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Pesquisa : D08.811.277.450.430.700 [Categoria DeCS]
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[PMID]:29202361
[Au] Autor:Weng A
[Ad] Endereço:Institut für Pharmazie, Freie Universität Berlin, Königin-Luise-Str 2+4, 14195 Berlin, Germany. Electronic address: alexander.weng@fu-berlin.de.
[Ti] Título:A novel adenine-releasing assay for ribosome-inactivating proteins.
[So] Source:J Chromatogr B Analyt Technol Biomed Life Sci;1072:300-304, 2018 Jan 01.
[Is] ISSN:1873-376X
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Ribosome-inactivating proteins (RIPs) are toxic enzymes that are mostly biosynthesized by plants. RIPs are N-glycosidases that cleave an essential adenine molecule from the 28S rRNA. This is followed by the irreversible inhibition of protein synthesis leading to cell death. By fusing RIPs to cancer cell specific targeting ligands RIPs have been utilized for targeted anti-tumor therapy. The anti-tumoral efficiency of such conjugates depends significantly on the N-glycosidase activity of the RIP domain. Different methods have been developed in order to determine the N-glycosidase activity of RIPs and RIP domain containing anti-tumor toxins. However the existing methods are elaborate and include radioassays, HPLC and enzymatic conversion assays. Here, a simple and cost effective N-glycosidase assay is presented, which is based on the direct determination of the released adenine by thin-layer chromatography (TLC) and TLC-densitometry. An adenine based single stranded oligonucleotide is used as substrate. Following TLC development the released adenine is quantified on silica glass plates by UV absorbance at 260nm.
[Mh] Termos MeSH primário: Adenina/análise
Cromatografia em Camada Delgada/métodos
Proteínas Inativadoras de Ribossomos/análise
Proteínas Inativadoras de Ribossomos/metabolismo
[Mh] Termos MeSH secundário: Adenina/metabolismo
Dianthus/enzimologia
Dianthus/genética
Ensaios Enzimáticos
Escherichia coli/genética
Modelos Lineares
Proteínas de Plantas/análise
Proteínas de Plantas/genética
Proteínas de Plantas/metabolismo
Proteínas Recombinantes/análise
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Proteínas Inativadoras de Ribossomos/genética
Saponaria/enzimologia
Saponaria/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Plant Proteins); 0 (Recombinant Proteins); EC 3.2.2.22 (Ribosome Inactivating Proteins); JAC85A2161 (Adenine)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180221
[Lr] Data última revisão:
180221
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171205
[St] Status:MEDLINE


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[PMID]:28471452
[Au] Autor:Chowdhury SR; Ray U; Chatterjee BP; Roy SS
[Ad] Endereço:Cell Biology and Physiology Division, CSIR-Indian Institute of Chemical Biology, Council of Scientific and Industrial Research, Kolkata, India.
[Ti] Título:Targeted apoptosis in ovarian cancer cells through mitochondrial dysfunction in response to Sambucus nigra agglutinin.
[So] Source:Cell Death Dis;8(5):e2762, 2017 May 04.
[Is] ISSN:2041-4889
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Ovarian carcinoma (OC) patients encounter the severe challenge of clinical management owing to lack of screening measures, chemoresistance and finally dearth of non-toxic therapeutics. Cancer cells deploy various defense strategies to sustain the tumor microenvironment, among which deregulated apoptosis remains a versatile promoter of cancer progression. Although recent research has focused on identifying agents capable of inducing apoptosis in cancer cells, yet molecules efficiently breaching their survival advantage are yet to be classified. Here we identify lectin, Sambucus nigra agglutinin (SNA) to exhibit selectivity towards identifying OC by virtue of its specific recognition of α-2, 6-linked sialic acids. Superficial binding of SNA to the OC cells confirm the hyper-sialylated status of the disease. Further, SNA activates the signaling pathways of AKT and ERK1/2, which eventually promotes de-phosphorylation of dynamin-related protein-1 (Drp-1). Upon its translocation to the mitochondrial fission loci Drp-1 mediates the central role of switch in the mitochondrial phenotype to attain fragmented morphology. We confirmed mitochondrial outer membrane permeabilization resulting in ROS generation and cytochrome-c release into the cytosol. SNA response resulted in an allied shift of the bioenergetics profile from Warburg phenotype to elevated mitochondrial oxidative phosphorylation, altogether highlighting the involvement of mitochondrial dysfunction in restraining cancer progression. Inability to replenish the SNA-induced energy crunch of the proliferating cancer cells on the event of perturbed respiratory outcome resulted in cell cycle arrest before G2/M phase. Our findings position SNA at a crucial juncture where it proves to be a promising candidate for impeding progression of OC. Altogether we unveil the novel aspect of identifying natural molecules harboring the inherent capability of targeting mitochondrial structural dynamics, to hold the future for developing non-toxic therapeutics for treating OC.
