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Pesquisa : D08.811.913.696.650.550 [Categoria DeCS]
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  1 / 1578 MEDLINE  
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[PMID]:28551817
[Au] Autor:Mishra AK; Singh N; Agnihotri P; Mishra S; Singh SP; Kolli BK; Chang KP; Sahasrabuddhe AA; Siddiqi MI; Pratap JV
[Ad] Endereço:Molecular and Structural Biology Division, CSIR-Central Drug Research Institute, B.S. 10/1, sector 10, Jankipuram Extension, Sitapur Road, Lucknow, Uttar Pradesh, 226031, India.
[Ti] Título:Discovery of novel inhibitors for Leishmania nucleoside diphosphatase kinase (NDK) based on its structural and functional characterization.
[So] Source:J Comput Aided Mol Des;31(6):547-562, 2017 Jun.
[Is] ISSN:1573-4951
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Nucleoside diphosphate kinases (NDKs) are ubiquitous enzymes that catalyze the transfer of the γ-phosphate moiety from an NTP donor to an NDP acceptor, crucial for maintaining the cellular level of nucleoside triphosphates (NTPs). The inability of trypanosomatids to synthesize purines de novo and their dependence on the salvage pathway makes NDK an attractive target to develop drugs for the diseases they cause. Here we report the discovery of novel inhibitors for Leishmania NDK based on the structural and functional characterization of purified recombinant NDK from Leishmania amazonensis. Recombinant LaNDK possesses auto-phosphorylation, phosphotransferase and kinase activities with Histidine 117 playing an essential role. LaNDK crystals were grown by hanging drop vapour diffusion method in a solution containing 18% PEG-MME 500, 100 mM Bis-Tris propane pH 6.0 and 50 mM MgCl . It belongs to the hexagonal space group P6 22 with unit cell parameters a = b = 115.18, c = 62.18 Å and α = ß = 90°, γ = 120°. The structure solved by molecular replacement methods was refined to crystallographic R-factor and R values of 22.54 and 26.52%, respectively. Molecular docking and dynamics simulation-based virtual screening identified putative binding compounds. Protein inhibition studies of selected hits identified five inhibitors effective at micromolar concentrations. One of the compounds showed ~45% inhibition of Leishmania promastigotes proliferation. Analysis of inhibitor-NDK complexes reveals the mode of their binding, facilitating design of new compounds for optimization of activities as drugs against leishmaniasis.
[Mh] Termos MeSH primário: Antiprotozoários/química
Leishmania/enzimologia
Núcleosídeo-Difosfato Quinase/antagonistas & inibidores
[Mh] Termos MeSH secundário: Ativação Enzimática
Seres Humanos
Simulação de Acoplamento Molecular
Simulação de Dinâmica Molecular
Estrutura Molecular
Núcleosídeo-Difosfato Quinase/química
Ligação Proteica
Conformação Proteica
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antiprotozoal Agents); EC 2.7.4.6 (Nucleoside-Diphosphate Kinase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171108
[Lr] Data última revisão:
171108
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170529
[St] Status:MEDLINE
[do] DOI:10.1007/s10822-017-0022-9


  2 / 1578 MEDLINE  
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[PMID]:28505172
[Au] Autor:Liu PF; Liu QH; Wu Y; Huang J
[Ad] Endereço:Key Laboratory of Sustainable Development of Marine Fisheries, Ministry of Agriculture, Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Qingdao, China.
[Ti] Título:Increased nucleoside diphosphate kinase activity induces white spot syndrome virus infection in Litopenaeus vannamei.
[So] Source:PLoS One;12(5):e0175741, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Nucleoside diphosphate kinase (NDK), which has the same sequence as oncoprotein (OP) in humans, can induce nucleoside triphosphates in DNA replication by maintenance of the deoxynucleotide triphosphate (dNTP's) and is known to be regulated by viral infection in the shrimp Litopenaeus vannamei. This paper describes the relationship between NDK and white spot syndrome virus (WSSV) infection. The recombinant NDK was produced by a prokaryotic expression system. WSSV copy numbers and mRNA levels of IE1 and VP28 were significantly increased in shrimp injected with recombinant NDK at 72 h after WSSV infection. After synthesizing dsRNA-NDK and confirming the efficacy of NDK silencing, we recorded the cumulative mortality of WSSV-infected shrimp injected with NDK and dsRNA-NDK. A comparison between the results demonstrated that silencing NDK delayed the death of shrimps. These findings indicate that NDK has an important role influencing the replication of WSSV replication in shrimp. Furthermore, NDK may have potential target as a new therapeutic strategy against WSSV infection in shrimp.
[Mh] Termos MeSH primário: Núcleosídeo-Difosfato Quinase/metabolismo
Penaeidae/enzimologia
Penaeidae/virologia
Vírus 1 da Síndrome da Mancha Branca
[Mh] Termos MeSH secundário: Animais
Ativação Enzimática
Dosagem de Genes
Expressão Gênica
Núcleosídeo-Difosfato Quinase/genética
Especificidade de Órgãos/genética
Penaeidae/genética
Interferência de RNA
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Recombinant Proteins); EC 2.7.4.6 (Nucleoside-Diphosphate Kinase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170920
[Lr] Data última revisão:
170920
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170516
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0175741


  3 / 1578 MEDLINE  
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[PMID]:28499874
[Au] Autor:Vieira PS; Souza TACB; Honorato RV; Zanphorlin LM; Severiano KU; Rocco SA; de Oliveira AHC; Cordeiro AT; Oliveira PSL; de Giuseppe PO; Murakami MT
[Ad] Endereço:Laboratório Nacional de Biociências (LNBio), Centro Nacional de Pesquisa em Energia e Materiais (CNPEM), Campinas, SP, Brazil.
[Ti] Título:Pyrrole-indolinone SU11652 targets the nucleoside diphosphate kinase from Leishmania parasites.
[So] Source:Biochem Biophys Res Commun;488(3):461-465, 2017 Jul 01.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Nucleoside diphosphate kinases (NDKs) are key enzymes in the purine-salvage pathway of trypanosomatids and have been associated with the maintenance of host-cell integrity for the benefit of the parasite, being potential targets for rational drug discovery and design. The NDK from Leishmania major (LmNDK) and mutants were expressed and purified to homogeneity. Thermal shift assays were employed to identify potential inhibitors for LmNDK. Calorimetric experiments, site-directed mutagenesis and molecular docking analysis were performed to validate the interaction and to evaluate the structural basis of ligand recognition. Furthermore, the anti-leishmanial activity of the newly identified and validated compound was tested in vitro against different Leishmania species. The molecule SU11652, a Sunitinib analog, was identified as a potential inhibitor for LmNDK and structural studies indicated that this molecule binds to the active site of LmNDK in a similar conformation to nucleotides, mimicking natural substrates. Isothermal titration calorimetry experiments combined with site-directed mutagenesis revealed that the residues H50 and H117, considered essential for catalysis, play an important role in ligand binding. In vitro cell studies showed that SU11652 had similar efficacy to Amphotericin b against some Leishmania species. Together, our results indicate the pyrrole-indolinone SU11652 as a promising scaffold for the rational design of new drugs targeting the enzyme NDK from Leishmania parasites.
[Mh] Termos MeSH primário: Antiprotozoários/farmacologia
Indóis/farmacologia
Leishmania major/enzimologia
Núcleosídeo-Difosfato Quinase/antagonistas & inibidores
Inibidores de Proteínas Quinases/farmacologia
Pirróis/farmacologia
[Mh] Termos MeSH secundário: Calorimetria
Sobrevivência Celular/efeitos dos fármacos
Relação Dose-Resposta a Droga
Leishmania major/efeitos dos fármacos
Simulação de Acoplamento Molecular
Mutagênese Sítio-Dirigida
Núcleosídeo-Difosfato Quinase/genética
Núcleosídeo-Difosfato Quinase/metabolismo
Testes de Sensibilidade Parasitária
Inibidores de Proteínas Quinases/química
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antiprotozoal Agents); 0 (Indoles); 0 (Protein Kinase Inhibitors); 0 (Pyrroles); 0 (SU 11652); EC 2.7.4.6 (Nucleoside-Diphosphate Kinase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171002
[Lr] Data última revisão:
171002
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170514
[St] Status:MEDLINE


  4 / 1578 MEDLINE  
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[PMID]:28481113
[Au] Autor:Dautant A; Meyer P; Georgescauld F
[Ad] Endereço:Université de Bordeaux, CNRS, Institut de Biochimie et Génétique Cellulaires, UMR 5095, Bordeaux, France.
[Ti] Título:Hydrogen/Deuterium Exchange Mass Spectrometry Reveals Mechanistic Details of Activation of Nucleoside Diphosphate Kinases by Oligomerization.
[So] Source:Biochemistry;56(23):2886-2896, 2017 Jun 13.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Most oligomeric proteins become active only after assembly, but why oligomerization is required to support function is not well understood. Here, we address this question using the wild type (WT) and a destabilized mutant (D93N) of the hexameric nucleoside diphosphate kinase from the pathogen Mycobacterium tuberculosis (Mt-NDPK). The conformational dynamics and oligomeric states of each were analyzed during unfolding and/or folding by hydrogen/deuterium exchange mass spectrometry (HDX-MS) at peptide resolution and by additional biochemical techniques. We found that WT and D93N native hexamers present a stable core and a flexible periphery, the latter being more flexible for the destabilized mutant. Stable but inactive species formed during unfolding of D93N and folding of WT were characterized. For the first time, we show that both of these species are nativelike dimers, each of its monomers having a major subdomain folded, while a minor subdomain (Kpn/α ) remains unfolded. The Kpn/α subdomain, which belongs to the catalytic site, becomes structured only upon hexamerization, explaining why oligomerization is required for NDPK activity. Further HDX-MS studies are necessary to establish the general activation mechanism for other homo-oligomers.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Modelos Moleculares
Mycobacterium tuberculosis/enzimologia
Núcleosídeo-Difosfato Quinase/metabolismo
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Biocatálise
Domínio Catalítico
Medição da Troca de Deutério
Dimerização
Ativação Enzimática
Estabilidade Enzimática
Cinética
Peso Molecular
Mutação
Núcleosídeo-Difosfato Quinase/química
Núcleosídeo-Difosfato Quinase/genética
Conformação Proteica
Redobramento de Proteína
Estrutura Quaternária de Proteína
Desdobramento de Proteína
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Recombinant Proteins); EC 2.7.4.6 (Nucleoside-Diphosphate Kinase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170706
[Lr] Data última revisão:
170706
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170509
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00282


  5 / 1578 MEDLINE  
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[PMID]:27908239
[Au] Autor:Hetmann A; Wujak M; Kowalczyk S
[Ad] Endereço:Nicolaus Copernicus University, Faculty of Biology and Environment Protection, Department of Biochemistry, Torun 87-100, Poland. mag_wuj@umk.pl.
[Ti] Título:Protein Transphosphorylation During the Mutual Interaction between Phytochrome A and a Nuclear Isoform of Nucleoside Diphosphate Kinase Is Regulated by Red Light.
[So] Source:Biochemistry (Mosc);81(10):1153-1162, 2016 Oct.
