Base de dados : MEDLINE
Pesquisa : E05.196.712.516.600.676.500 [Categoria DeCS]
Referências encontradas : 10446 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 1045 ir para página                         

  1 / 10446 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29339721
[Au] Autor:Kilic S; Felekyan S; Doroshenko O; Boichenko I; Dimura M; Vardanyan H; Bryan LC; Arya G; Seidel CAM; Fierz B
[Ad] Endereço:Laboratory of Biophysical Chemistry of Macromolecules, Institute of Chemical Sciences and Engineering (ISIC), Ecole Polytechnique Fédérale de Lausanne (EPFL), 1015, Lausanne, Switzerland.
[Ti] Título:Single-molecule FRET reveals multiscale chromatin dynamics modulated by HP1α.
[So] Source:Nat Commun;9(1):235, 2018 01 16.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The dynamic architecture of chromatin fibers, a key determinant of genome regulation, is poorly understood. Here, we employ multimodal single-molecule Förster resonance energy transfer studies to reveal structural states and their interconversion kinetics in chromatin fibers. We show that nucleosomes engage in short-lived (micro- to milliseconds) stacking interactions with one of their neighbors. This results in discrete tetranucleosome units with distinct interaction registers that interconvert within hundreds of milliseconds. Additionally, we find that dynamic chromatin architecture is modulated by the multivalent architectural protein heterochromatin protein 1α (HP1α), which engages methylated histone tails and thereby transiently stabilizes stacked nucleosomes. This compacted state nevertheless remains dynamic, exhibiting fluctuations on the timescale of HP1α residence times. Overall, this study reveals that exposure of internal DNA sites and nucleosome surfaces in chromatin fibers is governed by an intrinsic dynamic hierarchy from micro- to milliseconds, allowing the gene regulation machinery to access compact chromatin.
[Mh] Termos MeSH primário: Cromatina/metabolismo
Proteínas Cromossômicas não Histona/metabolismo
Transferência Ressonante de Energia de Fluorescência/métodos
Nucleossomos/metabolismo
[Mh] Termos MeSH secundário: Animais
Cromatina/química
Cromatina/genética
DNA/química
DNA/genética
DNA/metabolismo
Regulação da Expressão Gênica
Histonas/metabolismo
Cinética
Metilação
Microscopia de Fluorescência
Conformação Molecular
Conformação de Ácido Nucleico
Nucleossomos/química
Nucleossomos/genética
Ligação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Chromatin); 0 (Chromosomal Proteins, Non-Histone); 0 (Histones); 0 (Nucleosomes); 107283-02-3 (heterochromatin-specific nonhistone chromosomal protein HP-1); 9007-49-2 (DNA)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180118
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02619-5


  2 / 10446 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29297914
[Au] Autor:Swadling JB; Ishii K; Tahara T; Kitao A
[Ad] Endereço:School of Life Science and Technology, Tokyo Institute of Technology, 2-12-1 Ookayama, M6-13, Meguro, Tokyo 152-8550, Japan. akitao@bio.titech.ac.jp.
[Ti] Título:Origins of biological function in DNA and RNA hairpin loop motifs from replica exchange molecular dynamics simulation.
[So] Source:Phys Chem Chem Phys;20(5):2990-3001, 2018 Jan 31.
[Is] ISSN:1463-9084
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Deoxyribonucleic acid (DNA) and ribonucleic acid (RNA) have remarkably similar chemical structures, but despite this, they play significantly different roles in modern biology. In this article, we explore the possible conformations of DNA and RNA hairpins to better understand the fundamental differences in structure formation and stability. We use large parallel temperature replica exchange molecular dynamics ensembles to sample the full conformational landscape of these hairpin molecules so that we can identify the stable structures formed by the hairpin sequence. Our simulations show RNA adopts a narrower distribution of folded structures compared to DNA at room temperature, which forms both hairpins and many unfolded conformations. RNA is capable of forming twice as many hydrogen bonds than DNA which results in a higher melting temperature. We see that local chemical differences lead to emergent molecular properties such as increased persistence length in RNA that is weakly temperature dependant. These discoveries provide fundamental insight into how RNA forms complex folded tertiary structures which confer enzymatic-like function in ribozymes, whereas DNA retains structural motifs in order to facilitate function such as translation of sequence.
[Mh] Termos MeSH primário: DNA/química
Simulação de Dinâmica Molecular
RNA/química
[Mh] Termos MeSH secundário: Transferência Ressonante de Energia de Fluorescência
Ligações de Hidrogênio
Sequências Repetidas Invertidas/genética
Conformação de Ácido Nucleico
Termodinâmica
Temperatura de Transição
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
63231-63-0 (RNA); 9007-49-2 (DNA)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180104
[St] Status:MEDLINE
[do] DOI:10.1039/c7cp06355e


