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1.
Medicine (Baltimore) ; 100(19): e25762, 2021 May 14.
Artigo em Inglês | MEDLINE | ID: mdl-34106605

RESUMO

ABSTRACT: The aim of this study was to explore the association of rs1836724 single-nucleotide polymorphism (SNP) of ERBB4 with risk and prognosis of non-small cell lung cancer (NSCLC) in the Chinese Han population.The genotype of rs1836724 SNP of ERBB4 from 258 patients with NSCLC and 200 noncancer controls were detected the TaqMan-MGB probes real-time fluorescence polymerase chain reaction. The distribution of genotype and alleles between the 2 groups was compared, and the association between clinicopathological characteristic and rs1836724 SNP was analyzed. Prognosis and influencing factors were analyzed by Kaplan-Meier and Cox regression analysis.There were significant differences in the genotype and allele distribution of ERBB4 rs1836724 between the NSCLC group and control group (P < .05). And CC genotype of rs1836724 was associated with increased risk of NSCLC in the Chinese Han population. Rs1836724 SNP was associated with TNM stage and lymph nodal metastasis (P = .001, P = .007). The median follow-up was 29 months, and the progression-free survival and overall survival of 258 NSCLC patients were 27.91% and 31.39%, respectively. Patients with GG genotype of rs1836724 had poor progression-free survival and overall survival. Rs1836724 SNP was an independent prognostic marker of NSCLC patients, CC genotype had a high risk of poor prognosis (odds ratio = 1.587, 95% confidence interval: 1.079-2.335, P = .019).In Chinese Han populations, rs1836724 SNP of ERBB4 may contribute toward the increased risk and poor prognosis of NSCLC.


Assuntos
Carcinoma Pulmonar de Células não Pequenas/genética , Predisposição Genética para Doença , Neoplasias Pulmonares/genética , Polimorfismo de Nucleotídeo Único , Receptor ErbB-4/genética , Adulto , Idoso , Idoso de 80 Anos ou mais , Grupo com Ancestrais do Continente Asiático , Carcinoma Pulmonar de Células não Pequenas/diagnóstico , Carcinoma Pulmonar de Células não Pequenas/etnologia , Carcinoma Pulmonar de Células não Pequenas/mortalidade , Estudos de Casos e Controles , China/epidemiologia , Feminino , Seguimentos , Genótipo , Técnicas de Genotipagem , Humanos , Neoplasias Pulmonares/diagnóstico , Neoplasias Pulmonares/etnologia , Neoplasias Pulmonares/mortalidade , Masculino , Pessoa de Meia-Idade , Prognóstico , Fatores de Risco , Análise de Sobrevida
2.
J Med Chem ; 64(11): 7312-7330, 2021 06 10.
Artigo em Inglês | MEDLINE | ID: mdl-34009981

RESUMO

The A-type Aurora kinase is upregulated in many human cancers, and it stabilizes MYC-family oncoproteins, which have long been considered an undruggable target. Here, we describe the design and synthesis of a series of pyrimidine-based derivatives able to inhibit Aurora A kinase activity and reduce levels of cMYC and MYCN. Through structure-based drug design of a small molecule that induces the DFG-out conformation of Aurora A kinase, lead compound 13 was identified, which potently (IC50 < 200 nM) inhibited the proliferation of high-MYC expressing small-cell lung cancer (SCLC) cell lines. Pharmacokinetic optimization of 13 by prodrug strategies resulted in orally bioavailable 25, which demonstrated an 8-fold higher oral AUC (F = 62.3%). Pharmacodynamic studies of 25 showed it to effectively reduce cMYC protein levels, leading to >80% tumor regression of NCI-H446 SCLC xenograft tumors in mice. These results support the potential of 25 for the treatment of MYC-amplified cancers including SCLC.