[Is] ISSN:1608-3040
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The nuclear isoform of nucleoside diphosphate kinase isoenzyme NDPK-I undergoes strong catalytic activation upon its interaction with the active form of phytochrome A (Pfr) in red light. The autophosphorylation or intermolecular transphosphorylation of NDPK-I leads to the formation of phosphoester bonds stable in acidic solution. The phosphate residue of the phosphamide bond in the active center of NDPK-I can also be transferred to serine and threonine residues localized in other proteins, including phytochrome A. Phytochrome A, similarly to NDPK-I , undergoes autophosphorylation on serine and threonine residues and can phosphorylate some potential substrate proteins. The physical interaction between phytochrome A in the Pfr form and NDPK-I results in a significant increase in the kinase activity of NDPK-I . The results presented in this work indicate that NDPK-I may function as a protein kinase regulated by light.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo
Arabidopsis/enzimologia
Luz
Núcleosídeo-Difosfato Quinase/metabolismo
Fitocromo A/metabolismo
[Mh] Termos MeSH secundário: Arabidopsis/genética
Proteínas de Arabidopsis/genética
Núcleosídeo-Difosfato Quinase/genética
Fosforilação/genética
Fosforilação/efeitos da radiação
Fitocromo A/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Phytochrome A); EC 2.7.4.6 (Nucleoside-Diphosphate Kinase)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170113
[Lr] Data última revisão:
170113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161203
[St] Status:MEDLINE


  6 / 1578 MEDLINE  
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[PMID]:27542194
[Au] Autor:Srivastava S; Panda S; Li Z; Fuhs SR; Hunter T; Thiele DJ; Hubbard SR; Skolnik EY
[Ad] Endereço:Department of Biochemistry and Molecular Pharmacology, New York University School of Medicine, New York, United States.
[Ti] Título:Histidine phosphorylation relieves copper inhibition in the mammalian potassium channel KCa3.1.
[So] Source:Elife;5, 2016 Aug 19.
[Is] ISSN:2050-084X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:KCa2.1, KCa2.2, KCa2.3 and KCa3.1 constitute a family of mammalian small- to intermediate-conductance potassium channels that are activated by calcium-calmodulin. KCa3.1 is unique among these four channels in that activation requires, in addition to calcium, phosphorylation of a single histidine residue (His358) in the cytoplasmic region, by nucleoside diphosphate kinase-B (NDPK-B). The mechanism by which KCa3.1 is activated by histidine phosphorylation is unknown. Histidine phosphorylation is well characterized in prokaryotes but poorly understood in eukaryotes. Here, we demonstrate that phosphorylation of His358 activates KCa3.1 by antagonizing copper-mediated inhibition of the channel. Furthermore, we show that activated CD4(+) T cells deficient in intracellular copper exhibit increased KCa3.1 histidine phosphorylation and channel activity, leading to increased calcium flux and cytokine production. These findings reveal a novel regulatory mechanism for a mammalian potassium channel and for T-cell activation, and highlight a unique feature of histidine versus serine/threonine and tyrosine as a regulatory phosphorylation site.
[Mh] Termos MeSH primário: Cobre/metabolismo
Inibidores Enzimáticos/metabolismo
Histidina/metabolismo
Canais de Potássio Ativados por Cálcio de Condutância Intermediária/antagonistas & inibidores
Canais de Potássio Ativados por Cálcio de Condutância Intermediária/metabolismo
[Mh] Termos MeSH secundário: Animais
Linfócitos T CD4-Positivos/imunologia
Células Cultivadas
Citocinas/metabolismo
Seres Humanos
Camundongos
Núcleosídeo-Difosfato Quinase/metabolismo
Técnicas de Patch-Clamp
Fosforilação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cytokines); 0 (Enzyme Inhibitors); 0 (Intermediate-Conductance Calcium-Activated Potassium Channels); 0 (KCNN4 protein, human); 4QD397987E (Histidine); 789U1901C5 (Copper); EC 2.7.4.6 (Nucleoside-Diphosphate Kinase); EC 2.7.4.6. (NDPK-B protein, human)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171023
[Lr] Data última revisão:
171023
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160820
[St] Status:MEDLINE


  7 / 1578 MEDLINE  
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[PMID]:27453048
[Au] Autor:Panda S; Srivastava S; Li Z; Vaeth M; Fuhs SR; Hunter T; Skolnik EY
[Ad] Endereço:Department of Biochemistry and Molecular Pharmacology, New York University Langone Medical Center, New York, NY 10016, USA; The Helen L. and Martin S. Kimmel Center for Biology and Medicine, New York University Langone Medical Center, New York, NY 10016, USA; Skirball Institute for Biomolecular Medi
[Ti] Título:Identification of PGAM5 as a Mammalian Protein Histidine Phosphatase that Plays a Central Role to Negatively Regulate CD4(+) T Cells.
