Base de dados : MEDLINE
Pesquisa : G01.154 [Categoria DeCS]
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[PMID]:29351321
[Au] Autor:Khan MA; Arif Z; Khan MA; Moinuddin; Alam K
[Ad] Endereço:Department of Biochemistry, J.N. Medical College, Faculty of Medicine, Aligarh Muslim University, Aligarh, Uttar Pradesh, India.
[Ti] Título:Methylglyoxal produces more changes in biochemical and biophysical properties of human IgG under high glucose compared to normal glucose level.
[So] Source:PLoS One;13(1):e0191014, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Hyperglycaemia triggers increased production of methylglyoxal which can cause gross modification in proteins' structure vis-a-vis function though advanced glycation end products (AGEs). The AGEs may initiate vascular and nonvascular pathologies. In this study, we have examined the biochemical and biophysical changes in human IgG under normal and high glucose after introducing methylglyoxal into the assay mixture. This non-enzymatic reaction mainly engaged lysine residues as indicated by TNBS results. The UV results showed hyperchromicity in modified-IgG samples while fluorescence data supported AGEs formation during the course of reaction. Shift in amide I and amide II band position indicated perturbations in secondary structure. Increase carbonyl content and decrease in sulfhydryl suggests that the modification is accompanied by oxidative stress. All modified-IgG samples showed more thermostability than native IgG; the highest Tm was shown by IgG-high glucose-MGO variant. Results of ANS, Congo red and Thioflavin T dyes clearly suggest increase in hydrophobic patches and aggregation, respectively. SEM and TEM images support aggregates generation in modified-IgG samples.
[Mh] Termos MeSH primário: Glucose/química
Imunoglobulina G/química
Aldeído Pirúvico/farmacologia
[Mh] Termos MeSH secundário: Fenômenos Biofísicos
Seres Humanos
Microscopia Eletrônica de Varredura
Microscopia Eletrônica de Transmissão
Estresse Oxidativo
Desnaturação Proteica
Espectrometria de Fluorescência
Espectrofotometria Ultravioleta
Espectroscopia de Infravermelho com Transformada de Fourier
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Immunoglobulin G); 722KLD7415 (Pyruvaldehyde); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180120
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191014


  2 / 13814 MEDLINE  
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[PMID]:29317637
[Au] Autor:McCoy DE; Feo T; Harvey TA; Prum RO
[Ad] Endereço:Department of Organismic and Evolutionary Biology, Harvard University, Cambridge, MA, 02138, USA. dakotamccoy@g.harvard.edu.
[Ti] Título:Structural absorption by barbule microstructures of super black bird of paradise feathers.
[So] Source:Nat Commun;9(1):1, 2018 01 09.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Many studies have shown how pigments and internal nanostructures generate color in nature. External surface structures can also influence appearance, such as by causing multiple scattering of light (structural absorption) to produce a velvety, super black appearance. Here we show that feathers from five species of birds of paradise (Aves: Paradisaeidae) structurally absorb incident light to produce extremely low-reflectance, super black plumages. Directional reflectance of these feathers (0.05-0.31%) approaches that of man-made ultra-absorbent materials. SEM, nano-CT, and ray-tracing simulations show that super black feathers have titled arrays of highly modified barbules, which cause more multiple scattering, resulting in more structural absorption, than normal black feathers. Super black feathers have an extreme directional reflectance bias and appear darkest when viewed from the distal direction. We hypothesize that structurally absorbing, super black plumage evolved through sensory bias to enhance the perceived brilliance of adjacent color patches during courtship display.
[Mh] Termos MeSH primário: Plumas/ultraestrutura
Luz
Passeriformes/fisiologia
[Mh] Termos MeSH secundário: Animais
Fenômenos Biofísicos
Simulação por Computador
Plumas/fisiologia
Processamento de Imagem Assistida por Computador
Masculino
Microscopia Eletrônica de Varredura
Especificidade da Espécie
Tomografia Computadorizada por Raios X/métodos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[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:180111
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02088-w


