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Pesquisa : D08.811.399.475.800 [Categoria DeCS]
Referências encontradas : 15 [refinar]
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  1 / 15 MEDLINE  
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[PMID]:28159901
[Au] Autor:Feldman S; Wuerffel R; Achour I; Wang L; Carpenter PB; Kenter AL
[Ad] Endereço:Department of Microbiology and Immunology, University of Illinois College of Medicine, Chicago, IL 60612-7344; and.
[Ti] Título:53BP1 Contributes to Locus Chromatin Topology during Class Switch Recombination.
[So] Source:J Immunol;198(6):2434-2444, 2017 Mar 15.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In B lymphocytes, Ig class switch recombination (CSR) is induced by activation-induced cytidine deaminase, which initiates a cascade of events leading to DNA double-strand break formation in switch (S) regions. Resolution of DNA double-strand breaks proceeds through formation of S-S synaptic complexes. S-S synapsis is mediated by a chromatin loop that spans the C region domain of the locus. S-S junctions are joined via a nonhomologous end joining DNA repair process. CSR occurs via an intrachromosomal looping out and deletion mechanism that is 53BP1 dependent. However, the mechanism by which 53BP1 facilitates deletional CSR and inhibits inversional switching events remains unknown. We report a novel architectural role for 53BP1 in chromatin looping in mouse B cells. Long-range interactions between the Eµ and 3'Eα enhancers are significantly diminished in the absence of 53BP1. In contrast, germline transcript promoter:3'Eα looping interactions are unaffected by 53BP1 deficiency. Furthermore, 53BP1 chromatin occupancy at sites in the locus is B cell specific, is correlated with histone H4 lysine 20 marks, and is subject to chromatin spreading. Thus, 53BP1 is required for three-dimensional organization of the locus and provides a plausible explanation for the link with 53BP1 enforcement of deletional CSR.
[Mh] Termos MeSH primário: Linfócitos B/fisiologia
Cromatina/metabolismo
Switching de Imunoglobulina
Isomerases de Ligação Enxofre-Enxofre/metabolismo
Proteína 1 de Ligação à Proteína Supressora de Tumor p53/metabolismo
[Mh] Termos MeSH secundário: Animais
Diferenciação Celular/genética
Cromatina/imunologia
Citidina Desaminase/genética
Quebras de DNA de Cadeia Dupla
Elementos Facilitadores Genéticos/genética
Loci Gênicos/genética
Histonas/genética
Histonas/metabolismo
Imunoglobulina E/genética
Cadeias Pesadas de Imunoglobulinas/genética
Cadeias Pesadas de Imunoglobulinas/metabolismo
Ativação Linfocitária/genética
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Especificidade de Órgãos/genética
Recombinação Genética
Isomerases de Ligação Enxofre-Enxofre/genética
Proteína 1 de Ligação à Proteína Supressora de Tumor p53/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chromatin); 0 (Histones); 0 (Immunoglobulin Heavy Chains); 0 (Trp53bp1 protein, mouse); 0 (Tumor Suppressor p53-Binding Protein 1); 37341-29-0 (Immunoglobulin E); EC 3.5.4.5 (Cytidine Deaminase); EC 5.3.4.- (Sulfur-Sulfur Bond Isomerases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171121
[Lr] Data última revisão:
171121
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170205
[St] Status:MEDLINE
[do] DOI:10.4049/jimmunol.1601947


  2 / 15 MEDLINE  
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[PMID]:20067421
[Au] Autor:Hayashi T
[Ti] Título:JSCTR-CTR commentary. What is the function of proline in the collagen molecule?
[So] Source:Connect Tissue Res;51(1):81, 2010.