[Mh] Termos MeSH primário: Apoptose/efeitos dos fármacos
Mitocôndrias/metabolismo
Dinâmica Mitocondrial/efeitos dos fármacos
Lectinas de Plantas/farmacologia
Proteínas Inativadoras de Ribossomos/farmacologia
[Mh] Termos MeSH secundário: Sobrevivência Celular/efeitos dos fármacos
Citocromos c/metabolismo
Citosol/metabolismo
Feminino
GTP Fosfo-Hidrolases/metabolismo
Seres Humanos
Potencial da Membrana Mitocondrial/efeitos dos fármacos
Microscopia Confocal
Proteínas Associadas aos Microtúbulos/metabolismo
Proteínas Mitocondriais/metabolismo
Proteína Quinase 1 Ativada por Mitógeno/metabolismo
Proteína Quinase 3 Ativada por Mitógeno/metabolismo
Neoplasias Ovarianas/metabolismo
Neoplasias Ovarianas/patologia
Proteínas Proto-Oncogênicas c-akt/antagonistas & inibidores
Proteínas Proto-Oncogênicas c-akt/metabolismo
Espécies Reativas de Oxigênio/metabolismo
Pontos de Checagem da Fase S do Ciclo Celular/efeitos dos fármacos
Transdução de Sinais/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Microtubule-Associated Proteins); 0 (Mitochondrial Proteins); 0 (Plant Lectins); 0 (Reactive Oxygen Species); 0 (Sambucus nigra lectins); 9007-43-6 (Cytochromes c); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt); EC 2.7.11.24 (Mitogen-Activated Protein Kinase 1); EC 2.7.11.24 (Mitogen-Activated Protein Kinase 3); EC 3.2.2.22 (Ribosome Inactivating Proteins); EC 3.6.1.- (GTP Phosphohydrolases); EC 3.6.5.5 (DNM1L protein, human)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180129
[Lr] Data última revisão:
180129
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1038/cddis.2017.77


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[PMID]:28864671
[Au] Autor:Kutky M; Hudak KA
[Ad] Endereço:Department of Biology, York University, Toronto, Ontario, Canada.
[Ti] Título:Expression of an RNA glycosidase inhibits HIV-1 transactivation of transcription.
[So] Source:Biochem J;474(20):3471-3483, 2017 Oct 05.
[Is] ISSN:1470-8728
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:HIV-1 (human immunodeficiency virus) transcription is primarily controlled by the virally encoded Tat (transactivator of transcription) protein and its interaction with the viral TAR (transcription response element) RNA element. Specifically, binding of a Tat-containing complex to TAR recruits cellular factors that promote elongation of the host RNA polymerase engaging the viral DNA template. Disruption of this interaction halts viral RNA transcription. In the present study, we investigated the effect of pokeweed antiviral protein (PAP), an RNA glycosidase (EC#: 3.2.2.22) synthesized by the pokeweed plant ( ), on transcription of HIV-1 mRNA. We show that co-expression of PAP with a proviral clone in culture cells resulted in a Tat-dependent decrease in viral mRNA levels. PAP reduced HIV-1 transcriptional activity by inhibiting Tat protein synthesis. The effects of PAP expression on host factors AP-1 (activator protein 1), NF-κB (nuclear factor kappa-light-chain-enhancer of activated B-cells) and specificity protein 1, which modulate HIV-1 transcription by binding to the viral LTR (5'-long terminal repeat), were also investigated. Only AP-1 showed a modest JNK pathway-dependent increase in activity in the presence of PAP; however, this activation was not sufficient to significantly enhance transcription from a partial viral LTR containing AP-1 binding sites. Therefore, the primary effect of PAP on HIV-1 transcription is to reduce viral RNA synthesis by decreasing the abundance of Tat. These findings provide a mechanistic explanation for the observed decrease in viral RNAs in cells expressing PAP and contribute to our understanding of the antiviral effects of this plant protein.
