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1.
Biochem Biophys Res Commun ; 587: 9-15, 2021 Nov 26.
Artigo em Inglês | MEDLINE | ID: mdl-34861472

RESUMO

OBJECTIVE: The role of circadian clock in cementogenesis is unclear. This study examines the role of REV-ERBs, one of circadian clock proteins, in proliferation, migration and mineralization of cementoblasts to fill the gap in knowledge. METHODS: Expression pattern of REV-ERBα in cementoblasts was investigated in vivo and in vitro. CCK-8 assay, scratch wound healing assay, alkaline phosphatase (ALP) and alizarin red S (ARS) staining were performed to evaluate the effects of REV-ERBs activation by SR9009 on proliferation, migration and mineralization of OCCM-30, an immortalized cementoblast cell line. Furthermore, mineralization related markers including osterix (OSX), ALP, bone sialoprotein (BSP) and osteocalcin (OCN) were evaluated. RESULTS: Strong expression of REV-ERBα was found in cellular cementum around tooth apex. Rev-erbα mRNA oscillated periodically in OCCM-30 and declined after mineralization induction. REV-ERBs activation by SR9009 inhibited proliferation but promoted migration of OCCM-30 in vitro. Results of ALP and ARS staining suggested that REV-ERBs activation negatively regulated mineralization of OCCM-30. Mechanically, REV-ERBs activation attenuated the expression of OSX and its downstream targets including ALP, BSP and OCN. CONCLUSIONS: REV-ERBs are involved in cementogenesis and negatively regulate mineralization of cementoblasts via inhibiting OSX expression. Our study provides a potential target regarding periodontal and cementum regeneration.

2.
Nanoscale ; 13(42): 17912-17919, 2021 Nov 04.
Artigo em Inglês | MEDLINE | ID: mdl-34679146

RESUMO

Periodontitis is a common chronic inflammatory disease associated with biofilm formation, gingival recession, and supporting bone loss that can lead to the formation of periodontal pockets and, ultimately, tooth loss. Clinical treatment for periodontitis through scaling and antibiotics still faces the problems of unavoidable bleeding, injury to periodontal tissue, drug resistance, and insufficient treatment. Herein we prepared an injectable anti-periodontitis ointment with catalytic activity that consists of Pt nanocluster (PtNC) modified g-C3N4 (CN), and PEG400/PEG4000, which efficiently treated biofilm-infected periodontitis. PtNCs (<2 nm) with ultralow content (0.07%) were formed on the surface of CN using mild ultraviolet (UV) irradiation. Due to the strong O2 adsorption and activation ability of CN-PtNCs and their mutual electron transfer, they show both oxidase-like and peroxidase-like activities and produce reactive oxygen species (ROS) in the dark. CN-PtNCs showed strong biofilm elimination ability towards Staphylococcus aureus (S. aureus) and Escherichia coli (E. coli). Furthermore, benefiting from the good biocompatibility of CN-PtNCs and the injectable property of the PEG400/PEG4000 ointment, the CN-PtNC ointment with high bioavailability successfully treated periodontitis in rats, alleviating inflammation and reducing bone loss, and showed better performance than periocline. Therefore, this catalytic system is promising for an efficient, non-invasive, and antibiotic-free treatment of periodontitis.


Assuntos
Nanopartículas Metálicas/uso terapêutico , Periodontite , Platina/uso terapêutico , Animais , Biofilmes/efeitos dos fármacos , Catálise , Escherichia coli , Periodontite/tratamento farmacológico , Ratos , Staphylococcus aureus
3.
Nat Cell Biol ; 23(9): 978-991, 2021 09.
Artigo em Inglês | MEDLINE | ID: mdl-34497368

RESUMO

The extracellular-signal-regulated kinases ERK1 and ERK2 (hereafter ERK1/2) represent the foremost mitogenic pathway in mammalian cells, and their dysregulation drives tumorigenesis and confers therapeutic resistance. ERK1/2 are known to be activated by MAPK/ERK kinase (MEK)-mediated phosphorylation. Here, we show that ERK1/2 are also modified by lysine-63 (K63)-linked polyubiquitin chains. We identify the tripartite motif-containing protein TRIM15 as a ubiquitin ligase and the tumour suppressor CYLD as a deubiquitinase of ERK1/2. TRIM15 and CYLD regulate ERK ubiquitination at defined lysine residues through mutually exclusive interactions as well as opposing activities. K63-linked polyubiquitination enhances ERK interaction with and activation by MEK. Downregulation of TRIM15 inhibits the growth of both drug-responsive and drug-resistant melanomas. Moreover, high TRIM15 expression and low CYLD expression are associated with poor prognosis of patients with melanoma. These findings define a role of K63-linked polyubiquitination in the ERK signalling pathway and suggest a potential target for cancer therapy.


Assuntos
Proteínas de Ligação a DNA/metabolismo , Enzima Desubiquitinante CYLD/metabolismo , Lisina/metabolismo , Sistema de Sinalização das MAP Quinases/fisiologia , Poliubiquitina/metabolismo , Carcinogênese/genética , Carcinogênese/metabolismo , Genes Supressores de Tumor/fisiologia , Humanos , Fosforilação/fisiologia , Transdução de Sinais/fisiologia , Ubiquitina/metabolismo
4.
Nature ; 597(7874): 132-137, 2021 09.
Artigo em Inglês | MEDLINE | ID: mdl-34408321

RESUMO

Protein quality control systems are crucial for cellular function and organismal health. At present, most known protein quality control systems are multicomponent machineries that operate via ATP-regulated interactions with non-native proteins to prevent aggregation and promote folding1, and few systems that can broadly enable protein folding by a different mechanism have been identified. Moreover, proteins that contain the extensively charged poly-Asp/Glu (polyD/E) region are common in eukaryotic proteomes2, but their biochemical activities remain undefined. Here we show that DAXX, a polyD/E protein that has been implicated in diverse cellular processes3-10, possesses several protein-folding activities. DAXX prevents aggregation, solubilizes pre-existing aggregates and unfolds misfolded species of model substrates and neurodegeneration-associated proteins. Notably, DAXX effectively prevents and reverses aggregation of its in vivo-validated client proteins, the tumour suppressor p53 and its principal antagonist MDM2. DAXX can also restore native conformation and function to tumour-associated, aggregation-prone p53 mutants, reducing their oncogenic properties. These DAXX activities are ATP-independent and instead rely on the polyD/E region. Other polyD/E proteins, including ANP32A and SET, can also function as stand-alone, ATP-independent molecular chaperones, disaggregases and unfoldases. Thus, polyD/E proteins probably constitute a multifunctional protein quality control system that operates via a distinctive mechanism.


Assuntos
Proteínas Correpressoras/metabolismo , Chaperonas Moleculares/metabolismo , Dobramento de Proteína , Animais , Linhagem Celular , Células/metabolismo , Evolução Molecular , Humanos , Modelos Moleculares , Mutação , Agregados Proteicos , Agregação Patológica de Proteínas/prevenção & controle , Conformação Proteica , Domínios Proteicos , Desdobramento de Proteína , Deficiências na Proteostase/prevenção & controle , Proteínas Proto-Oncogênicas c-mdm2/química , Proteínas Proto-Oncogênicas c-mdm2/metabolismo , Proteína Supressora de Tumor p53/química , Proteína Supressora de Tumor p53/genética , Proteína Supressora de Tumor p53/metabolismo
5.
Int J Oral Sci ; 13(1): 14, 2021 04 12.
Artigo em Inglês | MEDLINE | ID: mdl-33846295

RESUMO

Mineralized tissue regeneration is an important and challenging part of the field of tissue engineering and regeneration. At present, autograft harvest procedures may cause secondary trauma to patients, while bone scaffold materials lack osteogenic activity, resulting in a limited application. Loaded with osteogenic induction growth factor can improve the osteoinductive performance of bone graft, but the explosive release of growth factor may also cause side effects. In this study, we innovatively used platelet-rich fibrin (PRF)-modified bone scaffolds (Bio-Oss®) to replace autograft, and used cytokine (BMP-2) to enhance osteogenesis. Encouragingly, this mixture, which we named "Autograft Mimic (AGM)", has multiple functions and advantages. (1) The fiber network provided by PRF binds the entire bone scaffold together, thereby shaping the bone grafts and maintaining the space of the defect area. (2) The sustained release of BMP-2 from bone graft promoted bone regeneration continuously. (3) AGM recruited bone marrow mesenchymal stem cells (BMSCs) and promote their proliferation, migration, and osteogenic differentiation. Thus, AGM developed in this study can improve osteogenesis, and provide new guidance for the development of clinical bone grafts.


Assuntos
Células-Tronco Mesenquimais , Osteogênese , Autoenxertos , Regeneração Óssea , Diferenciação Celular , Humanos , Engenharia Tecidual , Tecidos Suporte
6.
Cell Rep ; 33(9): 108418, 2020 12 01.
Artigo em Inglês | MEDLINE | ID: mdl-33264628

RESUMO

Neurodegenerative diseases are characterized by the formation and propagation of protein aggregates, especially amyloid fibrils. However, what normally suppresses protein misfolding and aggregation in metazoan cells remains incompletely understood. Here, we show that TRIM11, a member of the metazoan tripartite motif (TRIM) family, both prevents the formation of protein aggregates and dissolves pre-existing protein deposits, including amyloid fibrils. These molecular chaperone and disaggregase activities are ATP independent. They enhance folding and solubility of normal proteins and cooperate with TRIM11 SUMO ligase activity to degrade aberrant proteins. TRIM11 abrogates α-synuclein fibrillization and restores viability in cell models of Parkinson's disease (PD). Intracranial adeno-associated viral delivery of TRIM11 mitigates α-synuclein-mediated pathology, neurodegeneration, and motor impairments in a PD mouse model. Other TRIMs can also function as ATP-independent molecular chaperones and disaggregases. Thus, we define TRIMs as a potent and multifunctional protein quality-control system in metazoa, which might be applied to treat neurodegenerative diseases.

7.
Biochem Biophys Res Commun ; 505(1): 325-332, 2018 10 20.
Artigo em Inglês | MEDLINE | ID: mdl-30249398

RESUMO

Spindlin1 (SPIN1), a histone modification reader protein, was enriched in the cell nucleolus and facilitated rRNA expression. However, how SPIN1 localizes to the nucleolus and its functional role in rRNA gene expression remain unresolved. Here, we identified a nucleolar localization signal in the N-terminal region of SPIN1 that is essential for its enrichment and function in the nucleolus. We also discovered that, in addition to its H3K4me3 recognizing activity, the H3R8me2a-recognizing capacity of SPIN1 is also indispensable for stimulating rRNA expression. Chromatin immunoprecipitation results indicated that SPIN1 is required for the association or assembly of selective factor 1 (SL1) complex, probably facilitating the initiation of rDNA transcription through its H3 K4me3-R8me2a reader function.


Assuntos
Proteínas de Ciclo Celular/genética , Nucléolo Celular/genética , Expressão Gênica , Genes de RNAr/genética , Histonas/metabolismo , Proteínas Associadas aos Microtúbulos/genética , Fosfoproteínas/genética , Proteínas de Ciclo Celular/metabolismo , Linhagem Celular Tumoral , Nucléolo Celular/metabolismo , Imunoprecipitação da Cromatina , Células HEK293 , Células HeLa , Humanos , Metilação , Proteínas Associadas aos Microtúbulos/metabolismo , Fosfoproteínas/metabolismo , Proteínas Pol1 do Complexo de Iniciação de Transcrição/genética , Proteínas Pol1 do Complexo de Iniciação de Transcrição/metabolismo , Ligação Proteica , Interferência de RNA , Transdução de Sinais/genética
8.
Nat Commun ; 9(1): 1223, 2018 03 26.
Artigo em Inglês | MEDLINE | ID: mdl-29581427

RESUMO

The proteasome is a complex protease critical for protein quality control and cell regulation, and its dysfunction is associated with cancer and other diseases. However, the mechanisms that control proteasome activity  in normal and malignant cells remain unclear. Here we report that TRIM11 enhances degradation of aberrant and normal regulatory proteins, and augments overall rate of proteolysis. Mechanistically, TRIM11 binds to both the proteasome and USP14, a deubiquitinase that prematurely removes ubiquitins from proteasome-bound substrates and also noncatalytically inhibits the proteasome, and precludes their association, thereby increasing proteasome activity. TRIM11 promotes cell survival and is upregulated upon heat shock. Moreover, TRIM11 is required for tumor growth, and increased expression of TRIM11 correlates with poor clinical survival. These findings identify TRIM11 as an important activator of the proteasome, define a pathway that adjusts proteasome activity, and reveal a mechanism by which tumor cells acquire higher degradative power to support oncogenic growth.


