Base de dados : MEDLINE
Pesquisa : D02.033.800.175 [Categoria DeCS]
Referências encontradas : 283 [refinar]
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[PMID]:28438511
[Au] Autor:Tonazzi A; Giangregorio N; Console L; De Palma A; Indiveri C
[Ad] Endereço:CNR Institute of Biomembranes, Bioenergetics and Molecular Biotechnology, via Amendola 165/A, 70126 Bari, Italy.
[Ti] Título:Nitric oxide inhibits the mitochondrial carnitine/acylcarnitine carrier through reversible S-nitrosylation of cysteine 136.
[So] Source:Biochim Biophys Acta;1858(7):475-482, 2017 07.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:S-nitrosylation of the mitochondrial carnitine/acylcarnitine transporter (CACT) has been investigated on the native and the recombinant proteins reconstituted in proteoliposomes, and on intact mitochondria. The widely-used NO-releasing compound, GSNO, strongly inhibited the antiport measured in proteoliposomes reconstituted with the native CACT from rat liver mitochondria or the recombinant rat CACT over-expressed in E. coli. Inhibition was reversed by the reducing agent dithioerythritol, indicating a reaction mechanism based on nitrosylation of Cys residues of the CACT. The half inhibition constant (IC50) was very similar for the native and recombinant proteins, i.e., 74 and 71µM, respectively. The inhibition resulted to be competitive with respect the substrate, carnitine. NO competed also with NEM, correlating well with previous data showing interference of NEM with the substrate transport path. Using a site-directed mutagenesis approach on Cys residues of the recombinant CACT, the target of NO was identified. C136 plays a major role in the reaction mechanism. The occurrence of S-nitrosylation was demonstrated in intact mitochondria after treatment with GSNO, immunoprecipitation and immunostaining of CACT with a specific anti NO-Cys antibody. In parallel samples, transport activity of CACT measured in intact mitochondria, was strongly inhibited after GSNO treatment. The possible physiological and pathological implications of the post-translational modification of CACT are discussed.
[Mh] Termos MeSH primário: Carnitina Aciltransferases/antagonistas & inibidores
Cisteína/química
Mitocôndrias/metabolismo
Óxido Nítrico/farmacologia
Processamento de Proteína Pós-Traducional
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Transporte Biológico
Carnitina/análogos & derivados
Carnitina/metabolismo
Carnitina Aciltransferases/química
Carnitina Aciltransferases/genética
Carnitina Aciltransferases/metabolismo
Sequência Conservada
Ditioeritritol/farmacologia
Lipossomos
Mitocôndrias/efeitos dos fármacos
Modelos Moleculares
Doadores de Óxido Nítrico/farmacologia
Nitrogênio
Oxirredução
Conformação Proteica
Processamento de Proteína Pós-Traducional/efeitos dos fármacos
Ratos
S-Nitrosoglutationa/farmacologia
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Liposomes); 0 (Nitric Oxide Donors); 0 (acylcarnitine); 31C4KY9ESH (Nitric Oxide); 57564-91-7 (S-Nitrosoglutathione); 6892-68-8 (Dithioerythritol); EC 2.3.1.- (Carnitine Acyltransferases); EC 2.3.1.- (Slc25a20 protein, rat); K848JZ4886 (Cysteine); N762921K75 (Nitrogen); S7UI8SM58A (Carnitine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171027
[Lr] Data última revisão:
171027
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170426
[St] Status:MEDLINE


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[PMID]:28414288
[Au] Autor:Stepovaya EA; Shakhristova EV; Nosareva OL; Rudikov EV; Egorova MY; Egorova DY; Novitsky VV
[Ad] Endereço:Siberian State Medical University, Tomsk, Russia.
[Ti] Título:[Redox-dependent mechanisms of regulation of breast epithelial cell proliferation].
[Ti] Título:Redoks-zavisimye mekhanizmy reguliatsii proliferatsii kletok épiteliia molochnoi zhelezy..
[So] Source:Biomed Khim;63(2):159-164, 2017 Mar.
