Base de dados : MEDLINE
Pesquisa : G02.111.570.820.709.275 [Categoria DeCS]
Referências encontradas : 11 [refinar]
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  1 / 11 MEDLINE  
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[PMID]:28453724
[Au] Autor:Golden M; García-Portugués E; Sørensen M; Mardia KV; Hamelryck T; Hein J
[Ad] Endereço:Department of Statistics, University of Oxford, Oxford, United Kingdom.
[Ti] Título:A Generative Angular Model of Protein Structure Evolution.
[So] Source:Mol Biol Evol;34(8):2085-2100, 2017 Aug 01.
[Is] ISSN:1537-1719
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Recently described stochastic models of protein evolution have demonstrated that the inclusion of structural information in addition to amino acid sequences leads to a more reliable estimation of evolutionary parameters. We present a generative, evolutionary model of protein structure and sequence that is valid on a local length scale. The model concerns the local dependencies between sequence and structure evolution in a pair of homologous proteins. The evolutionary trajectory between the two structures in the protein pair is treated as a random walk in dihedral angle space, which is modeled using a novel angular diffusion process on the two-dimensional torus. Coupling sequence and structure evolution in our model allows for modeling both "smooth" conformational changes and "catastrophic" conformational jumps, conditioned on the amino acid changes. The model has interpretable parameters and is comparatively more realistic than previous stochastic models, providing new insights into the relationship between sequence and structure evolution. For example, using the trained model we were able to identify an apparent sequence-structure evolutionary motif present in a large number of homologous protein pairs. The generative nature of our model enables us to evaluate its validity and its ability to simulate aspects of protein evolution conditioned on an amino acid sequence, a related amino acid sequence, a related structure or any combination thereof.
[Mh] Termos MeSH primário: Proteínas/genética
Alinhamento de Sequência/métodos
Análise de Sequência de Proteína/métodos
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Simulação por Computador
Evolução Molecular
Modelos Genéticos
Modelos Moleculares
Conformação Proteica
Elementos Estruturais de Proteínas/genética
Proteínas/metabolismo
Análise de Sequência de Proteína/estatística & dados numéricos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Proteins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180201
[Lr] Data última revisão:
180201
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE
[do] DOI:10.1093/molbev/msx137


  2 / 11 MEDLINE  
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[PMID]:29177973
[Au] Autor:Niu Y; Moghimyfiroozabad S; Safaie S; Yang Y; Jonas EA; Alavian KN
[Ad] Endereço:Division of Brain Sciences, Department of Medicine, Imperial College London, E508, Burlington Danes Hammersmith Hospital, DuCane Road, London, W12 0NN, UK.
[Ti] Título:Phylogenetic Profiling of Mitochondrial Proteins and Integration Analysis of Bacterial Transcription Units Suggest Evolution of F1Fo ATP Synthase from Multiple Modules.
[So] Source:J Mol Evol;85(5-6):219-233, 2017 Dec.
[Is] ISSN:1432-1432
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:ATP synthase is a complex universal enzyme responsible for ATP synthesis across all kingdoms of life. The F-type ATP synthase has been suggested to have evolved from two functionally independent, catalytic (F1) and membrane bound (Fo), ancestral modules. While the modular evolution of the synthase is supported by studies indicating independent assembly of the two subunits, the presence of intermediate assembly products suggests a more complex evolutionary process. We analyzed the phylogenetic profiles of the human mitochondrial proteins and bacterial transcription units to gain additional insight into the evolution of the F-type ATP synthase complex. In this study, we report the presence of intermediary modules based on the phylogenetic profiles of the human mitochondrial proteins. The two main intermediary modules comprise the α ß hexamer in the F1 and the c-subunit ring in the Fo. A comprehensive analysis of bacterial transcription units of F1Fo ATP synthase revealed that while a long and constant order of F1Fo ATP synthase genes exists in a majority of bacterial genomes, highly conserved combinations of separate transcription units are present among certain bacterial classes and phyla. Based on our findings, we propose a model that includes the involvement of multiple modules in the evolution of F1Fo ATP synthase. The central and peripheral stalk subunits provide a link for the integration of the F1/Fo modules.
[Mh] Termos MeSH primário: ATPases Mitocondriais Próton-Translocadoras/genética
ATPases Mitocondriais Próton-Translocadoras/metabolismo
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/biossíntese
Evolução Molecular
Seres Humanos
Mitocôndrias/genética
Mitocôndrias/metabolismo
Proteínas Mitocondriais/genética
Proteínas Mitocondriais/metabolismo
Filogenia
Domínios Proteicos
Elementos Estruturais de Proteínas/genética
Transcrição Genética/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Mitochondrial Proteins); 8L70Q75FXE (Adenosine Triphosphate); EC 3.6.1.- (F1F0-ATP synthase); EC 3.6.3.- (Mitochondrial Proton-Translocating ATPases)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180102
[Lr] Data última revisão:
180102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE
[do] DOI:10.1007/s00239-017-9819-3


  3 / 11 MEDLINE  
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[PMID]:28333346
[Au] Autor:Sharir-Ivry A; Xia Y
[Ad] Endereço:Department of Bioengineering, McGill University, Montreal, QC, Canada.
[Ti] Título:The Impact of Native State Switching on Protein Sequence Evolution.
[So] Source:Mol Biol Evol;34(6):1378-1390, 2017 Jun 01.
[Is] ISSN:1537-1719
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:For proteins with a single well-defined native state, protein 3Dstructure is a major determinant of sequence evolution. On the other hand, many proteins adopt multiple, distinct native structures under different conditions ("conformational switches"), yet the impact of such native state switching on protein evolution is not fully understood. Here, we performed a proteome-wide analysis of how protein structure impacts sequence evolution for protein conformational switches in Saccharomyces cerevisiae using pooled analysis of sites with similar packing or burial. We observed a strong linear relationship between residue evolutionary rate and residue burial for conformational switches. In addition, we found that conformational switches evolve significantly and consistently more slowly than proteins with a single native state, even after controlling for degree of residue burial or packing. Next, we focused on proteins that switch conformations upon molecular binding. We found that interfacial residues in these conformational switches evolve more slowly than interfacial residues in proteins with a single native state, and that the bound conformation is a better predictor for residue evolutionary rate than the unbound conformation. Our findings suggest that for conformational switches, the necessity to encode multiple distinct native structures under different conditions imposes strong evolutionary constraints on the entire protein, rather than just a few key residues. Our results provide new insights into the structure-evolution relationship of protein conformational switches.
[Mh] Termos MeSH primário: Elementos Estruturais de Proteínas/genética
Proteínas/genética
Relação Estrutura-Atividade
[Mh] Termos MeSH secundário: Sequência de Aminoácidos/genética
Evolução Biológica
Simulação por Computador
Evolução Molecular
Modelos Moleculares
Ligação Proteica/genética
Conformação Proteica
Proteínas/metabolismo
Proteoma/genética
Saccharomyces cerevisiae/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Proteins); 0 (Proteome)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171018
[Lr] Data última revisão:
171018
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170324
[St] Status:MEDLINE
[do] DOI:10.1093/molbev/msx071


  4 / 11 MEDLINE  
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[PMID]:27521923
[Au] Autor:Zhang X; Li Y; Wang J; Zhang T; Li T; Dong W; Ma E; Zhang J
[Ad] Endereço:Research Institute of Applied Biology, Shanxi University, Taiyuan, Shanxi 030006, China.
[Ti] Título:Identification and characteristic analysis of the catalase gene from Locusta migratoria.
[So] Source:Pestic Biochem Physiol;132:125-31, 2016 Sep.
[Is] ISSN:1095-9939
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Catalase (CAT) is a ubiquitous antioxidant enzyme in almost all living organisms exposed to atmosphere, which involved in decomposing harmful hydrogen peroxide, into oxygen and water. In this study, a full-length cDNA (1524bp) encoding the catalase gene (LmCAT) from Locusta migratoria was cloned (accession number KT716445). The open reading frame of the LmCAT gene encoded 507 amino acids and shared 57.8%-97.8% amino acid identities with other insect CATs. The coding region was interrupted by 9 introns, while its promoter region contained 15 putative binding sites for 5 kinds of transcriptional regulation factors. For the stage-specific expression profile, LmCAT was highly expressed in the fourth-instar nymphs. For the tissue-specific expression profile, the LmCAT transcripts were highest in the fat bodies, and relatively abundant in the gastric caecum, Malpighian tubules, ovary and integument. Moreover, the result showed that quercetin could significantly induce the expression level of LmCAT. The expression of LmCAT could be silenced by RNAi, but the moralities were not significantly different between control and RNAi groups. Our results would provide valuable information for further study on the ROS regulation mechanism in insect.
[Mh] Termos MeSH primário: Catalase/genética
Locusta migratoria/genética
[Mh] Termos MeSH secundário: Animais
Catalase/metabolismo
Clonagem Molecular
Genoma de Inseto/genética
Locusta migratoria/enzimologia
Ninfa/metabolismo
Filogenia
Reação em Cadeia da Polimerase
Regiões Promotoras Genéticas/genética
Elementos Estruturais de Proteínas
Interferência de RNA
Alinhamento de Sequência
Fatores de Transcrição/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Transcription Factors); EC 1.11.1.6 (Catalase)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170314
[Lr] Data última revisão:
170314
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160814
[St] Status:MEDLINE


  5 / 11 MEDLINE  
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[PMID]:27395016
[Au] Autor:Prota AE; Setter J; Waight AB; Bargsten K; Murga J; Diaz JF; Steinmetz MO
[Ad] Endereço:Laboratory of Biomolecular Research, Department of Biology and Chemistry, Paul Scherrer Institut, 5232 Villigen, Switzerland. Electronic address: andrea.prota@psi.ch.
[Ti] Título:Pironetin Binds Covalently to αCys316 and Perturbs a Major Loop and Helix of α-Tubulin to Inhibit Microtubule Formation.
[So] Source:J Mol Biol;428(15):2981-8, 2016 Jul 31.
[Is] ISSN:1089-8638
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Microtubule-targeting agents are among the most powerful drugs used in chemotherapy to treat cancer patients. Pironetin is a natural product that displays promising anticancer properties by binding to and potently inhibiting tubulin assembly into microtubules; however, its molecular mechanism of action remained obscure. Here, we solved the crystal structure of the tubulin-pironetin complex and found that the compound covalently binds to Cys316 of α-tubulin. The structure further revealed that pironetin perturbs the T7 loop and helix H8 of α-tubulin. Since both these elements are essential for establishing longitudinal tubulin contacts in microtubules, this result explains how pironetin inhibits the formation of microtubules. Together, our data define the molecular details of the pironetin binding site on α-tubulin and thus offer a promising basis for the rational design of pironetin variants with improved activity profiles. They further extend our knowledge on strategies evolved by natural products to target and perturb the microtubule cytoskeleton.
[Mh] Termos MeSH primário: Antineoplásicos/farmacocinética
Microtúbulos/metabolismo
Pironas/farmacologia
Tubulina (Proteína)/metabolismo
[Mh] Termos MeSH secundário: Animais
Sítios de Ligação
Produtos Biológicos/farmacologia
Bovinos
Elementos Estruturais de Proteínas
Ovinos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Biological Products); 0 (Pyrones); 0 (Tubulin); 151519-02-7 (pironetin)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170609
[Lr] Data última revisão:
170609
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160711
[St] Status:MEDLINE


  6 / 11 MEDLINE  
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[PMID]:27385337
[Au] Autor:Liu Y; Lee IJ; Sun M; Lower CA; Runge KW; Ma J; Wu JQ
[Ad] Endereço:Department of Molecular Genetics, The Ohio State University, Columbus, OH 43210.
[Ti] Título:Roles of the novel coiled-coil protein Rng10 in septum formation during fission yeast cytokinesis.
[So] Source:Mol Biol Cell;27(16):2528-41, 2016 Aug 15.
[Is] ISSN:1939-4586
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Rho GAPs are important regulators of Rho GTPases, which are involved in various steps of cytokinesis and other processes. However, regulation of Rho-GAP cellular localization and function is not fully understood. Here we report the characterization of a novel coiled-coil protein Rng10 and its relationship with the Rho-GAP Rga7 in fission yeast. Both rng10Δ and rga7Δ result in defective septum and cell lysis during cytokinesis. Rng10 and Rga7 colocalize on the plasma membrane at the cell tips during interphase and at the division site during cell division. Rng10 physically interacts with Rga7 in affinity purification and coimmunoprecipitation. Of interest, Rga7 localization is nearly abolished without Rng10. Moreover, Rng10 and Rga7 work together to regulate the accumulation and dynamics of glucan synthases for successful septum formation in cytokinesis. Our results show that cellular localization and function of the Rho-GAP Rga7 are regulated by a novel protein, Rng10, during cytokinesis in fission yeast.
[Mh] Termos MeSH primário: Proteínas Ativadoras de GTPase/fisiologia
Schizosaccharomyces/fisiologia
[Mh] Termos MeSH secundário: Divisão Celular/fisiologia
Parede Celular/metabolismo
Citocinese
Proteínas Ativadoras de GTPase/genética
Proteínas Ativadoras de GTPase/metabolismo
Glucosiltransferases/metabolismo
Fatores de Troca do Nucleotídeo Guanina/genética
Fatores de Troca do Nucleotídeo Guanina/metabolismo
Elementos Estruturais de Proteínas
Schizosaccharomyces/citologia
Schizosaccharomyces/metabolismo
Proteínas rho de Ligação ao GTP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (GTPase-Activating Proteins); 0 (Guanine Nucleotide Exchange Factors); 0 (rho GTPase-activating protein); EC 2.4.1.- (Glucosyltransferases); EC 2.4.1.- (glucan synthase); EC 3.6.5.2 (rho GTP-Binding Proteins)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170808
[Lr] Data última revisão:
170808
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160708
[St] Status:MEDLINE
[do] DOI:10.1091/mbc.E16-03-0156