[Is] ISSN:1607-8438
[Cp] País de publicação:England
[La] Idioma:eng
[Mh] Termos MeSH primário: Colágeno/química
Colágeno/metabolismo
Prolina/química
Prolina/metabolismo
[Mh] Termos MeSH secundário: Animais
Sítios de Ligação/fisiologia
Sítios de Ligação/efeitos da radiação
Água Corporal/química
Colágeno/efeitos da radiação
Seres Humanos
Ligações de Hidrogênio
Interações Hidrofóbicas e Hidrofílicas
Isomerismo
Peptídeos/química
Peptídeos/metabolismo
Conformação Proteica/efeitos da radiação
Estabilidade Proteica/efeitos da radiação
Estrutura Secundária de Proteína/fisiologia
Estrutura Terciária de Proteína/fisiologia
Estrutura Terciária de Proteína/efeitos da radiação
Solubilidade
Isomerases de Ligação Enxofre-Enxofre/metabolismo
Raios Ultravioleta
cis-trans-Isomerases/metabolismo
[Pt] Tipo de publicação:EDITORIAL
[Nm] Nome de substância:
0 (Peptides); 9007-34-5 (Collagen); 9DLQ4CIU6V (Proline); EC 5.2.- (cis-trans-Isomerases); EC 5.3.4.- (Sulfur-Sulfur Bond Isomerases)
[Em] Mês de entrada:1004
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:100114
[St] Status:MEDLINE
[do] DOI:10.3109/03008200903471776


  3 / 15 MEDLINE  
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[PMID]:15147323
[Au] Autor:Pantò MR; Zappalà A; Tuorto F; Cicirata F
[Ad] Endereço:Department of Physiological Science, University of Catania, Viale A. Doria, 6, 95125-Catania, Italy.
[Ti] Título:Role of the Otx1 gene in cell differentiation of mammalian cortex.
[So] Source:Eur J Neurosci;19(10):2893-902, 2004 May.
[Is] ISSN:0953-816X
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:This study analyses by immunohistochemical methods the effects of the deletion of the Otx1 gene on 12 areas of the cerebral cortex and on neurons expressing Ca-binding proteins (CaBP), such as parvalbumin (Pv) and calbindin-D28K (Cb). We found that the deletion of the Otx1 gene modified differently the various cortical areas. The decrease in cortical thickness ranged from 29.35 to 9.85% and the reduction in cellular population from 35.90 to 3.65% in the different cortical areas. The influence of the Otx1 gene concerns all cortical layers with variable effects on different cortical areas. The cellular population of cerebral cortex considered as a whole was reduced by 20.67%, Pv-positive (Pv+) cells by 58.01% and Cb-positive (Cb+) cells by 51.54%. The quantitative distribution of Pv+ and Cb+ cells varied independently in the different cortical areas. Topographic analysis of CaBP cells in Otx1-null mice (Otx1(-/-)) showed that Pv+ cells were principally distributed in layers IV and V and Cb+ cells in layers V and VI. Given that in the development of wild-type mice both cell types first appear in deep layers and later spread to superficial ones, the segregation of CaBP neurons in inner layers of Otx1(-/-) animals is an index of the immaturity of the cerebral cortex of these animals. This study showed that the Otx1 gene has a more complex role than previously reported, as it is involved in the maturation and differentiation of various cerebral cortices, and, specifically, in the development of CaBP cells.
