Base de dados : MEDLINE
Pesquisa : D12.776.580.219.500 [Categoria DeCS]
Referências encontradas : 250 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 25 ir para página                         

  1 / 250 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28404751
[Au] Autor:Hanley ML; Yoo TY; Sonnett M; Needleman DJ; Mitchison TJ
[Ad] Endereço:Department of Systems Biology, Harvard Medical School, Boston, MA 02114-5701.
[Ti] Título:Chromosomal passenger complex hydrodynamics suggests chaperoning of the inactive state by nucleoplasmin/nucleophosmin.
[So] Source:Mol Biol Cell;28(11):1444-1456, 2017 Jun 01.
[Is] ISSN:1939-4586
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The chromosomal passenger complex (CPC) is a conserved, essential regulator of cell division. As such, significant anti-cancer drug development efforts have been focused on targeting it, most notably by inhibiting its AURKB kinase subunit. The CPC is activated by AURKB-catalyzed autophosphorylation on multiple subunits, but how this regulates CPC interactions with other mitotic proteins remains unclear. We investigated the hydrodynamic behavior of the CPC in egg cytosol using sucrose gradient sedimentation and in HeLa cells using fluorescence correlation spectroscopy. We found that autophosphorylation of the CPC decreases its sedimentation coefficient in egg cytosol and increases its diffusion coefficient in live cells, indicating a decrease in mass. Using immunoprecipitation coupled with mass spectrometry and immunoblots, we discovered that inactive, unphosphorylated CPC interacts with nucleophosmin/nucleoplasmin proteins, which are known to oligomerize into pentamers and decamers. Autophosphorylation of the CPC causes it to dissociate from nucleophosmin/nucleoplasmin. We propose that nucleophosmin/nucleoplasmin complexes serve as chaperones that negatively regulate the CPC and/or stabilize its inactive form, preventing CPC autophosphorylation and recruitment to chromatin and microtubules in mitosis.
[Mh] Termos MeSH primário: Proteínas Nucleares/metabolismo
Nucleoplasminas/metabolismo
[Mh] Termos MeSH secundário: Animais
Divisão Celular
Cromatina/metabolismo
Proteínas Cromossômicas não Histona/metabolismo
Cromossomos
Células HeLa/metabolismo
Seres Humanos
Hidrodinâmica
Microtúbulos/metabolismo
Mitose
Chaperonas Moleculares/metabolismo
Fuso Acromático/metabolismo
Proteínas de Xenopus/metabolismo
Xenopus laevis/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chromatin); 0 (Chromosomal Proteins, Non-Histone); 0 (Molecular Chaperones); 0 (Nuclear Proteins); 0 (Nucleoplasmins); 0 (Xenopus Proteins); 117896-08-9 (nucleophosmin)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170414
[St] Status:MEDLINE
[do] DOI:10.1091/mbc.E16-12-0860


  2 / 250 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28007046
[Au] Autor:Wasielak M; Wiesak T; Bogacka I; Jalali BM; Bogacki M
[Ad] Endereço:Department of Gamete and Embryo Biology,Institute of Animal Reproduction and Food Research of the Polish Academy of Sciences,Tuwima 10,10-747 Olsztyn,Poland.
[Ti] Título:Maternal effect gene expression in porcine metaphase II oocytes and embryos in vitro: effect of epidermal growth factor, interleukin-1ß and leukemia inhibitory factor.
[So] Source:Zygote;25(2):120-130, 2017 Apr.
