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[PMID]:29311464
[Au] Autor:Sato S; Tsushima M; Nakamura K; Nakamura H
[Ad] Endereço:Laboratory for Chemistry and Life Science, Institute of Innovative Research, Tokyo Institute of Technology.
[Ti] Título:[Development and Application of Catalytic Tyrosine Modification].
[So] Source:Yakugaku Zasshi;138(1):39-46, 2018.
[Is] ISSN:1347-5231
[Cp] País de publicação:Japan
[La] Idioma:jpn
[Ab] Resumo:The chemical labeling of proteins with synthetic probes is a key technique used in chemical biology, protein-based therapy, and material science. Much of the chemical labeling of native proteins, however, depends on the labeling of lysine and cysteine residues. While those methods have significantly contributed to native protein labeling, alternative methods that can modify different amino acid residues are still required. Herein we report the development of a novel methodology of tyrosine labeling, inspired by the luminol chemiluminescence reaction. Tyrosine residues are often exposed on a protein's surface and are thus expected to be good targets for protein functionalization. In our studies so far, we have found that 1) hemin oxidatively activates luminol derivatives as a catalyst, 2) N-methyl luminol derivative specifically forms a covalent bond with a tyrosine residue among the 20 kinds of natural amino acid residues, and 3) the efficiency of tyrosine labeling with N-methyl luminol derivative is markedly improved by using horseradish peroxidase (HRP) as a catalyst. We were able to use molecular oxygen as an oxidant under HRP/NADH conditions. By using these methods, the functionalization of purified proteins was carried out. Because N-methyl luminol derivative is an excellent protein labeling reagent that responds to the activation of peroxidase, this new method is expected to open doors to such biological applications as the signal amplification of HRP-conjugated antibodies and the detection of protein association in combination with peroxidase-tag technology.
[Mh] Termos MeSH primário: Tirosina/química
[Mh] Termos MeSH secundário: Catálise
Heme/química
Hemeproteínas/química
Luminescência
Luminol/química
Peroxidase/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Hemeproteins); 42HK56048U (Tyrosine); 42VZT0U6YR (Heme); 5EXP385Q4F (Luminol); EC 1.11.1.7 (Peroxidase)
[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:180110
[St] Status:MEDLINE
[do] DOI:10.1248/yakushi.17-00186-1


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[PMID]:28458146
[Au] Autor:Guimarães WG; Gondim ACS; Costa PMDS; Gilles-Gonzalez MA; Lopes LGF; Carepo MSP; Sousa EHS
[Ad] Endereço:Laboratório de Bioinorgânica, Departamento de Química Orgânica e Inorgânica, Universidade Federal do Ceará, CEP 60455-760 Fortaleza, Ceará, Brazil.
[Ti] Título:Insights into signal transduction by a hybrid FixL: Denaturation study of on and off states of a multi-domain oxygen sensor.
[So] Source:J Inorg Biochem;172:129-137, 2017 Jul.