[Mh] Termos MeSH primário: Diferenciação Celular/genética
Córtex Cerebral/citologia
Proteínas de Homeodomínio/fisiologia
Neurônios/citologia
Fatores de Transcrição/fisiologia
[Mh] Termos MeSH secundário: Animais
Calbindina 1
Calbindinas
Proteínas de Ligação ao Cálcio/metabolismo
Contagem de Células/métodos
Córtex Cerebral/metabolismo
Diagnóstico por Imagem/métodos
Proteínas de Homeodomínio/genética
Imuno-Histoquímica/métodos
Camundongos
Camundongos Transgênicos
Neurônios/metabolismo
Fatores de Transcrição Otx
Parvalbuminas/metabolismo
Proteína G de Ligação ao Cálcio S100/metabolismo
Isomerases de Ligação Enxofre-Enxofre/metabolismo
Fatores de Transcrição/genética
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Calb1 protein, mouse); 0 (Calbindin 1); 0 (Calbindins); 0 (Calcium-Binding Proteins); 0 (Homeodomain Proteins); 0 (Otx Transcription Factors); 0 (Otx1 protein, mouse); 0 (Parvalbumins); 0 (S100 Calcium Binding Protein G); 0 (Transcription Factors); EC 5.3.4.- (Ca2+-binding protein-1); EC 5.3.4.- (Sulfur-Sulfur Bond Isomerases)
[Em] Mês de entrada:0407
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:040519
[St] Status:MEDLINE


  4 / 15 MEDLINE  
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[PMID]:15140941
[Au] Autor:Zhou H; Kim SA; Kirk EA; Tippens AL; Sun H; Haeseleer F; Lee A
[Ad] Endereço:Department of Pharmacology and Center for Neurodegenerative Disease, Emory University School of Medicine, Atlanta, Georgia 30322, USA.
[Ti] Título:Ca2+-binding protein-1 facilitates and forms a postsynaptic complex with Cav1.2 (L-type) Ca2+ channels.
[So] Source:J Neurosci;24(19):4698-708, 2004 May 12.
[Is] ISSN:1529-2401
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ca2+-binding protein-1 (CaBP1) is a Ca2+-binding protein that is closely related to calmodulin (CaM) and localized in somatodendritic regions of principal neurons throughout the brain, but how CaBP1 participates in postsynaptic Ca2+ signaling is not known. Here, we describe a novel role for CaBP1 in the regulation of Ca2+ influx through Ca(v)1.2 (L-type) Ca2+ channels. CaBP1 interacts directly with the alpha1 subunit of Ca(v)1.2 at sites that also bind CaM. CaBP1 binding to one of these sites, the IQ domain, is Ca2+ dependent and competitive with CaM binding. The physiological significance of this interaction is supported by the association of Ca(v)1.2 and CaBP1 in postsynaptic density fractions purified from rat brain. Moreover, in double-label immunofluorescence experiments, CaBP1 and Ca(v)1.2 colocalize in numerous cell bodies and dendrites of neurons, particularly in pyramidal cells in the CA3 region of the hippocampus and in the dorsal cortex. In electrophysiological recordings of cells transfected with Ca(v)1.2, CaBP1 greatly prolonged Ca2+ currents, prevented Ca2+-dependent inactivation, and caused Ca2+-dependent facilitation of currents evoked by step depolarizations and repetitive stimuli. These effects contrast with those of CaM, which promoted strong Ca2+-dependent inactivation of Ca(v)1.2 with these same voltage protocols. Our findings reveal how Ca2+-binding proteins, such as CaM and CaBP1, differentially adjust Ca2+ influx through Ca(v)1.2 channels, which may specify diverse modes of Ca2+ signaling in neurons.
[Mh] Termos MeSH primário: Canais de Cálcio Tipo L/metabolismo
Proteínas de Ligação ao Cálcio/metabolismo
Isomerases de Ligação Enxofre-Enxofre/metabolismo
Sinapses/metabolismo
[Mh] Termos MeSH secundário: Animais
Ligação Competitiva/fisiologia
Química Encefálica
Cálcio/metabolismo
Canais de Cálcio Tipo L/genética
Sinalização do Cálcio/fisiologia
Calmodulina/metabolismo
Linhagem Celular
Córtex Cerebral/citologia
Córtex Cerebral/metabolismo
Hipocampo/citologia
Hipocampo/metabolismo
Seres Humanos
Substâncias Macromoleculares
Masculino
Técnicas de Patch-Clamp
Ligação Proteica/fisiologia
Estrutura Terciária de Proteína/fisiologia
Células Piramidais/metabolismo
Ratos
Ratos Sprague-Dawley
Sinapses/química
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, P.H.S.
