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1.
Aust Dent J ; 67(1): 5-11, 2022 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-34555206

RESUMO

This scoping review was carried out to evaluate the important role Australian university-based dental teaching clinics and dental students might have in promoting oral cancer awareness in their patients. Four Online database (PubMed, OVID, Scopus and Emcare) were searched for studies that assessed oral cancer awareness amongst patients attending Australian university-associated (teaching) clinics. A total of five articles were retrieved for full-text analysis. All studies showed significant variation in patient awareness and understanding regarding the principal risk factors associated with oral cancer development. Smoking was predominantly identified as a significant risk factor, but alcohol consumption was less frequently recognized as relevant. Non-healing ulceration was most commonly identified as a symptom of concern, whilst red and/or white mucosal patches were infrequently recognized as potentially malignant conditions. Our review confirms that a significant lack of patient awareness regarding oral cancer risk and the signs /symptoms of early malignancy or potentially malignant disease exist in patients attending dental teaching clinics. Important opportunities exist to involve dental students proactively in raising oral cancer awareness, delivering smoking cessation interventions and safe alcohol consumption advice to their patients. Incorporation of established health educational models might deliver effective support for such student-delivered patient education.


Assuntos
Clínicas Odontológicas , Neoplasias Bucais , Austrália/epidemiologia , Conhecimentos, Atitudes e Prática em Saúde , Humanos , Neoplasias Bucais/diagnóstico , Neoplasias Bucais/etiologia , Inquéritos e Questionários , Universidades
2.
Phys Chem Chem Phys ; 16(27): 14139-49, 2014 Jul 21.
Artigo em Inglês | MEDLINE | ID: mdl-24902514

RESUMO

Dithiol-substituted Zn-phthalocyanine derivatives (TAZnPc1, TAZnPc2 and TAZnPc3) were synthesized and functionalized on nanometals (Au and Ag) and nanometal-TiO2 hybrids were harnessed to cover the visible region of the absorption spectrum. Photophysical studies reveal that both H- and J-aggregation were present in the ZnPc-functionalized nanometal, and the extent of J-aggregation is superior on the surface of Ag nanoparticles. On the other hand, no H-aggregation was observed in the nanometal-TiO2 hybrid film, despite the fact that the tetra-anchoring derivative (TAZnPc3) shows lesser J-aggregation on the nanometal-TiO2 hybrid film than that of other two mono-anchoring derivatives (TAZnPc1 and TAZnPc2). Further, the electron injection and recombination processes were investigated by time-resolved fluorescence and absorption spectroscopy. All the derivatives furnish biexponential decay on the nanometal surface. The shorter component is due to electron injection of ZnPc-nanometal particles and the longer component is due to free ZnPc. The rate of electron injection is faster for ZnPc-gold nanoparticles than that of silver nanoparticles, predominantly in TAZnPc1. This is due to the greater aggregation tendency of ZnPc derivatives on Ag nanoparticles than Au nanoparticles. After electron injection, the electron-transfer product (i.e. the radical cation of ZnPc) was observed at 600 nm. Moreover, the fluorescence of ZnPc derivatives on nanometal-TiO2 films was completely quenched due to the shuttling of electrons from ZnPc to TiO2 efficiently by metal nanoparticles.

3.
J Biomed Opt ; 19(5): 057011, 2014 May.
Artigo em Inglês | MEDLINE | ID: mdl-24853147

RESUMO

Fluorescence spectral techniques are very sensitive, and hence they are gaining importance in cancer detection. The biomarkers indicative of cancer could be identified and quantified by spectral or time domain fluorescence spectroscopy. The results of an investigation of time-resolved spectra of cellular components of blood obtained from cervical cancer patients and normal controls are given. The cancer indicative biomarker in this paper is porphyrin; it has a fluorescence decay time of 60% more in samples of cancer patients than those of normal controls. Based on such measurements, a randomized set comprising samples from cancer patients and controls (N=27 in total) could be classified with sensitivity (92%) and specificity (86%).


