiting cell proliferation. Interestingly, unlike their parent compound pactamycin, the analogs do not inhibit synthesis of nascent protein in a cell-based assay. Furthermore, they do not induce apoptosis or autophagy in a dose- or a time-dependent manner, but induce mild senescence in the tested cell lines. Cell cycle analysis demonstrated that both analogs significantly induce cell cycle arrest of the HNSCC cells at S-phase resulting in reduced accumulation of G2/M-phase cells. The pactamycin analogs induce expression of cell cycle regulatory proteins including master regulator p53, its downstream target p21Cip1/WAF1, p27kip21, p19, cyclin E, total and phospho Cdc2 (Tyr15) and Cdc25C. Besides, the analogs mildly reduce cyclin D1 expression without affecting expression of cyclin B, Cdk2 and Cdk4. Specific inhibition of p53 by pifithrin-α reduces the percentage of cells accumulated in S-phase, suggesting contribution of p53 to S-phase increase. Altogether, our results demonstrate that Pactamycin analogs TM-025 and TM-026 induce senescence and inhibit proliferation of HNSCC cells via accumulation in S-phase through possible contribution of p53. The two PCT analogs can be widely used as research tools for cell cycle inhibition studies in proliferating cancer cells with specific mechanisms of action.
[Mh] Termos MeSH primário: Carcinoma de Células Escamosas/patologia
Pontos de Checagem do Ciclo Celular/efeitos dos fármacos
Neoplasias de Cabeça e Pescoço/patologia
Hidrocarbonetos Fluorados/farmacologia
Pactamicina/análogos & derivados
Fase S/efeitos dos fármacos
Proteína Supressora de Tumor p53/metabolismo
[Mh] Termos MeSH secundário: Apoptose/efeitos dos fármacos
Autofagia/efeitos dos fármacos
Linhagem Celular Tumoral
Proliferação Celular/efeitos dos fármacos
Sobrevivência Celular/efeitos dos fármacos
Senescência Celular/efeitos dos fármacos
Inibidor de Quinase Dependente de Ciclina p21/metabolismo
Relação Dose-Resposta a Droga
Inativação Gênica/efeitos dos fármacos
Seres Humanos
Modelos Biológicos
Pactamicina/farmacologia
Biossíntese de Proteínas/efeitos dos fármacos
Regulação para Cima/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cyclin-Dependent Kinase Inhibitor p21); 0 (Hydrocarbons, Fluorinated); 0 (TM-025); 0 (TM-026); 0 (Tumor Suppressor Protein p53); 23668-11-3 (Pactamycin)
[Em] Mês de entrada:1604
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150505
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0125322


  7 / 181 MEDLINE  
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[PMID]:25792144
[Au] Autor:Sharpe RJ; Malinowski JT; Sorana F; Luft JC; Bowerman CJ; DeSimone JM; Johnson JS
[Ad] Endereço:Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-3290, United States.
[Ti] Título:Preparation and biological evaluation of synthetic and polymer-encapsulated congeners of the antitumor agent pactamycin: insight into functional group effects and biological activity.
[So] Source:Bioorg Med Chem;23(8):1849-57, 2015 Apr 15.
[Is] ISSN:1464-3391
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The synthesis and biological analysis of a number of novel congeners of the aminocyclopentitol pactamycin is described. Specific attention was paid to the preparation of derivatives at crucial synthetic branch points of the parent structure, and biological assays revealed a number of insights into the source of pactamycin's biological activity. Additionally, the encapsulation of pactamycin and select derivatives into the PRINT© nanoparticle technology was investigated as a proof-of-concept, and evidence of bioactivity modulation through nanoparticle delivery is demonstrated. This work has provided heretofore unrealized access to a large number of novel compounds for further evaluation.
[Mh] Termos MeSH primário: Antineoplásicos/química
Antineoplásicos/farmacologia
Pactamicina/análogos & derivados
Pactamicina/farmacologia
[Mh] Termos MeSH secundário: Antineoplásicos/administração & dosagem
Linhagem Celular Tumoral
Portadores de Fármacos/química
Seres Humanos
Nanopartículas/química
Neoplasias/tratamento farmacológico
Pactamicina/administração & dosagem
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Drug Carriers); 23668-11-3 (Pactamycin)
[Em] Mês de entrada:1512
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150321
[St] Status:MEDLINE