[Nm] Nome de substância:
0 (Calcium Channels, L-Type); 0 (Calcium-Binding Proteins); 0 (Calmodulin); 0 (L-type calcium channel alpha(1C)); 0 (Macromolecular Substances); EC 5.3.4.- (Ca2+-binding protein-1); EC 5.3.4.- (Sulfur-Sulfur Bond Isomerases); SY7Q814VUP (Calcium)
[Em] Mês de entrada:0408
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:040514
[St] Status:MEDLINE


  5 / 15 MEDLINE  
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[PMID]:14711825
[Au] Autor:Chakrabarty P; Sethi DK; Padhan N; Kaur KJ; Salunke DM; Bhattacharya S; Bhattacharya A
[Ad] Endereço:School of Environmental Sciences, Jawaharlal Nehru University, New Mehrauli Road, New Delhi-110067, India.
[Ti] Título:Identification and characterization of EhCaBP2. A second member of the calcium-binding protein family of the protozoan parasite Entamoeba histolytica.
[So] Source:J Biol Chem;279(13):12898-908, 2004 Mar 26.
[Is] ISSN:0021-9258
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Entamoeba histolytica, an early branching eukaryote, is the etiologic agent of amebiasis. Calcium plays a pivotal role in the pathogenesis of amebiasis by modulating the cytopathic properties of the parasite. However, the mechanistic role of Ca(2+) and calcium-binding proteins in the pathogenesis of E. histolytica remains poorly understood. We had previously characterized a novel calcium-binding protein (EhCaBP1) from E. histolytica. Here, we report the identification and partial characterization of an isoform of this protein, EhCaBP2. Both EhCaBPs have four canonical EF-hand Ca(2+) binding domains. The two isoforms are encoded by genes of the same size (402 bp). Comparison between the two genes showed an overall identity of 79% at the nucleotide sequence level. This identity dropped to 40% in the 75-nucleotide central linker region between the second and third Ca(2+) binding domains. Both of these genes are single copy, as revealed by Southern hybridization. Analysis of the available E. histolytica genome sequence data suggested that the two genes are non-allelic. Homology-based structural modeling showed that the major differences between the two EhCaBPs lie in the central linker region, normally involved in binding target molecules. A number of studies indicated that EhCaBP1 and EhCaBP2 are functionally different. They bind different sets of E. histolytica proteins in a Ca(2+)-dependent manner. Activation of endogenous kinase was also found to be unique for the two proteins and the Ca(2+) concentration required for their optimal functionality was also different. In addition, a 12-mer peptide was identified from a random peptide library that could differentially bind the two proteins. Our data suggest that EhCaBP2 is a new member of a class of E. histolytica calcium-binding proteins involved in a novel calcium signal transduction pathway.
[Mh] Termos MeSH primário: Proteínas de Ligação ao Cálcio/química
Entamoeba histolytica/metabolismo
Isomerases de Ligação Enxofre-Enxofre/química
[Mh] Termos MeSH secundário: Alelos
Sequência de Aminoácidos
Animais
Sequência de Bases
Northern Blotting
Southern Blotting
Proteínas de Ligação ao Cálcio/metabolismo
Divisão Celular
Dicroísmo Circular
Biblioteca Gênica
Espectrometria de Massas
Modelos Moleculares
Dados de Sequência Molecular
Peptídeos/química
Filogenia
Reação em Cadeia da Polimerase
Ligação Proteica
Conformação Proteica
Isoformas de Proteínas
Estrutura Terciária de Proteína
Proteínas Recombinantes/química
Homologia de Sequência de Aminoácidos
Transdução de Sinais
Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz
Isomerases de Ligação Enxofre-Enxofre/metabolismo
Ressonância de Plasmônio de Superfície
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, P.H.S.
