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Pesquisa : A11.284.430.106.279.345.447 [Categoria DeCS]
Referências encontradas : 7 [refinar]
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  1 / 7 MEDLINE  
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[PMID]:26262858
[Au] Autor:Perroni DV; Baez-Cotto CM; Sorenson GP; Mahanthappa MK
[Ad] Endereço:Department of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, Wisconsin 53706, United States.
[Ti] Título:Linker Length-Dependent Control of Gemini Surfactant Aqueous Lyotropic Gyroid Phase Stability.
[So] Source:J Phys Chem Lett;6(6):993-8, 2015 Mar 19.
[Is] ISSN:1948-7185
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Network-phase lyotropic liquid crystals (LLCs) derived from the water-directed self-assembly of small molecule amphiphiles comprise a useful class of soft nanomaterials, with wide-ranging applications in structural biology and membrane science. However, few known surfactants enable access to these mesophases over wide temperature and amphiphile concentration phase windows. Recent studies have demonstrated that gemini ("twin tail") dicarboxylate surfactants, in which alkyl carboxylates are covalently linked near the headgroups by a hydrophobic bridge, exhibit increased propensities to form double gyroid network phase LLCs. We demonstrate herein that the lyotropic self-assembly behaviors of gemini dicarboxylates sensitively depend on the linker length, whereby odd-carbon linkers stabilize the double gyroid network LLC over unprecedented amphiphile concentration windows up to ∼45 wt % wide between T ≈ 22-80 °C. These self-assembly phenomena, which arise from the linker length-dependent preferred molecular conformations of these amphiphiles, will broaden the technological applications of these nanostructured LLCs.
[Mh] Termos MeSH primário: Transportadores de Ácidos Dicarboxílicos/química
Gêmeos de Corpos Enovelados/química
Interações Hidrofóbicas e Hidrofílicas
Cristais Líquidos/química
Tensoativos/química
[Mh] Termos MeSH secundário: Nanoestruturas/química
Água/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Dicarboxylic Acid Transporters); 0 (Surface-Active Agents); 059QF0KO0R (Water)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:150812
[Lr] Data última revisão:
150812
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150812
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jpclett.5b00092


  2 / 7 MEDLINE  
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[PMID]:25735748
[Au] Autor:Yu Y; Chi B; Xia W; Gangopadhyay J; Yamazaki T; Winkelbauer-Hurt ME; Yin S; Eliasse Y; Adams E; Shaw CE; Reed R
[Ad] Endereço:Department of Cell Biology, Harvard Medical School, 240 Longwood Ave., Boston, MA 02115, USA.
[Ti] Título:U1 snRNP is mislocalized in ALS patient fibroblasts bearing NLS mutations in FUS and is required for motor neuron outgrowth in zebrafish.
[So] Source:Nucleic Acids Res;43(6):3208-18, 2015 Mar 31.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Mutations in FUS cause amyotrophic lateral sclerosis (ALS), but the molecular pathways leading to neurodegeneration remain obscure. We previously found that U1 snRNP is the most abundant FUS interactor. Here, we report that components of the U1 snRNP core particle (Sm proteins and U1 snRNA), but not the mature U1 snRNP-specific proteins (U1-70K, U1A and U1C), co-mislocalize with FUS to the cytoplasm in ALS patient fibroblasts harboring mutations in the FUS nuclear localization signal (NLS). Similar results were obtained in HeLa cells expressing the ALS-causing FUS R495X NLS mutation, and mislocalization of Sm proteins is RRM-dependent. Moreover, as observed with FUS, knockdown of any of the U1 snRNP-specific proteins results in a dramatic loss of SMN-containing Gems. Significantly, knockdown of U1 snRNP in zebrafish results in motor axon truncations, a phenotype also observed with FUS, SMN and TDP-43 knockdowns. Our observations linking U1 snRNP to ALS patient cells with FUS mutations, SMN-containing Gems, and motor neurons indicate that U1 snRNP is a component of a molecular pathway associated with motor neuron disease. Linking an essential canonical splicing factor (U1 snRNP) to this pathway provides strong new evidence that splicing defects may be involved in pathogenesis and that this pathway is a potential therapeutic target.