[Is] ISSN:2310-6972
[Cp] País de publicação:Russia (Federation)
[La] Idioma:rus
[Ab] Resumo:Activation of free radical oxidation in different cell types, including breast epithelial cells, may result in damage to macromolecules, in particular, proteins taking part in regulation of cell proliferation and apoptosis. The glutathione, glutaredoxin and thioredoxin systems play an essential role in maintaining intracellular redox homeostasis. Due to this fact, modulation of cellular redox status under the effect of an SH group inhibitor and an SH group protector may be used as a model for studying the role of redox proteins and glutathione in regulating cell proliferation in different pathological processes. In this study we have evaluated the state of the thioredoxin, glutaredoxin and glutathione systems as well as their role in regulating proliferation of HBL-100 breast epithelial cells under redox status modulation with N-ethylmaleimide (NEM) and 1,4-dithioerythriol (DTE). Modulating the redox status of breast epithelial cells under the effect of NEM and DTE influences the functional activity of glutathione-dependent enzymes, glutaredoxin, thioredoxin, and thioredoxin reductase through changes in the GSH and GSSG concentrations. In HBL-100 cells under redox-status modulation, we have found an increase in the number of cells in the S-phase of the cell cycle and a decrease in the number of cells in the G0/G1 and G2/М phases, as opposed to the values in the intact culture. The proposed model of proliferative activity of cells under redox status modulation may be used for development of new therapeutic approaches for treatment of diseases accompanied by oxidative stress generation.
[Mh] Termos MeSH primário: Ditioeritritol/farmacologia
Inibidores Enzimáticos/farmacologia
Células Epiteliais/efeitos dos fármacos
Etilmaleimida/farmacologia
Substâncias Protetoras/farmacologia
[Mh] Termos MeSH secundário: Catalase/metabolismo
Ciclo Celular/efeitos dos fármacos
Linhagem Celular
Proliferação Celular/efeitos dos fármacos
Células Epiteliais/citologia
Células Epiteliais/metabolismo
Etilmaleimida/antagonistas & inibidores
Citometria de Fluxo
Glutarredoxinas/metabolismo
Glutationa/metabolismo
Glutationa Peroxidase/metabolismo
Glutationa Redutase/metabolismo
Seres Humanos
Glândulas Mamárias Humanas/citologia
Glândulas Mamárias Humanas/efeitos dos fármacos
Glândulas Mamárias Humanas/metabolismo
Oxirredução
Estresse Oxidativo/efeitos dos fármacos
Tiorredoxina Dissulfeto Redutase/metabolismo
Tiorredoxinas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (GLRX protein, human); 0 (Glutaredoxins); 0 (Protective Agents); 0 (TXN protein, human); 52500-60-4 (Thioredoxins); 6892-68-8 (Dithioerythritol); EC 1.11.1.6 (Catalase); EC 1.11.1.9 (Glutathione Peroxidase); EC 1.8.1.7 (Glutathione Reductase); EC 1.8.1.9 (Thioredoxin-Disulfide Reductase); GAN16C9B8O (Glutathione); O3C74ACM9V (Ethylmaleimide)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170912
[Lr] Data última revisão:
170912
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170418
[St] Status:MEDLINE
[do] DOI:10.18097/PBMC20176302159


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[PMID]:28323102
[Au] Autor:Zhou Z; Forbes RT; D'Emanuele A
[Ad] Endereço:School of Pharmacy and Biomedical Sciences, University of Central Lancashire, Preston PR1 2HE, UK. Electronic address: ZZhou2@uclan.ac.uk.
[Ti] Título:Preparation of core-crosslinked linear-dendritic copolymer micelles with enhanced stability and their application for drug solubilisation.
[So] Source:Int J Pharm;523(1):260-269, 2017 May 15.