Assuntos
Biomarcadores Tumorais/sangue , Análise Química do Sangue/métodos , Imagem Óptica/métodos , Espectrometria de Fluorescência/métodos , Neoplasias do Colo do Útero/sangue , Adulto , Análise de Variância , Análise Discriminante , Feminino , Humanos , Pessoa de Meia-Idade , Porfirinas/sangue , Reprodutibilidade dos Testes , Neoplasias do Colo do Útero/diagnóstico
4.
Phys Chem Chem Phys ; 16(3): 1015-21, 2014 Jan 21.
Artigo em Inglês | MEDLINE | ID: mdl-24281355

RESUMO

We have synthesized symmetrical and unsymmetrical Zn-phthalocyanine derivatives (PZnPc, MPZnPc and TPZnPc) for dye sensitized solar cells (DSSCs). Steady state and time-resolved absorption and fluorescence studies were performed in DMF solvent and on a TiO2 surface. The mode and extent of aggregation (H- and J-aggregates) of ZnPc adsorbed on a TiO2 surface were demonstrated. MPZnPc shows both H- and J-aggregation, while TPZnPc shows only H-aggregation. Moreover, the fluorescence of ZnP/TiO2 was completely quenched and this was assigned to electron injection from excited ZnPc to TiO2. Energy level calculations show both ZnPc deriviatives have enough driving force to inject electrons into the conduction band of TiO2. Furthermore, the radical cation of ZnPc was observed in nanosecond transient absorption measurements.

5.
J Phys Chem A ; 115(50): 14292-9, 2011 Dec 22.
Artigo em Inglês | MEDLINE | ID: mdl-22066705

RESUMO

Ratiometric sensors for the detection of metal ions have gained increasing attention due to its self-calibration tendency for the environmental effects. In this context, we have synthesized and characterized a dual emitting ratiometric Zn(2+) probe (1) having acridinedione as a fluorophore and N,N-bis(2-pyridylmethyl)amine (BPA) as a receptor unit. Existence of two different conformation of the molecule with photoinduced electron transfer (PET) from amine moiety to the acridinedione fluorophore leads to dual emission, namely locally excited (425 nm) and anomalous charge transfer emission (560 nm) in aprotic solvents. In the presence of one equivalent of Zn(2+), a 15-fold fluorescence enhancement in the locally excited state together with the quenching of charge transfer emission is observed. The intensity changes at the two emission peaks allow a ratiometric detection of Zn(2+) under PET signaling mechanism. The utilization of PET process for the ratiometric fluorescence change will further signify the importance of PET mechanism in sensing action. Addition of Zn(2+) to 1 in acetonitrile/water mixtures shows a single emission peak with fluorescence enhancement.


Assuntos
Acridinas/química , Elétrons , Corantes Fluorescentes/síntese química , Luz , Piridinas/química , Zinco/química , Acetonitrilas/química , Cátions Bivalentes , Transporte de Elétrons , Cinética , Estrutura Molecular , Espectrometria de Fluorescência
6.
J Fluoresc ; 21(6): 2165-72, 2011 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-21769603

RESUMO

Interaction of photoinduced electron transfer (PET) based acridinedione dye (ADR 1) with amides like formamide, acetamide and dimethylformamide (DMF) were investigated by fluorescence spectral techniques. A fluorescence enhancement accompanied with a blue shift in the emission maximum was observed on the addition of amides to ADR 1 dye, which possess C(6)H(4)(p-OCH(3)) in the 9th position of the basic acridinedione ring. The extent of fluorescence enhancement and the blue shift in the emission maximum of ADR 1 dye is of the order of DMF > acetamide > formamide. DMF, which is more hydrophobic and less polar, results in a higher extent of fluorescence enhancement and a larger shift in the emission maximum towards the blue region. On the addition of amides, the ADR 1 dye prefers to orient towards a more hydrophobic phase surrounded by more number of amide molecules. The fluorescence enhancement of ADR 1 dye is attributed to the suppression of PET process occurring through space. The influence of the hydrophobic nature and the polarity of the amides on the excited state properties of acridinedione dyes are elucidated by steady-state and time resolved fluorescence measurements.