[Is] ISSN:1873-3344
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:FixL from Rhizobium etli (ReFixL) is a hybrid oxygen sensor protein. Signal transduction in ReFixL is effected by a switch off of the kinase activity on binding of an oxygen molecule to ferrous heme iron in another domain. Cyanide can also inhibit the kinase activity upon binding to the heme iron in the ferric state. The unfolding by urea of the purified full-length ReFixL in both active pentacoordinate form, met-FixL(Fe ) and inactive cyanomet-FixL (Fe -CN ) form was monitored by UV-visible absorption spectroscopy, circular dichroism (CD) and fluorescence spectroscopy. The CD and UV-visible absorption spectroscopy revealed two states during unfolding, whereas fluorescence spectroscopy identified a three-state unfolding mechanism. The unfolding mechanism was not altered for the active compared to the inactive state; however, differences in the ΔG were observed. According to the CD results, compared to cyanomet-FixL, met-FixL was more stable towards chemical denaturation by urea (7.2 vs 4.8kJmol ). By contrast, electronic spectroscopy monitoring of the Soret band showed cyanomet-FixL to be more stable than met-FixL (18.5 versus 36.2kJmol ). For the three-state mechanism exhibited by fluorescence, the ΔG for both denaturation steps were higher for the active-state met-FixL than for cyanomet-FixL. The overall stability of met-FixL is higher in comparison to cyanomet-FixL suggesting a more compact protein in the active form. Nonetheless, hydrogen bonding by bound cyanide in the inactive state promotes the stability of the heme domain. This work supports a model of signal transduction by FixL that is likely shared by other heme-based sensors.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Hemeproteínas/metabolismo
Oxigênio/metabolismo
Transdução de Sinais/fisiologia
[Mh] Termos MeSH secundário: Fluorescência
Oxigênio/química
Desnaturação Proteica
Dobramento de Proteína
Análise Espectral
Ureia/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (FixL protein, Bacteria); 0 (Hemeproteins); 8W8T17847W (Urea); S88TT14065 (Oxygen)
[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:170502
[St] Status:MEDLINE


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[PMID]:28919415
[Au] Autor:Hoshino M; Nakakido M; Nagatoishi S; Aikawa C; Nakagawa I; Tsumoto K
[Ad] Endereço:Department of Bioengineering, School of Engineering, The University of Tokyo, Bunkyo-ku, Tokyo 113-8656, Japan.
[Ti] Título:Biophysical characterization of the interaction between heme and proteins responsible for heme transfer in Streptococcus pyogenes.
[So] Source:Biochem Biophys Res Commun;493(2):1109-1114, 2017 Nov 18.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Streptococcus pyogenes, an important pathogen that causes a wide range of diseases, possesses the sia gene cluster, which encodes proteins involved in the heme acquisition system. Although this system was previously described, the molecular mechanism of effective heme transfer remains to be elucidated. Here, we have characterized the interactions between heme and each domain of Streptococcal hemoprotein receptor (Shr) and Streptococcal heme-binding protein (Shp). Our kinetic and thermodynamic analyses suggested that effective heme transfer within this system is achieved not only by affinity-based transfer but also by the difference of the binding driving force. The biophysical characterization of the above-mentioned interaction will lead to an indication for the selection of the target for a chemical screening of inhibitors as novel antibacterial agents based on biophysical approaches.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Proteínas de Transporte/metabolismo
Heme/metabolismo
Hemeproteínas/metabolismo
Hemoglobinas/metabolismo
Infecções Estreptocócicas/metabolismo
Streptococcus pyogenes/fisiologia
[Mh] Termos MeSH secundário: Seres Humanos
Modelos Moleculares
Ligação Proteica
Infecções Estreptocócicas/microbiologia
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Carrier Proteins); 0 (Hemeproteins); 0 (Hemoglobins); 0 (heme-binding protein); 42VZT0U6YR (Heme)
[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:170919
[St] Status:MEDLINE


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[PMID]:28876054
[Au] Autor:Pavlou A; Loullis A; Yoshimura H; Aono S; Pinakoulaki E
[Ad] Endereço:Department of Chemistry, University of Cyprus , P.O. Box 20537, 1678 Nicosia, Cyprus.
[Ti] Título:Probing the Role of the Heme Distal and Proximal Environment in Ligand Dynamics in the Signal Transducer Protein HemAT by Time-Resolved Step-Scan FTIR and Resonance Raman Spectroscopy.
[So] Source:Biochemistry;56(40):5309-5317, 2017 Oct 10.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:HemAT is a heme-containing oxygen sensor protein that controls aerotaxis. Time-resolved step-scan FTIR studies were performed on the isolated sensor domain and full-length HemAT proteins as well as on the Y70F (B-helix), L92A (E-helix), T95A (E-helix), and Y133F (G-helix) mutants to elucidate the effect of the site-specific mutations on the ligand dynamics subsequent to CO photolysis. The mutations aimed to perturb H-bonding and electrostatic interactions near the heme Fe-bound gaseous ligand (CO) and the heme proximal environment. Rebinding of CO to the heme Fe is biphasic in the sensor domain and full-length HemAT as well as in the mutants, with the exception of the Y133F mutant protein. The monophasic rebinding of CO in Y133F suggests that in the absence of the H-bond between Y133 and the heme proximal H123 residue the ligand rebinding process is significantly affected. The role of the proximal environment is also probed by resonance Raman photodissociation experiments, in which the Fe-His mode of the photoproduct of sensor domain HemAT-CO is detected at a frequency higher than that of the deoxy form in the difference resonance Raman spectra. The role of the conformational changes of Y133 (G-helix) and the role of the distal L92 and T95 residues (E-helix) in regulating ligand dynamics in the heme pocket are discussed.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Proteínas de Bactérias/metabolismo
Heme/metabolismo
Hemeproteínas/química
Hemeproteínas/metabolismo
Espectroscopia de Infravermelho com Transformada de Fourier
Análise Espectral Raman
[Mh] Termos MeSH secundário: Ligantes
Modelos Moleculares
Ligação Proteica
Conformação Proteica
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Hemeproteins); 0 (Ligands); 0 (heme protein, bacteria); 42VZT0U6YR (Heme)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171019
[Lr] Data última revisão:
171019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170907
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00558


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[PMID]:28810849
[Au] Autor:Olanlokun JO; David OM; Afolayan AJ
[Ad] Endereço:Laboratories for Biomembrane Research and Biotechnology, Department of Biochemistry, Faculty of Basic Medical Sciences, College of Medicine, University of Ibadan, Ibadan, Nigeria. jodel72000@yahoo.com.
[Ti] Título:In vitro antiplasmodial activity and prophylactic potentials of extract and fractions of Trema orientalis (Linn.) stem bark.
[So] Source:BMC Complement Altern Med;17(1):407, 2017 Aug 15.
[Is] ISSN:1472-6882
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Trema orientalis (T. orientalis Linn) has been used in the management of malaria in the western part of Nigeria and despite its application in ethnomedicine, there is dearth of scientific evidence to justify the acclaimed prophylactic antimalarial usage of the plant. The aim of this study is to assess the in vitro antiplasmodial cell-free assay and chemopreventive efficacy of the methanol extract of the stem bark of T. orientalis and its fractions as a prophylactic regimen for malaria prevention. Also, the antimicrobial activities of the extract and the fractions were investigated. METHOD: Vacuum liquid chromatography was used to obtain dichloromethane, ethylacetate and methanol fractions from the methanol extract of T. orientalis. The fractions were tested for their prophylactic and cell-free antimalarial activity using murine models and ß-hematin formation assay respectively. Disc diffusion method was used to determine the antibacterial activity of the extract and its fractions against both Gram-positive and Gram-negative bacteria. RESULTS: In the prophylactic experiment, dichloromethane (DCMF), methanol fraction (MF) and extract (ME) (in this order) showed significant chemopreventive effects against P. berghei invasion of the red blood cells when compared with both Sulfadoxine-Pyrimethamine (SP) and untreated controls. Results of the in vitro study showed that the DCMF had the highest effect in preventing the formation of ß-hematin when compared with other fractions. The DCMF also had the highest percentage inhibition of ß-hematin formation when compared with chloroquine. The extract and fractions showed a concentration dependent antibacterial activity. Methanol extract had a pronounced inhibitory effect on Enterobacter cloaca ATCC 13047 and Enterococcus faecalis ATCC 29212. Serratia mercescens ATCC 9986 and Pseudomonas aeruginosa ATCC 19582 were the most susceptible bacteria. CONCLUSION: The results obtained showed that both extract and fractions of T. orientalis possessed antiplasmodial and antimicrobial activity.