[Mh] Termos MeSH primário: Regulação Enzimológica da Expressão Gênica
HIV-1/metabolismo
RNA Viral/biossíntese
Proteínas Inativadoras de Ribossomos/biossíntese
Transcrição Genética/fisiologia
Ativação Transcricional/fisiologia
[Mh] Termos MeSH secundário: Sobrevivência Celular/fisiologia
Células HEK293
HIV-1/genética
Seres Humanos
Células Jurkat
Phytolacca americana
RNA Viral/genética
Proteínas Inativadoras de Ribossomos/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Viral); EC 3.2.2.22 (Ribosome Inactivating Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171012
[Lr] Data última revisão:
171012
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170903
[St] Status:MEDLINE
[do] DOI:10.1042/BCJ20170353


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[PMID]:28797946
[Au] Autor:Wytynck P; Rougé P; Van Damme EJM
[Ad] Endereço:Lab Biochemistry and Glycobiology, Department of Molecular Biotechnology, Ghent University, Coupure Links 653, B-9000, Ghent, Belgium.
[Ti] Título:Genome-wide screening of Oryza sativa ssp. japonica and indica reveals a complex family of proteins with ribosome-inactivating protein domains.
[So] Source:Phytochemistry;143:87-97, 2017 Nov.
[Is] ISSN:1873-3700
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Ribosome-inactivating proteins (RIPs) are cytotoxic enzymes capable of halting protein synthesis by irreversible modification of ribosomes. Although RIPs are widespread they are not ubiquitous in the plant kingdom. The physiological importance of RIPs is not fully elucidated, but evidence suggests a role in the protection of the plant against biotic and abiotic stresses. Searches in the rice genome revealed a large and highly complex family of proteins with a RIP domain. A comparative analysis retrieved 38 RIP sequences from the genome sequence of Oryza sativa subspecies japonica and 34 sequences from the subspecies indica. The RIP sequences are scattered over different chromosomes but are mostly found on the third chromosome. The phylogenetic tree revealed the pairwise clustering of RIPs from japonica and indica. Molecular modeling and sequence analysis yielded information on the catalytic site of the enzyme, and suggested that a large part of RIP domains probably possess N-glycosidase activity. Several RIPs are differentially expressed in plant tissues and in response to specific abiotic stresses. This study provides an overview of RIP motifs in rice and will help to understand their biological role(s) and evolutionary relationships.
[Mh] Termos MeSH primário: Oryza/química
Oryza/genética
Proteínas Inativadoras de Ribossomos/isolamento & purificação
[Mh] Termos MeSH secundário: Sequência de Bases
Genoma de Planta
Filogenia
Domínios Proteicos
Proteínas Inativadoras de Ribossomos/química
Ribossomos
Especificidade da Espécie
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.2.2.22 (Ribosome Inactivating Proteins)
[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:170812
[St] Status:MEDLINE


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[PMID]:28218711
[Au] Autor:Van Damme EJ
[Ad] Endereço:Department of Molecular Biotechnology, Faculty of Bioscience Engineering, Ghent University, 9000 Ghent, Belgium. ElsJM.VanDamme@UGent.be.
[Ti] Título:Special Issue: Ribosome-Inactivating Proteins-Commemorative Issue in Honor of Professor Fiorenzo Stirpe.
[So] Source:Molecules;22(2), 2017 Feb 18.
[Is] ISSN:1420-3049
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:The family of ribosome-inactivating proteins (RIPs) groups all enzymes (EC.3.2.2.22) with a so-called RIP domain which comprises -glycosidase activity and enables these proteins to catalytically inactivate ribosomes.[...].