Assuntos
Complexo de Endopeptidases do Proteassoma/metabolismo , Proteínas com Motivo Tripartido/fisiologia , Ubiquitina Tiolesterase/metabolismo , Ubiquitina-Proteína Ligases/fisiologia , Animais , Carcinogênese , Linhagem Celular , Linhagem Celular Tumoral , Proliferação de Células/fisiologia , Sobrevivência Celular/fisiologia , Células Cultivadas , Enzimas Desubiquitinantes/metabolismo , Ativação Enzimática , Homeostase , Humanos , Camundongos , Ligação Proteica , Conformação Proteica , Dobramento de Proteína , Proteólise , Proteínas com Motivo Tripartido/química , Proteínas com Motivo Tripartido/metabolismo , Ubiquitina Tiolesterase/antagonistas & inibidores , Ubiquitina Tiolesterase/química , Ubiquitina-Proteína Ligases/química , Ubiquitina-Proteína Ligases/metabolismo , Regulação para Cima
9.
Opt Express ; 26(24): 31391-31401, 2018 Nov 26.
Artigo em Inglês | MEDLINE | ID: mdl-30650725

RESUMO

Simultaneously obtaining high photon emission rate and collection efficiency is highly desirable for applications of single photon sources. However, it remains great challenging and is seldom reported before. Here, we demonstrate that highly enhanced radiation of the emitter and efficient collection of the emitted photons can be simultaneously fulfilled in a hybrid photonic-plasmonic cavity which comprises of an Au nanorod dimer and a photonic crystal nanobeam cavity with a collecting waveguide, where the resonance wavelength of nanobeam cavity is red-detuned from that of the Au nanorod dimer. Our calculations show that the spontaneous emission rate of a single emitter can be enhanced by 5060 -folds, correspondingly, the far-field radiation efficiency and collection efficiency into a dielectric waveguide reaches ~97% and ~67%, respectively. The proposed mechanism paves the way towards the practical applications in ultra-bright on-chip single photon sources and plasmon-based nanolasers.

10.
J Cell Sci ; 127(Pt 22): 4833-45, 2014 Nov 15.
Artigo em Inglês | MEDLINE | ID: mdl-25236602

RESUMO

Wnt-ß-catenin (ß-catenin is also known as CTNNB1 in human) signaling through the ß-catenin-TCF complex plays crucial roles in tissue homeostasis. Wnt-stimulated ß-catenin-TCF complex accumulation in the nucleus regulates cell survival, proliferation and differentiation through the transcription of target genes. Compared with their levels in G1, activation of the receptor LRP6 and cytosolic ß-catenin are both upregulated in G2 cells. However, accumulation of the Wnt pathway negative regulator AXIN2 also occurs in this phase. Therefore, it is unclear whether Wnt signaling is active in G2 phase cells. Here, we established a bimolecular fluorescence complementation (BiFC) biosensor system for the direct visualization of the ß-catenin-TCF interaction in living cells. Using the BiFC biosensor and co-immunoprecipitation experiments, we demonstrate that levels of the nucleus-localized ß-catenin-TCF complex increase during the S and G2 phases, and declines in the next G1 phase. Accordingly, a subset of Wnt target genes is transcribed by the ß-catenin-TCF complex during both the S and G2 phases. By contrast, transient inhibition of this complex disturbs both cell survival and G2/M progression. Our results suggest that in S and G2 phase cells, Wnt-ß-catenin signaling is highly active and functions to ensure cell survival and cell cycle progression.


Assuntos
Fase G2/fisiologia , Fase S/fisiologia , beta Catenina/metabolismo , Linhagem Celular Tumoral , Núcleo Celular/metabolismo , Sobrevivência Celular/fisiologia , Expressão Gênica , Células HeLa , Humanos , Transdução de Sinais , Transcrição Genética , Ativação Transcricional , beta Catenina/genética
11.
J Biol Chem ; 289(22): 15482-94, 2014 May 30.
Artigo em Inglês | MEDLINE | ID: mdl-24737324

RESUMO

The Rac1/JNK cascade plays important roles in DNA damage-induced apoptosis. However, how this cascade is activated upon DNA damage remains to be fully understood. We show here that, in untreated cells, Tiam1, a Rac1-specific guanine nucleotide exchange factor, is phosphorylated by casein kinase 1 (CK1) at its C terminus, leading to Skp, Cullin, F-box-containing(ß-TrCP) recognition, ubiquitination, and proteasome-mediated degradation. Upon DNA-damaging anticancer drug treatment, CK1/ß-TrCP-mediated Tiam1 degradation is abolished, and the accumulated Tiam1 contributes to downstream activation of Rac1/JNK. Consistently, tumor cells overexpressing Tiam1 are hypersensitive to DNA-damaging drug treatment. In xenograft mice, Tiam1-high cells are more susceptible to doxorubicin treatment. Thus, our results uncover that inhibition of proteasome-mediated Tiam1 degradation is an upstream event leading to Rac1/JNK activation and cell apoptosis in response to DNA-damaging drug treatment.