[Mh] Termos MeSH primário: Antimaláricos/uso terapêutico
Malária/prevenção & controle
Fitoterapia
Extratos Vegetais/uso terapêutico
Plasmodium berghei/efeitos dos fármacos
Trema
[Mh] Termos MeSH secundário: Animais
Antibacterianos/farmacologia
Antimaláricos/farmacologia
Bactérias Gram-Negativas/efeitos dos fármacos
Bactérias Gram-Positivas/efeitos dos fármacos
Hemeproteínas/metabolismo
Malária/sangue
Malária/parasitologia
Masculino
Camundongos
Casca de Planta
Extratos Vegetais/farmacologia
Caules de Planta
Plasmodium berghei/crescimento & desenvolvimento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Antimalarials); 0 (Hemeproteins); 0 (Plant Extracts); 39404-00-7 (hemozoin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170901
[Lr] Data última revisão:
170901
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170817
[St] Status:MEDLINE
[do] DOI:10.1186/s12906-017-1914-x


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[PMID]:28732053
[Au] Autor:Maknitikul S; Luplertlop N; Grau GER; Ampawong S
[Ad] Endereço:Department of Tropical Pathology, Faculty of Tropical Medicine, Mahidol University, Ratchathewi, Bangkok, Thailand.
[Ti] Título:Dysregulation of pulmonary endothelial protein C receptor and thrombomodulin in severe falciparum malaria-associated ARDS relevant to hemozoin.
[So] Source:PLoS One;12(7):e0181674, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:To investigate the role of the protein C system, endothelial protein C receptor (EPCR) and thrombomodulin (TM) in the pathogenesis of malaria-associated acute respiratory distress syndrome (ARDS) in relation to hemozoin and proinflammatory cytokines-induced type II pneumocyte injury and -aggravated pulmonary resolution. A total of 29 left-over lung specimens that were obtained from patients who died from severe falciparum malaria were examined. Histopathological, immunohistochemical and electron microscopic analyses revealed that ARDS coexisted with pulmonary edema and systemic bleeding; the severity was dependent on the level of hemozoin deposition in the lung and internal alveolar hemorrhaging. The loss of EPCR and TM was primarily identified in ARDS patients and was related to the level of hemozoin, parasitized red blood cell (PRBC) and white blood cell accumulation in the lung. Moreover, an in vitro analysis demonstrated that interleukin-13 and -31 and hemozoin induced pneumocytic cell injury and apoptosis, as assessed by EB/AO staining, electron microscopy and the up-regulation of CARD-9 mRNA (caspase recruitment domain-9 messenger-ribonucleic acid). The dysregulation of EPCR and TM in the lung, especially in those with increased levels of hemozoin, may play an important role in the pathogenesis of malaria-associated ARDS through an apoptotic pathway.
[Mh] Termos MeSH primário: Antígenos CD/metabolismo
Hemeproteínas/uso terapêutico
Pulmão/metabolismo
Malária Falciparum/tratamento farmacológico
Receptores de Superfície Celular/metabolismo
Síndrome do Desconforto Respiratório do Adulto/metabolismo
Síndrome do Desconforto Respiratório do Adulto/parasitologia
Trombomodulina/metabolismo
[Mh] Termos MeSH secundário: Células A549
Adolescente
Adulto
Criança
Pré-Escolar
Citocinas/metabolismo
Receptor de Proteína C Endotelial
Feminino
Seres Humanos
Interleucina-13/metabolismo
Pulmão/parasitologia
Masculino
Meia-Idade
Proteína C/metabolismo
Edema Pulmonar/metabolismo
Edema Pulmonar/parasitologia
Regulação para Cima/efeitos dos fármacos
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, CD); 0 (Cytokines); 0 (Endothelial Protein C Receptor); 0 (Hemeproteins); 0 (Interleukin-13); 0 (PROCR protein, human); 0 (Protein C); 0 (Receptors, Cell Surface); 0 (Thrombomodulin); 39404-00-7 (hemozoin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170722
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0181674


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[PMID]:28710276
[Au] Autor:Qasem-Abdullah H; Perach M; Livnat-Levanon N; Lewinson O
[Ad] Endereço:From the Department of Biochemistry, The Bruce and Ruth Rappaport Faculty of Medicine, The Technion-Israel Institute of Technology, Haifa 31096, Israel.