  3 / 13814 MEDLINE  
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[PMID]:29424215
[Au] Autor:Chesnokova MG; Shalai VV; Kraus YA; Mironov AY; Blinova EG
[Ti] Título:[Informative indices of the biocorrosion activity for the determination of the character of the aggression ground].
[So] Source:Gig Sanit;95(6):513-7, 2016.
[Is] ISSN:0016-9900
[Cp] País de publicação:Russia (Federation)
[La] Idioma:rus
[Ab] Resumo:Underground corrosion is referred to the most difficult types of corrosion in connection with that it is multifactorial and differs in progressive dynamics of the participation of each parameter in the process of destruction of the metal. With the aim of the evaluation of the informativeness of the index of the biocorrosion activity caused by the influence of various factors to determine the character of the soil aggressiveness in the district of pipeline laying there was studied the complex of microbiological and physical-chemical indices). There was determined the amount of sulfur cycle bacteria (autotrophic thiobacteria and sulphate-reducing bacteria), the total concentration of sulfur and iron in the soil samples adjacent to the surface of the underground pipelines in the territory of the Khanty-Mansi Autonomous District of Yugra, and the ratio of these indices with a specific electrical resistance of the soil. There was established the predominance ofsamples with weak aggressiveness of the soil (55.17% of cases), with the criterion ofbiocorrosion soil activity of 2,44 ± 0,19. The results show significant differences in the thiobacteria content and mobile iron in the studied soil-ground samples. There was revealed a direct correlation of the average force of concentrations of identified bacteria and iron content in the soil. There was shown the necessity of the implementation of dynamic control and the development of methods of protection of metal structures to prevent biocorrosion in the design and in the process of the operation of the pipeline.
[Mh] Termos MeSH primário: Fenômenos Bioquímicos
Fenômenos Biofísicos
Microbiologia do Solo
Solo/química
[Mh] Termos MeSH secundário: Corrosão
Ecossistema
Bactérias Gram-Negativas Quimiolitotróficas/isolamento & purificação
Bactérias Redutoras de Enxofre/isolamento & purificação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Soil)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180301
[Lr] Data última revisão:
180301
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180210
[St] Status:MEDLINE


  4 / 13814 MEDLINE  
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[PMID]:29324815
[Au] Autor:Yerabham ASK; Müller-Schiffmann A; Ziehm T; Stadler A; Köber S; Indurkhya X; Marreiros R; Trossbach SV; Bradshaw NJ; Prikulis I; Willbold D; Weiergräber OH; Korth C
[Ad] Endereço:Department of Neuropathology, Heinrich Heine University Düsseldorf, Düsseldorf, Germany.
[Ti] Título:Biophysical insights from a single chain camelid antibody directed against the Disrupted-in-Schizophrenia 1 protein.
[So] Source:PLoS One;13(1):e0191162, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Accumulating evidence suggests an important role for the Disrupted-in-Schizophrenia 1 (DISC1) protein in neurodevelopment and chronic mental illness. In particular, the C-terminal 300 amino acids of DISC1 have been found to mediate important protein-protein interactions and to harbor functionally important phosphorylation sites and disease-associated polymorphisms. However, long disordered regions and oligomer-forming subdomains have so far impeded structural analysis. VHH domains derived from camelid heavy chain only antibodies are minimal antigen binding modules with appreciable solubility and stability, which makes them well suited for the stabilizing proteins prior to structural investigation. Here, we report on the generation of a VHH domain derived from an immunized Lama glama, displaying high affinity for the human DISC1 C region (aa 691-836), and its characterization by surface plasmon resonance, size exclusion chromatography and immunological techniques. The VHH-DISC1 (C region) complex was also used for structural investigation by small angle X-ray scattering analysis. In combination with molecular modeling, these data support predictions regarding the three-dimensional fold of this DISC1 segment as well as its steric arrangement in complex with our VHH antibody.
[Mh] Termos MeSH primário: Camelídeos Americanos/imunologia
Proteínas do Tecido Nervoso/imunologia
Anticorpos de Cadeia Única/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Complexo Antígeno-Anticorpo/química
Complexo Antígeno-Anticorpo/genética
Reações Antígeno-Anticorpo
Fenômenos Biofísicos
Camelídeos Americanos/genética
Mapeamento de Epitopos
Feminino
Seres Humanos
Cadeias Pesadas de Imunoglobulinas/química
Cadeias Pesadas de Imunoglobulinas/genética
Camundongos
Modelos Moleculares
Proteínas do Tecido Nervoso/química
Proteínas do Tecido Nervoso/genética
Fragmentos de Peptídeos/química
Fragmentos de Peptídeos/genética
Fragmentos de Peptídeos/imunologia
Domínios e Motivos de Interação entre Proteínas
Espalhamento a Baixo Ângulo
Anticorpos de Cadeia Única/genética
Ressonância de Plasmônio de Superfície
Difração de Raios X
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antigen-Antibody Complex); 0 (DISC1 protein, human); 0 (Disc1 protein, mouse); 0 (Immunoglobulin Heavy Chains); 0 (Nerve Tissue Proteins); 0 (Peptide Fragments); 0 (Single-Chain Antibodies)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180112
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191162