Assuntos
Apoptose/fisiologia , Dano ao DNA/fisiologia , Fatores de Troca do Nucleotídeo Guanina/metabolismo , Transdução de Sinais/fisiologia , Neoplasias do Colo do Útero , Proteínas Contendo Repetições de beta-Transducina/metabolismo , Animais , Antibióticos Antineoplásicos/toxicidade , Apoptose/genética , Caseína Quinase I/metabolismo , Dano ao DNA/efeitos dos fármacos , Doxorrubicina/toxicidade , Feminino , Fatores de Troca do Nucleotídeo Guanina/genética , Células HEK293 , Células HeLa , Humanos , Proteínas Quinases JNK Ativadas por Mitógeno/metabolismo , Camundongos , Camundongos Nus , Transdução de Sinais/genética , Proteína 1 Indutora de Invasão e Metástase de Linfoma de Células T , Ubiquitina-Proteína Ligases/metabolismo , Ubiquitinação/fisiologia , Neoplasias do Colo do Útero/tratamento farmacológico , Neoplasias do Colo do Útero/genética , Neoplasias do Colo do Útero/metabolismo , Ensaios Antitumorais Modelo de Xenoenxerto , Proteínas Contendo Repetições de beta-Transducina/genética , Proteínas rac1 de Ligação ao GTP/metabolismo
12.
Genes Dev ; 28(6): 622-36, 2014 Mar 15.
Artigo em Inglês | MEDLINE | ID: mdl-24589551

RESUMO

Histone modification patterns and their combinatorial readout have emerged as a fundamental mechanism for epigenetic regulation. Here we characterized Spindlin1 as a histone effector that senses a cis-tail histone H3 methylation pattern involving trimethyllysine 4 (H3K4me3) and asymmetric dimethylarginine 8 (H3R8me2a) marks. Spindlin1 consists of triple tudor-like Spin/Ssty repeats. Cocrystal structure determination established concurrent recognition of H3K4me3 and H3R8me2a by Spin/Ssty repeats 2 and 1, respectively. Both H3K4me3 and H3R8me2a are recognized using an "insertion cavity" recognition mode, contributing to a methylation state-specific layer of regulation. In vivo functional studies suggest that Spindlin1 activates Wnt/ß-catenin signaling downstream from protein arginine methyltransferase 2 (PRMT2) and the MLL complex, which together are capable of generating a specific H3 "K4me3-R8me2a" pattern. Mutagenesis of Spindlin1 reader pockets impairs activation of Wnt target genes. Taken together, our work connects a histone "lysine-arginine" methylation pattern readout by Spindlin1-to-Wnt signaling at the transcriptional level.


Assuntos
Proteínas de Ciclo Celular/química , Proteínas de Ciclo Celular/metabolismo , Histonas/química , Histonas/metabolismo , Proteínas Associadas aos Microtúbulos/química , Proteínas Associadas aos Microtúbulos/metabolismo , Modelos Moleculares , Fosfoproteínas/química , Fosfoproteínas/metabolismo , Transdução de Sinais , Fatores de Transcrição de Zíper de Leucina e Hélice-Alça-Hélix Básicos/metabolismo , Proteínas de Ciclo Celular/genética , Células HCT116 , Células HEK293 , Humanos , Metilação , Repetições de Microssatélites , Proteínas Associadas aos Microtúbulos/genética , Mutagênese , Fosfoproteínas/genética , Estrutura Terciária de Proteína , Fator de Transcrição 4 , Fatores de Transcrição/metabolismo , Proteínas Wnt/metabolismo
14.
J Biol Chem ; 285(14): 10890-901, 2010 Apr 02.
Artigo em Inglês | MEDLINE | ID: mdl-20103590