  7 / 11 MEDLINE  
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[PMID]:27113476
[Au] Autor:Wunder EA; Figueira CP; Benaroudj N; Hu B; Tong BA; Trajtenberg F; Liu J; Reis MG; Charon NW; Buschiazzo A; Picardeau M; Ko AI
[Ad] Endereço:Department of Epidemiology of Microbial Disease, Yale School of Public Health, New Haven, CT, 06520, USA.
[Ti] Título:A novel flagellar sheath protein, FcpA, determines filament coiling, translational motility and virulence for the Leptospira spirochete.
[So] Source:Mol Microbiol;101(3):457-70, 2016 Aug.
[Is] ISSN:1365-2958
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Leptospira are unique among bacteria based on their helical cell morphology with hook-shaped ends and the presence of periplasmic flagella (PF) with pronounced spontaneous supercoiling. The factors that provoke such supercoiling, as well as the role that PF coiling plays in generating the characteristic hook-end cell morphology and motility, have not been elucidated. We have now identified an abundant protein from the pathogen L. interrogans, exposed on the PF surface, and named it Flagellar-coiling protein A (FcpA). The gene encoding FcpA is highly conserved among Leptospira and was not found in other bacteria. fcpA(-) mutants, obtained from clinical isolates or by allelic exchange, had relatively straight, smaller-diameter PF, and were not able to produce translational motility. These mutants lost their ability to cause disease in the standard hamster model of leptospirosis. Complementation of fcpA restored the wild-type morphology, motility and virulence phenotypes. In summary, we identified a novel Leptospira 36-kDa protein, the main component of the spirochete's PF sheath, and a key determinant of the flagella's coiled structure. FcpA is essential for bacterial translational motility and to enable the spirochete to penetrate the host, traverse tissue barriers, disseminate to cause systemic infection and reach target organs.
[Mh] Termos MeSH primário: Flagelos/fisiologia
Leptospira/fisiologia
[Mh] Termos MeSH secundário: Animais
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Cricetinae
Cães
Flagelos/genética
Flagelos/metabolismo
Flagelina/genética
Flagelina/metabolismo
Teste de Complementação Genética
Leptospira/genética
Leptospira/metabolismo
Leptospira/patogenicidade
Leptospirose/microbiologia
Células Madin Darby de Rim Canino
Masculino
Mesocricetus
Mutação
Periplasma/metabolismo
Elementos Estruturais de Proteínas
Virulência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 12777-81-0 (Flagellin)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170801
[Lr] Data última revisão:
170801
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160427
[St] Status:MEDLINE
[do] DOI:10.1111/mmi.13403


  8 / 11 MEDLINE  
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[PMID]:27059018
[Au] Autor:Polanco C; Buhse T; Uversky VN
[Ad] Endereço:Department of Mathematics, Faculty of Sciences, Universidad Nacional Autónoma de México, C.P. 04510 D.F., México.
[Ti] Título:Structure and function relationships of proteins based on polar profile: a review.
[So] Source:Acta Biochim Pol;63(2):229-33, 2016.
[Is] ISSN:1734-154X
[Cp] País de publicação:Poland
[La] Idioma:eng
[Ab] Resumo:Proteins in the post-genome era impose diverse research challenges, the main are the understanding of their structure-function mechanism, and the growing need for new pharmaceutical drugs, particularly antibiotics that help clinicians treat the ever- increasing number of Multidrug-Resistant Organisms (MDROs). Although, there is a wide range of mathematical-computational algorithms to satisfy the demand, among them the Quantitative Structure-Activity Relationship algorithms that have shown better performance using a characteristic training data of the property searched; their performance has stagnated regardless of the number of metrics they evaluate and their complexity. This article reviews the characteristics of these metrics, and the need to reconsider the mathematical structure that expresses them, directing their design to a more comprehensive algebraic structure. It also shows how the main function of a protein can be determined by measuring the polarity of its linear sequence, with a high level of accuracy, and how such exhaustive metric stands as a "fingerprint" that can be applied to scan the protein regions to obtain new pharmaceutical drugs, and thus to establish how the singularities led to the specialization of the protein groups known today.
[Mh] Termos MeSH primário: Proteínas/química
[Mh] Termos MeSH secundário: Algoritmos
Animais
Biologia Computacional
Seres Humanos
Interações Hidrofóbicas e Hidrofílicas
Modelos Moleculares
Elementos Estruturais de Proteínas
Relação Quantitativa Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Proteins)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170124
[Lr] Data última revisão:
170124
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160410
[St] Status:MEDLINE
[do] DOI:10.18388/abp.2014_919