  3 / 10446 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27771990
[Au] Autor:Pawar SK; Punith R; Naik RS; Seetharamappa J
[Ad] Endereço:a Department of Chemistry , Karnatak University , Dharwad 580003 , India.
[Ti] Título:Spectroscopic and molecular modeling approaches to investigate the binding of proton pump inhibitors to human serum albumin.
[So] Source:J Biomol Struct Dyn;35(15):3205-3220, 2017 Nov.
[Is] ISSN:1538-0254
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The interaction between two proton pump inhibitors viz., omeprazole (OME) and esomeprazole (EPZ) with human serum albumin (HSA) was studied by fluorescence, absorption, circular dichroism (CD), Fourier transform infrared spectroscopy (FT-IR), voltammetry, and molecular modeling approaches. The Stern-Volmer quenching constants (K ) for OME-HSA and EPZ-HSA systems obtained at different temperatures revealed that both OME and EPZ quenched the intensity of HSA through dynamic mode of quenching mechanism. The binding constants of OME-HSA and EPZ-HSA increased with temperature, indicating the increased stability of these systems at higher temperatures. Thermodynamic parameters viz., ∆H , ∆S , and ∆G were determined for both systems. These values revealed that both systems were stabilized by hydrophobic forces. The competitive displacement and molecular docking studies suggested that OME/EPZ was bound to Sudlow's site I in subdomain IIA in HSA. The extent of energy transfer from HSA to OME/EPZ and the distance of separation in tryptophan (Trp214) Trp214-OME and Trp214-EPZ was determined based on the theory of fluorescence resonance energy transfer. UV absorption, 3D fluorescence, and CD studies indicated that the binding of OME/EPZ to HSA has induced micro environmental changes around the protein which resulted changes in its secondary structure.
[Mh] Termos MeSH primário: Inibidores da Bomba de Prótons/química
Albumina Sérica Humana/química
[Mh] Termos MeSH secundário: Sítios de Ligação
Dicroísmo Circular
Transferência Ressonante de Energia de Fluorescência
Seres Humanos
Ligações de Hidrogênio
Interações Hidrofóbicas e Hidrofílicas
Simulação de Acoplamento Molecular
Ligação Proteica
Estrutura Secundária de Proteína
Espectroscopia de Infravermelho com Transformada de Fourier
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Proton Pump Inhibitors); ZIF514RVZR (Serum Albumin, Human)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180223
[Lr] Data última revisão:
180223
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161025
[St] Status:MEDLINE
[do] DOI:10.1080/07391102.2016.1251337