Assuntos
Acridinas/química , Amidas/química , Corantes Fluorescentes/química , Formamidas/química , Água/química , Transporte de Elétrons , Processos Fotoquímicos
7.
J Fluoresc ; 21(4): 1499-508, 2011 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-21287251

RESUMO

Urea and alkyl urea derivatives, which posses a free N-H moiety in the urea molecular framework is responsible for the fluorescence quenching of BSA. Fluorescence quenching accompanied with a blue initially and subsequently a red shift in the emission maximum of BSA is observed on the addition of urea derivatives containing N-H moieties. On the contrary, a fluorescence enhancement accompanied with a shift in the emission maximum towards the blue region is observed on the addition of tetramethylurea (TMU). Urea derivatives, which posses a free N-H moiety acts as a perfect denaturant by direct hydrogen-bonding interaction with BSA resulting in the unfolding process. The unfolding of the buried tryptophan moieties to the aqueous phase does not occur, when all the N-H moieties in the urea are methyl substituted (TMU). Fluorescence spectral techniques reveal that the direct hydrogen-bonding interaction of the N-H moiety of urea molecular framework with the carbonyl oxygen moieties of BSA results in the unfolding of the tryptophan moieties to the aqueous phase, while that of the carbonyl oxygen of urea with the N-H moieties of BSA is definitely not involved in the denaturation process. Steady state and time-resolved fluorescence studies illustrate that the extent of protein folding occurs at a relatively lower concentration of unsymmetrical alkyl urea derivatives (butyl urea (BU) and ethyl urea (EU)), compared to that of urea.


Assuntos
Fluorescência , Soroalbumina Bovina/química , Ureia/química , Animais , Bovinos , Ligação de Hidrogênio , Desnaturação Proteica , Espectrometria de Fluorescência , Ureia/análogos & derivados
8.
J Phys Chem B ; 115(1): 84-92, 2011 Jan 13.
Artigo em Inglês | MEDLINE | ID: mdl-21158409

RESUMO

Acridinedione-based heteroditopic hosts 1a-c, which contain a flexible oxyethylene moiety as a metal ion binding site and amino hydrogen as an anion receptor unit, were synthesized and characterized. Metal ion and anion binding studies were carried out in different solvents to understand the solvent-induced selectivity of the metal ion binding and anion interactions. In acetonitrile, Ca(2+) alone shows a binding with the oxyethylene unit and -OCH(3) group, which results in a fluorescence enhancement without any spectral shift due to the suppression of the photoinduced electron transfer (PET) process. In chloroform, in addition to Ca(2+), Na(+) also shows a fluorescence enhancement with a 14 nm red shift in the emission maximum. (1)H NMR titration studies confirm that the addition of Na(+) does not involve binding at the oxyethylene moiety, while it shows a binding at the acridinedione carbonyl group and -OCH(3) group, which results in the red shift and fluorescence enhancement, respectively. In the anion interaction studies, F(-) shows a neat deprotonation in polar aprotic solvents, whereas in chloroform, it shows a H-bond complex due to the lower anion desolvation energy. The present study clearly signifies the role of solvent in metal ion selectivity, which is an often unnoticed parameter in metal ion binding.

9.
J Fluoresc ; 20(5): 993-1002, 2010 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-20372999

RESUMO

Photophysical studies of photoinduced electron transfer (PET) and non-PET based acridinedione dyes with guanidine hydrochloride (GuHCl) were carried out in water and methanol. Addition of GuHCl to photoinduced electron transfer (PET) based acridinedione dye (ADR 1) results in a fluorescence enhancement, whereas a non-PET based dye (ADR 2) shows no significant change in the fluorescence intensity and lifetime. Addition of GuHCl to ADR 1 dye in methanol results in single exponential decay behaviour, on the contrary a biexponential decay pattern was observed on the addition of GuHCl in water. Absorption and emission spectral studies of ADR 1 dye interaction with GuHCl reveals that the dye molecule is not in the protonated form in aqueous GuHCl solution, and the dye is confined to two distinguishable microenvironment in the aqueous phase. A large variation in the microenvironment around the dye molecule is created on the addition of GuHCl and this was ascertained by time-resolved area normalized emission spectroscopy (TRANES) and time-resolved emission spectroscopy (TRES). The dye molecule prefers to reside in the hydrophobic microenvironment, rather in the hydrophilic aqueous phase is well emphasized by time-resolved fluorescence lifetime studies. The mechanism of fluorescence enhancement of ADR 1 dye by GuHCl is attributed to the suppression of the PET process occurring through space.