[Is] ISSN:1469-8730
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Maternal effect genes (MEG) play a crucial role in early embryogenesis. In vitro culture conditions may affect MEG expression in porcine oocytes and embryos. We investigated whether in vitro culture medium supplementation with epidermal growth factor (EGF), IL-1ß or LIF (leukemia inhibitory factor) affects the mRNA level of ZAR-1 (zygote arrest 1), NPM2 (nucleoplasmin 2) and DPPA3 (developmental associated protein 3) in porcine MII oocytes and embryos. Cumulus-oocyte complexes (COCs) were matured in NCSU-37 medium (control) or in NCSU-37 with EGF 10 ng/ml, IL-1ß 10 ng/ml or LIF 50 ng/ml. After maturation for 44-46 h, MII oocytes were preserved for the analysis of MEG mRNA levels (experiment 1). In experiment 2, COCs were fertilized, and the presumptive zygotes were cultured in the same groups. Then, 2-, 4-, 8-cell embryos, morulae and blastocysts were collected for the analysis of MEG mRNA levels. LIF addition to the maturation medium increased MII oocyte numbers (P < 0.05), while EGF and IL-1ß did not affect oocyte maturation. Medium supplementation with EGF resulted in lower DPPA3 mRNA levels in MII oocytes and in 2- and 4-cell embryos versus control embryos (P < 0.05). LIF treatment increased DPPA3 mRNA levels in morulae and blastocysts (P < 0.05). Culture with EGF and IL-1ß decreased ZAR-1 and NPM2 mRNA levels in 2-cell embryos (P < 0.05). The inclusion of EGF or IL-1ß in the porcine in vitro production system influences ZAR-1, NPM2 and DPPA3 mRNA in MII oocytes and embryos but not beyond the 4-cell stage. LIF stimulates oocyte maturation and affects DPPA3 mRNA in porcine morulae and blastocysts in vitro.
[Mh] Termos MeSH primário: Proteínas do Ovo/metabolismo
Embrião de Mamíferos/metabolismo
Fator de Crescimento Epidérmico/farmacologia
Interleucina-1beta/farmacologia
Fator Inibidor de Leucemia/farmacologia
Metáfase/fisiologia
Oócitos/metabolismo
[Mh] Termos MeSH secundário: Animais
Proteínas do Ovo/genética
Embrião de Mamíferos/citologia
Embrião de Mamíferos/efeitos dos fármacos
Desenvolvimento Embrionário/efeitos dos fármacos
Feminino
Fertilização In Vitro/veterinária
Fármacos Gastrointestinais/farmacologia
Regulação da Expressão Gênica/efeitos dos fármacos
Técnicas In Vitro
Metáfase/efeitos dos fármacos
Nucleoplasminas/metabolismo
Oócitos/citologia
Oócitos/efeitos dos fármacos
Suínos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Egg Proteins); 0 (Gastrointestinal Agents); 0 (Interleukin-1beta); 0 (Leukemia Inhibitory Factor); 0 (Nucleoplasmins); 62229-50-9 (Epidermal Growth Factor)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161224
[St] Status:MEDLINE
[do] DOI:10.1017/S0967199416000332


  3 / 250 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27983985
[Au] Autor:Lin J; Hisaoka M; Nagata K; Okuwaki M
[Ad] Endereço:PhD Program in Human Biology, School of Integrative and Global Majors, University of Tsukuba, 1-1-1, Tennodai, Tsukuba, 305-8575, Japan; Department of Infection Biology, Faculty of Medicine, University of Tsukuba, 1-1-1, Tennodai, Tsukuba, 305-8575, Japan.
[Ti] Título:Functional characterization and efficient detection of Nucleophosmin/NPM1 oligomers.
[So] Source:Biochem Biophys Res Commun;480(4):702-708, 2016 Nov 25.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:NPM1/nucleophosmin is a multifunctional and oligomeric phosphoprotein. A number of observations have suggested that changes in the oligomer formation of NPM1 could influence its biological functions, especially its oncogenic functions. To understand the functional meaning of oligomerization of NPM1/nucleophosmin, we have established a novel method to monitor protein oligomerization in cells. We utilized the split synthetic Renilla luciferase protein fragment-assisted complementation (SRL-PFAC) bioluminescence activity and observed the change of NPM1 oligomer levels under various cell culture conditions. Our study provides a method for systematic characterization of NPM1 oligomer formation changes and for screening inhibitors of NPM1 oligomerization.
[Mh] Termos MeSH primário: Proteínas Nucleares/metabolismo
Nucleoplasminas/metabolismo
[Mh] Termos MeSH secundário: Sítios de Ligação
Dimerização
Células HEK293
Células HeLa
Seres Humanos
Microscopia de Fluorescência
Ligação Proteica
Mapeamento de Interação de Proteínas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nuclear Proteins); 0 (Nucleoplasmins); 117896-08-9 (nucleophosmin)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170529
[Lr] Data última revisão:
170529
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161217
[St] Status:MEDLINE


  4 / 250 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27566850
[Au] Autor:Wasielak M; Wiesak T; Bogacka I; Jalali BM; Bogacki M
[Ad] Endereço:Department of Gamete and Embryo Biology, Institute of Animal Reproduction and Food Research of the Polish Academy of Sciences, Olsztyn, Poland. Electronic address: m.wasielak@pan.olsztyn.pl.