[Is] ISSN:1873-3476
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:In this study we explore the preparation of core-crosslinked micelles of linear-dendritic methoxy-poly(ethylene glycol) (MPEG)-co-poly(ester-sulfide) (PES) polymers to improve the stability of such polymeric micelle systems against premature disintegration and drug release. A series of MPEG-PES copolymers were synthesised via stepwise reactions of acetylation and thiol-ene photoreaction. Surface tension measurement showed that the copolymers with ethenyl surface groups could self-associate in dilute aqueous solutions to form micelles. Crosslinking within the micelle cores in the presence of dithioerythritol (DTT) linker was initiated under UV radiation. The formation of core-crosslinked micelles was confirmed by HPLC in combination with charged aerosol detection (CAD). The copolymers were found to readily hydrolyse under acidic conditions due to the ester-containing dendrons. Drug solubilisation capacities of the micellar solutions were determined using griseofulvin as a poorly water-soluble model drug. The solubility of griseofulvin showed a 10-fold enhancement in 1% w/v micelle solution and increased with the concentration of the copolymers. Drug release studies indicated that a more sustained release of griseofulvin was achieved for the core-crosslinked micelles compared to the non-crosslinked micelles, attributable to greater stability of the crosslinked core structure. The findings of this study present a new pathway towards developing biodegradable polymeric nanocarriers.
[Mh] Termos MeSH primário: Dendrímeros/química
Micelas
Poliésteres/química
Polietilenoglicóis/química
[Mh] Termos MeSH secundário: Reagentes para Ligações Cruzadas/química
Reagentes para Ligações Cruzadas/efeitos da radiação
Dendrímeros/efeitos da radiação
Ditioeritritol/química
Ditioeritritol/efeitos da radiação
Liberação Controlada de Fármacos
Griseofulvina/química
Poliésteres/efeitos da radiação
Polietilenoglicóis/efeitos da radiação
Propano/análogos & derivados
Propano/química
Propano/efeitos da radiação
Solubilidade
Raios Ultravioleta
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (2-hydroxy-1-(4-(hydroxyethoxy)phenyl)-2-methyl-1-propanone); 0 (Cross-Linking Reagents); 0 (Dendrimers); 0 (Micelles); 0 (Polyesters); 30IQX730WE (Polyethylene Glycols); 32HRV3E3D5 (Griseofulvin); 6892-68-8 (Dithioerythritol); 9004-74-4 (monomethoxypolyethylene glycol); T75W9911L6 (Propane)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170807
[Lr] Data última revisão:
170807
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170322
[St] Status:MEDLINE


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[PMID]:27780711
[Au] Autor:Nesci S; Trombetti F; Pirini M; Ventrella V; Pagliarani A
[Ad] Endereço:Department of Veterinary Medical Sciences, University of Bologna, Italy.
[Ti] Título:Mercury and protein thiols: Stimulation of mitochondrial F F -ATPase and inhibition of respiration.
[So] Source:Chem Biol Interact;260:42-49, 2016 Dec 25.
[Is] ISSN:1872-7786
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:In spite of the known widespread toxicity of mercury, its impact on mitochondrial bioenergetics is a still poorly explored topic. Even if many studies have dealt with mercury poisoning of mitochondrial respiration, as far as we are aware Hg effects on individual complexes are not so clear. In the present study changes in swine heart mitochondrial respiration and F F -ATPase (F-ATPase) activity promoted by micromolar Hg concentrations were investigated. Hg was found to inhibit the respiration of NADH-energized mitochondria, whereas it was ineffective when the substrate was succinate. Interestingly, the same micromolar Hg doses which inhibited the NADH-O activity stimulated the F-ATPase, most likely by interacting with adjacent thiol residues. Accordingly, Hg dose-dependently decreased protein thiols and all the elicited effects on mitochondrial complexes were reversed by the thiol reducing agent DTE. These findings clearly indicate that Hg interacts with Cys residues of these complexes and differently modulate their functionality by modifying the redox state of thiol groups. The results, which cast light on some implications of metal-thiol interactions up to now not fully explored, may contribute to clarify the molecular mechanisms of mercury toxicity to mitochondria.