  8 / 181 MEDLINE  
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[PMID]:24913268
[Au] Autor:Wong W; Bai XC; Brown A; Fernandez IS; Hanssen E; Condron M; Tan YH; Baum J; Scheres SH
[Ad] Endereço:Division of Infection and Immunity, Walter and Eliza Hall Institute of Medical Research, Melbourne, Australia.
[Ti] Título:Cryo-EM structure of the Plasmodium falciparum 80S ribosome bound to the anti-protozoan drug emetine.
[So] Source:Elife;3, 2014 Jun 09.
[Is] ISSN:2050-084X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Malaria inflicts an enormous burden on global human health. The emergence of parasite resistance to front-line drugs has prompted a renewed focus on the repositioning of clinically approved drugs as potential anti-malarial therapies. Antibiotics that inhibit protein translation are promising candidates for repositioning. We have solved the cryo-EM structure of the cytoplasmic ribosome from the human malaria parasite, Plasmodium falciparum, in complex with emetine at 3.2 Å resolution. Emetine is an anti-protozoan drug used in the treatment of ameobiasis that also displays potent anti-malarial activity. Emetine interacts with the E-site of the ribosomal small subunit and shares a similar binding site with the antibiotic pactamycin, thereby delivering its therapeutic effect by blocking mRNA/tRNA translocation. As the first cryo-EM structure that visualizes an antibiotic bound to any ribosome at atomic resolution, this establishes cryo-EM as a powerful tool for screening and guiding the design of drugs that target parasite translation machinery.
[Mh] Termos MeSH primário: Emetina/química
Plasmodium falciparum/metabolismo
Ribossomos/química
Ribossomos/ultraestrutura
[Mh] Termos MeSH secundário: Animais
Antimaláricos/química
Sítios de Ligação
Microscopia Crioeletrônica
Citoplasma/metabolismo
Desenho de Drogas
Eritrócitos/parasitologia
Seres Humanos
Modelos Moleculares
Pactamicina/química
Ligação Proteica
RNA Mensageiro/metabolismo
Proteínas Ribossômicas/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antimalarials); 0 (RNA, Messenger); 0 (Ribosomal Proteins); 23668-11-3 (Pactamycin); X8D5EPO80M (Emetine)
[Em] Mês de entrada:1507
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140611
[St] Status:MEDLINE
[do] DOI:10.7554/eLife.03080


  9 / 181 MEDLINE  
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[PMID]:24245656
[Au] Autor:Sharpe RJ; Malinowski JT; Johnson JS
[Ad] Endereço:Department of Chemistry, University of North Carolina at Chapel Hill , Chapel Hill, North Carolina 27599-3290, United States.
[Ti] Título:Asymmetric synthesis of the aminocyclitol pactamycin, a universal translocation inhibitor.
[So] Source:J Am Chem Soc;135(47):17990-8, 2013 Nov 27.
[Is] ISSN:1520-5126
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:An asymmetric total synthesis of the aminocyclopentitol pactamycin is described. The title compound is delivered in 15 steps from 2,4-pentanedione. Critical to this approach was the exploitation of a complex symmetry-breaking reduction strategy to assemble the C1, C2, and C7 relative stereochemistry within the first four steps of the synthesis. Multiple iterations of this reduction strategy are described, and a thorough analysis of stereochemical outcomes is detailed. In the final case, an asymmetric Mannich reaction was developed to install a protected amine directly at the C2 position. Symmetry-breaking reduction of this material gave way to a remarkable series of stereochemical outcomes leading to the title compound without recourse to nonstrategic downstream manipulations. This synthesis is immediately accommodating to the preparation of structural analogs.
[Mh] Termos MeSH primário: Antibióticos Antineoplásicos/síntese química
Pactamicina/síntese química
Inibidores da Síntese de Proteínas/síntese química
[Mh] Termos MeSH secundário: Oxirredução
Pentanonas/química
Estereoisomerismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Antibiotics, Antineoplastic); 0 (Pentanones); 0 (Protein Synthesis Inhibitors); 23668-11-3 (Pactamycin); 46R950BP4J (acetylacetone)
[Em] Mês de entrada:1407
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131120
[St] Status:MEDLINE
[do] DOI:10.1021/ja409944u


  10 / 181 MEDLINE  
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[PMID]:24039046
[Au] Autor:Kisunzu JK; Sarpong R
[Ad] Endereço:Department of Chemistry, University of California, Berkeley, Berkeley, CA 94720 (USA).
[Ti] Título:Hidden symmetry enables a 15-step total synthesis of pactamycin.
[So] Source:Angew Chem Int Ed Engl;52(41):10694-6, 2013 Oct 04.
[Is] ISSN:1521-3773
[Cp] País de publicação:Germany
[La] Idioma:eng
[Mh] Termos MeSH primário: Antibióticos Antineoplásicos/síntese química
Técnicas de Química Sintética
Pactamicina/síntese química
[Pt] Tipo de publicação:COMMENT; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antibiotics, Antineoplastic); 23668-11-3 (Pactamycin)
[Em] Mês de entrada:1504
[Cu] Atualização por classe:140509
[Lr] Data última revisão:
140509
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130917
[St] Status:MEDLINE
[do] DOI:10.1002/anie.201305464



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BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde