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Pesquisa : G02.111.694 [Categoria DeCS]
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[PMID]:29382836
[Au] Autor:Füzik T; Formanová P; Ruzek D; Yoshii K; Niedrig M; Plevka P
[Ad] Endereço:Structural Virology, Central European Institute of Technology, Masaryk University, Kamenice 753/5, 62500, Brno, Czech Republic.
[Ti] Título:Structure of tick-borne encephalitis virus and its neutralization by a monoclonal antibody.
[So] Source:Nat Commun;9(1):436, 2018 01 30.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Tick-borne encephalitis virus (TBEV) causes 13,000 cases of human meningitis and encephalitis annually. However, the structure of the TBEV virion and its interactions with antibodies are unknown. Here, we present cryo-EM structures of the native TBEV virion and its complex with Fab fragments of neutralizing antibody 19/1786. Flavivirus genome delivery depends on membrane fusion that is triggered at low pH. The virion structure indicates that the repulsive interactions of histidine side chains, which become protonated at low pH, may contribute to the disruption of heterotetramers of the TBEV envelope and membrane proteins and induce detachment of the envelope protein ectodomains from the virus membrane. The Fab fragments bind to 120 out of the 180 envelope glycoproteins of the TBEV virion. Unlike most of the previously studied flavivirus-neutralizing antibodies, the Fab fragments do not lock the E-proteins in the native-like arrangement, but interfere with the process of virus-induced membrane fusion.
[Mh] Termos MeSH primário: Anticorpos Neutralizantes/química
Anticorpos Antivirais/química
Vírus da Encefalite Transmitidos por Carrapatos/ultraestrutura
Fragmentos Fab das Imunoglobulinas/química
Proteínas Virais/química
Vírion/ultraestrutura
[Mh] Termos MeSH secundário: Anticorpos Neutralizantes/biossíntese
Anticorpos Antivirais/biossíntese
Linhagem Celular Tumoral
Microscopia Crioeletrônica
Vírus da Encefalite Transmitidos por Carrapatos/genética
Vírus da Encefalite Transmitidos por Carrapatos/metabolismo
Expressão Gênica
Seres Humanos
Concentração de Íons de Hidrogênio
Fragmentos Fab das Imunoglobulinas/biossíntese
Fusão de Membrana/genética
Neurônios/patologia
Neurônios/virologia
Domínios Proteicos
Multimerização Proteica
Proteínas Virais/genética
Proteínas Virais/metabolismo
Vírion/genética
Vírion/metabolismo
Internalização do Vírus
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antibodies, Neutralizing); 0 (Antibodies, Viral); 0 (Immunoglobulin Fab Fragments); 0 (Viral Proteins)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180307
[Lr] Data última revisão:
180307
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180201
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-018-02882-0


  2 / 16853 MEDLINE  
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[PMID]:29295984
[Au] Autor:Goyal N; Rossi MJ; Mazina OM; Chi Y; Moritz RL; Clurman BE; Mazin AV
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, PA, 19102, USA.
[Ti] Título:RAD54 N-terminal domain is a DNA sensor that couples ATP hydrolysis with branch migration of Holliday junctions.
[So] Source:Nat Commun;9(1):34, 2018 01 02.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In eukaryotes, RAD54 catalyzes branch migration (BM) of Holliday junctions, a basic process during DNA repair, replication, and recombination. RAD54 also stimulates RAD51 recombinase and has other activities. Here, we investigate the structural determinants for different RAD54 activities. We find that the RAD54 N-terminal domain (NTD) is responsible for initiation of BM through two coupled, but distinct steps; specific binding to Holliday junctions and RAD54 oligomerization. Furthermore, we find that the RAD54 oligomeric state can be controlled by NTD phosphorylation at S49, a CDK2 consensus site, which inhibits RAD54 oligomerization and, consequently, BM. Importantly, the effect of phosphorylation on RAD54 oligomerization is specific for BM, as it does not affect stimulation of RAD51 recombinase by RAD54. Thus, the transition of the oligomeric states provides an important control of the biological functions of RAD54 and, likely, other multifunctional proteins.
[Mh] Termos MeSH primário: Adenosina Trifosfatases/metabolismo
DNA Helicases/metabolismo
DNA Cruciforme/metabolismo
Proteínas Nucleares/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Sítios de Ligação/genética
Linhagem Celular
DNA Helicases/química
DNA Helicases/genética
Reparo do DNA
DNA Cruciforme/química
DNA Cruciforme/genética
Seres Humanos
Hidrólise
Proteínas Nucleares/química
Proteínas Nucleares/genética
Conformação de Ácido Nucleico
Fosforilação
Multimerização Proteica
Recombinação Genética
Homologia de Sequência de Aminoácidos
Células Sf9
Spodoptera
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (DNA, Cruciform); 0 (Nuclear Proteins); 0 (RAD54L protein, human); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.4.- (DNA Helicases)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180306
[Lr] Data última revisão:
180306
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180104
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02497-x


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[PMID]:29362354
[Au] Autor:Garcia-Alai MM; Heidemann J; Skruzny M; Gieras A; Mertens HDT; Svergun DI; Kaksonen M; Uetrecht C; Meijers R
[Ad] Endereço:European Molecular Biology Laboratory (EMBL), Hamburg Outstation, Notkestrasse 85, 22607, Hamburg, Germany.
[Ti] Título:Epsin and Sla2 form assemblies through phospholipid interfaces.
[So] Source:Nat Commun;9(1):328, 2018 01 23.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In clathrin-mediated endocytosis, adapter proteins assemble together with clathrin through interactions with specific lipids on the plasma membrane. However, the precise mechanism of adapter protein assembly at the cell membrane is still unknown. Here, we show that the membrane-proximal domains ENTH of epsin and ANTH of Sla2 form complexes through phosphatidylinositol 4,5-bisphosphate (PIP2) lipid interfaces. Native mass spectrometry reveals how ENTH and ANTH domains form assemblies by sharing PIP2 molecules. Furthermore, crystal structures of epsin Ent2 ENTH domain from S. cerevisiae in complex with PIP2 and Sla2 ANTH domain from C. thermophilum illustrate how allosteric phospholipid binding occurs. A comparison with human ENTH and ANTH domains reveal only the human ENTH domain can form a stable hexameric core in presence of PIP2, which could explain functional differences between fungal and human epsins. We propose a general phospholipid-driven multifaceted assembly mechanism tolerating different adapter protein compositions to induce endocytosis.
[Mh] Termos MeSH primário: Proteínas Adaptadoras de Transporte Vesicular/química
Proteínas Fúngicas/química
Fosfatidilinositol 4,5-Difosfato/química
Domínios Proteicos
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transporte Vesicular/genética
Proteínas Adaptadoras de Transporte Vesicular/metabolismo
Sequência de Aminoácidos
Sítios de Ligação/genética
Membrana Celular/metabolismo
Chaetomium/genética
Chaetomium/metabolismo
Cristalografia por Raios X
Endocitose
Proteínas Fúngicas/genética
Proteínas Fúngicas/metabolismo
Seres Humanos
Modelos Moleculares
Fosfatidilinositol 4,5-Difosfato/metabolismo
Ligação Proteica
Multimerização Proteica
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/metabolismo
Homologia de Sequência de Aminoácidos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adaptor Proteins, Vesicular Transport); 0 (Fungal Proteins); 0 (Phosphatidylinositol 4,5-Diphosphate); 0 (epsin)
[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:180125
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02443-x


  4 / 16853 MEDLINE  
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[PMID]:29348551
[Au] Autor:Jin H; Ding YH; Wang M; Song Y; Liao Z; Newcomb CJ; Wu X; Tang XQ; Li Z; Lin Y; Yan F; Jian T; Mu P; Chen CL
[Ad] Endereço:Physical Sciences Division, Pacific Northwest National Laboratory, Richland, WA, 99352, USA.
[Ti] Título:Designable and dynamic single-walled stiff nanotubes assembled from sequence-defined peptoids.
[So] Source:Nat Commun;9(1):270, 2018 01 18.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Despite recent advances in the assembly of organic nanotubes, conferral of sequence-defined engineering and dynamic response characteristics to the tubules remains a challenge. Here we report a new family of highly designable and dynamic nanotubes assembled from sequence-defined peptoids through a unique "rolling-up and closure of nanosheet" mechanism. During the assembly process, amorphous spherical particles of amphiphilic peptoid oligomers crystallize to form well-defined nanosheets before folding to form single-walled nanotubes. These nanotubes undergo a pH-triggered, reversible contraction-expansion motion. By varying the number of hydrophobic residues of peptoids, we demonstrate tuning of nanotube wall thickness, diameter, and mechanical properties. Atomic force microscopy-based mechanical measurements show peptoid nanotubes are highly stiff (Young's Modulus ~13-17 GPa). We further demonstrate the precise incorporation of functional groups within nanotubes and their applications in water decontamination and cellular adhesion and uptake. These nanotubes provide a robust platform for developing biomimetic materials tailored to specific applications.
[Mh] Termos MeSH primário: Nanotubos/química
Peptoides/química
Dobramento de Proteína
Multimerização Proteica
[Mh] Termos MeSH secundário: Células A549
Cristalografia por Raios X
Seres Humanos
Concentração de Íons de Hidrogênio
Interações Hidrofóbicas e Hidrofílicas
Microscopia de Força Atômica
Microscopia Confocal
Microscopia Eletrônica de Transmissão
Nanotubos/ultraestrutura
Peptidomiméticos/química
Água/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Peptidomimetics); 0 (Peptoids); 059QF0KO0R (Water)
[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:180120
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02059-1


  5 / 16853 MEDLINE  
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[PMID]:29348429
[Au] Autor:Goto-Ito S; Yamagata A; Sato Y; Uemura T; Shiroshima T; Maeda A; Imai A; Mori H; Yoshida T; Fukai S
[Ad] Endereço:Institute of Molecular and Cellular Biosciences, The University of Tokyo, Tokyo, 113-0032, Japan.
[Ti] Título:Structural basis of trans-synaptic interactions between PTPδ and SALMs for inducing synapse formation.
[So] Source:Nat Commun;9(1):269, 2018 01 18.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Synapse formation is triggered by trans-synaptic interactions of cell adhesion molecules, termed synaptic organizers. Three members of type-II receptor protein tyrosine phosphatases (classified as type-IIa RPTPs; PTPδ, PTPσ and LAR) are known as presynaptic organizers. Synaptic adhesion-like molecules (SALMs) have recently emerged as a family of postsynaptic organizers. Although all five SALM isoforms can bind to the type-IIa RPTPs, only SALM3 and SALM5 reportedly have synaptogenic activities depending on their binding. Here, we report the crystal structures of apo-SALM5, and PTPδ-SALM2 and PTPδ-SALM5 complexes. The leucine-rich repeat (LRR) domains of SALMs interact with the second immunoglobulin-like (Ig) domain of PTPδ, whereas the Ig domains of SALMs interact with both the second and third Ig domains of PTPδ. Unexpectedly, the structures exhibit the LRR-mediated 2:2 complex. Our synaptogenic co-culture assay using site-directed SALM5 mutants demonstrates that presynaptic differentiation induced by PTPδ-SALM5 requires the dimeric property of SALM5.
[Mh] Termos MeSH primário: Moléculas de Adesão Celular Neuronais/química
Proteínas Tirosina Fosfatases Classe 2 Semelhantes a Receptores/química
Sinapses/metabolismo
Transmissão Sináptica
[Mh] Termos MeSH secundário: Animais
Moléculas de Adesão Celular Neuronais/genética
Moléculas de Adesão Celular Neuronais/metabolismo
Cristalografia por Raios X
Células HEK293
Seres Humanos
Modelos Moleculares
Mutação
Ligação Proteica
Domínios Proteicos
Isoformas de Proteínas/química
Isoformas de Proteínas/genética
Isoformas de Proteínas/metabolismo
Multimerização Proteica
Proteínas Tirosina Fosfatases Classe 2 Semelhantes a Receptores/genética
Proteínas Tirosina Fosfatases Classe 2 Semelhantes a Receptores/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cell Adhesion Molecules, Neuronal); 0 (Protein Isoforms); 0 (SALM5 protein, human); EC 3.1.3.48 (Receptor-Like Protein Tyrosine Phosphatases, Class 2)
[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:180120
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02417-z


  6 / 16853 MEDLINE  
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[PMID]:28460485
[Au] Autor:Lv LX; Zhou ZX; Zhou Z; Zhang LJ; Yan R; Zhao Z; Yang LY; Bian XY; Jiang HY; Li YD; Sun YS; Xu QQ; Hu GL; Guan WJ; Li YQ
[Ad] Endereço:Institute of Pharmaceutical Biotechnology and College of Pharmaceutical Sciences, Zhejiang University, 310058 Hangzhou, China.
[Ti] Título:Hispidin induces autophagic and necrotic death in SGC-7901 gastric cancer cells through lysosomal membrane permeabilization by inhibiting tubulin polymerization.