[Ti] Título:Zygote arrest 1, nucleoplasmin 2, and developmentally associated protein 3 mRNA profiles throughout porcine embryo development in vitro.
[So] Source:Theriogenology;86(9):2254-2262, 2016 Dec.
[Is] ISSN:1879-3231
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Maternal effect genes (MEGs) are expressed in oocytes and embryos and play an important role in activation of the embryonic genome. An abnormality in the expression of these genes may lead to arrest of embryonic cleavage or to altered transcription of factors responsible for further embryonic development. In vitro-produced porcine embryos have a lower developmental potential than embryos produced in vivo. We hypothesized that in vitro embryo culture conditions have an effect on the expression of MEGs at various developmental stages, which may affect their developmental potential. Here, using real-time polymerase chain reaction, we examined mRNA profiles of the MEGs, zygote arrest 1 (ZAR-1), nucleoplasmin 2 (NPM2), and developmentally associated pluripotency protein 3 (DPPA3), in porcine oocytes and embryos produced in vitro and in vivo. Further, we evaluated the effect of the combined addition of EGF, interleukin 1ß, and leukemia inhibitory factor to the porcine in vitro embryo production system on mRNA profiles of selected MEGs. Finally, we studied localization of the MEG protein products in in vitro-obtained oocytes and embryos using confocal microscopy. We found that the ZAR-1 mRNA profile differed throughout in vitro and in vivo embryo development. In the embryos produced in vitro, the decrease in ZAR-1 mRNA levels was observed at the 2-cell stage, whereas in in vivo embryos, ZAR-1 mRNA levels declined significantly starting at the 4-cell stage (P < 0.05). In vitro culture conditions affected transiently also DPPA3 mRNA levels at the 4-cell stage (P < 0.05). There was no difference in the NPM2 mRNA profile during in vitro and in vivo embryo development. The ZAR-1 and DPPA3 proteins were localized in the cytoplasm of the oocytes and embryos, whereas the NPM2 protein was found both in the cytoplasm and in the nucleus. All proteins were expressed until blastocyst stage. The addition of EGF and cytokines to the culture medium decreased DPPA3 mRNA levels in 8-cell embryos (P < 0.05). This study indicated that IVC conditions affect ZAR-1 mRNA levels before the 4-cell stage, which may disturb the activation of the embryonic genome in pigs. The expression of the proteins after the 4-cell to 8-cell transition indicates that these factors play a role beyond activation of the embryonic genome. Supplementation of the culture media with EGF and cytokines affects DPPA3 mRNA levels after maternal to embryonic transition.
[Mh] Termos MeSH primário: Proteínas do Ovo/metabolismo
Desenvolvimento Embrionário/fisiologia
Regulação da Expressão Gênica no Desenvolvimento/fisiologia
Nucleoplasminas/metabolismo
RNA Mensageiro/metabolismo
Suínos/embriologia
[Mh] Termos MeSH secundário: Animais
Proteínas do Ovo/genética
Técnicas de Cultura Embrionária
Fator de Crescimento Epidérmico/farmacologia
Técnicas de Maturação in Vitro de Oócitos
Interleucina-1beta/farmacologia
Fator Inibidor de Leucemia/farmacologia
Nucleoplasminas/genética
RNA Mensageiro/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Egg Proteins); 0 (Interleukin-1beta); 0 (Leukemia Inhibitory Factor); 0 (Nucleoplasmins); 0 (RNA, Messenger); 62229-50-9 (Epidermal Growth Factor)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170421
[Lr] Data última revisão:
170421
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160828
[St] Status:MEDLINE


  5 / 250 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27260798
[Au] Autor:Xi R; Lee S; Xia Y; Kim TM; Park PJ
[Ad] Endereço:School of Mathematical Sciences and Center for Statistical Science, Peking University, Beijing 100871, China ruibinxi@math.pku.edu.cn.
[Ti] Título:Copy number analysis of whole-genome data using BIC-seq2 and its application to detection of cancer susceptibility variants.