Assuntos
Acridinas/química , Corantes/química , Guanidina/química , Desnaturação Proteica , Transporte de Elétrons/efeitos da radiação , Fluorescência , Metanol/química , Oxirredução , Fotoquímica , Soluções/química , Espectrometria de Fluorescência , Água/química
10.
Artigo em Inglês | MEDLINE | ID: mdl-16872879

RESUMO

Fluorescence quenching of 9,10-dimethyl-3, 4,6,7,9,10-hexahydro-1,8(2H,5H) acridinedione (ADD) dye by N,N-dimethylaniline (DMA) in SDS and CTAB were studied by steady state fluorescence and time resolved techniques. The Stern-Volmer plots for the quenching of ADD by DMA is found to be linear and the Stern-Volmer constant K(SV) depends on the micellar concentration. The fluorescence quenching analysis reveals the binding of DMA with the micelles. The perturbation of the probe on the position of DMA molecule in micelle is inferred in the present investigation. The ADD fluorophore drives the DMA molecule into the non-polar region (core) of the micelle whereas other fluorophores like pyrene and rhodamine6G do not affect the position of DMA. In this report, the importance of the nature of fluorophores in determining the position and association of the quencher molecules in the aggregated systems is being discussed.


Assuntos
Acridinas/química , Compostos de Anilina/química , Corantes Fluorescentes/química , Micelas , Cetrimônio , Compostos de Cetrimônio , Fluorescência , Cinética , Espectrometria de Fluorescência
11.
J Phys Chem B ; 110(47): 23783-9, 2006 Nov 30.
Artigo em Inglês | MEDLINE | ID: mdl-17125340

RESUMO

Spectroscopic investigations involving the interaction of acridinedione dyes with urea and its derivatives in water and methanol were carried out by absorption, steady-state fluorescence, and time-resolved fluorescence measurements. The hydrogen-bonding properties of urea and derivatives in aqueous solutions are found to be distinctly different from those observed in methanol. Urea, which can serve both as a hydrogen bond donor as well as an acceptor and has a unique hydrogen-bonding feature, helps in studying urea interaction with fluorophores in aqueous solutions, micelles, and alcohol. In our studies, we have used acridinedione dyes as the probe. We report that the hydrophobic interaction of urea with dye predominates by weakening of the hydrogen-bonding interaction of the solvent and urea derivatives with increase in the hydrophobicity of urea derivatives. In methanol, the hydrogen bonding between solvent and urea derivatives predominating over the hydrophobicity of the urea derivatives is observed. The presence of alkyl group substitution in the N-H moiety with a function of increasing concentration resulting in the creation of a more favorable hydrophobic environment to the dye molecule to reside in the hydrophobic shell phase rather than in the bulk aqueous phase is illustrated. The hydrophobic interaction of dye with urea in aqueous solution predominates because of the weakening of the hydrogen bonding of the solvent and urea derivatives, and the photoinduced electron transfer (PET) process is used as a marker to identify the hydrophobic interaction illustrated in our studies.


Assuntos
Acridinas/química , Corantes Fluorescentes/química , Solventes/química , Ureia/farmacologia , Transporte de Elétrons/efeitos da radiação , Hidrogênio/química , Ligação de Hidrogênio , Interações Hidrofóbicas e Hidrofílicas , Metanol/química , Micelas , Nitrogênio/química , Fotoquímica , Espectrometria de Fluorescência , Fatores de Tempo , Água/química
12.
Spectrochim Acta A Mol Biomol Spectrosc ; 58(8): 1535-43, 2002 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-12166722

RESUMO

1,6-Naphthyridines are a class of compounds that exhibit second harmonic generation on excitation with a Nd-YAG laser (1064 nm). Solvatochromism has been used to estimate enhancement in the dipole moments on excitation and the values of first-order hyperpolarizability, beta. Photophysical studies on the title compounds show that they have a fluorescence lifetime of about 10 ns and fluorescence quantum yield of approximately 0.05-0.1 in different solvents. Kurtz powder method has been used to find the NLO efficiency of the compounds with reference to urea.