[So] Source:Oncotarget;8(16):26992-27006, 2017 Apr 18.
[Is] ISSN:1949-2553
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Hispidin and its derivatives are widely distributed in edible mushrooms. Hispidin is more cytotoxic to A549, SCL-1, Bel7402 and Capan-1 cancer cells than to MRC5 normal cells; by contrast, hispidin protects H9c2 cardiomyoblast cells from hydrogen peroxide-induced or doxorubicin-induced apoptosis. Consequently, further research on how hispidin affects normal and cancer cells may help treat cancer and reduce chemotherapy-induced side effects. This study showed that hispidin caused caspase-independent death in SGC-7901 cancer cells but not in GES-1 normal cells. Hispidin-induced increases in LC3-II occurred in SGC-7901 cells in a time independent manner. Cell death can be partially inhibited by treatment with ATG5 siRNA but not by autophagy or necroptosis inhibitors. Ultrastructural evidence indicated that hispidin-induced necrotic cell death involved autophagy. Hispidin-induced lysosomal membrane permeabilization (LMP) related to complex cell death occurred more drastically in SGC-7901 cells than in GES-1 cells. Ca2+ rather than cathepsins from LMP contributed more to cell death. Hispidin induced microtubule depolymerization, which can cause LMP, more drastically in SGC-7901 cells than in GES-1 cells. At 4.1 µM, hispidin promoted cell-free tubulin polymerization but at concentrations higher than 41 µM, hispidin inhibited polymerization. Hispidin did not bind to tubulin. Alterations in microtubule regulatory proteins, such as stathmin phosphorylation at Ser16, contributed to hispidin-induced SGC-7901 cell death. In conclusion, hispidin at concentrations higher than 41 µM may inhibit tubulin polymerization by modulating microtubule regulatory proteins, such as stathmin, causing LMP and complex SGC-7901 cell death. This mechanism suggests a promising novel treatment for human cancer.
[Mh] Termos MeSH primário: Autofagia/efeitos dos fármacos
Membranas Intracelulares/efeitos dos fármacos
Lisossomos/metabolismo
Multimerização Proteica/efeitos dos fármacos
Pironas/farmacologia
Tubulina (Proteína)/metabolismo
[Mh] Termos MeSH secundário: Apoptose/efeitos dos fármacos
Caspases/metabolismo
Morte Celular/efeitos dos fármacos
Linhagem Celular Tumoral
Seres Humanos
Microtúbulos/química
Microtúbulos/metabolismo
Óxido Nítrico/biossíntese
Permeabilidade
Fosforilação
Estatmina/metabolismo
Tubulina (Proteína)/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Pyrones); 0 (STMN1 protein, human); 0 (Stathmin); 0 (Tubulin); 31C4KY9ESH (Nitric Oxide); EC 3.4.22.- (Caspases); SSJ18CG55E (hispidin)
[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:170503
[St] Status:MEDLINE
[do] DOI:10.18632/oncotarget.15935


  7 / 16853 MEDLINE  
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[PMID]:28741733
[Au] Autor:Tsukamoto H; Yamagata Y; Ukai I; Takeuchi S; Okubo M; Kobayashi Y; Kozakai S; Kubota K; Numasaki M; Kanemitsu Y; Matsumoto Y; Tomioka Y
[Ad] Endereço:Laboratory of Oncology, Pharmacy Practice and Sciences, Graduate School of Pharmaceutical Sciences, Tohoku University, Sendai, Japan.
[Ti] Título:An inhibitory epitope of human Toll-like receptor 4 resides on leucine-rich repeat 13 and is recognized by a monoclonal antibody.
[So] Source:FEBS Lett;591(16):2406-2416, 2017 08.
[Is] ISSN:1873-3468
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Lipopolysaccharide (LPS)-induced activation of Toll-like receptor 4 (TLR4) elicits the innate immune response and can trigger septic shock if excessive. Two antibodies (HT4 and HT52) inhibit LPS-induced human TLR4 activation via novel LPS binding-independent mechanisms. The HT52 epitope resides on leucine-rich repeat 2 (LRR2) and is a feature of many inhibitory antibodies; antigen specificity of HT4 does not reside in LRR2. Here, we identified an HT4 epitope on LRR13 located close to the TLR4 dimerization interface that plays a role in NFκB activation. HT4 and HT52 mutually enhanced TLR4 inhibition. LRR13 is a novel inhibitory epitope and may be useful for developing anti-TLR4 antibodies. Combination therapy with LRR2 and LRR13 may effectively inhibit TLR4 activation.