RESUMO

The beta-catenin-lymphoid enhancer factor (LEF) protein complex is the key mediator of canonical Wnt signaling and initiates target gene transcription upon ligand stimulation. In addition to beta-catenin and LEF themselves, many other proteins have been identified as necessary cofactors. Here we report that the evolutionally conserved splicing factor and transcriptional co-regulator, SKIP/SNW/NcoA62, forms a ternary complex with LEF1 and HDAC1 and mediates the repression of target genes. Loss-of-function studies showed that SKIP is obligatory for Wnt signaling-induced target gene transactivation, suggesting an important role of SKIP in the canonical Wnt signaling. Consistent with its involvement in beta-catenin signaling, the C-terminally truncated forms of SKIP are able to stabilize beta-catenin and enhance Wnt signaling. In Xenopus embryos, both overexpression and knockdown of Skip lead to reduced neural crest induction, consistent with down-regulated Wnt signaling in both cases. Our results indicate that SKIP is a novel component of the beta-catenin transcriptional complex.


Assuntos
Proteínas Adaptadoras de Transdução de Sinal/metabolismo , Regulação da Expressão Gênica no Desenvolvimento , Crista Neural/metabolismo , Transdução de Sinais , Proteína Wnt1/metabolismo , beta Catenina/metabolismo , Proteínas Adaptadoras de Transdução de Sinal/antagonistas & inibidores , Proteínas Adaptadoras de Transdução de Sinal/genética , Animais , Western Blotting , Imunoprecipitação da Cromatina , Embrião não Mamífero/citologia , Embrião não Mamífero/metabolismo , Biblioteca Gênica , Células HeLa , Humanos , Técnicas Imunoenzimáticas , Luciferases/metabolismo , Camundongos , Crista Neural/citologia , RNA Mensageiro/genética , RNA Mensageiro/metabolismo , RNA Interferente Pequeno/farmacologia , Reação em Cadeia da Polimerase Via Transcriptase Reversa , Proteína Wnt1/genética , Xenopus laevis , beta Catenina/genética
15.
Cell Motil Cytoskeleton ; 65(7): 581-93, 2008 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-18498124

RESUMO

In an attempt to discover novel proteins functioning in both interphase nucleus and mitotic spindle as NuMA does, we carried out cDNA library screening with pooled autoimmune antibodies. Among positive clones we found a recently identified transcription regulatory protein (CDCA4) with the distinctive nuclear-mitotic apparatus distribution. CDCA4 localizes at metaphase spindle poles and the midzone in later stages. Additionally, an intensive CDCA4 accumulation parallel to spindle was observed in half of metaphase cells but not in later stages, implying a transient form of CDCA4 binding to midzone from anaphase. Mitotic arrest dissolved CDCA4 from centrosomes but during the spindle recovery, CDCA4 invariably colocalized with the microtubule nucleation foci as a component of microtubule organization center. RNA interference of CDCA4 resulted in significant increase of multinuclei and multipolar spindles, suggesting impaired function in chromosome segregation or cytokinesis. However, the spindle checkpoint and the centrosome cycle appeared not to be affected by such interference. Furthermore, CDCA4 depletion resulted in accelerated cell proliferation, perhaps due to the disruption of CDCA4 nuclear function as a transcription suppressor. Interphase CDCA4 is localized in nucleoli by immunofluorescence, although GFP-CDCA4 expressed in the nucleoplasm. An N-terminal KRKC domain appears to be the nuclear localization signal as identified by sequence alignment and the expression of truncated mutants. Taken together, our results suggested that as a novel nuclearmitotic apparatus protein, CDCA4 is involved in spindle organization from prometaphase. When anaphase begins, CDCA4 may play a different role as a midzone factor involved in chromosome segregation or cytokinesis.


Assuntos
Proteínas de Ciclo Celular/metabolismo , Proteínas Nucleares/metabolismo , Fuso Acromático/metabolismo , Antígenos Nucleares/genética , Antígenos Nucleares/metabolismo , Proteínas de Ciclo Celular/genética , Núcleo Celular/metabolismo , Núcleo Celular/ultraestrutura , Células HeLa , Humanos , Mitose/fisiologia , Proteínas Associadas à Matriz Nuclear/genética , Proteínas Associadas à Matriz Nuclear/metabolismo , Proteínas Nucleares/genética , Interferência de RNA , Proteínas Recombinantes de Fusão/genética , Proteínas Recombinantes de Fusão/metabolismo , Fuso Acromático/ultraestrutura
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