  4 / 10446 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29177353
[Au] Autor:Shah R; Zhou A; Wagner CR
[Ad] Endereço:Department of Medicinal Chemistry University of Minnesota, USA. wagne003@umn.edu.
[Ti] Título:Switch-on fluorescent/FRET probes to study human histidine triad nucleotide binding protein 1 (hHint1), a novel target for opioid tolerance and neuropathic pain.
[So] Source:Org Biomol Chem;15(48):10230-10237, 2017 Dec 13.
[Is] ISSN:1477-0539
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Histidine Triad Nucleotide Binding Protein 1 (Hint1) has emerged to be an important post-synaptic protein associated with a variety of central nervous system disorders such as pain, addiction, and schizophrenia. Recently, inhibition of histidine nucleotide binding protein 1 (Hint1) with a small nucleoside inhibitor has shown promise as a new therapeutic strategy for the treatment of neuropathic pain. Herein, we describe the first rationally designed small molecule switch-on probes with dual fluorescence and FRET properties to study Hint1. Two non-natural fluorescent nucleosides with a fluorescent lifetime of 20 and 25 ns were each coupled through a linker to the indole ring, i.e. probes 7 and 8. Both probes were found to be water soluble and quenched intramolecularly via photoinduced electron transfer (PET) resulting in minimal background fluorescence. Upon incubating with Hint1, compound 7 and 8 exhibited a 40- and 16-fold increase in the fluorescence intensity compared to the control. Compounds 7 and 8 bind Hint1 with a dissociation constant of 0.121 ± 0.02 and 2.2 ± 0.36 µM, respectively. We demonstrate that probe 8 exhibits a switch-on FRET property with an active site tryptophan residue (W123). We show the utility of probes in performing quantitative ligand displacement studies, as well as in selective detection of Hint1 in the cell lysates. These probes should be useful for studying the dynamics of the active site, as well as for the development of fluorescence lifetime based high throughput screening assay to identify novel inhibitors for Hint1 in future.
[Mh] Termos MeSH primário: Transferência Ressonante de Energia de Fluorescência
Fluorescência
Corantes Fluorescentes/química
Proteínas do Tecido Nervoso/química
Neuralgia/tratamento farmacológico
Receptores Opioides/metabolismo
[Mh] Termos MeSH secundário: Sítios de Ligação
Corantes Fluorescentes/síntese química
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fluorescent Dyes); 0 (HINT1 protein, human); 0 (Nerve Tissue Proteins); 0 (Receptors, Opioid)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE
[do] DOI:10.1039/c7ob02472j


  5 / 10446 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29293509
[Au] Autor:Martin KJ; McGhee EJ; Schwarz JP; Drysdale M; Brachmann SM; Stucke V; Sansom OJ; Anderson KI
[Ad] Endereço:Beatson Institute for Cancer Research, Glasgow, United Kingdom.
[Ti] Título:Accepting from the best donor; analysis of long-lifetime donor fluorescent protein pairings to optimise dynamic FLIM-based FRET experiments.
[So] Source:PLoS One;13(1):e0183585, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:FRET biosensors have proven very useful tools for studying the activation of specific signalling pathways in living cells. Most biosensors designed to date have been predicated on fluorescent protein pairs that were identified by, and for use in, intensity based measurements, however fluorescence lifetime provides a more reliable measurement of FRET. Both the technology and fluorescent proteins available for FRET have moved on dramatically in the last decade. Lifetime imaging systems have become increasingly accessible and user-friendly, and there is an entire field of biology dedicated to refining and adapting different characteristics of existing and novel fluorescent proteins. This growing pool of fluorescent proteins includes the long-lifetime green and cyan fluorescent proteins Clover and mTurquoise2, the red variant mRuby2, and the dark acceptor sREACh. Here, we have tested these donors and acceptors in appropriate combinations against the standard or recommended norms (EGFP and mTFP as donors, mCherry and either Ypet or Venus as acceptors) to determine if they could provide more reliable, reproducible and quantifiable FLIM-FRET data to improve on the dynamic range compared to other donors and breadth of application of biosensor technologies. These tests were performed for comparison on both a wide-field, frequency domain system and a multiphoton, TCSPC time domain FLIM system. Clover proved to be an excellent donor with extended dynamic range in combination with mCherry on both platforms, while mRuby2 showed a high degree of variability and poor FRET efficiencies in all cases. mTFP-Venus was the most consistent cyan-yellow pair between the two FLIM methodologies, but mTurquoise2 has better dynamic range and transfers energy consistently over time to the dark acceptor sRCh. Combination of mTFP-sRCh with Clover-mCherry would allow the simultaneous use of two FLIM-FRET biosensors within one sample by eliminating the crosstalk between the yellow acceptor and green donor emissions.
[Mh] Termos MeSH primário: Transferência Ressonante de Energia de Fluorescência/métodos
Proteínas Luminescentes/metabolismo
[Mh] Termos MeSH secundário: Técnicas Biossensoriais
Fluorescência
Ligação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Luminescent Proteins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180215
[Lr] Data última revisão:
180215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180103
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0183585