[So] Source:Mol Cell;63(3):457-69, 2016 Aug 04.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Whereas phosphorylation of serine, threonine, and tyrosine is exceedingly well characterized, the role of histidine phosphorylation in mammalian signaling is largely unexplored. Here we show that phosphoglycerate mutase family 5 (PGAM5) functions as a phosphohistidine phosphatase that specifically associates with and dephosphorylates the catalytic histidine on nucleoside diphosphate kinase B (NDPK-B). By dephosphorylating NDPK-B, PGAM5 negatively regulates CD4(+) T cells by inhibiting NDPK-B-mediated histidine phosphorylation and activation of the K(+) channel KCa3.1, which is required for TCR-stimulated Ca(2+) influx and cytokine production. Using recently developed monoclonal antibodies that specifically recognize phosphorylation of nitrogens at the N1 (1-pHis) or N3 (3-pHis) positions of the imidazole ring, we detect for the first time phosphoisoform-specific regulation of histidine-phosphorylated proteins in vivo, and we link these modifications to TCR signaling. These results represent an important step forward in studying the role of histidine phosphorylation in mammalian biology and disease.
[Mh] Termos MeSH primário: Linfócitos T CD4-Positivos/enzimologia
Ativação Linfocitária
Proteínas Mitocondriais/metabolismo
Fosfoproteínas Fosfatases/metabolismo
[Mh] Termos MeSH secundário: Animais
Linfócitos T CD4-Positivos/imunologia
Sinalização do Cálcio
Citocinas/metabolismo
Predisposição Genética para Doença
Doença Enxerto-Hospedeiro/enzimologia
Doença Enxerto-Hospedeiro/genética
Doença Enxerto-Hospedeiro/imunologia
Células HEK293
Transplante de Células-Tronco Hematopoéticas/efeitos adversos
Histidina
Seres Humanos
Mediadores da Inflamação/metabolismo
Canais de Potássio Ativados por Cálcio de Condutância Intermediária/metabolismo
Células Jurkat
Camundongos Endogâmicos BALB C
Camundongos Endogâmicos C57BL
Camundongos Knockout
Proteínas Mitocondriais/genética
Núcleosídeo-Difosfato Quinase/metabolismo
Fenótipo
Fosfoproteínas Fosfatases/deficiência
Fosfoproteínas Fosfatases/genética
Fosforilação
Interferência de RNA
Receptores de Antígenos de Linfócitos T/metabolismo
Fatores de Tempo
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cytokines); 0 (Inflammation Mediators); 0 (Intermediate-Conductance Calcium-Activated Potassium Channels); 0 (KCNN4 protein, human); 0 (Kcnn4 protein, mouse); 0 (Mitochondrial Proteins); 0 (Receptors, Antigen, T-Cell); 4QD397987E (Histidine); EC 2.7.4.6 (Nucleoside-Diphosphate Kinase); EC 2.7.4.6. (NDPK-B protein, human); EC 3.1.3.16 (PGAM5 protein, human); EC 3.1.3.16 (PGAM5 protein, mouse); EC 3.1.3.16 (Phosphoprotein Phosphatases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171111
[Lr] Data última revisão:
171111
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160726
[St] Status:MEDLINE


  8 / 1578 MEDLINE  
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[PMID]:27449069
[Au] Autor:Romani P; Papi A; Ignesti M; Soccolini G; Hsu T; Gargiulo G; Spisni E; Cavaliere V
[Ad] Endereço:Dipartimento di Farmacia e biotecnologie, Alma Mater Studiorum Università di Bologna, Bologna, Italy.
[Ti] Título:Dynamin controls extracellular level of Awd/Nme1 metastasis suppressor protein.
