Base de dados : MEDLINE
Pesquisa : A10.615 [Categoria DeCS]
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  1 / 17981 MEDLINE  
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[PMID]:29281629
[Au] Autor:Ojeda Naharros I; Gesemann M; Mateos JM; Barmettler G; Forbes A; Ziegler U; Neuhauss SCF; Bachmann-Gagescu R
[Ad] Endereço:Institute of Molecular Life Sciences, University of Zurich, Zurich, Switzerland.
[Ti] Título:Loss-of-function of the ciliopathy protein Cc2d2a disorganizes the vesicle fusion machinery at the periciliary membrane and indirectly affects Rab8-trafficking in zebrafish photoreceptors.
[So] Source:PLoS Genet;13(12):e1007150, 2017 12.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ciliopathies are human disorders caused by dysfunction of primary cilia, ubiquitous organelles involved in transduction of environmental signals such as light sensation in photoreceptors. Concentration of signal detection proteins such as opsins in the ciliary membrane is achieved by RabGTPase-regulated polarized vesicle trafficking and by a selective barrier at the ciliary base, the transition zone (TZ). Dysfunction of the TZ protein CC2D2A causes Joubert/Meckel syndromes in humans and loss of ciliary protein localization in animal models, including opsins in retinal photoreceptors. The link between the TZ and upstream vesicle trafficking has been little explored to date. Moreover, the role of the small GTPase Rab8 in opsin-carrier vesicle (OCV) trafficking has been recently questioned in a mouse model. Using correlative light and electron microscopy and live imaging in zebrafish photoreceptors, we provide the first live characterization of Rab8-mediated trafficking in photoreceptors in vivo. Our results support a possibly redundant role for both Rab8a/b paralogs in OCV trafficking, based on co-localization of Rab8 and opsins in vesicular structures, and joint movement of Rab8-tagged particles with opsin. We further investigate the role of the TZ protein Cc2d2a in Rab8-mediated trafficking using cc2d2a zebrafish mutants and identify a requirement for Cc2d2a in the latest step of OCV trafficking, namely vesicle fusion. Progressive accumulation of opsin-containing vesicles in the apical portion of photoreceptors lacking Cc2d2a is caused by disorganization of the vesicle fusion machinery at the periciliary membrane with mislocalization and loss of the t-SNAREs SNAP25 and Syntaxin3 and of the exocyst component Exoc4. We further observe secondary defects on upstream Rab8-trafficking with cytoplasmic accumulation of Rab8. Taken together, our results support participation of Rab8 in OCV trafficking and identify a novel role for the TZ protein Cc2d2a in fusion of incoming ciliary-directed vesicles, through organization of the vesicle fusion machinery at the periciliary membrane.
[Mh] Termos MeSH primário: Proteínas de Transporte Vesicular/genética
Proteínas de Transporte Vesicular/metabolismo
Proteínas de Peixe-Zebra/genética
Proteínas de Peixe-Zebra/metabolismo
Proteínas rab de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Animais
Animais Geneticamente Modificados
Transporte Biológico
Movimento Celular
Cílios/genética
Cílios/metabolismo
Seres Humanos
Membranas/metabolismo
Opsinas/genética
Opsinas/metabolismo
Células Fotorreceptoras de Vertebrados/metabolismo
Transporte Proteico
Peixe-Zebra
Proteínas rab de Ligação ao GTP/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (CC2D2A protein, zebrafish); 0 (Opsins); 0 (Vesicular Transport Proteins); 0 (Zebrafish Proteins); EC 3.6.1.- (Rab8a protein, zebrafish); EC 3.6.1.-. (RAB8A protein, human); EC 3.6.5.2 (rab GTP-Binding Proteins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180227
[Lr] Data última revisão:
180227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171228
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1007150