Assuntos
Aurora Quinase A/antagonistas & inibidores , Desenho de Fármacos , Inibidores de Proteínas Quinases/síntese química , Proteínas Proto-Oncogênicas c-myc/metabolismo , Pirimidinas/química , Animais , Aurora Quinase A/metabolismo , Aurora Quinase B/antagonistas & inibidores , Aurora Quinase B/metabolismo , Sítios de Ligação , Proliferação de Células/efeitos dos fármacos , Regulação para Baixo/efeitos dos fármacos , Avaliação Pré-Clínica de Medicamentos , Humanos , Neoplasias Pulmonares/tratamento farmacológico , Masculino , Camundongos , Camundongos Endogâmicos ICR , Simulação de Acoplamento Molecular , Inibidores de Proteínas Quinases/metabolismo , Inibidores de Proteínas Quinases/farmacologia , Inibidores de Proteínas Quinases/uso terapêutico , Pirimidinas/metabolismo , Pirimidinas/farmacologia , Pirimidinas/uso terapêutico , Carcinoma de Pequenas Células do Pulmão/tratamento farmacológico , Relação Estrutura-Atividade , Ensaios Antitumorais Modelo de Xenoenxerto
3.
Aging Cell ; 19(2): e13090, 2020 02.
Artigo em Inglês | MEDLINE | ID: mdl-31833196

RESUMO

Mutations in lamin A (LMNA) are responsible for a variety of human dystrophic and metabolic diseases. Here, we created a mouse model in which progerin, the lamin A mutant protein that causes Hutchinson-Gilford progeria syndrome (HGPS), can be inducibly overexpressed. Muscle-specific overexpression of progerin was sufficient to induce muscular dystrophy and alter whole-body energy expenditure, leading to premature death. Intriguingly, sarcolipin (Sln), an endoplasmic reticulum (ER)-associated protein involved in heat production, is upregulated in progerin-expressing and Lmna knockout (Lmna-/- ) skeletal muscle. The depletion of Sln accelerated the early death of Lmna-/- mice. An examination at the molecular level revealed that progerin recruits Sln and Calnexin to the nuclear periphery. Furthermore, progerin-expressing myoblasts presented enhanced store-operated Ca2+ entry, as well as increased co-localization of STIM1 and ORAI1. These findings suggest that progerin dysregulates calcium homeostasis through an interaction with a subset of ER-associated proteins, resulting in thermogenic and metabolic abnormalities.


Assuntos
Cálcio/metabolismo , Lamina Tipo A/metabolismo , Distrofias Musculares/metabolismo , Progéria/metabolismo , Termogênese/genética , Animais , Calnexina/metabolismo , Núcleo Celular/metabolismo , Modelos Animais de Doenças , Retículo Endoplasmático/metabolismo , Retículo Endoplasmático/ultraestrutura , Estresse do Retículo Endoplasmático/genética , Lamina Tipo A/genética , Camundongos , Camundongos Knockout , Microscopia Eletrônica de Transmissão , Proteínas Musculares/metabolismo , Músculo Esquelético/metabolismo , Músculo Esquelético/fisiopatologia , Distrofias Musculares/fisiopatologia , Mutação , Mioblastos/metabolismo , Mioblastos/patologia , Proteína ORAI1/metabolismo , Progéria/genética , Progéria/mortalidade , Progéria/fisiopatologia , Proteolipídeos/metabolismo , Molécula 1 de Interação Estromal/metabolismo , Regulação para Cima
4.
Stem Cells Dev ; 28(16): 1116-1127, 2019 08 15.
Artigo em Inglês | MEDLINE | ID: mdl-31140357

RESUMO

Interkinetic nuclear migration (INM) is a process by which nuclei oscillate between the basal and apical surfaces of epithelial cells in coordination with the cell cycle. The cytoskeletal machinery including microtubules and actin has been reported to drive apical INM; however, the role of nuclear proteins in this process has yet to be fully elucidated. Here, we investigated the function of a SUN-domain protein, Sun1, in zebrafish. We found that zebrafish sun1 is highly expressed in the ventricular zone of the brain. Knocking down sun1 with antisense morpholino oligonucleotides reduced the abundance of nestin- and gfap-expressing neural stem cells and progenitor cells. The live-cell imaging results showed that sun1 morphant cells migrated toward the basal side during the S phase but failed to migrate apically during the G2 phase. On the contrary, the passive stochastic movement during the G2 phase was unaffected. Furthermore, down regulation of sun1 was shown to reduce the expression of genes associated with the Notch pathway, whereas the expression of genes in the Wnt pathway was less perturbed. Findings from this research suggest that the Sun1-mediated nucleo-cytoskeletal interaction contributes to apical nuclear migration, and may thus affect exposure to Notch signal, thereby altering the composition of the progenitor pool in the embryonic neurogenesis of zebrafish.


Assuntos
Núcleo Celular/metabolismo , Proteínas Associadas aos Microtúbulos/metabolismo , Neurogênese/fisiologia , Proteínas Nucleares/metabolismo , Receptores Notch/metabolismo , Transdução de Sinais/fisiologia , Peixe-Zebra/metabolismo , Actinas/metabolismo , Animais , Ciclo Celular/fisiologia , Divisão Celular/fisiologia , Proliferação de Células/fisiologia , Centrossomo/metabolismo , Citoesqueleto/metabolismo , Células-Tronco Neurais , Neurônios/metabolismo
5.
Eur J Med Chem ; 151: 533-545, 2018 May 10.
Artigo em Inglês | MEDLINE | ID: mdl-29656197

RESUMO

Twenty five novel chemical analogs of the previously reported Aurora kinase inhibitor BPR1K653 (1-(4-(2-((5-chloro-6-phenylfuro[2,3-d]pyrimidin-4-yl)amino)ethyl)phenyl)-3-(2-((dimethylamino)methyl)phenyl)urea) have been designed, synthesized, and evaluated by Aurora-A and Aurora-B enzymatic kinase activity assays. Similar to BPR1K653, analogs 3b-3h bear alkyl or tertiary amino group at the ortho position of the phenylurea, and showed equal or better inhibition activity for Aurora-B over Aurora-A. Conversely, preferential Aurora-A inhibition activity was observed when the same functional group was moved to the meta position of the phenylurea. Compounds 3m and 3n, both of which harbor a tertiary amino group at the meta position of the phenylurea, showed 10-16 fold inhibition selectivity for Aurora-A over Aurora-B. The in vitro kinase inhibition results were verified by Western blot analysis, and indicated that compounds 3m and 3n were more than 75-fold superior in inhibiting T-loop autophosphorylation of Aurora-A (Thr288), compared to Aurora-B (Thr232) in HCT116 colon carcinoma cells. The computational docking analysis suggested that the tertiary amine at the meta position of the phenylurea formed a more stable interaction with residues in the back pocket of Aurora-A than in Aurora-B, a possible explanation for the observed discrepancy in the selectivity. These results support an alternative small molecule design strategy targeting the back pocket of Aurora kinases for selective isoform inhibition.


Assuntos
Aurora Quinase A/antagonistas & inibidores , Aurora Quinase B/antagonistas & inibidores , Compostos Bicíclicos Heterocíclicos com Pontes/química , Compostos Bicíclicos Heterocíclicos com Pontes/farmacologia , Compostos de Fenilureia/química , Compostos de Fenilureia/farmacologia , Inibidores de Proteínas Quinases/química , Inibidores de Proteínas Quinases/farmacologia , Aurora Quinase A/metabolismo , Aurora Quinase B/metabolismo , Compostos Bicíclicos Heterocíclicos com Pontes/síntese química , Neoplasias do Colo/tratamento farmacológico , Neoplasias do Colo/enzimologia , Neoplasias do Colo/metabolismo , Desenho de Fármacos , Células HCT116 , Células HeLa , Humanos , Mitose/efeitos dos fármacos , Simulação de Acoplamento Molecular , Compostos de Fenilureia/síntese química , Fosforilação/efeitos dos fármacos , Inibidores de Proteínas Quinases/síntese química
6.
Phytochemistry ; 145: 93-102, 2018 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-29107811

RESUMO

A phytochemical investigation on the aerial part of Euphorbia helioscopia (Euphorbiaceae) led to the isolation of 22 highly oxygenated diterpenoids with structural types of ent-abietane, ent-kaurane, lathyrane, ent-atisane and ingenane. 17 of them, named euphelionolides A - N, 16-epi-18-hydroxy-abbeokutone, as well as eupheliotriols A and B, were identified to be previously undescribed compounds by extensive analysis of spectroscopic data. The stereostructures of euphelionolides A - K were determined by single crystal X-ray diffraction combined with analysis of substituent effects and comparison of optical characteristics. Eupheliotriol B is the first example of natural occurring lathyrol with 12Z-ene, while ent-atisanes are the first reported from the title plant. Furthermore, euphelionolides F and L exhibited significant cytotoxicity against MCF-7 and PANC-1 cell lines.