[Mh] Termos MeSH primário: Mercúrio/farmacologia
Mitocôndrias/enzimologia
ATPases Translocadoras de Prótons/metabolismo
Compostos de Sulfidrila/farmacologia
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/farmacologia
Animais
Arsenicais
Respiração Celular/efeitos dos fármacos
Ditioeritritol/farmacologia
Transporte de Elétrons/efeitos dos fármacos
Ativação Enzimática/efeitos dos fármacos
Cinética
Magnésio/farmacologia
Mitocôndrias/efeitos dos fármacos
Proteínas Mitocondriais/metabolismo
Sus scrofa
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arsenicals); 0 (Mitochondrial Proteins); 0 (Sulfhydryl Compounds); 0HUR2WY345 (oxophenylarsine); 6892-68-8 (Dithioerythritol); 8L70Q75FXE (Adenosine Triphosphate); EC 3.6.3.14 (Proton-Translocating ATPases); FXS1BY2PGL (Mercury); I38ZP9992A (Magnesium)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170131
[Lr] Data última revisão:
170131
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161107
[St] Status:MEDLINE


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[PMID]:27132865
[Au] Autor:Parsons ZD; Ruddraraju KV; Santo N; Gates KS
[Ad] Endereço:University of Missouri, Department of Chemistry, 125 Chemistry Building, Columbia, MO 65211, United States.
[Ti] Título:Sulfone-stabilized carbanions for the reversible covalent capture of a posttranslationally-generated cysteine oxoform found in protein tyrosine phosphatase 1B (PTP1B).
[So] Source:Bioorg Med Chem;24(12):2631-40, 2016 Jun 15.
[Is] ISSN:1464-3391
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Redox regulation of protein tyrosine phosphatase 1B (PTP1B) involves oxidative conversion of the active site cysteine thiolate into an electrophilic sulfenyl amide residue. Reduction of the sulfenyl amide by biological thiols regenerates the native cysteine residue. Here we explored fundamental chemical reactions that may enable covalent capture of the sulfenyl amide residue in oxidized PTP1B. Various sulfone-containing carbon acids were found to react readily with a model peptide sulfenyl amide via attack of the sulfonyl carbanion on the electrophilic sulfur center in the sulfenyl amide. Both the products and the rates of these reactions were characterized. The results suggest that capture of a peptide sulfenyl amide residue by sulfone-stabilized carbanions can slow, but not completely prevent, thiol-mediated generation of the corresponding cysteine-containing peptide. Sulfone-containing carbon acids may be useful components in the construction of agents that knock down PTP1B activity in cells via transient covalent capture of the sulfenyl amide oxoform generated during insulin signaling processes.
[Mh] Termos MeSH primário: Cisteína/análogos & derivados
Proteína Tirosina Fosfatase não Receptora Tipo 1/antagonistas & inibidores
Sulfonas/química
Sulfonas/farmacologia
[Mh] Termos MeSH secundário: Amidas/química
Amidas/metabolismo
Domínio Catalítico/efeitos dos fármacos
Cisteína/química
Cisteína/metabolismo
Diabetes Mellitus Tipo 2/tratamento farmacológico
Diabetes Mellitus Tipo 2/enzimologia
Ditioeritritol/metabolismo
Seres Humanos
Insulina/metabolismo
Modelos Moleculares
Oxirredução/efeitos dos fármacos
Proteína Tirosina Fosfatase não Receptora Tipo 1/química
Proteína Tirosina Fosfatase não Receptora Tipo 1/metabolismo
Reagentes de Sulfidrila/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amides); 0 (Insulin); 0 (Sulfhydryl Reagents); 0 (Sulfones); 0 (cysteine thiolate); 6892-68-8 (Dithioerythritol); EC 3.1.3.48 (Protein Tyrosine Phosphatase, Non-Receptor Type 1); K848JZ4886 (Cysteine)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170713
[Lr] Data última revisão:
170713
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160503
[St] Status:MEDLINE


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[PMID]:26973189
[Au] Autor:Stepovaya EA; Shakhristova EV; Ryazantseva NV; Nosareva OL; Yakushina VD; Nosova AI; Gulaya VS; Stepanova EA; Chil'chigashev RI; Novitsky VV
[Ad] Endereço:Siberian State Medical University, Tomsk, Russia.