Assuntos
Naftiridinas/química , Fenômenos Químicos , Físico-Química , Espectroscopia de Ressonância Magnética , Óptica e Fotônica , Fotoquímica , Espectrometria de Fluorescência , Espectrofotometria , Espectroscopia de Infravermelho com Transformada de Fourier
13.
Spectrochim Acta A Mol Biomol Spectrosc ; 58(7): 1443-51, 2002 May.
Artigo em Inglês | MEDLINE | ID: mdl-12083667

RESUMO

Spectroscopic properties of a new family of acridinedione dyes are reported. The absorption and fluorescence spectra of the different substituted acridinediones have been recorded in different solvents and the difference in the dipole moment between ground and excited state has been obtained by solvatochromic shift method. The value of the Onsager cavity radius was calculated from the total surface area using software PCMODEL. Fluorescence quantum yield and fluorescence lifetime were determined. Radiative and non-radiative constants have been calculated. The triplet-triplet absorption maxima and triplet lifetime show variation depending on the substitution.


Assuntos
Acridinas/química , Corantes/química , Solventes/química , Acetonitrilas/química , Lasers , Luz , Modelos Químicos , Software , Espectrometria de Fluorescência
14.
J Biol Chem ; 271(32): 19571-7, 1996 Aug 09.
Artigo em Inglês | MEDLINE | ID: mdl-8702651

RESUMO

Biglycan is a small chondroitin sulfate proteoglycan found in many tissues and is structurally related to decorin, fibromodulin, and lumican. The biological function of biglycan is poorly understood, although several studies have indicated interaction with other extracellular matrix components. We have initiated studies of structural and functional domains of biglycan by transient eukaryotic expression using the vaccinia virus/T7 bacteriophage expression system. A recombinant vaccinia virus, vBGN4 encoding the mature biglycan core protein as a polyhistidine fusion protein under control of the T7 phage promoter was expressed in HT-1080 cells and UMR106 cells. The structure of the recombinant biglycan secreted by these cells was defined by analyzing molecules labeled in the presence of [35S]sulfate, [3H]glucosamine, and [35S]methionine. Glycoforms of biglycan were separated by imidazole gradient elution, under non-denaturing conditions, and comprised: a large proteoglycan form substituted with two chondroitin sulfate chains of molecular mass approximately 34 kDa (HT-1080 cells) or approximately 40 kDa (UMR106 cells); a small proteoglycan form substituted with two chondroitin sulfate chains with a median molecular mass approximately 28 kDa; and a core protein form secreted devoid of glycosaminoglycan chains. All the glycoforms were substituted with two N-linked oligosaccharides, and the disaccharide composition of the two glycosaminoglycan populations were identical. Approximately 70% of the recombinant biglycan secreted by HT-1080 cells was substituted with chondroitin sulfate chains, whereas about 50% of the biglycan expressed by UMR106 cells was substituted with chondroitin sulfate chains. Infection with vBGN4 in both HT-1080 and UMR106 cells resulted in the production of approximately 10 mg of biglycan/10(9) cells per 24 h. The native recombinant biglycan was shown to bind to collagen type V and the complement protein, C1q. However, when the secondary structure of recombinant biglycan was disrupted by exposure to 4 M guanidine hydrochloride, the affinity for collagen type V was dramatically reduced. These data demonstrate the importance of secondary structure to the function of this small proteoglycan.


Assuntos
Proteoglicanas/genética , Sequência de Aminoácidos , Sequência de Bases , Biglicano , Linhagem Celular , Cromatografia Líquida , Colágeno/metabolismo , Complemento C1q/metabolismo , DNA Complementar , Eletroforese em Gel de Poliacrilamida , Proteínas da Matriz Extracelular , Humanos , Dados de Sequência Molecular , Ligação Proteica , Processamento de Proteína Pós-Traducional , Estrutura Secundária de Proteína , Proteoglicanas/isolamento & purificação , Proteoglicanas/metabolismo , Proteínas Recombinantes/genética , Proteínas Recombinantes/isolamento & purificação , Proteínas Recombinantes/metabolismo
15.
J Biol Chem ; 271(32): 19578-84, 1996 Aug 09.
Artigo em Inglês | MEDLINE | ID: mdl-8702652