[Mh] Termos MeSH primário: Motivos de Aminoácidos
Anticorpos Monoclonais/imunologia
Epitopos/imunologia
Receptor 4 Toll-Like/química
Receptor 4 Toll-Like/imunologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Linhagem Celular
Seres Humanos
Lipopolissacarídeos/farmacologia
Camundongos
Multimerização Proteica
Estrutura Quaternária de Proteína
Receptor 4 Toll-Like/metabolismo
[Pt] Tipo de publicação:LETTER; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antibodies, Monoclonal); 0 (Epitopes); 0 (Lipopolysaccharides); 0 (TLR4 protein, human); 0 (Toll-Like Receptor 4)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:180302
[Lr] Data última revisão:
180302
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE
[do] DOI:10.1002/1873-3468.12768


  8 / 16853 MEDLINE  
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[PMID]:29200284
[Au] Autor:He X; Liao X; Li H; Xia W; Sun H
[Ad] Endereço:MOE Key Laboratory of Bioinorganic and Synthetic Chemistry, School of Chemistry, Sun Yat-sen University , Guangzhou 510275, China.
[Ti] Título:Bismuth-Induced Inactivation of Ferric Uptake Regulator from Helicobacter pylori.
[So] Source:Inorg Chem;56(24):15041-15048, 2017 Dec 18.
[Is] ISSN:1520-510X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ferric uptake regulator (Fur) of Helicobacter pylori is a global regulator that is important for bacterial colonization and survival within the gastric mucosa. H. pylori Fur (HpFur) is unique in its ability to regulate gene expression in both metal-bound (holo-Fur) and metal-free (apo-Fur) forms. Bismuth-based drugs are widely used for the treatment of H. pylori infection. However, the mechanism of action of bismuth drug was not fully understood. Recently, it has been reported that bismuth drugs could interfere with the bacterial ferric uptake pathway and inhibit bacterial growth, implying intrinsic correlation between bismuth drug and bacterial iron metabolism. Herein, we demonstrate that Bi(III) binds to HpFur protein specifically at the physiologically important S1 site, which further leads to protein oligomerization and loss of DNA binding capability. The targeting of HpFur by bismuth drugs significantly reduced transcription levels of its regulated genes, which are crucial for bacterial physiology and metabolism. Our studies present direct evidence that perturbation of iron metabolism in H. pylori by bismuth might serve as one of the mechanisms for the antimicrobial activity of bismuth drugs.
[Mh] Termos MeSH primário: Antibacterianos/farmacologia
Proteínas de Bactérias/antagonistas & inibidores
Bismuto/farmacologia
Inibidores Enzimáticos/farmacologia
Helicobacter pylori/efeitos dos fármacos
Proteínas Repressoras/antagonistas & inibidores
[Mh] Termos MeSH secundário: Proteínas de Bactérias/química
Proteínas de Bactérias/metabolismo
DNA Bacteriano/metabolismo
Estabilidade Enzimática/efeitos dos fármacos
Infecções por Helicobacter/tratamento farmacológico
Infecções por Helicobacter/microbiologia
Helicobacter pylori/metabolismo
Seres Humanos
Modelos Moleculares
Conformação Proteica/efeitos dos fármacos
Multimerização Proteica/efeitos dos fármacos
Proteínas Repressoras/química
Proteínas Repressoras/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Bacterial Proteins); 0 (DNA, Bacterial); 0 (Enzyme Inhibitors); 0 (Repressor Proteins); 0 (ferric uptake regulating proteins, bacterial); U015TT5I8H (Bismuth)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180228
[Lr] Data última revisão:
180228
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171205
[St] Status:MEDLINE
[do] DOI:10.1021/acs.inorgchem.7b02380


  9 / 16853 MEDLINE  
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[PMID]:29182243
[Au] Autor:Liao X; Yang F; Li H; So PK; Yao Z; Xia W; Sun H
[Ad] Endereço:MOE Key Laboratory of Bioinorganic and Synthetic Chemistry, School of Chemistry, Sun Yat-sen University , Guangzhou, China , 510275.
[Ti] Título:Targeting the Thioredoxin Reductase-Thioredoxin System from Staphylococcus aureus by Silver Ions.
[So] Source:Inorg Chem;56(24):14823-14830, 2017 Dec 18.