  5 / 13814 MEDLINE  
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[PMID]:29262375
[Au] Autor:Cochet-Escartin O; Locke TT; Shi WH; Steele RE; Collins ES
[Ad] Endereço:Department of Physics, University of California, San Diego, La Jolla, California.
[Ti] Título:Physical Mechanisms Driving Cell Sorting in Hydra.
[So] Source:Biophys J;113(12):2827-2841, 2017 Dec 19.
[Is] ISSN:1542-0086
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cell sorting, whereby a heterogeneous cell mixture organizes into distinct tissues, is a fundamental patterning process in development. Hydra is a powerful model system for carrying out studies of cell sorting in three dimensions, because of its unique ability to regenerate after complete dissociation into individual cells. The physicists Alfred Gierer and Hans Meinhardt recognized Hydra's self-organizing properties more than 40 years ago. However, what drives cell sorting during regeneration of Hydra from cell aggregates is still debated. Differential motility and differential adhesion have been proposed as driving mechanisms, but the available experimental data are insufficient to distinguish between these two. Here, we answer this longstanding question by using transgenic Hydra expressing fluorescent proteins and a multiscale experimental and numerical approach. By quantifying the kinematics of single cell and whole aggregate behaviors, we show that no differences in cell motility exist among cell types and that sorting dynamics follow a power law with an exponent of ∼0.5. Additionally, we measure the physical properties of separated tissues and quantify their viscosities and surface tensions. Based on our experimental results and numerical simulations, we conclude that tissue interfacial tensions are sufficient to explain cell sorting in aggregates of Hydra cells. Furthermore, we demonstrate that the aggregate's geometry during sorting is key to understanding the sorting dynamics and explains the exponent of the power law behavior. Our results answer the long standing question of the physical mechanisms driving cell sorting in Hydra cell aggregates. In addition, they demonstrate how powerful this organism is for biophysical studies of self-organization and pattern formation.
[Mh] Termos MeSH primário: Fenômenos Biofísicos
Hydra/citologia
[Mh] Termos MeSH secundário: Animais
Adesão Celular
Agregação Celular
Modelos Biológicos
Análise de Célula Única
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180210
[Lr] Data última revisão:
180210
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171221
[St] Status:MEDLINE


  6 / 13814 MEDLINE  
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[PMID]:29205241
[Au] Autor:Dong G; Ryde U; Aa Jensen HJ; Hedegård ED
[Ad] Endereço:Department of Theoretical Chemistry, Lund University, Chemical Centre, P. O. Box 124, SE-221 00 Lund, Sweden. ulf.ryde@teokem.lu.se erik.hedegard@teokem.lu.se.
[Ti] Título:Exploration of H binding to the [NiFe]-hydrogenase active site with multiconfigurational density functional theory.
[So] Source:Phys Chem Chem Phys;20(2):794-801, 2018 Jan 03.
[Is] ISSN:1463-9084
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The combination of density functional theory (DFT) with a multiconfigurational wave function is an efficient way to include dynamical correlation in calculations with multiconfiguration self-consistent field wave functions. These methods can potentially be employed to elucidate reaction mechanisms in bio-inorganic chemistry, where many other methods become either too computationally expensive or too inaccurate. In this paper, a complete active space (CAS) short-range DFT (CAS-srDFT) hybrid was employed to investigate a bio-inorganic system, namely H binding to the active site of [NiFe] hydrogenase. This system was previously investigated with coupled-cluster (CC) and multiconfigurational methods in the form of cumulant-approximated second-order perturbation theory, based on the density matrix renormalization group (DMRG). We find that it is more favorable for H to bind to Ni than to Fe, in agreement with previous CC and DMRG calculations. The accuracy of CAS-srDFT is comparable to both CC and DMRG, despite much smaller active spaces were employed than in the corresponding DMRG calculations. This enhanced efficiency at the smaller active spaces shows that CAS-srDFT can become a useful method for bio-inorganic chemistry.
[Mh] Termos MeSH primário: Hidrogenase/química
Modelos Moleculares
[Mh] Termos MeSH secundário: Fenômenos Biofísicos
Domínio Catalítico
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 1.12.- (nickel-iron hydrogenase); EC 1.12.7.2 (Hydrogenase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180209
[Lr] Data última revisão:
180209
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171206
[St] Status:MEDLINE
[do] DOI:10.1039/c7cp06767d