[Mh] Termos MeSH primário: Esclerose Amiotrófica Lateral/genética
Esclerose Amiotrófica Lateral/metabolismo
Sinais de Localização Nuclear/genética
Proteína FUS de Ligação a RNA/genética
Ribonucleoproteína Nuclear Pequena U1/metabolismo
[Mh] Termos MeSH secundário: Esclerose Amiotrófica Lateral/patologia
Animais
Animais Geneticamente Modificados
Citoplasma/metabolismo
Gêmeos de Corpos Enovelados/metabolismo
Gêmeos de Corpos Enovelados/patologia
Técnicas de Silenciamento de Genes
Células HeLa
Seres Humanos
Neurônios Motores/metabolismo
Neurônios Motores/patologia
Mutação
Domínios e Motivos de Interação entre Proteínas
Proteína FUS de Ligação a RNA/química
Proteína FUS de Ligação a RNA/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Ribonucleoproteína Nuclear Pequena U1/antagonistas & inibidores
Ribonucleoproteína Nuclear Pequena U1/genética
Peixe-Zebra/embriologia
Peixe-Zebra/genética
Peixe-Zebra/metabolismo
Proteínas Centrais de snRNP/genética
Proteínas Centrais de snRNP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Nuclear Localization Signals); 0 (RNA-Binding Protein FUS); 0 (Recombinant Proteins); 0 (Ribonucleoprotein, U1 Small Nuclear); 0 (SNRPB protein, human); 0 (snRNP Core Proteins)
[Em] Mês de entrada:1506
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150305
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkv157


  3 / 7 MEDLINE  
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[PMID]:25052091
[Au] Autor:Stejskalová E; Stanek D
[Ad] Endereço:Department of RNA Biology, Institute of Molecular Genetics AS CR, 142 20 Prague, Czech Republic Faculty of Science, Charles University in Prague, 128 43 Prague, Czech Republic.
[Ti] Título:The splicing factor U1-70K interacts with the SMN complex and is required for nuclear gem integrity.
[So] Source:J Cell Sci;127(Pt 18):3909-15, 2014 Sep 15.
[Is] ISSN:1477-9137
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The nuclear SMN complex localizes to specific structures called nuclear gems. The loss of gems is a cellular marker for several neurodegenerative diseases. Here, we identify that the U1-snRNP-specific protein U1-70K localizes to nuclear gems, and we show that U1-70K is necessary for gem integrity. Furthermore, we show that the interaction between U1-70K and the SMN complex is RNA independent, and we map the SMN complex binding site to the unstructured N-terminal tail of U1-70K. Consistent with these results, the expression of the U1-70K N-terminal tail rescues gem formation. These findings show that U1-70K is an SMN-complex-associating protein, and they suggest a new function for U1-70K in the formation of nuclear gems.
[Mh] Termos MeSH primário: Gêmeos de Corpos Enovelados/metabolismo
Ribonucleoproteína Nuclear Pequena U1/metabolismo
Proteínas do Complexo SMN/metabolismo
[Mh] Termos MeSH secundário: Sítios de Ligação
Núcleo Celular/química
Núcleo Celular/genética
Núcleo Celular/metabolismo
Gêmeos de Corpos Enovelados/química
Células HeLa
Seres Humanos
Ligação Proteica
Transporte Proteico
Processamento de RNA
Ribonucleoproteína Nuclear Pequena U1/química
Ribonucleoproteína Nuclear Pequena U1/genética
Proteínas do Complexo SMN/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Ribonucleoprotein, U1 Small Nuclear); 0 (SMN Complex Proteins); 0 (SNRNP70 protein, human)
[Em] Mês de entrada:1506
[Cu] Atualização por classe:140916
[Lr] Data última revisão:
140916
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140724
[St] Status:MEDLINE
[do] DOI:10.1242/jcs.155838


  4 / 7 MEDLINE  
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[PMID]:24112438
[Au] Autor:Onodera O; Ishihara T; Shiga A; Ariizumi Y; Yokoseki A; Nishizawa M
[Ad] Endereço:Department of Molecular Neuroscience, Brain Research Institute, Niigata University, Niigata, Japan.
[Ti] Título:Minor splicing pathway is not minor any more: implications for the pathogenesis of motor neuron diseases.
[So] Source:Neuropathology;34(1):99-107, 2014 Feb.