RESUMO

The vaccinia virus/T7 bacteriophage expression system was used to express human decorin in HT-1080 cells by co-infection with vTF7-3, encoding T7 RNA polymerase, and vDCN1, encoding the decorin core protein fused to a polyhistidine-insulin signal sequence fusion-protein cassette. Overexpression using the vaccinia virus/T7 phage system resulted in secretion of approximately 30 mg of decorin/10(9) cells per 24 h which enabled purification and separation of multiple glycoforms under native conditions. Cells were cultured in the presence of [35S]methionine or a mixture of [3H]glucosamine and [35S]sulfate, and recombinant glycoprotein purified by metal affinity chromatography which resolved the secreted decorin into two classes, a proteoglycan form and a core protein form. About 25% of the recombinant protein was secreted into the culture medium as core protein devoid of glycosaminoglycan chains. The decorin core protein was resolved into two forms (approximately 49 and approximately 53 kDa) that differed in the extent of N-linked oligosaccharide substitution (2 and 3 N-linked oligosaccharides, respectively). Deglycosylation of the recombinant proteoglycans and core proteins resulted in a single band migrating with an apparent molecular mass approximately 43 kDa when analyzed by SDS-polyacrylamide gel electrophoresis. Far-UV circular dichroism spectra of native decorin proteoglycan showed a minima at 218 nm, consistent with a secondary structure that is predominantly beta-sheet. Circular dichroism spectra of bovine decorin extracted from articular cartilage and recombinant decorin similarly treated revealed a minima of 205 nm indicating a loss of secondary structure. The affinity of decorin proteoglycan and core protein for collagen-like molecules was demonstrated, with the complement component C1q exhibiting the most striking affinity for decorin, although adherence to collagen types I and V was also observed. The extensive secondary structure maintained in the purified recombinant protein is likely to be important for the biological function of decorin.


Assuntos
Proteoglicanas/química , Proteoglicanas/isolamento & purificação , Animais , Sequência de Bases , Bovinos , Cromatografia de Afinidade , Dicroísmo Circular , DNA Complementar , Decorina , Eletroforese em Gel de Poliacrilamida , Proteínas da Matriz Extracelular/metabolismo , Vetores Genéticos , Glicosilação , Humanos , Dados de Sequência Molecular , Ligação Proteica , Proteoglicanas/metabolismo , Proteínas Recombinantes/química , Proteínas Recombinantes/isolamento & purificação , Proteínas Recombinantes/metabolismo
16.
Virology ; 222(1): 100-14, 1996 Aug 01.
Artigo em Inglês | MEDLINE | ID: mdl-8806491

RESUMO

This paper identifies two structural proteins of the occluded derived viral envelope of Autographa californica nuclear polyhedrosis virus (AcMNPV): ODV-E18 and ODV-E35. In addition, we identify a protein, ODV-EC27, that is incorporated into the capsid of occluded virus, which is not detected in budded virus. The genes for these proteins reside within the IE0 intron. The intron was sequenced, and five open reading frames (ORF) were identified. ORF 3 (genomic ORF 143) codes for the ODV envelope protein, ODV-E18. ORF 4 (genomic ORF 144) codes for ODV-EC27, and Western blot analyses locate this protein to both the ODV capsid and envelope. Transcripts for both ODV-E18 and ODV-EC27 initiate from conserved TAAG motifs, and transcripts are detected from 16 through 72 hr p.i. Antiserum to ODV-E18 recognizes a band of 18 kDa on Western blots of extracts from infected cells and bands of 18 and 35 kDa on Western blots of proteins from purified ODV envelope. N-terminal amino acid sequencing reveals that both ODV-E18 and ODV-E35 contain the same N-terminus. Antiserum to ODV-EC27 recognizes a protein of 27 kDa on Western blots of extracts from infected cells and bands of 27 and 35 kDa on Western blots of proteins from purified ODV. Using immunogold labeling techniques, ODV-E18 and/or ODV-E35 are detected in viral induced intranuclear microvesicles and are not detected in the plasma membrane, cytoplasmic membranes, or the nuclear envelope. Immunogold labeling using antisera to ODV-EC27 detects this protein on both the ODV envelope and capsid.


Assuntos
Nucleopoliedrovírus/genética , Biossíntese de Proteínas , Transcrição Gênica , Proteínas do Envelope Viral/genética , Proteínas Estruturais Virais/genética , Sequência de Aminoácidos , Animais , Sequência de Bases , Proteínas do Capsídeo , Linhagem Celular , Genes Virais , Microscopia Imunoeletrônica , Dados de Sequência Molecular , Nucleopoliedrovírus/metabolismo , Nucleopoliedrovírus/ultraestrutura , Homologia de Sequência de Aminoácidos , Spodoptera/citologia , Proteínas do Envelope Viral/metabolismo , Proteínas Estruturais Virais/metabolismo
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