  2 / 17981 MEDLINE  
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[PMID]:29351334
[Au] Autor:Chang W; Lajko M; Fawzi AA
[Ad] Endereço:Department of Ophthalmology, Northwestern University, Feinberg School of Medicine, Chicago, IL, United States of America.
[Ti] Título:Endothelin-1 is associated with fibrosis in proliferative diabetic retinopathy membranes.
[So] Source:PLoS One;13(1):e0191285, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:PURPOSE: To characterize the relationship between endothelin-1 and fibrosis in epiretinal membranes in proliferative diabetic retinopathy and explore the role of endothelial-mesenchymal transition in these membranes. METHODS: Membranes were obtained from eyes undergoing pars plana vitrectomy for complicated proliferative diabetic retinopathy or idiopathic epiretinal membrane. Through standard immunohistochemical techniques, we labeled membranes to explore the distribution of endothelin-1 and endothelin receptor B, comparing proliferative diabetic retinopathy and idiopathic epiretinal membranes. In addition, membranes were also labeled with markers for fibroblasts, endothelial, and glial cells and studied with confocal laser scanning microscopy. The intensity of endothelin-1 labeling was quantified using standard image analysis software. RESULTS: Fourteen membranes were included in the analysis, nine from eyes with proliferative diabetic retinopathy and five idiopathic membranes. Flatmount diabetic membranes showed co-localization of endothelin-1 with S100A4 and CD31. Immunohistochemistry and quantitative analysis of cross-sectional membranes showed significantly higher endothelin-1 labeling in proliferative diabetic retinopathy membranes compared to idiopathic membranes (p<0.05). Diabetic membranes showed more elements staining positive for S100A4 compared to idiopathic membranes. CONCLUSION: Epiretinal membrane formation in proliferative diabetic retinopathy involves higher tissue levels of endothelin-1 and fibroblastic activity. Furthermore, endothelin-1, endothelial and fibroblastic staining appear to be correlated, suggestive of endothelial-to-mesenchymal transition in proliferative diabetic retinopathy.
[Mh] Termos MeSH primário: Retinopatia Diabética/metabolismo
Retinopatia Diabética/patologia
Endotelina-1/metabolismo
[Mh] Termos MeSH secundário: Adulto
Proliferação Celular
Feminino
Fibrose
Proteína Glial Fibrilar Ácida/metabolismo
Seres Humanos
Masculino
Membranas/patologia
Meia-Idade
Molécula-1 de Adesão Celular Endotelial de Plaquetas/metabolismo
Retina/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Endothelin-1); 0 (Glial Fibrillary Acidic Protein); 0 (Platelet Endothelial Cell Adhesion Molecule-1)
[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:180120
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191285


  3 / 17981 MEDLINE  
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[PMID]:29190425
[Au] Autor:Sebastian B; Favero T; Dittrich PS
[Ad] Endereço:Department of Biosystems Science and Engineering, ETH Zurich , Mattenstrasse 26, 4058 Basel, Switzerland.
[Ti] Título:The Effects of Shear Force Transmission Across Vesicle Membranes.
[So] Source:J Phys Chem Lett;8(24):6128-6134, 2017 Dec 21.
[Is] ISSN:1948-7185
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We report a comprehensive study on mechanotransmission of shear forces across lipid bilayer membranes of giant unilamellar vesicles (GUVs). GUVs containing fluorescent tracer particles were immobilized on a microfluidic platform and exposed to shear flows. A method was developed for the visualization of three-dimensional flows at high precision by defocusing microscopy. We quantify the symmetry of external flow around the GUV and show its effects on vortex flows and luminal dynamics. With increasing asymmetry, luminal vortices merged while liquid exchange in between them increased. The effect of membrane composition was studied through addition of cholesterol. Mechanotransmission efficacy, quantified by the ratio of luminal flow to external flow, ranged from ε = 0.094 (0 mol % cholesterol) to ε = 0.043 (16 mol % cholesterol). Our findings give new cues to the mechanisms underlying the sensing of strength and spatial distribution of shear forces by cells and the impact of membrane composition.
[Mh] Termos MeSH primário: Bicamadas Lipídicas
Microscopia de Fluorescência
Modelos Biológicos
Lipossomas Unilamelares
[Mh] Termos MeSH secundário: Colesterol
Lipossomos
Membranas
Resistência ao Cisalhamento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Lipid Bilayers); 0 (Liposomes); 0 (Unilamellar Liposomes); 97C5T2UQ7J (Cholesterol)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180205
[Lr] Data última revisão:
180205
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171201
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jpclett.7b02676