[So] Source:Nucleic Acids Res;44(13):6274-86, 2016 Jul 27.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Whole-genome sequencing data allow detection of copy number variation (CNV) at high resolution. However, estimation based on read coverage along the genome suffers from bias due to GC content and other factors. Here, we develop an algorithm called BIC-seq2 that combines normalization of the data at the nucleotide level and Bayesian information criterion-based segmentation to detect both somatic and germline CNVs accurately. Analysis of simulation data showed that this method outperforms existing methods. We apply this algorithm to low coverage whole-genome sequencing data from peripheral blood of nearly a thousand patients across eleven cancer types in The Cancer Genome Atlas (TCGA) to identify cancer-predisposing CNV regions. We confirm known regions and discover new ones including those covering KMT2C, GOLPH3, ERBB2 and PLAG1 Analysis of colorectal cancer genomes in particular reveals novel recurrent CNVs including deletions at two chromatin-remodeling genes RERE and NPM2 This method will be useful to many researchers interested in profiling CNVs from whole-genome sequencing data.
[Mh] Termos MeSH primário: Neoplasias Colorretais/genética
Variações do Número de Cópias de DNA/genética
Genoma Humano
Análise de Sequência de DNA/métodos
[Mh] Termos MeSH secundário: Algoritmos
Composição de Bases/genética
Teorema de Bayes
Proteínas de Transporte/genética
Montagem e Desmontagem da Cromatina/genética
Neoplasias Colorretais/patologia
Proteínas de Ligação a DNA/genética
Seres Humanos
Proteínas de Membrana/genética
Proteínas de Neoplasias/genética
Nucleoplasminas/genética
Receptor ErbB-2/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (DNA-Binding Proteins); 0 (GOLPH3 protein, human); 0 (MLL2 protein, human); 0 (Membrane Proteins); 0 (NPM2 protein, human); 0 (Neoplasm Proteins); 0 (Nucleoplasmins); 0 (PLAG1 protein, human); 0 (RERE protein, human); EC 2.7.10.1 (ERBB2 protein, human); EC 2.7.10.1 (Receptor, ErbB-2)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170613
[Lr] Data última revisão:
170613
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160605
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkw491


  6 / 250 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:27258022
[Au] Autor:Geraldo MT; Takeda AA; Braz AS; Lemke N
[Ad] Endereço:Laboratório de Bioinformática e Biofísica Computacional, Departamento de Física e Biofísica, Instituto de Biociências de Botucatu, UNESP - Universidade Estadual Paulista, Botucatu, SP, 18618-970, Brazil.
[Ti] Título:Bending-Twisting Motions and Main Interactions in Nucleoplasmin Nuclear Import.
[So] Source:PLoS One;11(6):e0157162, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Alpha solenoid proteins play a key role in regulating the classical nuclear import pathway, recognizing a target protein and transporting it into the nucleus. Importin-α (Impα) is the solenoid responsible for cargo protein recognition, and it has been extensively studied by X-ray crystallography to understand the binding specificity. To comprehend the main motions of Impα and to extend the information about the critical interactions during carrier-cargo recognition, we surveyed different conformational states based on molecular dynamics (MD) and normal mode (NM) analyses. Our model of study was a crystallographic structure of Impα complexed with the classical nuclear localization sequence (cNLS) from nucleoplasmin (Npl), which was submitted to multiple 100 ns of MD simulations. Representative conformations were selected for calculating the 87 lowest frequencies NMs of vibration, and a displacement approach was applied along each NM. Based on geometric criteria, using the radius of curvature and inter-repeat angles as the reference metrics, the main motions of Impα were described. Moreover, we determined the salt bridges, hydrogen bonds and hydrophobic interactions in the Impα-NplNLS interface. Our results show the bending and twisting motions participating in the recognition of nuclear proteins, allowing the accommodation and adjustment of a classical bipartite NLS sequence. The essential contacts for the nuclear import were also described and were mostly in agreement with previous studies, suggesting that the residues in the cNLS linker region establish important contacts with Impα adjusting the cNLS backbone. The MD simulations combined with NM analysis can be applied to the Impα-NLS system to help understand interactions between Impα and cNLSs and the analysis of non-classic NLSs.