Assuntos
Antineoplásicos Fitogênicos/farmacologia , Diterpenos/farmacologia , Euphorbia/química , Oxigênio/química , Antineoplásicos Fitogênicos/química , Antineoplásicos Fitogênicos/isolamento & purificação , Linhagem Celular Tumoral , Proliferação de Células/efeitos dos fármacos , Sobrevivência Celular/efeitos dos fármacos , Diterpenos/química , Diterpenos/isolamento & purificação , Relação Dose-Resposta a Droga , Ensaios de Seleção de Medicamentos Antitumorais , Humanos , Estrutura Molecular , Relação Estrutura-Atividade
7.
Dis Model Mech ; 8(8): 957-67, 2015 Aug 01.
Artigo em Inglês | MEDLINE | ID: mdl-26035387

RESUMO

Migration and organization of the nucleus are essential for the proliferation and differentiation of cells, including neurons. However, the relationship between the positioning of the nucleus and cellular morphogenesis remains poorly understood. Inherited recessive cerebellar ataxia has been attributed to mutations in SYNE1, a component of the linker of nucleoskeleton and cytoskeleton (LINC) complex. Regardless, Syne1-mutant mice present with normal cerebellar development. The Sad1-Unc-84 homology (SUN)-domain proteins are located at the inner nuclear membrane and recruit Syne proteins through the KASH domain to the outer nuclear membrane. Here, we report an unrecognized contribution of Sun1 and Sun2 to the postnatal development of murine cerebellum. Mice depleted of Sun1 showed a marked reduction in the cerebellar volume, and this phenotype is exacerbated with additional loss of a Sun2 allele. Consistent with these histological changes, Sun1(-/-) and Sun1(-/-)Sun2(+/-) mice exhibited defective motor coordination. Results of immunohistochemical analyses suggested that Sun1 is highly expressed in Purkinje cells and recruits Syne2 to the periphery of the nucleus. Approximately 33% of Purkinje cells in Sun1(-/-) mice and 66% of Purkinje cells in Sun1(-/-)Sun2(+/-) mice were absent from the surface of the internal granule layer (IGL), whereas the proliferation and migration of granule neurons were unaffected. Furthermore, the Sun1(-/-)Sun2(+/-) Purkinje cells exhibited retarded primary dendrite specification, reduced dendritic complexity and aberrant patterning of synapses. Our findings reveal a cell-type-specific role for Sun1 and Sun2 in nucleokinesis during cerebellar development, and we propose the use of Sun-deficient mice as a model for studying cerebellar ataxia that is associated with mutation of human SYNE genes or loss of Purkinje cells.


Assuntos
Ataxia Cerebelar/metabolismo , Proteínas Associadas aos Microtúbulos/deficiência , Animais , Ataxia Cerebelar/patologia , Ataxia Cerebelar/fisiopatologia , Cerebelo/embriologia , Cerebelo/patologia , Dendritos/metabolismo , Proteínas de Membrana/metabolismo , Camundongos Knockout , Proteínas Associadas aos Microtúbulos/metabolismo , Atividade Motora , Proteínas do Tecido Nervoso/metabolismo , Membrana Nuclear/metabolismo , Proteínas Nucleares/metabolismo , Transporte Proteico , Células de Purkinje/metabolismo , Sinapses/metabolismo , Proteínas de Ligação a Telômeros/metabolismo
8.
Cancer Res ; 74(24): 7333-43, 2014 Dec 15.
Artigo em Inglês | MEDLINE | ID: mdl-25477335

RESUMO

Aberrant histone methylation is a frequent event during tumor development and progression. KMT1E (also known as SETDB1) is a histone H3K9 methyltransferase that contributes to epigenetic silencing of both oncogenes and tumor suppressor genes in cancer cells. In this report, we demonstrate that KMT1E acts as a metastasis suppressor that is strongly downregulated in highly metastatic lung cancer cells. Restoring KMT1E expression in this setting suppressed filopodia formation, migration, and invasive behavior. Conversely, loss of KMT1E in lung cancer cells with limited metastatic potential promoted migration in vitro and restored metastatic prowess in vivo. Mechanistic investigations indicated that KMT1E cooperates with the TGFß-regulated complex SMAD2/3 to repress metastasis through ANXA2. Together, our findings defined an essential role for the KMT1E/SMAD2/3 repressor complex in TGFß-mediated lung cancer metastasis.