  4 / 17981 MEDLINE  
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[PMID]:29286816
[Au] Autor:Ryzhkov II; Lebedev DV; Solodovnichenko VS; Shiverskiy AV; Simunin MM
[Ad] Endereço:Institute of Computational Modelling SB RAS, Federal Research Center KSC SB RAS, Akademgorodok 50, 660036 Krasnoyarsk, Russia.
[Ti] Título:Induced-Charge Enhancement of the Diffusion Potential in Membranes with Polarizable Nanopores.
[So] Source:Phys Rev Lett;119(22):226001, 2017 Dec 01.
[Is] ISSN:1079-7114
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:When a charged membrane separates two salt solutions of different concentrations, a potential difference appears due to interfacial Donnan equilibrium and the diffusion junction. Here, we report a new mechanism for the generation of a membrane potential in polarizable conductive membranes via an induced surface charge. It results from an electric field generated by the diffusion of ions with different mobilities. For uncharged membranes, this effect strongly enhances the diffusion potential and makes it highly sensitive to the ion mobilities ratio, electrolyte concentration, and pore size. Theoretical predictions on the basis of the space-charge model extended to polarizable nanopores fully agree with experimental measurements in KCl and NaCl aqueous solutions.
[Mh] Termos MeSH primário: Membranas/química
Modelos Teóricos
Nanoporos
[Mh] Termos MeSH secundário: Potenciais da Membrana
[Pt] Tipo de publicação:JOURNAL ARTICLE
[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:171230
[St] Status:MEDLINE
[do] DOI:10.1103/PhysRevLett.119.226001


  5 / 17981 MEDLINE  
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[PMID]:29183798
[Au] Autor:McElhanon KE; Bhattacharya S
[Ad] Endereço:Department of Physiology and Cell Biology, Davis Heart and Lung Research Institute, The Ohio State University Wexner Medical Center, 473 W. 12th Ave, Columbus, OH 43210-1252, United States.
[Ti] Título:Altered membrane integrity in the progression of muscle diseases.
[So] Source:Life Sci;192:166-172, 2018 Jan 01.
[Is] ISSN:1879-0631
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Sarcolemmal integrity is orchestrated through the interplay of preserving membrane strength and fast tracking the membrane repair process during an event of compromised membrane fragility. Several molecular players have been identified that act in a concerted fashion to maintain the barrier function of the muscle membrane. Substantial research findings in the field of muscle biology point out the importance of maintaining membrane integrity as a key contributory factor to cellular homeostasis. Innumerable data on the progression of membrane pathology associated with compromised muscle membrane integrity support targeting sarcolemmal integrity in skeletal and cardiac muscle as a model therapeutic strategy to alleviate some of the pathologic conditions. This review will discuss strategies that researchers have undertaken to compensate for an imbalance in sarcolemma membrane fragility and membrane repair to maintain muscle membrane integrity.
[Mh] Termos MeSH primário: Membranas/patologia
Doenças Musculares/patologia
[Mh] Termos MeSH secundário: Animais
Seres Humanos
Músculo Esquelético/patologia
Miocárdio/patologia
Miócitos Cardíacos/patologia
Sarcolema/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180108
[Lr] Data última revisão:
180108
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171130
[St] Status:MEDLINE