[Mh] Termos MeSH primário: Pessoas Famosas
Proteínas de Plantas
Pesquisa
Proteínas Inativadoras de Ribossomos
[Mh] Termos MeSH secundário: Antineoplásicos/farmacologia
Antineoplásicos/uso terapêutico
Neoplasias/tratamento farmacológico
Proteínas de Plantas/química
Proteínas de Plantas/metabolismo
Proteínas de Plantas/farmacologia
Proteínas de Plantas/uso terapêutico
Proteínas Inativadoras de Ribossomos/química
Proteínas Inativadoras de Ribossomos/metabolismo
Proteínas Inativadoras de Ribossomos/farmacologia
Proteínas Inativadoras de Ribossomos/uso terapêutico
[Pt] Tipo de publicação:EDITORIAL
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Plant Proteins); EC 3.2.2.22 (Ribosome Inactivating Proteins)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170509
[Lr] Data última revisão:
170509
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170221
[St] Status:MEDLINE


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[PMID]:28134797
[Au] Autor:Bolognesi A; Bortolotti M; Battelli MG; Polito L
[Ad] Endereço:Department of Experimental, Diagnostic and Specialty Medicine-DIMES, Alma Mater Studiorum, University of Bologna, Via San Giacomo 14, 40126 Bologna, Italy. andrea.bolognesi@unibo.it.
[Ti] Título:Hyperuricaemia, Xanthine Oxidoreductase and Ribosome-Inactivating Proteins from Plants: The Contributions of Fiorenzo Stirpe to Frontline Research.
[So] Source:Molecules;22(2), 2017 Jan 27.
[Is] ISSN:1420-3049
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:The enzymes called ribosome-inactivating proteins (RIPs) that are able to depurinate  nucleic acids and arrest vital cellular functions, including protein synthesis, are still a frontline  research field, mostly because of their promising medical applications. The contributions of Stirpe  to the development of these studies has been one of the most relevant. After a short biographical  introduction, an overview is offered of the main results obtained by his investigations during last  55 years on his main research lines: hyperuricaemia, xanthine oxidoreductase and RIPs.
[Mh] Termos MeSH primário: Hiperuricemia/tratamento farmacológico
Hiperuricemia/metabolismo
Proteínas de Plantas/farmacologia
Pesquisa
Proteínas Inativadoras de Ribossomos/farmacologia
Xantina Desidrogenase/metabolismo
[Mh] Termos MeSH secundário: Animais
Pessoas Famosas
Frutose/metabolismo
História do Século XX
Seres Humanos
Hiperuricemia/diagnóstico
Hiperuricemia/etiologia
Itália
Pesquisa/história
Ricina/farmacologia
Pesquisa Médica Translacional/história
[Pt] Tipo de publicação:BIOGRAPHY; HISTORICAL ARTICLE; JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Plant Proteins); 30237-26-4 (Fructose); 9009-86-3 (Ricin); EC 1.17.1.4 (Xanthine Dehydrogenase); EC 3.2.2.22 (Ribosome Inactivating Proteins)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170509
[Lr] Data última revisão:
170509
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170131
[St] Status:MEDLINE


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[PMID]:28028039
[Au] Autor:Urasaki N; Takagi H; Natsume S; Uemura A; Taniai N; Miyagi N; Fukushima M; Suzuki S; Tarora K; Tamaki M; Sakamoto M; Terauchi R; Matsumura H
[Ad] Endereço:Okinawa Prefectural Agricultural Research Center, Itoman, Okinawa 901-0336, Japan.
[Ti] Título:Draft genome sequence of bitter gourd (Momordica charantia), a vegetable and medicinal plant in tropical and subtropical regions.
[So] Source:DNA Res;24(1):51-58, 2017 Feb 01.