  7 / 13814 MEDLINE  
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[PMID]:28746830
[Au] Autor:Gilardi A; Bhamidimarri SP; Brönstrup M; Bilitewski U; Marreddy RKR; Pos KM; Benier L; Gribbon P; Winterhalter M; Windshügel B
[Ad] Endereço:Fraunhofer Institute for Molecular Biology and Applied Ecology IME, Department Screening Port, Schnackenburgallee 114, 22525 Hamburg, Germany; Jacobs University Bremen, Campus Ring 1, 28759 Bremen, Germany.
[Ti] Título:Biophysical characterization of E. coli TolC interaction with the known blocker hexaamminecobalt.
[So] Source:Biochim Biophys Acta;1861(11 Pt A):2702-2709, 2017 11.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The tripartite efflux pump AcrAB-TolC in E. coli is involved in drug resistance by transporting antibiotics out of the cell. The outer membrane protein TolC can be blocked by various cations, including hexaamminecobalt, thereby TolC represents a potential target for reducing antimicrobial resistance as its blockage may improve efficacy of antibiotics. METHODS: We utilized single channel electrophysiology measurements for studying TolC conductance in the absence and presence of the known TolC blocker hexaamminecobalt. Association and dissociation constants of hexaamminecobalt were determined using surface plasmon resonance measurements. Minimum inhibitory concentration (MIC) assays in the absence and presence of antibiotics were carried out for investigating the antibacterial effect of hexaamminecobalt and its potential to reduce MICs. RESULTS: TolC gating in the absence of any ligand is voltage dependent and asymmetric at high applied voltages. Hexaamminecobalt binds to TolC with high affinity and kinetic data revealed fast association and dissociation rates. Despite potent binding to TolC, hexaamminecobalt does not possess an intrinsic antimicrobial activity against E. coli nor does it reduce MIC values of antibiotics erythromycin and fusidic acid. CONCLUSIONS: TolC opening can be effectively blocked by small molecules. More potent channel blockers are needed in order to investigate the eligibility of TolC as drug target. GENERAL SIGNIFICANCE: TolC, a potentially interesting pharmaceutical target can be addressed by small molecules, blocking the channel. Biophysical characterization of the binding processes will support future identification and optimisation of more potent TolC blockers in order to validate TolC as a pharmaceutical target.
[Mh] Termos MeSH primário: Proteínas da Membrana Bacteriana Externa/química
Farmacorresistência Bacteriana Múltipla/genética
Proteínas de Escherichia coli/química
Escherichia coli/efeitos dos fármacos
Proteínas de Membrana Transportadoras/química
[Mh] Termos MeSH secundário: Proteínas da Membrana Bacteriana Externa/antagonistas & inibidores
Proteínas da Membrana Bacteriana Externa/efeitos dos fármacos
Proteínas da Membrana Bacteriana Externa/genética
Fenômenos Biofísicos
Cobalto/farmacologia
Farmacorresistência Bacteriana Múltipla/efeitos dos fármacos
Escherichia coli/genética
Proteínas de Escherichia coli/antagonistas & inibidores
Proteínas de Escherichia coli/genética
Regulação Bacteriana da Expressão Gênica/efeitos dos fármacos
Proteínas de Membrana Transportadoras/genética
Ressonância de Plasmônio de Superfície
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Outer Membrane Proteins); 0 (Escherichia coli Proteins); 0 (Membrane Transport Proteins); 0 (tolC protein, E coli); 15365-75-0 (hexaamminecobalt(II)); 3G0H8C9362 (Cobalt)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180208
[Lr] Data última revisão:
180208
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170727
[St] Status:MEDLINE


  8 / 13814 MEDLINE  
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[PMID]:29183939
[Au] Autor:Kumar A; Placone JK; Engler AJ
[Ad] Endereço:Department of Bioengineering, University of California, San Diego, La Jolla, CA 92093, USA.
[Ti] Título:Understanding the extracellular forces that determine cell fate and maintenance.
[So] Source:Development;144(23):4261-4270, 2017 Dec 01.
[Is] ISSN:1477-9129
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Stem cells interpret signals from their microenvironment while simultaneously modifying the niche through secreting factors and exerting mechanical forces. Many soluble stem cell cues have been determined over the past century, but in the past decade, our molecular understanding of mechanobiology has advanced to explain how passive and active forces induce similar signaling cascades that drive self-renewal, migration, differentiation or a combination of these outcomes. Improvements in stem cell culture methods, materials and biophysical tools that assess function have improved our understanding of these cascades. Here, we summarize these advances and offer perspective on ongoing challenges.
[Mh] Termos MeSH primário: Células-Tronco/fisiologia
[Mh] Termos MeSH secundário: Actomiosina/fisiologia
Animais
Fenômenos Biomecânicos
Fenômenos Biofísicos
Técnicas de Cultura de Células
Diferenciação Celular/fisiologia
Montagem e Desmontagem da Cromatina/fisiologia
Matriz Extracelular/fisiologia
Seres Humanos
Transdução de Sinais
Nicho de Células-Tronco/fisiologia
Células-Tronco/citologia
Fatores de Transcrição/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Transcription Factors); 9013-26-7 (Actomyosin)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171204
[Lr] Data última revisão:
171204
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171130
[St] Status:MEDLINE
[do] DOI:10.1242/dev.158469