[So] Source:Naunyn Schmiedebergs Arch Pharmacol;389(11):1171-1182, 2016 Nov.
[Is] ISSN:1432-1912
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Dynamin GTPase (Dyn) plays a critical role in membrane-remodelling events underlying endocytosis. Studies in Drosophila identified a functional interaction between the Dyn homologue, encoded by the shibire (shi) gene, and Abnormal wing discs (Awd), a nucleoside diphosphate kinase (NDPK) that is the homologue of group I Nme human genes. These Drosophila studies showed that awd mutations enhance mutant shi phenotype and thus indicated the existence of a highly specific interaction between these genes. Furthermore, in human cells, it has been shown that Nme proteins promote Dyn activity in different membrane compartments through spatially controlled supply of GTP. Interestingly, Awd and Nme proteins have been detected in the extracellular environment. While no role has been inferred to extracellular Awd, presence of Nme1 in cancer patient serum is an unfavourable prognostic marker. In the present work, we used Drosophila and human cell line models to investigate the shuttling Awd/Nme1 proteins between intracellular and extracellular spaces. By using classic and reverse genetic approaches, we show that downregulation of Shi/Dyn1 activity enhances extracellular Awd/Nme1 in both Drosophila and human colon cell lines. We extended our analyses to colon cancer cell lines and found that knocking down Dyn1, besides to raise Nme1 extracellular amount, downregulates expression of molecular components that play key roles in tumour invasion. Interestingly, in vivo analyses of Drosophila larval adipocytes show that the conditional block of Shi activity greatly reduces intracellular amount of Awd confirming that Shi plays a key role in controlling the balance between intracellular and extracellular Awd.
[Mh] Termos MeSH primário: Neoplasias do Colo/enzimologia
Proteínas de Drosophila/metabolismo
Drosophila melanogaster/enzimologia
Dinamina I/metabolismo
Dinaminas/metabolismo
Nucleosídeo NM23 Difosfato Quinases/metabolismo
Núcleosídeo-Difosfato Quinase/metabolismo
[Mh] Termos MeSH secundário: Adipócitos/enzimologia
Animais
Animais Geneticamente Modificados
Neoplasias do Colo/genética
Proteínas de Drosophila/genética
Drosophila melanogaster/genética
Dinamina I/genética
Dinaminas/genética
Regulação Enzimológica da Expressão Gênica
Regulação Neoplásica da Expressão Gênica
Genótipo
Células HT29
Seres Humanos
Larva/enzimologia
Mutação
Nucleosídeo NM23 Difosfato Quinases/genética
Núcleosídeo-Difosfato Quinase/genética
Fenótipo
Interferência de RNA
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Drosophila Proteins); 0 (NM23 Nucleoside Diphosphate Kinases); EC 2.7.4.6 (NME1 protein, human); EC 2.7.4.6 (Nucleoside-Diphosphate Kinase); EC 2.7.4.6 (awd protein, Drosophila); EC 3.5.1.50 (Dynamin I); EC 3.6.5.5 (Dynamins); EC 3.6.5.5 (shibire protein, Drosophila)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160725
[St] Status:MEDLINE


  9 / 1578 MEDLINE  
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[PMID]:27268980
[Au] Autor:Yamaguchi N; Yoshinaga M; Kamino K; Ueki T
[Ad] Endereço:1 Marine Biological Laboratory, Graduate School of Science, Hiroshima University, Mukaishima-cho 2445, Onomichi city, Hiroshima 722-0073, Japan.
[Ti] Título:Vanadium-Binding Ability of Nucleoside Diphosphate Kinase from the Vanadium-Rich Fan Worm, Pseudopotamilla occelata.
[So] Source:Zoolog Sci;33(3):266-71, 2016 Jun.