[Is] ISSN:1756-1663
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Bitter gourd (Momordica charantia) is an important vegetable and medicinal plant in tropical and subtropical regions globally. In this study, the draft genome sequence of a monoecious bitter gourd inbred line, OHB3-1, was analyzed. Through Illumina sequencing and de novo assembly, scaffolds of 285.5 Mb in length were generated, corresponding to ∼84% of the estimated genome size of bitter gourd (339 Mb). In this draft genome sequence, 45,859 protein-coding gene loci were identified, and transposable elements accounted for 15.3% of the whole genome. According to synteny mapping and phylogenetic analysis of conserved genes, bitter gourd was more related to watermelon (Citrullus lanatus) than to cucumber (Cucumis sativus) or melon (C. melo). Using RAD-seq analysis, 1507 marker loci were genotyped in an F2 progeny of two bitter gourd lines, resulting in an improved linkage map, comprising 11 linkage groups. By anchoring RAD tag markers, 255 scaffolds were assigned to the linkage map. Comparative analysis of genome sequences and predicted genes determined that putative trypsin-inhibitor and ribosome-inactivating genes were distinctive in the bitter gourd genome. These genes could characterize the bitter gourd as a medicinal plant.
[Mh] Termos MeSH primário: Genoma de Planta
Momordica charantia/genética
Plantas Medicinais/genética
Clima Tropical
[Mh] Termos MeSH secundário: Elementos de DNA Transponíveis
Filogenia
Proteínas Inativadoras de Ribossomos/genética
Inibidores da Tripsina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA Transposable Elements); 0 (Trypsin Inhibitors); EC 3.2.2.22 (Ribosome Inactivating Proteins)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170512
[Lr] Data última revisão:
170512
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161229
[St] Status:MEDLINE
[do] DOI:10.1093/dnares/dsw047


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[PMID]:27742744
[Au] Autor:Chatterjee B; Ghosh K; Yadav N; Kanade SR
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Central University of Kerala, Kasaragod, Kerala, 671314, India.
[Ti] Título:A novel L-fucose-binding lectin from Fenneropenaeus indicus induced cytotoxicity in breast cancer cells.
[So] Source:J Biochem;161(1):87-97, 2017 Jan.
[Is] ISSN:1756-2651
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Lectins are omnipresent in almost all life forms, being the proteins which specifically bind to carbohydrate moieties on the cell surface; they have been explored for their anti-tumour activities. In this study, we purified a fucose specific-lectin (IFL) from Fenneropenaeus indicus haemolymph using fucose-affinity column and characterized for its haemagglutination activity, carbohydrate specificity, dependency on cations and cytotoxicity against cancer cells. The lectin showed non-specificity against human erythrocytes. It was a Ca -dependent lectin which remained stable over wide pH and temperature ranges. The lectin showed effective dose dependent cytotoxicity against different human cancer cell lines and induced apoptosis in MCF-7 cells as evidenced by DNA ladder assay and PARP cleavage in a dose dependent manner. Moreover, an increased p21 level corresponding to cyclin D downregulation in response to IFL treatment was observed which might work as probable factors to inhibit cell growth and induce apoptosis of MCF-7 cells. Therefore, we report a novel lectin from the prawn haemolymph with high specificity for L-fucose and antiproliferative towards human cancer cells. However, further establishment of the modus operandi of this lectin is required to enable its biotechnological applications.
[Mh] Termos MeSH primário: Proteínas de Artrópodes/farmacologia
Neoplasias da Mama/tratamento farmacológico
Citotoxinas/farmacologia
Fucose
Penaeidae/química
Lectinas de Plantas/farmacologia
Proteínas Inativadoras de Ribossomos/farmacologia
[Mh] Termos MeSH secundário: Animais
Proteínas de Artrópodes/química
Neoplasias da Mama/metabolismo
Citotoxinas/química
Feminino
Seres Humanos
Células MCF-7
Lectinas de Plantas/química
Proteínas Inativadoras de Ribossomos/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arthropod Proteins); 0 (Cytotoxins); 0 (Plant Lectins); 0 (Sambucus nigra lectins); 28RYY2IV3F (Fucose); EC 3.2.2.22 (Ribosome Inactivating Proteins)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161016
[St] Status:MEDLINE
[do] DOI:10.1093/jb/mvw057


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[PMID]:27898041
[Au] Autor:Bolognesi A; Bortolotti M; Maiello S; Battelli MG; Polito L
[Ad] Endereço:Department of Experimental, Diagnostic and Specialty Medicine-DIMES, Alma Mater Studiorum, University of Bologna, Via San Giacomo 14, 40126 Bologna, Italy. andrea.bolognesi@unibo.it.