[Is] ISSN:1520-510X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The thioredoxin system, which is composed of NADPH, thioredoxin reductase (TrxR), and thioredoxin (Trx), is one of the major disulfide reductase systems used by bacteria against oxidative stress. In particular, this reductase system is crucial for the survival of the pathogenic bacterium Staphylococcus aureus, which lacks a natural glutathione/glutaredoxin (Grx) system. Although silver ions and silver-containing materials have been used as antibacterial agents for centuries, the antibacterial mechanism of silver is not well-understood. Herein, we demonstrate that silver ions bind to the active sites of S. aureus TrxR and Trx with dissociation constants of 1.4 ± 0.1 µM and 15.0 ± 5.0 µM and stoichiometries of 1 and 2 Ag ions per protein, respectively. Importantly, silver ion binding leads to oligomerization and functional disruption of TrxR as well as Trx. Silver also depleted intracellular thiol levels in S. aureus, disrupting bacterial thiol-redox homeostasis. Our study provides new insights into the antibacterial mechanism of silver ions. Moreover, the Trx and TrxR system might serve as a feasible target for the design of antibacterial drugs.
[Mh] Termos MeSH primário: Antibacterianos/farmacologia
Proteínas de Bactérias/antagonistas & inibidores
Prata/farmacologia
Staphylococcus aureus/efeitos dos fármacos
Tiorredoxina Dissulfeto Redutase/antagonistas & inibidores
Tiorredoxinas/antagonistas & inibidores
[Mh] Termos MeSH secundário: Proteínas de Bactérias/metabolismo
Domínio Catalítico/efeitos dos fármacos
Seres Humanos
Modelos Moleculares
Multimerização Proteica/efeitos dos fármacos
Infecções Estafilocócicas/tratamento farmacológico
Infecções Estafilocócicas/microbiologia
Staphylococcus aureus/metabolismo
Tiorredoxina Dissulfeto Redutase/metabolismo
Tiorredoxinas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Bacterial Proteins); 3M4G523W1G (Silver); 52500-60-4 (Thioredoxins); EC 1.8.1.9 (Thioredoxin-Disulfide Reductase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180228
[Lr] Data última revisão:
180228
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171129
[St] Status:MEDLINE
[do] DOI:10.1021/acs.inorgchem.7b01904


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[PMID]:29381728
[Au] Autor:Belousov MV; Bondarev SA; Kosolapova AO; Antonets KS; Sulatskaya AI; Sulatsky MI; Zhouravleva GA; Kuznetsova IM; Turoverov KK; Nizhnikov AA
[Ad] Endereço:Department of Genetics and Biotechnology, St. Petersburg State University, Universitetskaya nab., St. Petersburg, Russian Federation.
[Ti] Título:M60-like metalloprotease domain of the Escherichia coli YghJ protein forms amyloid fibrils.
[So] Source:PLoS One;13(1):e0191317, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Amyloids are protein fibrils with a characteristic spatial structure. Amyloids were long perceived as the pathogens involved in a set of lethal diseases in humans and animals. In recent decades, it has become clear that amyloids represent a quaternary protein structure that is not only pathological but also functionally important and is widely used by different organisms, ranging from archaea to animals, to implement diverse biological functions. The greatest biological variety of amyloids is found in prokaryotes, where they control the formation of biofilms and cell wall sheaths, facilitate the overcoming of surface tension, and regulate the metabolism of toxins. Several amyloid proteins were identified in the important model, biotechnological and pathogenic bacterium Escherichia coli. In previous studies, using a method for the proteomic screening and identification of amyloids, we identified 61 potentially amyloidogenic proteins in the proteome of E. coli. Among these proteins, YghJ was the most enriched with bioinformatically predicted amyloidogenic regions. YghJ is a lipoprotein with a zinc metalloprotease M60-like domain that is involved in mucin degradation in the intestine as well as in proinflammatory responses. In this study, we analyzed the amyloid properties of the YghJ M60-like domain and demonstrated that it forms amyloid-like fibrils in vitro and in vivo.
[Mh] Termos MeSH primário: Amiloide/química
Proteínas de Escherichia coli/química
Metaloproteases/química
Multimerização Proteica
[Mh] Termos MeSH secundário: Domínios Proteicos
Estrutura Secundária de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amyloid); 0 (Escherichia coli Proteins); EC 3.4.- (Metalloproteases); EC 3.4.- (YghJ protein, E coli)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180131
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191317



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