[Ti] Título:ATP binding and hydrolysis disrupt the high-affinity interaction between the heme ABC transporter HmuUV and its cognate substrate-binding protein.
[So] Source:J Biol Chem;292(35):14617-14624, 2017 Sep 01.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Using the energy of ATP hydrolysis, ABC transporters catalyze the trans-membrane transport of molecules. In bacteria, these transporters partner with a high-affinity substrate-binding protein (SBP) to import essential micronutrients. ATP binding by Type I ABC transporters (importers of amino acids, sugars, peptides, and small ions) stabilizes the interaction between the transporter and the SBP, thus allowing transfer of the substrate from the latter to the former. In Type II ABC transporters (importers of trace elements, vitamin B , heme, and iron-siderophores) the role of ATP remains debatable. Here we studied the interaction between the ABC heme importer (HmuUV) and its partner substrate-binding protein (HmuT). Using real-time surface plasmon resonance experiments and interaction studies in membrane vesicles, we find that in the absence of ATP the transporter and the SBP tightly bind. Substrate in excess inhibits this interaction, and ATP binding by the transporter completely abolishes it. To release the stable docked SBP from the transporter hydrolysis of ATP is required. Based on these results we propose a mechanism for heme acquisition by HmuUV-T where the substrate-loaded SBP docks to the nucleotide-free outward-facing conformation of the transporter. ATP binding leads to formation of an occluded state with the substrate trapped in the trans-membrane translocation cavity. Subsequent ATP hydrolysis leads to substrate delivery to the cytoplasm, release of the SBP, and resetting of the system. We propose that other Type II ABC transporters likely share the fundamentals of this mechanism.
[Mh] Termos MeSH primário: Transportadores de Cassetes de Ligação de ATP/metabolismo
Trifosfato de Adenosina/metabolismo
Proteínas de Bactérias/metabolismo
Proteínas de Transporte/metabolismo
Heme/metabolismo
Hemeproteínas/metabolismo
Modelos Moleculares
Yersinia pestis/metabolismo
[Mh] Termos MeSH secundário: Transportadores de Cassetes de Ligação de ATP/química
Transportadores de Cassetes de Ligação de ATP/genética
Trifosfato de Adenosina/química
Apoenzimas/química
Apoenzimas/genética
Apoenzimas/metabolismo
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Proteínas de Transporte/química
Proteínas de Transporte/genética
Membrana Celular/química
Membrana Celular/metabolismo
Dimerização
Heme/química
Hemeproteínas/química
Hemeproteínas/genética
Holoenzimas/química
Holoenzimas/genética
Holoenzimas/metabolismo
Hidrólise
Proteínas Imobilizadas/química
Proteínas Imobilizadas/genética
Proteínas Imobilizadas/metabolismo
Cinética
Simulação de Acoplamento Molecular
Domínios e Motivos de Interação entre Proteínas
Multimerização Proteica
Receptores de Superfície Celular/química
Receptores de Superfície Celular/genética
Receptores de Superfície Celular/metabolismo
Proteínas Recombinantes
Ressonância de Plasmônio de Superfície
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Apoenzymes); 0 (Bacterial Proteins); 0 (Carrier Proteins); 0 (Hemeproteins); 0 (Holoenzymes); 0 (Immobilized Proteins); 0 (Receptors, Cell Surface); 0 (Recombinant Proteins); 0 (heme-binding protein); 42VZT0U6YR (Heme); 8L70Q75FXE (Adenosine Triphosphate)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170716
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.779975


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[PMID]:28581477
[Au] Autor:Sinclair J; Pinter K; Samuel T; Beardsley S; Yuan X; Zhang J; Meng K; Yun S; Krause M; Hamza I
[Ad] Endereço:Department of Animal &Avian Sciences and Department of Cell Biology &Molecular Genetics, University of Maryland, College Park, Maryland 20742, USA.