[Ti] Título:[The role of oxidative protein modification and the gluthatione system in modulation of the redox status of breast epithelial cells].
[So] Source:Biomed Khim;62(1):64-8, 2016 Jan-Feb.
[Is] ISSN:2310-6972
[Cp] País de publicação:Russia (Federation)
[La] Idioma:rus
[Ab] Resumo:The effects of the SH-group blocker N-ethylmaleimide (NEM) and thiol group protector 1,4-dithioerythritol (DTE) on the redox status of cells HBL-100 cells, oxidative modification of their proteins and the state of glutathione and thioredoxin systems have been investigated. Breast epithelial cells cultivated in the presence of NEM were characterized by decreased redox status, increased glutathione reductase activity, and increased concentrations of products of irreversible oxidative modification of protein and amino acids. Cultivation of HBL-100 cells in the presence of DTE resulted in a shift of the redox status towards reduction processes and increased reversible protein modification by glutathionylation. The proposed model of intracellular redox modulation may be used in the development of new therapeutic approaches to treat diseases accompanied by impaired redox homeostasis (e.g. oncologic, inflammatory, cardiovascular and neurodegenerative disease).
[Mh] Termos MeSH primário: Ditioeritritol/farmacologia
Células Epiteliais/metabolismo
Glutationa/metabolismo
Glândulas Mamárias Humanas/metabolismo
Processamento de Proteína Pós-Traducional/efeitos dos fármacos
[Mh] Termos MeSH secundário: Linhagem Celular
Feminino
Seres Humanos
Oxirredução/efeitos dos fármacos
[Pt] Tipo de publicação:ENGLISH ABSTRACT; JOURNAL ARTICLE
[Nm] Nome de substância:
6892-68-8 (Dithioerythritol); GAN16C9B8O (Glutathione)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:160314
[Lr] Data última revisão:
160314
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160315
[St] Status:MEDLINE
[do] DOI:10.18097/PBMC20166201064


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[PMID]:25821118
[Au] Autor:Anand U; Ray S; Ghosh S; Banerjee R; Mukherjee S
[Ad] Endereço:Department of Chemistry, Indian Institute of Science Education and Research Bhopal, ITI Campus (Gas Rahat) Building, Govindpura, Bhopal, 462 023, Madhya Pradesh, India.
[Ti] Título:Structural aspects of a protein-surfactant assembly: native and reduced States of human serum albumin.
[So] Source:Protein J;34(2):147-57, 2015 Apr.
[Is] ISSN:1875-8355
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The inherently present seventeen disulfide bonds of the circulatory protein, human serum albumin (HSA) provide the necessary structural stability. Various spectroscopic approaches were used to investigate the effect of reduction of these disulfide bonds and its binding with the anionic surfactant, sodium dodecyl sulfate (SDS). Based on several spectroscopic analyses, our investigations highlight the following interesting aspects: (1) HSA on reduction loses not only its tertiary structure but also a significant amount of secondary structure as well. However, the reduced state of the protein is not like the molten-globule, (2) this structural loss of the protein due to reduction is more prominent than that caused by higher SDS concentrations alone and can certainly be attributed to the role of disulfide bonds, (3) lower surfactant concentrations provide marginal structural rigidity to the native state of the protein, whereas, higher concentrations of SDS induces secondary structure to the reduced state of HSA, (4) the binding of SDS with both the native and reduced states of HSA, occurred in three distinct stages which was followed by a saturation stage. However, the nature of such binding is different for both the states as investigated by using the Stern-Volmer equations and estimating the thermodynamic parameters. Besides, in contrast to the native state, the reduced state of HSA shows that the lone tryptophan residue gets more buried. However, there occurs a sudden decrement in the lifetime of the tryptophan and the hydrodynamic diameter increases by twofold.