[Mh] Termos MeSH primário: Nucleoplasminas/metabolismo
[Mh] Termos MeSH secundário: Transporte Ativo do Núcleo Celular/fisiologia
Núcleo Celular/metabolismo
Cristalografia por Raios X
Simulação de Acoplamento Molecular
Sinais de Localização Nuclear/metabolismo
Proteínas Nucleares/metabolismo
Transporte Proteico/fisiologia
alfa Carioferinas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nuclear Localization Signals); 0 (Nuclear Proteins); 0 (Nucleoplasmins); 0 (alpha Karyopherins)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170818
[Lr] Data última revisão:
170818
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160604
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0157162


  7 / 250 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:26649967
[Au] Autor:Huynh LM; Shinagawa T; Ishii S
[Ad] Endereço:1 Laboratory of Molecular Genetics, RIKEN Tsukuba Institute , Tsukuba, Japan .
[Ti] Título:Two Histone Variants TH2A and TH2B Enhance Human Induced Pluripotent Stem Cell Generation.
[So] Source:Stem Cells Dev;25(3):251-8, 2016 Feb 01.
[Is] ISSN:1557-8534
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:There are two major methods of reprogramming: generation of induced pluripotent stem cells (iPSCs) by overexpressing embryonic stem cell-specific transcription factors (OCT4, SOX2, KLF4, and c-MYC) and somatic cell nuclear transfer by oocyte-specific factors. Previously, we reported oocyte-enriched histone variants TH2A, TH2B, and the histone chaperone nucleoplasmin (NPM2) enhance the reprogramming by OSKM in mice by inducing open chromatin structure. In this study, we showed that human TH2A, TH2B, and NPM2 enhance the OSKM-induced reprogramming of adult and neonatal human dermal fibroblasts and umbilical vein endothelial cells. Pluripotency of iPSCs generated by coexpressing OSKM, TH2A, TH2B, and NPM2 was shown by in vitro and in vivo differentiation assays. These iPSCs gave rise to highly differentiated teratomas compared to iPSCs induced by OSKM alone. Genome-wide analysis suggests a possibility that TH2A, TH2B, and NPM2 might regulate genes that are involved in naïve stem cell stage. Thus, TH2A, TH2B, and NPM2 enhance reprogramming of human somatic cells and improve the quality of human iPSCs.
[Mh] Termos MeSH primário: Reprogramação Celular
Histonas/metabolismo
Células-Tronco Pluripotentes Induzidas/metabolismo
[Mh] Termos MeSH secundário: Fibroblastos/citologia
Fibroblastos/metabolismo
Histonas/genética
Células Endoteliais da Veia Umbilical Humana/citologia
Células Endoteliais da Veia Umbilical Humana/metabolismo
Seres Humanos
Células-Tronco Pluripotentes Induzidas/citologia
Fatores de Transcrição Kruppel-Like/genética
Fatores de Transcrição Kruppel-Like/metabolismo
Nucleoplasminas/genética
Nucleoplasminas/metabolismo
Fator 3 de Transcrição de Octâmero/genética
Fator 3 de Transcrição de Octâmero/metabolismo
Isoformas de Proteínas/genética
Isoformas de Proteínas/metabolismo
Proteínas Proto-Oncogênicas c-myc/genética
Proteínas Proto-Oncogênicas c-myc/metabolismo
Fatores de Transcrição SOXB1/genética
Fatores de Transcrição SOXB1/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (GKLF protein); 0 (Histones); 0 (Kruppel-Like Transcription Factors); 0 (NPM2 protein, human); 0 (Nucleoplasmins); 0 (Octamer Transcription Factor-3); 0 (POU5F1 protein, human); 0 (Protein Isoforms); 0 (Proto-Oncogene Proteins c-myc); 0 (SOX2 protein, human); 0 (SOXB1 Transcription Factors)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151210
[St] Status:MEDLINE
[do] DOI:10.1089/scd.2015.0264


  8 / 250 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:26476135
[Au] Autor:Vega S; Abian O; Velazquez-Campoy A
[Ad] Endereço:Institute of Biocomputation and Physics of Complex Systems (BIFI), Joint Unit IQFR-CSIC-BIFI, Universidad de Zaragoza, Zaragoza, Spain.
[Ti] Título:On the link between conformational changes, ligand binding and heat capacity.