Assuntos
Epigênese Genética , Neoplasias Pulmonares/genética , Metástase Neoplásica/genética , Proteínas Metiltransferases/genética , Animais , Anexina A2/metabolismo , Linhagem Celular Tumoral , Inativação Gênica , Histona-Lisina N-Metiltransferase , Humanos , Neoplasias Pulmonares/patologia , Metilação , Metástase Neoplásica/patologia , Regiões Promotoras Genéticas , Proteínas Metiltransferases/metabolismo , Transdução de Sinais/genética , Proteína Smad2/metabolismo , Proteína Smad3/metabolismo , Ensaios Antitumorais Modelo de Xenoenxerto , Peixe-Zebra
9.
J Cell Sci ; 127(Pt 8): 1792-804, 2014 Apr 15.
Artigo em Inglês | MEDLINE | ID: mdl-24522183

RESUMO

Hutchinson-Gilford progeria syndrome (HGPS) is a human progeroid disease caused by a point mutation on the LMNA gene. We reported previously that the accumulation of the nuclear envelope protein SUN1 contributes to HGPS nuclear aberrancies. However, the mechanism by which interactions between mutant lamin A (also known as progerin or LAΔ50) and SUN1 produce HGPS cellular phenotypes requires further elucidation. Using light and electron microscopy, this study demonstrated that SUN1 contributes to progerin-elicited structural changes in the nuclear envelope and the endoplasmic reticulum (ER) network. We further identified two domains through which full-length lamin A associates with SUN1, and determined that the farnesylated cysteine within the CaaX motif of lamin A has a stronger affinity for SUN1 than does the lamin A region containing amino acids 607 to 656. Farnesylation of progerin enhanced its interaction with SUN1 and reduced SUN1 mobility, thereby promoting the aberrant recruitment of progerin to the ER membrane during postmitotic assembly of the nuclear envelope, resulting in the accumulation of SUN1 over consecutive cellular divisions. These results indicate that the dysregulated interaction of SUN1 and progerin in the ER during nuclear envelope reformation determines the progression of HGPS.


Assuntos
Retículo Endoplasmático/metabolismo , Lamina Tipo A/metabolismo , Proteínas de Membrana/metabolismo , Proteínas Associadas aos Microtúbulos/metabolismo , Membrana Nuclear/metabolismo , Proteínas Nucleares/metabolismo , Progéria/patologia , Retículo Endoplasmático/patologia , Fibroblastos/metabolismo , Células HeLa , Humanos , Lamina Tipo A/genética , Mitose , Membrana Nuclear/patologia , Mutação Puntual , Prenilação , Progéria/genética , Precursores de Proteínas/metabolismo , Processamento de Proteína Pós-Traducional , Transporte Proteico , Pele/patologia
10.
PLoS One ; 7(12): e52556, 2012.
Artigo em Inglês | MEDLINE | ID: mdl-23272250

RESUMO

POU5F1 is essential for maintaining pluripotency in embryonic stem cells (ESCs). It has been reported that the constitutive activation of POU5F1 is sustained by the core transcriptional regulatory circuitry in ESCs; however, the means by which POU5F1 is epigenetically regulated remains enigmatic. In this study a fluorescence-based reporter system was used to monitor the interplay of 5 reprogramming-associated TFs and 17 chromatin regulators in the transcription of POU5F1. We show the existence of a stoichiometric effect for SOX2, POU5F1, NANOG, MYC and KLF4, in regulating POU5F1 transcription. Chromatin regulators EP300, KDM5A, KDM6A and KDM6B cooperate with KLF4 in promoting the transcription of POU5F1. Moreover, inhibiting HDAC activities induced the expression of Pou5f1 in mouse neural stem cells (NSCs) in a spatial- and temporal- dependent manner. Quantitative chromatin immunoprecipitation-PCR (ChIP-qPCR) shows that treatment with valproic acid (VPA) increases the recruitment of Kdm5a and Kdm6a to proximal promoter (PP) and proximal enhancer (PE) of Pou5f1 whereas enrichment of Ep300 and Kdm6b was seen in PP but not PE of Pou5f1 promoter. These findings reveal the interplay between the chromatin regulators and histone modifications in the expression of POU5F1.