  9 / 11 MEDLINE  
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[PMID]:27059017
[Au] Autor:Polanco C; Castañón-González JA; Buhse T; Uversky VN; Amkie RZ
[Ad] Endereço:Department of Mathematics, Faculty of Sciences, Universidad Nacional Autónoma de México, C.P. 04510 D.F., México.
[Ti] Título:Classifying lipoproteins based on their polar profiles.
[So] Source:Acta Biochim Pol;63(2):235-41, 2016.
[Is] ISSN:1734-154X
[Cp] País de publicação:Poland
[La] Idioma:eng
[Ab] Resumo:The lipoproteins are an important group of cargo proteins known for their unique capability to transport lipids. By applying the Polarity index algorithm, which has a metric that only considers the polar profile of the linear sequences of the lipoprotein group, we obtained an analytical and structural differentiation of all the lipoproteins found in UniProt Database. Also, the functional groups of lipoproteins, and particularly of the set of lipoproteins relevant to atherosclerosis, were analyzed with the same method to reveal their structural preference, and the results of Polarity index analysis were verified by an alternate test, the Cumulative Distribution Function algorithm, applied to the same groups of lipoproteins.
[Mh] Termos MeSH primário: Lipoproteínas/classificação
[Mh] Termos MeSH secundário: Algoritmos
Aterosclerose
Biologia Computacional
Seres Humanos
Interações Hidrofóbicas e Hidrofílicas
Lipoproteínas/química
Dobramento de Proteína
Elementos Estruturais de Proteínas
Relação Quantitativa Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Lipoproteins)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170124
[Lr] Data última revisão:
170124
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160410
[St] Status:MEDLINE
[do] DOI:10.18388/abp.2014_918


  10 / 11 MEDLINE  
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[PMID]:26830137
[Au] Autor:Ozcelik S; Sprenger F; Skachokova Z; Fraser G; Abramowski D; Clavaguera F; Probst A; Frank S; Müller M; Staufenbiel M; Goedert M; Tolnay M; Winkler DT
[Ad] Endereço:Institute of Pathology, University Hospital Basel, Basel, Switzerland.
[Ti] Título:Co-expression of truncated and full-length tau induces severe neurotoxicity.
[So] Source:Mol Psychiatry;21(12):1790-1798, 2016 Dec.
[Is] ISSN:1476-5578
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Abundant tau inclusions are a defining hallmark of several human neurodegenerative diseases, including Alzheimer's disease. Protein fragmentation is a widely observed event in neurodegenerative proteinopathies. The relevance of tau fragmentation for the neurodegenerative process in tauopathies has yet remained unclear. Here we found that co-expression of truncated and full-length human tau in mice provoked the formation of soluble high-molecular-weight tau, the failure of axonal transport, clumping of mitochondria, disruption of the Golgi apparatus and missorting of synaptic proteins. This was associated with extensive nerve cell dysfunction and severe paralysis by the age of 3 weeks. When the expression of truncated tau was halted, most mice recovered behaviorally and functionally. In contrast, co-expression of full-length tau isoforms did not result in paralysis. Truncated tau thus induces extensive but reversible neurotoxicity in the presence of full-length tau through the formation of nonfilamentous high-molecular-weight tau aggregates, in the absence of tau filaments. Targeting tau fragmentation may provide a novel approach for the treatment of human tauopathies.
[Mh] Termos MeSH primário: Tauopatias/metabolismo
Proteínas tau/metabolismo
[Mh] Termos MeSH secundário: Doença de Alzheimer/metabolismo
Animais
Transporte Axonal
Encéfalo/metabolismo
Modelos Animais de Doenças
Seres Humanos
Camundongos
Camundongos Transgênicos
Neurônios/metabolismo
Síndromes Neurotóxicas/metabolismo
Isoformas de Proteínas/metabolismo
Elementos Estruturais de Proteínas/fisiologia
Proteínas tau/análise
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Protein Isoforms); 0 (tau Proteins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160203
[St] Status:MEDLINE
[do] DOI:10.1038/mp.2015.228



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