[So] Source:Biochim Biophys Acta;1860(5):868-878, 2016 May.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Conformational changes coupled to ligand binding constitute the structural and energetics basis underlying cooperativity, allostery and, in general, protein regulation. These conformational rearrangements are associated with heat capacity changes. ITC is a unique technique for studying binding interactions because of the simultaneous determination of the binding affinity and enthalpy, and for providing the best estimates of binding heat capacity changes. SCOPE OF REVIEW: Still controversial issues in ligand binding are the discrimination between the "conformational selection model" and the "induced fit model", and whether or not conformational changes lead to temperature dependent apparent binding heat capacities. The assessment of conformational changes associated with ligand binding by ITC is discussed. In addition, the "conformational selection" and "induced fit" models are reconciled, and discussed within the context of intrinsically (partially) unstructured proteins. MAJOR CONCLUSIONS: Conformational equilibrium is a major contribution to binding heat capacity changes. A simple model may explain both conformational selection and induced fit scenarios. A temperature-independent binding heat capacity does not necessarily indicate absence of conformational changes upon ligand binding. ITC provides information on the energetics of conformational changes associated with ligand binding (and other possible additional coupled equilibria). GENERAL SIGNIFICANCE: Preferential ligand binding to certain protein states leads to an equilibrium shift that is reflected in the coupling between ligand binding and additional equilibria. This represents the structural/energetic basis of the widespread dependence of ligand binding parameters on temperature, as well as pH, ionic strength and the concentration of other chemical species.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Modelos Químicos
Nucleoplasminas/química
Receptores de LDL/química
[Mh] Termos MeSH secundário: Regulação Alostérica
Sítios de Ligação
Flavodoxina/química
Protease de HIV/química
Temperatura Alta
Seres Humanos
Cinética
Ligantes
Ligação Proteica
Conformação Proteica
Termodinâmica
Proteínas não Estruturais Virais/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Flavodoxin); 0 (LDLR protein, human); 0 (Ligands); 0 (NS3 protein, hepatitis C virus); 0 (Nucleoplasmins); 0 (Receptors, LDL); 0 (Viral Nonstructural Proteins); EC 3.4.23.- (HIV Protease); EC 3.4.23.- (p16 protease, Human immunodeficiency virus 1)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:170802
[Lr] Data última revisão:
170802
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151018
[St] Status:MEDLINE


  9 / 250 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:26435174
[Au] Autor:Rossi RO; da Cunha EV; Portela AM; Passos JR; Costa JJ; Silva AW; Saraiva MV; Peixoto CA; Donato MA; van den Hurk R; Silva JR
[Ad] Endereço:Biotechnology Nucleus of Sobral - NUBIS, Federal University of Ceara, Sobral, CE, Brazil.
[Ti] Título:Influence of BMP-2 on early follicular development and mRNA expression of oocyte specific genes in bovine preantral follicles cultured in vitro.
[So] Source:Histol Histopathol;31(3):339-48, 2016 Mar.
[Is] ISSN:1699-5848
[Cp] País de publicação:Spain
[La] Idioma:eng
[Ab] Resumo:This study evaluates the effect of different concentrations (0, 10, 50 and 100ng/mL) of bone morphogenetic protein-2 (BMP-2) on primordial and secondary follicle development. It also investigates the effects of FSH and BMP-2 on the growth, morphology, ultrastructure and expression of mRNA for GDF9, NLRP5 and NPM2 genes in secondary follicles cultured for 18 days. The presence of BMP-2 at all tested concentrations increased the development of primordial follicles in vitro, but the highest concentration of BMP-2 (100 ng/mL) reduced the percentage of normal follicles when compared with tissues cultured with 10 ng/mL BMP-2. During culture of secondary follicles, in contrast to higher concentrations (50 or 100 ng/mL), 10 ng/mL BMP-2 kept the morphology of follicles during initial stages of in vitro culture. This concentration of BMP-2 also benefits maintenance of the ultrastructure of 18-day cultured follicles. The presence of both BMP-2 and FSH in culture medium resulted in a significant (P<0.05) increase in follicular diameter after 18 days of culture. However, both FSH and BMP-2 reduced follicular mRNA expression of GDF9 and NLRP5 when compared to follicles cultured in media containing only FSH. In combination with FSH, BMP-2 reduced the mRNA levels of NPM2, when compared to follicles cultured in control medium. It is concluded from these data that 10 ng/mL BMP-2 promotes the growth of primordial in vitro and it helps to maintain the ultrastructure of secondary follicles, while FSH is more important for better expression of follicular markers like GDF9 and NLRP5.