[Is] ISSN:1440-1789
[Cp] País de publicação:Australia
[La] Idioma:eng
[Ab] Resumo:To explore the molecular pathogenesis of amyotrophic lateral sclerosis (ALS), the nuclear function of TAR-DNA binding protein 43 kDa (TDP-43) must be elucidated. TDP-43 is a nuclear protein that colocalizes with Cajal body or Gem in cultured cells. Several recent studies have reported that the decreasing number of Gems accompanied the depletion of the causative genes for ALS, TDP-43 and FUS. Gems play an important role in the pathogenesis of spinal muscular atrophy. Gems are the sites of the maturation of spliceosomes, which are composed of uridylate-rich (U) snRNAs (small nuclear RNAs) and protein complex, small nuclear ribonuclearprotein (snRNP). Spliceosomes regulate the splicing of pre-mRNA and are classified into the major or minor classes, according to the consensus sequence of acceptor and donor sites of pre-mRNA splicing. Although the major class of spliceosomes regulates most pre-mRNA splicing, minor spliceosomes also play an important role in regulating the splicing or global speed of pre-mRNA processing. A mouse model of spinal muscular atrophy, in which the number of Gems is decreased, shows fewer subsets U snRNAs. Interestingly, in the central nervous system, U snRNAs belonging to the minor spliceosomes are markedly reduced. In ALS, the U12 snRNA is decreased only in the tissue affected by ALS and not in other tissues. Although the molecular mechanisms underlying the decreased U12 snRNA resulting in cell dysfunction and cell death in motor neuron diseases remain unclear, these findings suggest that the disturbance of nuclear bodies and minor splicing may underlie the common molecular pathogenesis of motor neuron diseases.
[Mh] Termos MeSH primário: Esclerose Amiotrófica Lateral/etiologia
Proteínas de Ligação a DNA/metabolismo
Gêmeos de Corpos Enovelados/metabolismo
Doença dos Neurônios Motores/etiologia
[Mh] Termos MeSH secundário: Esclerose Amiotrófica Lateral/genética
Esclerose Amiotrófica Lateral/metabolismo
Esclerose Amiotrófica Lateral/patologia
Núcleo Celular/metabolismo
Núcleo Celular/ultraestrutura
Gêmeos de Corpos Enovelados/ultraestrutura
Seres Humanos
Doença dos Neurônios Motores/genética
Doença dos Neurônios Motores/metabolismo
Doença dos Neurônios Motores/patologia
RNA/metabolismo
Processamento de RNA
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (DNA-Binding Proteins); 63231-63-0 (RNA)
[Em] Mês de entrada:1409
[Cu] Atualização por classe:160826
[Lr] Data última revisão:
160826
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131012
[St] Status:MEDLINE
[do] DOI:10.1111/neup.12070


  5 / 7 MEDLINE  
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[PMID]:23740936
[Au] Autor:Ishihara T; Ariizumi Y; Shiga A; Kato T; Tan CF; Sato T; Miki Y; Yokoo M; Fujino T; Koyama A; Yokoseki A; Nishizawa M; Kakita A; Takahashi H; Onodera O
[Ad] Endereço:These authors contributed equally to this work.
[Ti] Título:Decreased number of Gemini of coiled bodies and U12 snRNA level in amyotrophic lateral sclerosis.
[So] Source:Hum Mol Genet;22(20):4136-47, 2013 Oct 15.
[Is] ISSN:1460-2083
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Disappearance of TAR-DNA-binding protein 43 kDa (TDP-43) from the nucleus contributes to the pathogenesis of amyotrophic lateral sclerosis (ALS), but the nuclear function of TDP-43 is not yet fully understood. TDP-43 associates with nuclear bodies including Gemini of coiled bodies (GEMs). GEMs contribute to the biogenesis of uridine-rich small nuclear RNA (U snRNA), a component of splicing machinery. The number of GEMs and a subset of U snRNAs decrease in spinal muscular atrophy, a lower motor neuron disease, suggesting that alteration of U snRNAs may also underlie the molecular pathogenesis of ALS. Here, we investigated the number of GEMs and U11/12-type small nuclear ribonucleoproteins (snRNP) by immunohistochemistry and the level of U snRNAs using real-time quantitative RT-PCR in ALS tissues. GEMs decreased in both TDP-43-depleted HeLa cells and spinal motor neurons in ALS patients. Levels of several U snRNAs decreased in TDP-43-depleted SH-SY5Y and U87-MG cells. The level of U12 snRNA was decreased in tissues affected by ALS (spinal cord, motor cortex and thalamus) but not in tissues unaffected by ALS (cerebellum, kidney and muscle). Immunohistochemical analysis revealed the decrease in U11/12-type snRNP in spinal motor neurons of ALS patients. These findings suggest that loss of TDP-43 function decreases the number of GEMs, which is followed by a disturbance of pre-mRNA splicing by the U11/U12 spliceosome in tissues affected by ALS.