  6 / 10446 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29295996
[Au] Autor:Jepsen MDE; Sparvath SM; Nielsen TB; Langvad AH; Grossi G; Gothelf KV; Andersen ES
[Ad] Endereço:Interdisciplinary Nanoscience Center, Aarhus University, 8000, Aarhus C, Denmark.
[Ti] Título:Development of a genetically encodable FRET system using fluorescent RNA aptamers.
[So] Source:Nat Commun;9(1):18, 2018 01 02.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Fluorescent RNA aptamers are useful as markers for tracking RNA molecules inside cells and for creating biosensor devices. Förster resonance energy transfer (FRET) based on fluorescent proteins has been used to detect conformational changes, however, such FRET devices have not yet been produced using fluorescent RNA aptamers. Here we develop an RNA aptamer-based FRET (apta-FRET) system using single-stranded RNA origami scaffolds. To obtain FRET, the fluorescent aptamers Spinach and Mango are placed in close proximity on the RNA scaffolds and a new fluorophore is synthesized to increase spectral overlap. RNA devices that respond to conformational changes are developed, and finally, apta-FRET constructs are expressed in E. coli where FRET is observed, demonstrating that the apta-FRET system is genetically encodable and that the RNA nanostructures fold correctly in bacteria. We anticipate that the RNA apta-FRET system could have applications as ratiometric sensors for real-time studies in cell and synthetic biology.
[Mh] Termos MeSH primário: Aptâmeros de Nucleotídeos
Transferência Ressonante de Energia de Fluorescência/métodos
[Mh] Termos MeSH secundário: Escherichia coli
[Pt] Tipo de publicação:EVALUATION STUDIES; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Aptamers, Nucleotide)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180104
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02435-x


  7 / 10446 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29341672
[Au] Autor:Lin W; Ma J; Nong D; Xu C; Zhang B; Li J; Jia Q; Dou S; Ye F; Xi X; Lu Y; Li M
[Ad] Endereço:Beijing National Laboratory for Condensed Matter Physics and CAS Key Laboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing 100190, China.
[Ti] Título:Helicase Stepping Investigated with One-Nucleotide Resolution Fluorescence Resonance Energy Transfer.
[So] Source:Phys Rev Lett;119(13):138102, 2017 Sep 29.
[Is] ISSN:1079-7114
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Single-molecule Förster resonance energy transfer is widely applied to study helicases by detecting distance changes between a pair of dyes anchored to overhangs of a forked DNA. However, it has been lacking single-base pair (1-bp) resolution required for revealing stepping kinetics of helicases. We designed a nanotensioner in which a short DNA is bent to exert force on the overhangs, just as in optical or magnetic tweezers. The strategy improved the resolution of Förster resonance energy transfer to 0.5 bp, high enough to uncover differences in DNA unwinding by yeast Pif1 and E. coli RecQ whose unwinding behaviors cannot be differentiated by currently practiced methods. We found that Pif1 exhibits 1-bp-stepping kinetics, while RecQ breaks 1 bp at a time but sequesters the nascent nucleotides and releases them randomly. The high-resolution data allowed us to propose a three-parameter model to quantitatively interpret the apparently different unwinding behaviors of the two helicases which belong to two superfamilies.
[Mh] Termos MeSH primário: DNA Helicases/metabolismo
DNA/química
Escherichia coli/metabolismo
[Mh] Termos MeSH secundário: Transferência Ressonante de Energia de Fluorescência
Cinética
Conformação de Ácido Nucleico
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
9007-49-2 (DNA); EC 3.6.4.- (DNA Helicases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180205
[Lr] Data última revisão:
180205
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180118
[St] Status:MEDLINE
[do] DOI:10.1103/PhysRevLett.119.138102