[Mh] Termos MeSH primário: Albumina Sérica/química
Dodecilsulfato de Sódio/química
Tensoativos/química
[Mh] Termos MeSH secundário: Dicroísmo Circular
Dissulfetos/química
Ditioeritritol/química
Difusão Dinâmica da Luz
Seres Humanos
Ligação Proteica
Estabilidade Proteica
Espectrometria de Fluorescência
Reagentes de Sulfidrila/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Disulfides); 0 (Serum Albumin); 0 (Sulfhydryl Reagents); 0 (Surface-Active Agents); 368GB5141J (Sodium Dodecyl Sulfate); 6892-68-8 (Dithioerythritol)
[Em] Mês de entrada:1602
[Cu] Atualização por classe:171027
[Lr] Data última revisão:
171027
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150331
[St] Status:MEDLINE
[do] DOI:10.1007/s10930-015-9606-1


  8 / 283 MEDLINE  
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[PMID]:25579883
[Au] Autor:Gani AR; Uppala JK; Ramaiah KV
[Ad] Endereço:Department of Biochemistry, University of Hyderabad, Hyderabad 500046, India.
[Ti] Título:Tauroursodeoxycholic acid prevents stress induced aggregation of proteins in vitro and promotes PERK activation in HepG2 cells.
[So] Source:Arch Biochem Biophys;568:8-15, 2015 Feb 15.
[Is] ISSN:1096-0384
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Tauroursodeoxycholic acid (TUDCA) a bile salt and chemical chaperone reduces stress-induced aggregation of proteins; activates PERK [PKR (RNA-dependent protein kinase)-like ER (endoplasmic reticulum) kinase] or EIF2AK3, one of the hall marks of ER stress induced unfolded protein response (UPR) in human hepatoblastoma HepG2 cells; prevents heat and dithiothreitol (DTT) induced aggregation of BSA (bovine serum albumin), and reduces ANS (1-anilino-naphthalene-8-sulfonate) bound BSA fluorescence in vitro. TUDCA inactivates heat treated, but not the native EcoR1 enzyme, and reduces heat-induced aggregation and activity of COX-1 (cyclooxygenase enzyme-1) in vitro. These findings suggest that TUDCA binds to the hydrophobic regions of proteins and prevents their subsequent aggregation. This may stabilize unfolded proteins that can mount UPR or facilitate their degradation through cellular degradation pathways.
[Mh] Termos MeSH primário: Ativação Enzimática
Células Hep G2/metabolismo
Agregados Proteicos
Soroalbumina Bovina/metabolismo
Ácido Tauroquenodesoxicólico/metabolismo
eIF-2 Quinase/metabolismo
[Mh] Termos MeSH secundário: Ciclo-Oxigenase 1/metabolismo
Desoxirribonuclease EcoRI/metabolismo
Ditioeritritol/metabolismo
Estresse do Retículo Endoplasmático
Temperatura Alta
Seres Humanos
Resposta a Proteínas não Dobradas
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Protein Aggregates); 27432CM55Q (Serum Albumin, Bovine); 516-35-8 (Taurochenodeoxycholic Acid); 60EUX8MN5X (tauroursodeoxycholic acid); 6892-68-8 (Dithioerythritol); EC 1.14.99.1 (Cyclooxygenase 1); EC 1.14.99.1 (PTGS1 protein, human); EC 2.7.11.1 (EIF2AK3 protein, human); EC 2.7.11.1 (eIF-2 Kinase); EC 3.1.21.- (Deoxyribonuclease EcoRI)
[Em] Mês de entrada:1504
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150113
[St] Status:MEDLINE


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[PMID]:24717128
[Au] Autor:Ruff Y; Garavini V; Giuseppone N
[Ad] Endereço:SAMS Research Group, University of Strasbourg, Institut Charles Sadron, CNRS, 23 rue du Loess, BP 84047, 67034 Strasbourg Cedex 2, France.
[Ti] Título:Reversible native chemical ligation: a facile access to dynamic covalent peptides.
[So] Source:J Am Chem Soc;136(17):6333-9, 2014 Apr 30.
[Is] ISSN:1520-5126
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The broad interest of using reversible covalent bonds in chemistry, in particular at its interfaces with biology and materials science, has been recently established through numerous examples in the literature. However, the challenging exchange of peptide fragments using a dynamic covalent peptide bond has not yet been achieved without enzymatic catalysis because of its high thermodynamic stability. Here we show that peptide fragments can be exchanged by a chemoselective and reversible native chemical ligation (NCL) which can take place at N-(methyl)-cysteine residues. This very mild reaction is efficient in aqueous solution, is buffered at physiological pH in the presence of dithiothreitol (DTT), and shows typical half-times of equilibration in the 10 h range.