[Nm] Nome de substância:
0 (Calcium-Binding Proteins); 0 (Peptides); 0 (Protein Isoforms); 0 (Recombinant Proteins); EC 5.3.4.- (Ca-binding protein 2); EC 5.3.4.- (Sulfur-Sulfur Bond Isomerases)
[Em] Mês de entrada:0405
[Cu] Atualização por classe:061115
[Lr] Data última revisão:
061115
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:040109
[St] Status:MEDLINE


  6 / 15 MEDLINE  
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[PMID]:12630900
[Au] Autor:Du C; Wolfe JL
[Ad] Endereço:Department of Pharmaceutical Sciences, College of Pharmacy, University of Tennessee-Memphis, Memphis, TN 38163, U.S.A. chengan.du@hamptonu.edu
[Ti] Título:Kinetic study of recombinant human protein disulphide isomerase-assisted C125A recombinant human interleukin-2 folding.
[So] Source:Biotechnol Appl Biochem;37(Pt 2):129-38, 2003 Apr.
[Is] ISSN:0885-4513
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A kinetic model was developed to describe recombinant human protein disulphide isomerase (rhPDI)-assisted folding of a substrate protein, C125A recombinant human interleukin-2 (C125A rhIL-2). A series of progress curves showing native C125A rhIL-2 formation under different reaction conditions were generated. Non-linear regression analysis of the progress curves of rhPDI-assisted C125A rhIL-2 folding was used to fit the differential equations of the described kinetic models. The goodness-of-fit of the model to the experimental datasets was used to support or exclude a particular kinetic model of rhPDI-assisted C125A rhIL-2 folding. The results suggest that the formation of native C125A rhIL-2 results from both glutathione-dependent oxidative folding and rhPDI-catalysed folding reactions. During oxidative folding of C125A rhIL-2, both rhPDI and reduced C125A rhIL-2 aggregated in folding buffer. The aggregation rates of rhPDI and C125A rhIL-2 followed second-order kinetics. Guanidinium chloride inactivated rhPDI but also decreased the aggregation of reduced C125A rhIL-2. These results demonstrate that during rhPDI-assisted C125A rhIL-2 folding, reduced C125A rhIL-2 aggregation competes with the productive folding pathway. While rhPDI enhances the oxidative folding of C125A rhIL-2, inactivation of rhPDI by the residual guanidinium chloride compromises its catalytic efficiency. The established model can be used to optimize the folding components in the folding mixture, and thus improve the folding efficiency.
[Mh] Termos MeSH primário: Interleucina-2/química
Modelos Químicos
Modelos Moleculares
Movimento (Física)
Dobramento de Proteína
Isomerases de Ligação Enxofre-Enxofre/química
[Mh] Termos MeSH secundário: Simulação por Computador
Seres Humanos
Cinética
Substâncias Macromoleculares
Modelos Biológicos
Ligação Proteica
Proteínas Recombinantes/química
[Pt] Tipo de publicação:COMPARATIVE STUDY; EVALUATION STUDIES; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; VALIDATION STUDIES
[Nm] Nome de substância:
0 (Interleukin-2); 0 (Macromolecular Substances); 0 (Recombinant Proteins); EC 5.3.4.- (Sulfur-Sulfur Bond Isomerases)
[Em] Mês de entrada:0311
[Cu] Atualização por classe:070321
[Lr] Data última revisão:
070321
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:030313
[St] Status:MEDLINE


  7 / 15 MEDLINE  
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PubMed Central Texto completo
[PMID]:11415439
[Au] Autor:Kramer B; Ferrari DM; Klappa P; Pöhlmann N; Söling HD
[Ad] Endereço:Department of Neurobiology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, D37077 Göttingen, Germany.
[Ti] Título:Functional roles and efficiencies of the thioredoxin boxes of calcium-binding proteins 1 and 2 in protein folding.
[So] Source:Biochem J;357(Pt 1):83-95, 2001 Jul 01.