  6 / 17981 MEDLINE  
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[PMID]:28893506
[Au] Autor:Cheng F; Fransson LÅ; Mani K
[Ad] Endereço:Department of Experimental Medical Science, Division of Neuroscience, Glycobiology Group, Lund University, Biomedical Center A13, SE-221 84, Lund, Sweden.
[Ti] Título:Cytochrome b561, copper, ß-cleaved amyloid precursor protein and niemann-pick C1 protein are involved in ascorbate-induced release and membrane penetration of heparan sulfate from endosomal S-nitrosylated glypican-1.
[So] Source:Exp Cell Res;360(2):171-179, 2017 Nov 15.
[Is] ISSN:1090-2422
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ascorbate-induced release of heparan sulfate from S-nitrosylated heparan sulfate proteoglycan glypican-1 takes place in endosomes. Heparan sulfate penetrates the membrane and is transported to the nucleus. This process is dependent on copper and on expression and processing of the amyloid precursor protein. It remains unclear how exogenously supplied ascorbate can generate HS-anMan in endosomes and how passage through the membrane is facilitated. Here we have examined wild-type, Alzheimer Tg2576 and amyloid precursor protein (-/-) mouse fibroblasts and human fetal and Niemann-Pick C1 fibroblasts by using deconvolution immunofluorescence microscopy, siRNA technology and [S ]sulfate-labeling, vesicle isolation and gel chromatography. We found that ascorbate-induced release of heparan sulfate was dependent on expression of endosomal cytochrome b561. Formation and nuclear transport of heparan sulfate was suppressed by inhibition of ß-processing of the amyloid precursor protein and formation was restored by copper (I) ions. Membrane penetration was not dependent on amyloid beta channel formation. Inhibition of endosomal exit resulted in accumulation of heparan sulfate in vesicles that exposed the C-terminal of the amyloid precursor protein externally. Endosome-to-nucleus transport was also dependent on expression of the Niemann-Pick C1 protein. We propose that ascorbate is taken up from the medium and is oxidized by cytochrome b561 which, in turn, reduces copper (II) to copper (I) present in the N-terminal, ß-cleaved domain of the amyloid precursor protein. Re-oxidation of copper (I) is coupled to reductive, deaminative release of heparan sulfate from glypican-1. Passage through the membrane may be facilitated by the C-terminal, ß-cleaved fragment of the amyloid precursor protein and the Niemann-Pick C1 protein.
[Mh] Termos MeSH primário: Precursor de Proteína beta-Amiloide/fisiologia
Ácido Ascórbico/farmacologia
Proteínas de Transporte/fisiologia
Cobre/fisiologia
Grupo dos Citocromos b/fisiologia
Endossomos/metabolismo
Glipicanas/metabolismo
Glicoproteínas de Membrana/fisiologia
[Mh] Termos MeSH secundário: Precursor de Proteína beta-Amiloide/metabolismo
Animais
Células Cultivadas
Endossomos/efeitos dos fármacos
Heparitina Sulfato
Seres Humanos
Membranas/efeitos dos fármacos
Membranas/metabolismo
Camundongos
Camundongos Transgênicos
Nitrosação
Processamento de Proteína Pós-Traducional
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amyloid beta-Protein Precursor); 0 (Carrier Proteins); 0 (Cytochrome b Group); 0 (Glypicans); 0 (Membrane Glycoproteins); 0 (NPC1 protein, human); 11130-51-1 (cytochrome b561); 789U1901C5 (Copper); 9050-30-0 (Heparitin Sulfate); PQ6CK8PD0R (Ascorbic Acid)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171103
[Lr] Data última revisão:
171103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170913
[St] Status:MEDLINE


  7 / 17981 MEDLINE  
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[PMID]:28813228
[Au] Autor:Braun R; Holler E
[Ad] Endereço:Universitätsklinikum Regensburg, Regensburg, Germany regine.braun@ukr.de.
[Ti] Título:Acute Ocular Graft-versus-Host Disease.
[So] Source:N Engl J Med;377(7):676, 2017 Aug 17.
[Is] ISSN:1533-4406
[Cp] País de publicação:United States
[La] Idioma:eng
[Mh] Termos MeSH primário: Doenças da Túnica Conjuntiva/patologia
Doença Enxerto-Hospedeiro/patologia
Transplante de Células-Tronco Hematopoéticas/efeitos adversos
[Mh] Termos MeSH secundário: Doença Aguda
Doenças da Túnica Conjuntiva/etiologia
Seres Humanos
Leucemia Mieloide Aguda/terapia
Masculino
Membranas
Adulto Jovem
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170830
[Lr] Data última revisão:
170830
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170817
[St] Status:MEDLINE
[do] DOI:10.1056/NEJMicm1701185