[Ti] Título:Inter-organ signalling by HRG-7 promotes systemic haem homeostasis.
[So] Source:Nat Cell Biol;19(7):799-807, 2017 Jul.
[Is] ISSN:1476-4679
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Growing evidence in vertebrates predicts that cellular haem levels in animals are maintained not only by a cell's internal capacity for haem synthesis in a cell-autonomous manner, but also by an inter-organ haem trafficking network through cell-non-autonomous regulation. Using Caenorhabditis elegans, a genetically and optically amenable animal model for visualizing haem-dependent signalling, we show that HRG-7, a protein with homology to aspartic proteases, mediates inter-organ signalling between the intestine and extra-intestinal tissues. Intestinal HRG-7 functions as a secreted signalling factor during haem starvation in extra-intestinal tissues and is regulated through a DBL-1, homologous to BMP5, dependent signal from neurons. Given the evidence that vertebrate homologues exist for each of the components of the HRG-7-mediated signalling pathway, it is conceivable that the cell-non-autonomous signalling framework that we uncovered in C. elegans may have functional relevance for inter-organ regulation of iron and haem metabolism in humans.
[Mh] Termos MeSH primário: Proteínas de Caenorhabditis elegans/metabolismo
Caenorhabditis elegans/metabolismo
Heme/metabolismo
Hemeproteínas/metabolismo
Intestinos/metabolismo
Transdução de Sinais
[Mh] Termos MeSH secundário: Animais
Animais Geneticamente Modificados
Transporte Biológico
Caenorhabditis elegans/genética
Proteínas de Caenorhabditis elegans/genética
Proteínas de Transporte/genética
Proteínas de Transporte/metabolismo
Regulação da Expressão Gênica
Heme/deficiência
Hemeproteínas/genética
Homeostase
Neurônios/metabolismo
Neuropeptídeos/genética
Neuropeptídeos/metabolismo
Interferência de RNA
Fatores de Tempo
Fatores de Transcrição/genética
Fatores de Transcrição/metabolismo
Fator de Crescimento Transformador beta/genética
Fator de Crescimento Transformador beta/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Caenorhabditis elegans Proteins); 0 (Carrier Proteins); 0 (Dbl-1 protein, C elegans); 0 (Hemeproteins); 0 (Hrg-1 protein, C elegans); 0 (Neuropeptides); 0 (Sma-9 protein, C elegans); 0 (Transcription Factors); 0 (Transforming Growth Factor beta); 42VZT0U6YR (Heme)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170913
[Lr] Data última revisão:
170913
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170606
[St] Status:MEDLINE
[do] DOI:10.1038/ncb3539


  9 / 3526 MEDLINE  
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[PMID]:28549573
[Au] Autor:Sterkel M; Oliveira JHM; Bottino-Rojas V; Paiva-Silva GO; Oliveira PL
[Ad] Endereço:Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21941-902, Brazil.
[Ti] Título:The Dose Makes the Poison: Nutritional Overload Determines the Life Traits of Blood-Feeding Arthropods.
[So] Source:Trends Parasitol;33(8):633-644, 2017 08.