Assuntos
Proteína p300 Associada a E1A/metabolismo , Histona Desmetilases/metabolismo , Histona Desmetilases com o Domínio Jumonji/metabolismo , Fatores de Transcrição Kruppel-Like/metabolismo , Proteínas Nucleares/metabolismo , Fator 3 de Transcrição de Octâmero/genética , Proteína 2 de Ligação ao Retinoblastoma/metabolismo , Ativação Transcricional , Animais , Linhagem Celular , Cromatina/metabolismo , Regulação da Expressão Gênica/efeitos dos fármacos , Inibidores de Histona Desacetilases/farmacologia , Proteínas de Homeodomínio/metabolismo , Humanos , Camundongos , Proteína Homeobox Nanog , Células-Tronco Neurais/metabolismo , Ligação Proteica , Proteínas Proto-Oncogênicas c-myc/metabolismo , Sequências Reguladoras de Ácido Nucleico , Ativação Transcricional/efeitos dos fármacos
11.
Virchows Arch ; 450(2): 215-9, 2007 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-17149613

RESUMO

Pediatric renal cell carcinoma (RCC) associated with ASPL-TFE3 gene fusion resulting from balanced translocation, t(X;17)(p11.2;q25), is a distinctive tumor entity. It is uncommon, and most reported cases have exclusively come from Western societies. We report a case of t(X;17)(p11.2;q25) RCC in a 6-year-old Taiwanese boy. The patient presented with dysuria and intermittent hematuria for 1 year. Nonenhanced CT showed a well-defined homogeneous hyperdensity lesion in the upper pole of the left kidney. This patient refused to receive immediate surgical procedures but had routine follow-ups. After a 9-month follow-up, the patient underwent total nephrectomy with a favorable outcome. Final diagnosis is established based on the characteristic microscopic features, strong nuclear TFE-3 immunoreactivity, and the presence of type 1 TFE3-ASPL fusion gene detected by reverse transcriptasepolymerase chain reactions. No adjuvant therapy is given, and the patient is alive without evidence of disease for 1 year and 6 months.


Assuntos
Carcinoma de Células Renais/genética , Cromossomos Humanos Par 17 , Cromossomos Humanos X , Neoplasias Renais/genética , Translocação Genética , Fatores de Transcrição de Zíper de Leucina e Hélice-Alça-Hélix Básicos/genética , Criança , Fusão Gênica , Humanos , Peptídeos e Proteínas de Sinalização Intracelular , Masculino , Proteínas de Neoplasias/genética , Proteínas de Fusão Oncogênica/genética , Reação em Cadeia da Polimerase Via Transcriptase Reversa
12.
Development ; 131(21): 5417-27, 2004 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-15469976

RESUMO

During development, the role of the phosphatidylserine receptor (PSR) in the removal of apoptotic cells that have died is poorly understood. We have investigated this role of PSR in developing zebrafish. Programmed cell death began during the shield stage, with dead cells being engulfed by a neighboring cell that showed a normal-looking nucleus and the nuclear condensation multi-micronuclei of an apoptotic cell. The zebrafish PSR engulfing receptor was cloned (zfpsr), and its nucleotide sequence was compared with corresponding sequences in Drosophila melanogaster (76% identity), human (74%), mouse (72%) and Caenorhabditis elegans (60%). The PSR receptor contained a jmjC domain (residues 143-206) that is a member of the cupin metalloenzyme superfamily, but in this case serves an as yet unknown function(s). psr knockdown by a PSR morpholino oligonucleotide led to accumulation of a large number of dead apoptotic cells in whole early embryo. These cells interfered with embryonic cell migration. In addition, normal development of the somite, brain, heart and notochord was sequentially disrupted up to 24 hours post-fertilization. Development could be rescued in defective embryos by injecting psr mRNA. These results are consistent with a PSR-dependent system in zebrafish embryos that engulfs apoptotic cells mediated by PSR-phagocytes during development, with the system assuming an important role in the normal development of tissues such as the brain, heart, notochord and somite.


Assuntos
Apoptose , Embrião não Mamífero/citologia , Embrião não Mamífero/metabolismo , Desenvolvimento Embrionário , Receptores de Superfície Celular/metabolismo , Peixe-Zebra/embriologia , Peixe-Zebra/metabolismo , Sequência de Aminoácidos , Animais , Movimento Celular , Clonagem Molecular , Embrião não Mamífero/embriologia , Perfilação da Expressão Gênica , Regulação da Expressão Gênica no Desenvolvimento , Humanos , Histona Desmetilases com o Domínio Jumonji , Microscopia Eletrônica , Dados de Sequência Molecular , Organogênese , Fenótipo , Estrutura Terciária de Proteína , RNA Mensageiro/genética , RNA Mensageiro/metabolismo , Receptores de Superfície Celular/química , Receptores de Superfície Celular/genética , Alinhamento de Sequência , Fatores de Tempo , Peixe-Zebra/genética
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