[Mh] Termos MeSH primário: Esclerose Amiotrófica Lateral/metabolismo
Esclerose Amiotrófica Lateral/patologia
Proteínas de Ligação a DNA/genética
Gêmeos de Corpos Enovelados/metabolismo
Neurônios Motores/patologia
RNA Nuclear Pequeno/genética
Ribonucleoproteínas Nucleares Pequenas/metabolismo
[Mh] Termos MeSH secundário: Esclerose Amiotrófica Lateral/genética
Células Cultivadas
Proteínas de Ligação a DNA/metabolismo
Células HeLa
Seres Humanos
Córtex Motor/metabolismo
Córtex Motor/patologia
Neurônios Motores/metabolismo
Processamento de RNA
RNA Nuclear Pequeno/metabolismo
Reação em Cadeia da Polimerase em Tempo Real
Ribonucleoproteínas Nucleares Pequenas/genética
Proteínas do Complexo SMN/genética
Proteínas do Complexo SMN/metabolismo
Medula Espinal/metabolismo
Medula Espinal/patologia
Tálamo/metabolismo
Tálamo/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA-Binding Proteins); 0 (RNA, Small Nuclear); 0 (Ribonucleoproteins, Small Nuclear); 0 (SMN Complex Proteins); 0 (U11-U12 small nuclear ribonucleoprotein); 0 (U12 small nuclear RNA)
[Em] Mês de entrada:1404
[Cu] Atualização por classe:160826
[Lr] Data última revisão:
160826
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130607
[St] Status:MEDLINE
[do] DOI:10.1093/hmg/ddt262


  6 / 7 MEDLINE  
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[PMID]:22220673
[Au] Autor:Hsu YY; Jong YJ; Tsai HH; Tseng YT; An LM; Lo YC
[Ad] Endereço:Graduate Institute of Medicine, Kaohsiung Medical University, Kaohsiung, Taiwan.
[Ti] Título:Triptolide increases transcript and protein levels of survival motor neurons in human SMA fibroblasts and improves survival in SMA-like mice.
[So] Source:Br J Pharmacol;166(3):1114-26, 2012 Jun.
[Is] ISSN:1476-5381
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND AND PURPOSE: Spinal muscular atrophy (SMA) is a progressive neuromuscular disease. Since disease severity is related to the amount of survival motor neuron (SMN) protein, up-regulated functional SMN protein levels from the SMN2 gene are considered a major SMA drug-discovery strategy. In this study, we investigated the possible effects of triptolide, a diterpene triepoxide purified from Tripterygium wilfordii Hook. F., as a new compound for increasing SMN protein. EXPERIMENTAL APPROACH: The effects and mechanisms of triptolide on the production of SMA protein were determined by cell-based assays using the motor neuronal cell line NSC34 and skin fibroblasts from SMA patients. Wild-type (Smn(+/+) SMN2(-/-) , C57BL/6) and SMA-like (Smn(-/-) SMN2) mice were injected with triptolide (0.01 or 0.1 mg·kg(-1) ·day(-1) , i.p.) and their survival rate and level of change in SMN protein in neurons and muscle tissue measured. KEY RESULTS: In NSC34 cells and human SMA fibroblasts, pM concentrations of triptolide significantly increased SMN protein expression and the levels of SMN complex component (Gemin2 and Gemin3). In human SMA fibroblasts, triptolide increased SMN-containing nuclear gems and the ratio of full-length transcripts (FL-SMN2) to SMN2 transcripts lacking exon 7 (SMN2Δ7). Furthermore, in SMA-like mice, triptolide significantly increased SMN protein levels in the brain, spinal cord and gastrocnemius muscle. Furthermore, triptolide treatment increased survival and reduced weight loss in SMA-like mice. CONCLUSION AND IMPLICATIONS: Triptolide enhanced SMN protein production by promoting SMN2 activation, exon 7 inclusion and increasing nuclear gems, and increased survival in SMA mice, which suggests triptolide might be a potential candidate for SMA therapy.