[Is] ISSN:0264-6021
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The rat luminal endoplasmic-recticulum calcium-binding proteins 1 and 2 (CaBP1 and CaBP2 respectively) are members of the protein disulphide-isomerase (PDI) family. They contain two and three thioredoxin boxes (Cys-Gly-His-Cys) respectively and, like PDI, may be involved in the folding of nascent proteins. We demonstrate here that CaBP1, similar to PDI and CaBP2, can complement the lethal phenotype of the disrupted Saccharomyces cerevisiae PDI gene, provided that the natural C-terminal Lys-Asp-Glu-Leu sequence is replaced by His-Asp-Glu-Leu. Both the in vitro RNase AIII-re-activation assays and in vivo pro-(carboxypeptidase Y) processing assays using CaBP1 and CaBP2 thioredoxin (trx)-box mutants revealed that, whereas the three trx boxes in CaBP2 seem to be functionally equivalent, the first trx box of CaBP1 is significantly more active than the second trx box. Furthermore, only about 65% re-activation of denatured reduced RNase AIII could be obtained with CaBP1 or CaBP2 compared with PDI, and the yield of PDI-catalysed reactions was significantly reduced in the presence of either CaBP1 or CaBP2. In contrast with PDI, neither CaBP1 nor CaBP2 could catalyse the renaturation of denatured glyceraldehyde-3-phosphate dehydrogenase (GAPDH), which is a redox-independent process, and neither protein had any effect on the PDI-catalysed refolding of GAPDH. Furthermore, although PDI can bind peptides via its b' domain, a property it shares with PDIp, the pancreas-specific PDI homologue, and although PDI can bind malfolded proteins such as 'scrambled' ribonuclease, no such interactions could be detected for CaBP2. We conclude that: (1) both CaBP2 and CaBP1 lack peptide-binding activity for GAPDH attributed to the C-terminal region of the a' domain of PDI; (2) CaBP2 lacks the general peptide-binding activity attributed to the b' domain of PDI; (3) interaction of CaBP2 with substrate (RNase AIII) is different from that of PDI and substrate; and (4) both CaBP2 and CaBP1 may promote oxidative folding by different kinetic pathways.
[Mh] Termos MeSH primário: Proteínas de Ligação ao Cálcio/química
Proteínas de Ligação ao Cálcio/metabolismo
Dobramento de Proteína
Saccharomyces cerevisiae/enzimologia
Isomerases de Ligação Enxofre-Enxofre/química
Isomerases de Ligação Enxofre-Enxofre/metabolismo
Tiorredoxinas/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Substituição de Aminoácidos
Animais
Proteínas de Ligação ao Cálcio/genética
Carboxipeptidases/química
Carboxipeptidases/metabolismo
Catepsina A
Retículo Endoplasmático/metabolismo
Cinética
Mutagênese Sítio-Dirigida
Plasmídeos
Regiões Promotoras Genéticas
Desnaturação Proteica
Isomerases de Dissulfetos de Proteínas/genética
Isomerases de Dissulfetos de Proteínas/metabolismo
Ratos
Ribonucleases/química
Ribonucleases/metabolismo
Saccharomyces cerevisiae/genética
Isomerases de Ligação Enxofre-Enxofre/genética
Tiorredoxinas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Calcium-Binding Proteins); 52500-60-4 (Thioredoxins); EC 3.1.- (Ribonucleases); EC 3.1.- (ribonuclease AIII); EC 3.4.- (Carboxypeptidases); EC 3.4.16.5 (Cathepsin A); EC 5.3.4.- (Ca-binding protein 2); EC 5.3.4.- (Ca2+-binding protein-1); EC 5.3.4.- (Sulfur-Sulfur Bond Isomerases); EC 5.3.4.1 (Protein Disulfide-Isomerases)
[Em] Mês de entrada:0108
[Cu] Atualização por classe:140613
[Lr] Data última revisão:
140613
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:010621
[St] Status:MEDLINE


  8 / 15 MEDLINE  
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[PMID]:12501640
[Au] Autor:Zhao M; Zhang NH
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Beijing Medical University, Beijing 100083.