  8 / 10446 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
[PMID]:27774548
[Au] Autor:Shi WJ; Lo PC; Zhao S; Wong RC; Wang Q; Fong WP; Ng DK
[Ad] Endereço:Department of Chemistry, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong, China. dkpn@cuhk.edu.hk.
[Ti] Título:A biotin-conjugated glutathione-responsive FRET-based fluorescent probe with a ferrocenyl BODIPY as the dark quencher.
[So] Source:Dalton Trans;45(44):17798-17806, 2016 Nov 28.
[Is] ISSN:1477-9234
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:An efficient ferrocenyl BODIPY based dark quencher has been developed and employed to construct a FRET-based fluorescent probe that contains a biotin moiety as a potential directing ligand for cancer cells and a glutathione-cleavable disulfide linker connecting the quencher and a distyryl BODIPY fluorophore. This molecular probe is deactivated in the native form through FRET followed by intramolecular charge transfer due to the ferrocenyl unit. However, upon interaction with glutathione in phosphate buffered saline and inside cancer cells, the fluorescence emission is significantly increased due to detachment of the fluorophore from the quencher. As shown by flow cytometry, this probe also exhibits preferential uptake by the biotin-receptor-expressing A549 human lung adenocarcinoma epithelial cells over the Chinese hamster ovary CHO-K1 cells used as the negative control. On the basis that both biotin receptor and GSH level are often overexpressed or elevated in cancer cells, this dual functional fluorescent probe serves as a promising agent for cancer imaging.
[Mh] Termos MeSH primário: Biotina/química
Compostos de Boro/química
Corantes Fluorescentes/química
Glutationa/análise
[Mh] Termos MeSH secundário: Células A549
Animais
Células CHO
Cricetulus
Compostos Ferrosos/química
Transferência Ressonante de Energia de Fluorescência
Seres Humanos
Neoplasias/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (4,4-difluoro-4-bora-3a,4a-diaza-s-indacene); 0 (Boron Compounds); 0 (Ferrous Compounds); 0 (Fluorescent Dyes); 6SO6U10H04 (Biotin); GAN16C9B8O (Glutathione)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180131
[Lr] Data última revisão:
180131
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161025
[St] Status:MEDLINE


  9 / 10446 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28247940
[Au] Autor:Olli KE; Li K; Galileo DS; Martin-DeLeon PA
[Ad] Endereço:Department of Biological Sciences, University of Delaware, Newark, Delaware.
[Ti] Título:Plasma membrane calcium ATPase 4 (PMCA4) co-ordinates calcium and nitric oxide signaling in regulating murine sperm functional activity.
[So] Source:J Cell Physiol;233(1):11-22, 2018 Jan.
[Is] ISSN:1097-4652
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Reduced sperm motility (asthenospermia) and resulting infertility arise from deletion of the Plasma Membrane Ca -ATPase 4 (Pmca4) gene which encodes the highly conserved Ca efflux pump, PMCA4. This is the major Ca clearance protein in murine sperm. Since the mechanism underlying asthenospermia in PMCA4's absence or reduced activity is unknown, we investigated if sperm PMCA4 negatively regulates nitric oxide synthases (NOSs) and when absent NO, peroxynitrite, and oxidative stress levels are increased. Using co-immunoprecipitation (Co-IP) and Fluorescence Resonance Energy Transfer (FRET), we show an association of PMCA4 with the NOSs in elevated cytosolic [Ca ] in capacitated and Ca ionophore-treated sperm and with neuronal (nNOS) at basal [Ca ] (ucapacitated sperm). FRET efficiencies for PMCA4-eNOS were 35% and 23% in capacitated and uncapacitated sperm, significantly (p < 0.01) different, with the molecules being <10 nm apart. For PMCA4-nNOS, this interaction was seen only for capacitated sperm where FRET efficiency was 24%, significantly (p < 0.05) higher than in uncapacitated sperm (6%). PMCA4 and the NOSs were identified as interacting partners in a quaternary complex that includes Caveolin1, which co-immunoprecipitated with eNOS in a Ca -dependent manner. In Pmca4 sperm NOS activity was elevated twofold in capacitated/uncapacitated sperm (vs. wild-type), accompanied by a twofold increase in peroxynitrite levels and significantly (p < 0.001) increased numbers of apoptotic germ cells. The data support a quaternary complex model in which PMCA4 co-ordinates Ca and NO signaling to maintain motility, with increased NO levels resulting in asthenospermia in Pmca4 males. They suggest the involvement of PMCA4 mutations in human asthenospermia, with diagnostic relevance.
[Mh] Termos MeSH primário: Astenozoospermia/enzimologia
Sinalização do Cálcio
ATPases Transportadoras de Cálcio/metabolismo
Membrana Celular/enzimologia
Óxido Nítrico/metabolismo
Motilidade Espermática
Espermatozoides/enzimologia
[Mh] Termos MeSH secundário: Animais
Apoptose
Astenozoospermia/genética
Astenozoospermia/patologia
Astenozoospermia/fisiopatologia
ATPases Transportadoras de Cálcio/deficiência
ATPases Transportadoras de Cálcio/genética
Caveolina 1/metabolismo
Fertilidade
Transferência Ressonante de Energia de Fluorescência
Predisposição Genética para Doença
Masculino
Camundongos Endogâmicos C57BL
Camundongos Endogâmicos ICR
Camundongos Knockout
Complexos Multienzimáticos
Óxido Nítrico Sintase Tipo I/metabolismo
Óxido Nítrico Sintase Tipo III/metabolismo
Estresse Oxidativo
Ácido Peroxinitroso/metabolismo
Fenótipo
Espermatozoides/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cav1 protein, mouse); 0 (Caveolin 1); 0 (Multienzyme Complexes); 14691-52-2 (Peroxynitrous Acid); 31C4KY9ESH (Nitric Oxide); EC 1.14.13.39 (Nitric Oxide Synthase Type I); EC 1.14.13.39 (Nitric Oxide Synthase Type III); EC 1.14.13.39 (Nos1 protein, mouse); EC 1.14.13.39 (Nos3 protein, mouse); EC 3.6.3.8 (Calcium-Transporting ATPases); EC 3.6.3.8 (PMCA4 protein, mouse)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:180124
[Lr] Data última revisão:
180124
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170302
[St] Status:MEDLINE
[do] DOI:10.1002/jcp.25882