  9 / 13814 MEDLINE  
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[PMID]:29183936
[Au] Autor:Graner F; Riveline D
[Ad] Endereço:Laboratoire Matière et Systèmes Complexes, Université Denis Diderot - Paris 7, CNRS UMR 7057, 75205 Paris Cedex 13, France francois.graner@univ-paris-diderot.fr riveline@unistra.fr.
[Ti] Título:'The Forms of Tissues, or Cell-aggregates': D'Arcy Thompson's influence and its limits.
[So] Source:Development;144(23):4226-4237, 2017 Dec 01.
[Is] ISSN:1477-9129
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In two chapters of his book , D'Arcy Thompson used numerous biological and physical observations to show how principles from mathematics and physics - such as pressure differences, surface tension and viscosity - could explain cell shapes and packing within tissues. In this Review, we depict influences that enabled the genesis of his ideas, report examples of his visionary observations and trace his impact over the past 100 years. Recently, his ideas have been revisited as a new field of research emerged, linking cell-level physics with epithelial tissue structure and development. We critically discuss the potential and the limitations of both Thompson's and the modern approaches.
[Mh] Termos MeSH primário: Biologia do Desenvolvimento
[Mh] Termos MeSH secundário: Animais
Fenômenos Biofísicos
Agregação Celular
Forma Celular
Seres Humanos
Modelos Biológicos
Morfogênese
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171204
[Lr] Data última revisão:
171204
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171130
[St] Status:MEDLINE
[do] DOI:10.1242/dev.151233


  10 / 13814 MEDLINE  
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[PMID]:29020104
[Au] Autor:Aik WS; Lin MH; Tan D; Tripathy A; Marzluff WF; Dominski Z; Chou CY; Tong L
[Ad] Endereço:Department of Biological Sciences, Columbia University, New York, New York, United States of America.
[Ti] Título:The N-terminal domains of FLASH and Lsm11 form a 2:1 heterotrimer for histone pre-mRNA 3'-end processing.
[So] Source:PLoS One;12(10):e0186034, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Unlike canonical pre-mRNAs, animal replication-dependent histone pre-mRNAs lack introns and are processed at the 3'-end by a mechanism distinct from cleavage and polyadenylation. They have a 3' stem loop and histone downstream element (HDE) that are recognized by stem-loop binding protein (SLBP) and U7 snRNP, respectively. The N-terminal domain (NTD) of Lsm11, a component of U7 snRNP, interacts with FLASH NTD and these two proteins recruit the histone cleavage complex containing the CPSF-73 endonuclease for the cleavage reaction. Here, we determined crystal structures of FLASH NTD and found that it forms a coiled-coil dimer. Using solution light scattering, we characterized the stoichiometry of the FLASH NTD-Lsm11 NTD complex and found that it is a 2:1 heterotrimer, which is supported by observations from analytical ultracentrifugation and crosslinking.
[Mh] Termos MeSH primário: Proteínas de Transporte/química
Proteínas de Transporte/metabolismo
Histonas/metabolismo
Multimerização Proteica
Precursores de RNA/metabolismo
Processamento Pós-Transcricional do RNA
Proteínas de Ligação a RNA/química
Proteínas de Ligação a RNA/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Fenômenos Biofísicos
Cromatografia em Gel
Cristalografia por Raios X
Cisteína/genética
Luz
Mutação/genética
Ligação Proteica
Domínios Proteicos
Estrutura Secundária de Proteína
Espalhamento de Radiação
Alinhamento de Sequência
Ultracentrifugação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (Histones); 0 (RNA Precursors); 0 (RNA-Binding Proteins); K848JZ4886 (Cysteine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171101
[Lr] Data última revisão:
171101
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171012
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0186034



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