  8 / 17981 MEDLINE  
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[PMID]:28765363
[Au] Autor:Keren K; Shemesh T
[Ad] Endereço:Department of Physics, Russell Berrie Nanotechnology Institute, Technion - Israel Institute of Technology, Haifa, Israel kinneret@ph.technion.ac.il.
[Ti] Título:Buckle up: Membrane tension drives lamellipodial network compression and adhesion deposition.
[So] Source:J Cell Biol;216(9):2619-2621, 2017 Sep 04.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Whether to spread on a surface or to crawl, cells must apply traction forces to the underlying substrate via adhesion complexes. In this issue, Pontes et al. (2017. https://doi.org/10.1083/jcb.201611117) shed new light on how the interplay among membrane tension, the lamellipodial actin network, and adhesions coordinate the dynamics of spreading fibroblasts.
[Mh] Termos MeSH primário: Actinas/química
Pseudópodes
[Mh] Termos MeSH secundário: Fibroblastos/citologia
Fenômenos Mecânicos
Membranas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170803
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201706111


  9 / 17981 MEDLINE  
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[PMID]:28763639
[Au] Autor:Xie M; Luo W; Gray SR
[Ad] Endereço:Institute for Sustainability and Innovation, College of Engineering and Science, Victoria University, PO Box 14428, Melbourne, Victoria, 8001, Australia. Electronic address: ming.xie@vu.edu.au.
[Ti] Título:Surface pattern by nanoimprint for membrane fouling mitigation: Design, performance and mechanisms.
[So] Source:Water Res;124:238-243, 2017 Nov 01.
[Is] ISSN:1879-2448
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Imparting water treatment membrane with surface pattern by nanoimprint offered a novel approach to fouling resistance. We employed nanoimprint to fabricate line-shape nanostructure on membrane distillation (MD) membrane surface. Patterned MD membrane exhibited strong antifouling property to Bovine Serum Albumin (BSA) protein during MD separation. Water flux decline and protein deposition were substantially minimized on the patterned MD membrane in comparison with the pristine one. Such lower fouling propensity on the patterned MD membrane was mainly driven by the weak hydrophobic interaction between BSA protein and patterned MD membrane surface. Weaker adhesion force mapping of the patterned MD membrane was quantified. Representative force-distance curve of pristine MD membrane showed a strong attractive depletion force comparing with that of patterned one. The simple, chemical-free, and scalable nanofabrication approach enables varying designs on membrane surface for special membrane properties.
[Mh] Termos MeSH primário: Membranas Artificiais
Purificação da Água
[Mh] Termos MeSH secundário: Animais
Bovinos
Destilação
Interações Hidrofóbicas e Hidrofílicas
Membranas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Membranes, Artificial)
[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:170802
[St] Status:MEDLINE


  10 / 17981 MEDLINE  
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[PMID]:28715971
[Au] Autor:Lippincott-Schwartz J; Freed EO; van Engelenburg SB
[Ad] Endereço:Janelia Research Campus, Howard Hughes Medical Institute, Ashburn, Virginia 20147.
[Ti] Título:A Consensus View of ESCRT-Mediated Human Immunodeficiency Virus Type 1 Abscission.
[So] Source:Annu Rev Virol;4(1):309-325, 2017 Sep 29.
[Is] ISSN:2327-0578
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The strong dependence of retroviruses, such as human immunodeficiency virus type 1 (HIV-1), on host cell factors is no more apparent than when the endosomal sorting complex required for transport (ESCRT) machinery is purposely disengaged. The resulting potent inhibition of retrovirus release underscores the importance of understanding fundamental structure-function relationships at the ESCRT-HIV-1 interface. Recent studies utilizing advanced imaging technologies have helped clarify these relationships, overcoming hurdles to provide a range of potential models for ESCRT-mediated virus abscission. Here, we discuss these models in the context of prior work detailing ESCRT machinery and the HIV-1 release process. To provide a template for further refinement, we propose a new working model for ESCRT-mediated HIV-1 release that reconciles disparate and seemingly conflicting studies.
[Mh] Termos MeSH primário: Complexos Endossomais de Distribuição Requeridos para Transporte/fisiologia
HIV-1/metabolismo
Liberação de Vírus
[Mh] Termos MeSH secundário: Transporte Biológico
Linhagem Celular
Produtos do Gene gag/genética
Produtos do Gene gag/metabolismo
Seres Humanos
Membranas/metabolismo
Modelos Biológicos
Transporte Proteico
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Endosomal Sorting Complexes Required for Transport); 0 (Gene Products, gag)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171027
[Lr] Data última revisão:
171027
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170719
[St] Status:MEDLINE
[do] DOI:10.1146/annurev-virology-101416-041840



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