[Ti] Título:[Recent advances of heterologous gene expression in E. coli].
[So] Source:Sheng Li Ke Xue Jin Zhan;29(3):226-30, 1998 Jul.
[Is] ISSN:0559-7765
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:In recent years, along with the rapid development of genetic engineering technologies, a vast amount of valuable proteins have been expressed in E. coli with high productivity. The problems concerning the productivity and purity of the heterologous proteins are no longer the major ones, as many expression system and protein purification schemes have been developed and perfected. More attention is being payed to the activity, specific activity, correct folding and intactness of the heterologous proteins. Perhaps it is the solutions to such problems that will finally lead to the maturity of the application of recombinant proteins.
[Mh] Termos MeSH primário: Escherichia coli/genética
Proteínas Recombinantes/biossíntese
[Mh] Termos MeSH secundário: Animais
Dissulfetos/metabolismo
Escherichia coli/metabolismo
Engenharia Genética
Seres Humanos
Chaperonas Moleculares/genética
Chaperonas Moleculares/fisiologia
Regiões Promotoras Genéticas/genética
Dobramento de Proteína
Proteínas Recombinantes/genética
Isomerases de Ligação Enxofre-Enxofre/metabolismo
[Pt] Tipo de publicação:ENGLISH ABSTRACT; JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Disulfides); 0 (Molecular Chaperones); 0 (Recombinant Proteins); EC 5.3.4.- (Sulfur-Sulfur Bond Isomerases)
[Em] Mês de entrada:0301
[Cu] Atualização por classe:081121
[Lr] Data última revisão:
081121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:021228
[St] Status:MEDLINE


  9 / 15 MEDLINE  
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[PMID]:9770267
[Au] Autor:Li Y; Musacchio M; Finkelstein R
[Ad] Endereço:Department of Neuroscience, University of Pennsylvania School of Medicine, Philadelphia 19104, USA.finkels@mail.med.upenn.edu.
[Ti] Título:A homologue of the calcium-binding disulfide isomerase CaBP1 is expressed in the developing CNS of Drosophila melanogaster.
[So] Source:Dev Genet;23(2):104-10, 1998.
[Is] ISSN:0192-253X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Previous studies identified a group of proteins localized to the endoplasmic reticulum (ER) that bind calcium and direct protein folding. Three of these proteins, CaBP1, CaBP2, and protein disulfide isomerase, have been purified from rat microsomes and analyzed biochemically. However, their function in vivo has not been determined. Here, we report the isolation of a homologue of the CaBP1 gene from the fruitfly Drosophila melanogaster (DmCaBP1). The predicted sequence of the Drosophila protein is very similar to that of rat CaBP1 and retains motifs thought to be functionally important in the mammalian protein. We show that DmCaBP1 is expressed in a specific spatiotemporal pattern during embryogenesis. In particular, it is expressed in midline precursor cells in the developing CNS. This is the first demonstration of tissue-specific expression for a member of this group of ER proteins and suggests a possible role for DmCABP1 as a molecular chaperone involved in nervous system development. The identification of the DmCaBP1 gene provides a basis for future genetic studies of its function.
[Mh] Termos MeSH primário: Proteínas de Ligação ao Cálcio/biossíntese
Sistema Nervoso Central/metabolismo
Drosophila melanogaster/enzimologia
Genes de Insetos
Proteínas de Insetos/biossíntese
Proteínas do Tecido Nervoso/biossíntese
Isomerases de Ligação Enxofre-Enxofre/biossíntese
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Sequência de Bases
Proteínas de Ligação ao Cálcio/genética
Sistema Nervoso Central/embriologia
Clonagem Molecular
DNA Complementar/genética
Drosophila melanogaster/embriologia
Embrião não Mamífero/metabolismo
Retículo Endoplasmático/enzimologia
Elementos Facilitadores Genéticos
Regulação da Expressão Gênica no Desenvolvimento
Proteínas de Insetos/genética
Dados de Sequência Molecular
Proteínas do Tecido Nervoso/genética
Especificidade de Órgãos
Dobramento de Proteína
Ratos
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
Especificidade da Espécie
Isomerases de Ligação Enxofre-Enxofre/genética
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, P.H.S.