[Is] ISSN:0289-0003
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:Polychaete fan worms and ascidians accumulate high levels of vanadium ions. Several vanadiumbinding proteins, known as vanabins, have been found in ascidians. However, no vanadium-binding factors have been isolated from the fan worm. In the present study, we sought to identify vanadiumbinding proteins in the branchial crown of the fan worm using immobilized metal ion affinity chromatography. A nucleoside diphosphate kinase (NDK) homolog was isolated and determined to be a vanadium-binding protein. Kinase activity of the NDK homologue, PoNDK, was suppressed by the addition of V(IV), but was unaffected by V(V). The effect of V(IV) on PoNDK precedes its activation by Mg(II). This is the first report to describe the relationship between NDK and V(IV). PoNDK is located in the epidermis of the branchial crown, and its distribution is very similar to that of vanadium. These results suggest that PoNDK is associated with vanadium accumulation and metabolism in P. occelata.
[Mh] Termos MeSH primário: Núcleosídeo-Difosfato Quinase/metabolismo
Poliquetos/enzimologia
Vanádio/metabolismo
[Mh] Termos MeSH secundário: Animais
Proteínas de Transporte
Cromatografia de Afinidade
Epiderme/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carrier Proteins); 00J9J9XKDE (Vanadium); EC 2.7.4.6 (Nucleoside-Diphosphate Kinase)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160609
[St] Status:MEDLINE
[do] DOI:10.2108/zs150188


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[PMID]:27072556
[Au] Autor:Lopez-Zavala AA; Sotelo-Mundo RR; Hernandez-Flores JM; Lugo-Sanchez ME; Sugich-Miranda R; Garcia-Orozco KD
[Ad] Endereço:Departamento de Ciencias Químico Biológicas, Universidad de Sonora, Calle Rosales y Blvd. Luis Encinas s/n, Col. Centro, Hermosillo, Sonora, 83000, México.
[Ti] Título:Arginine kinase shows nucleoside diphosphate kinase-like activity toward deoxythymidine diphosphate.
[So] Source:J Bioenerg Biomembr;48(3):301-8, 2016 06.
[Is] ISSN:1573-6881
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Arginine kinase (AK) (ATP: L-arginine phosphotransferase, E.C. 2.7.3.3) catalyzes the reversible transfer of ATP γ-phosphate group to L-arginine to synthetize phospho-arginine as a high-energy storage. Previous studies suggest additional roles for AK in cellular processes. Since AK is found only in invertebrates and it is homologous to creatine kinase from vertebrates, the objective of this work was to demonstrate nucleoside diphosphate kinase-like activity for shrimp AK. For this, AK from marine shrimp Litopenaeus vannamei (LvAK) was purified and its activity was assayed for phosphorylation of TDP using ATP as phosphate donor. Moreover, by using high-pressure liquid chromatography (HPLC) the phosphate transfer reaction was followed. Also, LvAK tryptophan fluorescence emission changes were detected by dTDP titration, suggesting that the hydrophobic environment of Trp 221, which is located in the top of the active site, is perturbed upon dTDP binding. The kinetic constants for both substrates Arg and dTDP were calculated by isothermal titration calorimetry (ITC). Besides, docking calculations suggested that dTDP could bind LvAK in the same cavity where ATP bind, and LvAK basic residues (Arg124, 126 and 309) stabilize the dTDP phosphate groups and the pyrimidine base interact with His284 and Ser122. These results suggest that LvAK bind and phosphorylate dTDP being ATP the phosphate donor, thus describing a novel alternate nucleoside diphosphate kinase-like activity for this enzyme.
[Mh] Termos MeSH primário: Arginina Quinase/metabolismo
Núcleosídeo-Difosfato Quinase/metabolismo
Penaeidae/enzimologia
Nucleotídeos de Timina/metabolismo
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Animais
Simulação de Acoplamento Molecular
Fosforilação
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Thymine Nucleotides); 2863-04-9 (thymidine 3',5'-diphosphate); 8L70Q75FXE (Adenosine Triphosphate); EC 2.7.3.3 (Arginine Kinase); EC 2.7.4.6 (Nucleoside-Diphosphate Kinase)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:171021
[Lr] Data última revisão:
171021
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160414
[St] Status:MEDLINE
[do] DOI:10.1007/s10863-016-9660-1



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