[Mh] Termos MeSH primário: Proteína Morfogenética Óssea 2/metabolismo
Folículo Ovariano/fisiologia
[Mh] Termos MeSH secundário: Animais
Proteína Morfogenética Óssea 2/farmacologia
Bovinos
Células Cultivadas
Feminino
Hormônio Foliculoestimulante/metabolismo
Hormônio Foliculoestimulante/farmacologia
Regulação da Expressão Gênica
Fator 9 de Diferenciação de Crescimento/biossíntese
Técnicas In Vitro
Nucleoplasminas/biossíntese
Oócitos
Folículo Ovariano/efeitos dos fármacos
RNA Mensageiro/análise
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bone Morphogenetic Protein 2); 0 (Growth Differentiation Factor 9); 0 (Nucleoplasmins); 0 (RNA, Messenger); 9002-68-0 (Follicle Stimulating Hormone)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151006
[St] Status:MEDLINE
[do] DOI:10.14670/HH-11-674


  10 / 250 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:26075356
[Au] Autor:Shintomi K; Takahashi TS; Hirano T
[Ad] Endereço:Chromosome Dynamics Laboratory, RIKEN, Wako, Saitama 351-0198, Japan.
[Ti] Título:Reconstitution of mitotic chromatids with a minimum set of purified factors.
[So] Source:Nat Cell Biol;17(8):1014-23, 2015 Aug.
[Is] ISSN:1476-4679
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The assembly of mitotic chromosomes, each composed of a pair of rod-shaped chromatids, is an essential prerequisite for accurate transmission of the genome during cell division. It remains poorly understood, however, how this fundamental process might be achieved and regulated in the cell. Here we report an in vitro system in which mitotic chromatids can be reconstituted by mixing a simple substrate with only six purified factors: core histones, three histone chaperones (nucleoplasmin, Nap1 and FACT), topoisomerase II (topo II) and condensin I. We find that octameric nucleosomes containing the embryonic variant H2A.X-F are highly susceptible to FACT and function as the most productive substrate for subsequent actions of topo II and condensin I. Cdk1 phosphorylation of condensin I is the sole mitosis-specific modification required for chromatid reconstitution. This experimental system will enhance our understanding of the mechanisms of action of individual factors and their cooperation during this process.
[Mh] Termos MeSH primário: Cromátides/enzimologia
Montagem e Desmontagem da Cromatina
Histonas/metabolismo
Mitose
Chaperonas Moleculares/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Espermatozoides/enzimologia
Proteínas de Xenopus/metabolismo
[Mh] Termos MeSH secundário: Adenosina Trifosfatases/metabolismo
Animais
Proteína Quinase CDC2/metabolismo
DNA Topoisomerases Tipo II/metabolismo
Proteínas de Ligação a DNA/metabolismo
Células HeLa
Proteínas de Grupo de Alta Mobilidade/metabolismo
Histonas/genética
Seres Humanos
Masculino
Chaperonas Moleculares/genética
Complexos Multiproteicos/metabolismo
Nucleoplasminas/metabolismo
Nucleossomos/enzimologia
Fosforilação
Saccharomyces cerevisiae
Proteínas de Saccharomyces cerevisiae/genética
Fatores de Elongação da Transcrição/metabolismo
Transfecção
Proteínas de Xenopus/genética
Xenopus laevis
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA-Binding Proteins); 0 (High Mobility Group Proteins); 0 (Histones); 0 (Molecular Chaperones); 0 (Multiprotein Complexes); 0 (Nucleoplasmins); 0 (Nucleosomes); 0 (SSRP1 protein, human); 0 (Saccharomyces cerevisiae Proteins); 0 (Transcriptional Elongation Factors); 0 (Xenopus Proteins); 0 (condensin complexes); EC 2.7.11.22 (CDC2 Protein Kinase); EC 3.6.1.- (Adenosine Triphosphatases); EC 5.99.1.3 (DNA Topoisomerases, Type II)
[Em] Mês de entrada:1510
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150616
[St] Status:MEDLINE
[do] DOI:10.1038/ncb3187



página 1 de 25 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