[Mh] Termos MeSH primário: Cisteína/análogos & derivados
Peptídeos/síntese química
[Mh] Termos MeSH secundário: Cisteína/síntese química
Cisteína/química
Ditioeritritol/química
Peptídeos/química
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Peptides); 6892-68-8 (Dithioerythritol); K848JZ4886 (Cysteine); RQ6L463N3B (mecysteine)
[Em] Mês de entrada:1509
[Cu] Atualização por classe:140430
[Lr] Data última revisão:
140430
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140411
[St] Status:MEDLINE
[do] DOI:10.1021/ja4129845


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[PMID]:24125699
[Au] Autor:Nesci S; Ventrella V; Trombetti F; Pirini M; Pagliarani A
[Ad] Endereço:Department of Veterinary Medical Sciences, University of Bologna, Via Tolara di Sopra 50, 40064 Ozzano Emilia, Bologna, Italy.
[Ti] Título:The mitochondrial F1FO-ATPase desensitization to oligomycin by tributyltin is due to thiol oxidation.
[So] Source:Biochimie;97:128-37, 2014 Feb.
[Is] ISSN:1638-6183
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:The antibiotic oligomycin is known to inhibit mitochondrial F-type ATP synthases. The antibiotic inhibits both ATP synthesis and hydrolysis by blocking the H(+) translocation through FO which is coupled to the catalytic activity of F1. The amphiphilic organotin tri-n-butyltin (TBT), a known mitochondrial poison, can penetrate into biological membranes and covalently bind to electron-donor atoms of biomolecules such as sulfur. This study aims at exploring the mechanism(s) involved in the enzyme desensitization to oligomycin which occurs at concentrations >1 µM TBT. This poorly known effect of TBT, which only appeared at temperatures above the break in the Arrhenius plot of the enzyme activity, was found to be accompanied by the oxidation of isolated thiol groups of the mitochondrial complex. The oligomycin sensitivity was restored by the reducing agents glutathione and dithioerythritol and not influenced by antioxidants. The whole of data is consistent with the hypothesis that thiol oxidation is caused by TBT covalent binding to cysteine residues in a low-affinity site on FO and not by other possible oxidative events. According to this putative model, the onset of tin-sulfur bonds would trigger conformational changes and weaken the oligomycin interaction with FO.
[Mh] Termos MeSH primário: ATPase de Ca(2+) e Mg(2+)/antagonistas & inibidores
Mitocôndrias Cardíacas/efeitos dos fármacos
Proteínas Mitocondriais/antagonistas & inibidores
Oligomicinas/farmacologia
ATPases Translocadoras de Prótons/antagonistas & inibidores
Compostos de Trialquitina/farmacologia
[Mh] Termos MeSH secundário: Animais
Antioxidantes/farmacologia
ATPase de Ca(2+) e Mg(2+)/metabolismo
Ditioeritritol/farmacologia
Antagonismo de Drogas
Glutationa/farmacologia
Cinética
Mitocôndrias Cardíacas/enzimologia
Proteínas Mitocondriais/metabolismo
ATPases Translocadoras de Prótons/metabolismo
Quercetina/farmacologia
Compostos de Sulfidrila/química
Suínos
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antioxidants); 0 (Mitochondrial Proteins); 0 (Oligomycins); 0 (Sulfhydryl Compounds); 0 (Trialkyltin Compounds); 4XDX163P3D (tributyltin); 6892-68-8 (Dithioerythritol); 9IKM0I5T1E (Quercetin); EC 3.6.1.- (Ca(2+) Mg(2+)-ATPase); EC 3.6.3.14 (Proton-Translocating ATPases); GAN16C9B8O (Glutathione)
[Em] Mês de entrada:1408
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131016
[St] Status:MEDLINE



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