[Mh] Termos MeSH primário: Diterpenos/uso terapêutico
Fibroblastos/efeitos dos fármacos
Neurônios Motores/efeitos dos fármacos
Atrofia Muscular Espinal/tratamento farmacológico
Fármacos Neuroprotetores/uso terapêutico
Fenantrenos/uso terapêutico
Proteína 2 de Sobrevivência do Neurônio Motor/biossíntese
Transcrição Genética/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Apoptose/efeitos dos fármacos
Western Blotting
Peso Corporal/efeitos dos fármacos
Técnicas de Cultura de Células
Linhagem Celular
Sobrevivência Celular/efeitos dos fármacos
Modelos Animais de Doenças
Diterpenos/administração & dosagem
Diterpenos/isolamento & purificação
Diterpenos/farmacologia
Relação Dose-Resposta a Droga
Compostos de Epóxi/administração & dosagem
Compostos de Epóxi/isolamento & purificação
Compostos de Epóxi/farmacologia
Compostos de Epóxi/uso terapêutico
Fibroblastos/metabolismo
Fibroblastos/patologia
Gêmeos de Corpos Enovelados/efeitos dos fármacos
Gêmeos de Corpos Enovelados/metabolismo
Seres Humanos
Estimativa de Kaplan-Meier
Camundongos
Camundongos Knockout
Estrutura Molecular
Neurônios Motores/metabolismo
Atrofia Muscular Espinal/metabolismo
Atrofia Muscular Espinal/patologia
Fármacos Neuroprotetores/administração & dosagem
Fármacos Neuroprotetores/isolamento & purificação
Fármacos Neuroprotetores/farmacologia
Fenantrenos/administração & dosagem
Fenantrenos/isolamento & purificação
Fenantrenos/farmacologia
Reação em Cadeia da Polimerase em Tempo Real
Proteína 2 de Sobrevivência do Neurônio Motor/genética
Tripterygium/química
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Diterpenes); 0 (Epoxy Compounds); 0 (Neuroprotective Agents); 0 (Phenanthrenes); 0 (Survival of Motor Neuron 2 Protein); 19ALD1S53J (triptolide)
[Em] Mês de entrada:1210
[Cu] Atualização por classe:150128
[Lr] Data última revisão:
150128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120107
[St] Status:MEDLINE
[do] DOI:10.1111/j.1476-5381.2012.01829.x


  7 / 7 MEDLINE  
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[PMID]:19617559
[Au] Autor:Bruns AF; van Bergeijk J; Lorbeer C; Nölle A; Jungnickel J; Grothe C; Claus P
[Ad] Endereço:Hannover Medical School, Department of Neuroanatomy, Hannover, Germany.
[Ti] Título:Fibroblast growth factor-2 regulates the stability of nuclear bodies.
[So] Source:Proc Natl Acad Sci U S A;106(31):12747-52, 2009 Aug 04.
[Is] ISSN:1091-6490
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Nuclear bodies are distinct subnuclear structures. The survival of motoneuron (SMN) gene is mutated or deleted in patients with the neurodegenerative disease spinal muscular atrophy (SMA). The gene product SMN is a marker protein for one class of nuclear bodies denoted as nuclear gems. SMN has also been found in Cajal bodies, which co-localize with gems in many cell types. Interestingly, SMA patients display a reduced number of gems. Little is known about the regulation of nuclear body formation and stabilization. We have previously shown that a nuclear isoform of the fibroblast growth factor-2 (FGF-2(23)) binds directly to SMN. In this study, we analyzed the consequences of FGF-2(23) binding to SMN with regard to nuclear body formation. On a molecular level, we showed that FGF-2(23) competed with Gemin2 (a component of the SMN complex that is necessary for gem stabilization) for binding to SMN. Down-regulation of Gemin2 by siRNA caused destabilization of SMN-positive nuclear bodies. This process is reflected in both cellular and in vivo systems by a negative regulatory function of FGF-2 in nuclear body formation: in HEK293 cells, FGF-2(23) decreased the number of SMN-positive nuclear bodies. The same effect could be observed in motoneurons of FGF-2 transgenic mice. This study demonstrates the functional role of a growth factor in the regulation of structural entities of the nucleus.
[Mh] Termos MeSH primário: Corpos Enovelados/fisiologia
Fator 2 de Crescimento de Fibroblastos/fisiologia
Gêmeos de Corpos Enovelados/fisiologia
[Mh] Termos MeSH secundário: Animais
Seres Humanos
Imunoprecipitação
Camundongos
Camundongos Transgênicos
Proteínas do Tecido Nervoso/fisiologia
Proteínas de Ligação a RNA/fisiologia
Receptor Tipo 1 de Fator de Crescimento de Fibroblastos/fisiologia
Proteínas do Complexo SMN/análise
Proteínas do Complexo SMN/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (GEMIN2 protein, human); 0 (Nerve Tissue Proteins); 0 (RNA-Binding Proteins); 0 (SMN Complex Proteins); 103107-01-3 (Fibroblast Growth Factor 2); EC 2.7.10.1 (Receptor, Fibroblast Growth Factor, Type 1)
[Em] Mês de entrada:0908
[Cu] Atualização por classe:141207
[Lr] Data última revisão:
141207
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:090721
[St] Status:MEDLINE
[do] DOI:10.1073/pnas.0900122106



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