  10 / 10446 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29211986
[Au] Autor:Jamiolkowski RM; Chen C; Cooperman BS; Goldman YE
[Ad] Endereço:Pennsylvania Muscle Institute, Perelman School of Medicine at the University of Pennsylvania, Philadelphia, Pennsylvania.
[Ti] Título:tRNA Fluctuations Observed on Stalled Ribosomes Are Suppressed during Ongoing Protein Synthesis.
[So] Source:Biophys J;113(11):2326-2335, 2017 Dec 05.
[Is] ISSN:1542-0086
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The pretranslocation complex of the ribosome can undergo spontaneous fluctuations of messenger RNA and transfer RNAs (tRNAs) between classical and hybrid states, and occupation of the hybrid tRNA positions has been proposed to precede translocation. The classical and hybrid state tRNA positions have been extensively characterized when the ribosome is stalled along the messenger RNA by either the absence or delayed addition of elongation factor G (EF-G), or by the presence of antibiotics or GTP analogs that block translocation. However, during multiple ongoing elongation cycles when both EF-G and ternary complexes are present, EF-G can bind to the pretranslocation complex much faster than the timescale of the classic-hybrid transitions. Using single-molecule fluorescence resonance energy transfer between adjacent tRNAs and between A-site tRNA and ribosomal protein L11, we found that the tRNAs do not fluctuate between the hybrid and classical states, but instead adopt a position with fluorescence resonance energy transfer efficiencies between those of the stalled classical and hybrid states.
[Mh] Termos MeSH primário: Biossíntese de Proteínas
RNA de Transferência/genética
Ribossomos/genética
Ribossomos/metabolismo
[Mh] Termos MeSH secundário: Transferência Ressonante de Energia de Fluorescência
Fator G para Elongação de Peptídeos/metabolismo
Proteínas Ribossômicas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Peptide Elongation Factor G); 0 (Ribosomal Proteins); 0 (ribosomal protein L11); 9014-25-9 (RNA, Transfer)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180104
[Lr] Data última revisão:
180104
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171207
[St] Status:MEDLINE



página 1 de 1045 ir para página                         
   


Refinar a pesquisa
  Base de dados : MEDLINE Formulário avançado   

    Pesquisar no campo  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

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