[Ti] Título:Ribosome-Inactivating Proteins from Plants: A Historical Overview.
[So] Source:Molecules;21(12), 2016 Nov 26.
[Is] ISSN:1420-3049
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:This review provides a historical overview of the research on plant ribosome-inactivating proteins (RIPs), starting from the first studies at the end of eighteenth century involving the purification of abrin and ricin, as well as the immunological experiments of Paul Erlich. Interest in these plant toxins was revived in 1970 by the observation of their anticancer activity, which has given rise to a large amount of research contributing to the development of various scientific fields. Biochemistry analyses succeeded in identifying the enzymatic activity of RIPs and allowed for a better understanding of the ribosomal machinery. Studies on RIP/cell interactions were able to detail the endocytosis and intracellular routing of ricin, thus increasing our knowledge of how cells handle exogenous proteins. The identification of new RIPs and the finding that most RIPs are single-chain polypeptides, together with their genetic sequencing, has aided in the development of new phylogenetic theories. Overall, the biological properties of these proteins, including their abortifacient, anticancer, antiviral and neurotoxic activities, suggest that RIPs could be utilized in agriculture and in many biomedical fields, including clinical drug development.
[Mh] Termos MeSH primário: Proteínas de Plantas/metabolismo
Proteínas Inativadoras de Ribossomos/metabolismo
[Mh] Termos MeSH secundário: Animais
Endocitose
Seres Humanos
Imunotoxinas/efeitos adversos
Imunotoxinas/química
Imunotoxinas/metabolismo
Filogenia
Proteínas de Plantas/efeitos adversos
Proteínas de Plantas/química
Conformação Proteica
Proteínas Inativadoras de Ribossomos/efeitos adversos
Proteínas Inativadoras de Ribossomos/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Immunotoxins); 0 (Plant Proteins); EC 3.2.2.22 (Ribosome Inactivating Proteins)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170509
[Lr] Data última revisão:
170509
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161130
[St] Status:MEDLINE


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[PMID]:27879643
[Au] Autor:Shi WW; Mak AN; Wong KB; Shaw PC
[Ad] Endereço:Centre for Protein Science and Crystallography, School of Life Sciences, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong, China. Shiww@cuhk.edu.hk.
[Ti] Título:Structures and Ribosomal Interaction of Ribosome-Inactivating Proteins.
[So] Source:Molecules;21(11), 2016 Nov 21.
[Is] ISSN:1420-3049
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Ribosome-inactivating proteins (RIPs) including ricin, Shiga toxin, and trichosanthin, are RNA -glycosidases that depurinate a specific adenine residue (A-4324 in rat 28S ribosomal RNA, rRNA) in the conserved α-sarcin/ricin loop (α-SRL) of rRNA. RIPs are grouped into three types according to the number of subunits and the organization of the precursor sequences. RIPs are two-domain proteins, with the active site located in the cleft between the N- and C-terminal domains. It has been found that the basic surface residues of the RIPs promote rapid and specific targeting to the ribosome and a number of RIPs have been shown to interact with the C-terminal regions of the P proteins of the ribosome. At present, the structural basis for the interaction of trichosanthin and ricin-A chain toward P2 peptide is known. This review surveys the structural features of the representative RIPs and discusses how they approach and interact with the ribosome.
[Mh] Termos MeSH primário: Modelos Moleculares
Estrutura Molecular
Proteínas Inativadoras de Ribossomos/química
Ribossomos/química
[Mh] Termos MeSH secundário: Domínio Catalítico
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
Proteínas Inativadoras de Ribossomos/classificação
Proteínas Inativadoras de Ribossomos/metabolismo
Subunidades Ribossômicas/genética
Subunidades Ribossômicas/metabolismo
Relação Estrutura-Atividade
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
EC 3.2.2.22 (Ribosome Inactivating Proteins)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170411
[Lr] Data última revisão:
170411
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161124
[St] Status:MEDLINE



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