[Nm] Nome de substância:
0 (Calcium-Binding Proteins); 0 (DNA, Complementary); 0 (Insect Proteins); 0 (Nerve Tissue Proteins); EC 5.3.4.- (Ca2+-binding protein-1); EC 5.3.4.- (Sulfur-Sulfur Bond Isomerases)
[Em] Mês de entrada:9811
[Cu] Atualização por classe:081121
[Lr] Data última revisão:
081121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:981014
[St] Status:MEDLINE


  10 / 15 MEDLINE  
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[PMID]:9642148
[Au] Autor:Janson IM; Toomik R; O'Farrell F; Ek P
[Ad] Endereço:Biomedical Centre, Uppsala University, Uppsala, S-751 23, Sweden. Janson@medkem.uu.se
[Ti] Título:KDEL motif interacts with a specific sequence in mammalian erd2 receptor.
[So] Source:Biochem Biophys Res Commun;247(2):447-51, 1998 Jun 18.
[Is] ISSN:0006-291X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The ER retention of lumenal proteins is achieved by a process which involves binding of escaped proteins via the C-terminal KDEL-tags to a KDEL receptor (erd2 receptor) in a post-ER compartment and return of the protein-receptor complex back to the ER. The transmembrane topology of the human KDEL receptor, which is an integral membrane protein, has been proposed. We have synthesised sets of cellulose-bound overlapping peptides covering the complete se quence of the receptor to study the interaction of the erd2 receptor with lumenal ER proteins, CaBP1 and CaBP2. At the next stage, the proposed lumenal loops of the receptor were more closely mapped. A short sequence, essential for the protein binding to the most efficient binding site of the receptor, was identified as 22KIWK25, which is in accordance with one of the proposed structural models of the receptor. The binding was of high specificity and was almost completely inhibited by KDEL-containing soluble peptides. The phosphorylation state of CaBP1/CaBP2 did not affect their binding to the KDEL receptor.
[Mh] Termos MeSH primário: Proteínas de Membrana/genética
Proteínas de Membrana/metabolismo
Oligopeptídeos/metabolismo
Sinais Direcionadores de Proteínas
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Albuminas/metabolismo
Sequência de Aminoácidos
Sítios de Ligação/genética
Proteínas de Ligação ao Cálcio/química
Proteínas de Ligação ao Cálcio/metabolismo
Retículo Endoplasmático/metabolismo
Seres Humanos
Técnicas In Vitro
Proteínas de Membrana/química
Fragmentos de Peptídeos/química
Fragmentos de Peptídeos/genética
Fragmentos de Peptídeos/metabolismo
Fosforilação
Ligação Proteica
Receptores de Peptídeos/química
Receptores de Peptídeos/genética
Receptores de Peptídeos/metabolismo
Isomerases de Ligação Enxofre-Enxofre/química
Isomerases de Ligação Enxofre-Enxofre/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Albumins); 0 (Calcium-Binding Proteins); 0 (KDEL receptor); 0 (KDELR1 protein, human); 0 (Membrane Proteins); 0 (Oligopeptides); 0 (Peptide Fragments); 0 (Protein Sorting Signals); 0 (Receptors, Peptide); 113516-56-6 (lysyl-aspartyl-glutamyl-leucine); 8L70Q75FXE (Adenosine Triphosphate); EC 5.3.4.- (Ca-binding protein 2); EC 5.3.4.- (Ca2+-binding protein-1); EC 5.3.4.- (Sulfur-Sulfur Bond Isomerases)
[Em] Mês de entrada:9807
[Cu] Atualização por classe:141120
[Lr] Data última revisão:
141120
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:980627
[St] Status:MEDLINE



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