[Is] ISSN:1471-5007
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Vertebrate blood composition is heavily biased towards proteins, and hemoglobin, which is a hemeprotein, is by far the most abundant protein. Typically, hematophagous insects ingest blood volumes several times their weight before the blood meal. This barbarian feast offers an abundance of nutrients, but the degradation of blood proteins generates toxic concentrations of amino acids and heme, along with unparalleled microbiota growth. Despite this challenge, hematophagous arthropods have successfully developed mechanisms that bypass the toxicity of these molecules. While these adaptations allow hematophagous arthropods to tolerate their diet, they also constitute a unique mode of operation for cell signaling, immunity, and metabolism, the study of which may offer insights into the biology of disease vectors and may lead to novel vector-specific control methods.
[Mh] Termos MeSH primário: Vetores Artrópodes/metabolismo
Artrópodes/metabolismo
Hemeproteínas/metabolismo
Fenômenos Fisiológicos da Nutrição/fisiologia
[Mh] Termos MeSH secundário: Adaptação Fisiológica
Animais
Vetores Artrópodes/imunologia
Vetores Artrópodes/microbiologia
Artrópodes/imunologia
Artrópodes/microbiologia
Comportamento Alimentar/fisiologia
Transdução de Sinais/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Hemeproteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171121
[Lr] Data última revisão:
171121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170528
[St] Status:MEDLINE


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[PMID]:28521711
[Au] Autor:Rai J
[Ad] Endereço:Institute of Forensic Science and Criminology, Panjab University, Chandigarh, Pin code 160014. India.
[Ti] Título:Mini Heme-Proteins: Designability of Structure and Diversity of Functions.
[So] Source:Curr Protein Pept Sci;18(11):1132-1140, 2017 Aug 30.
[Is] ISSN:1875-5550
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Natural heme proteins may have heme bound to poly-peptide chain as a cofactor via noncovalent forces or heme as a prosthetic group may be covalently bound to the proteins. Nature has used porphyrins in diverse functions like electron transfer, oxidation, reduction, ligand binding, photosynthesis, signaling, etc. by modulating its properties through diverse protein matrices. Synthetic chemists have tried to utilize these molecules in equally diverse industrial and medical applications due to their versatile electro-chemical and optical properties. The heme iron has catalytic activity which can be modulated and enhanced for specific applications by protein matrix around it. Heme proteins can be designed into novel enzymes for sterio specific catalysis ranging from oxidation to reduction. These designed heme-proteins can have applications in industrial catalysis and biosensing. A peptide folds around heme easily due to hydrophobic effect of the large aromatic ring of heme. The directional property of co-ordinate bonding between peptide and metal ion in heme further specifies the structure. Therefore heme proteins can be easily designed for targeted structure and catalytic activity. The central aromatic chemical entity in heme viz. porphyrin is a very ancient molecule. Its presence in the prebiotic soup and in all forms of life suggests that it has played a vital role in the origin and progressive evolution of living organisms. Porphyrin macrocycles are highly conjugated systems composed of four modified pyrrole subunits interconnected at their α -carbon atoms via methine (=CH-) bridges. Initial minimalist models of hemoproteins focused on effect of heme-ligand co-ordinate bonding on chemical reactivity, spectroscopy, electrochemistry and magnetic properties of heme. The great sensitivity of these spectroscopic features of heme to its surrounding makes them extremely useful in structural elucidation of designed heme-peptide complexes. Therefore heme proteins are easier to work on for designing novel proteins for industrial and medical applications.
[Mh] Termos MeSH primário: Técnicas Eletroquímicas
Heme/química
Hemeproteínas/química
Porfirinas/química
Engenharia de Proteínas
[Mh] Termos MeSH secundário: Evolução Biológica
Hemeproteínas/síntese química
Seres Humanos
Interações Hidrofóbicas e Hidrofílicas
Ligantes
Modelos Moleculares
Oxirredução
Dobramento de Proteína
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Hemeproteins); 0 (Ligands); 0 (Porphyrins); 42VZT0U6YR (Heme)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171106
[Lr] Data última revisão:
171106
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170520
[St] Status:MEDLINE
[do] DOI:10.2174/1389203718666170515144037



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