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1.
Acta Otorrinolaringol Esp ; 62(3): 246-8, 2011.
Artigo em Espanhol | MEDLINE | ID: mdl-20466354

RESUMO

Synovial sarcoma is a rare tumour found in soft tissue; it is a mesenchymal spindle cell tumour that is not related to the synovial membrane. This tumour has a low incidence, the most frequent place of occurrence being the lower extremities in young adults. Synovial sarcoma of the head and neck accounts for 3-5% of sarcomas in this anatomical region. The treatment of choice for synovial sarcoma of the head and neck is complete surgical excision of the tumour mass followed by adjuvant radiotherapy.


Assuntos
Cavidade Nasal/patologia , Neoplasias Nasais/patologia , Sarcoma Sinovial/patologia , Biomarcadores Tumorais/análise , Terapia Combinada , Dura-Máter/cirurgia , Epistaxe/etiologia , Humanos , Masculino , Pessoa de Meia-Idade , Cavidade Nasal/diagnóstico por imagem , Obstrução Nasal/etiologia , Proteínas de Neoplasias/análise , Neoplasias Nasais/química , Neoplasias Nasais/complicações , Neoplasias Nasais/diagnóstico , Neoplasias Nasais/radioterapia , Neoplasias Nasais/cirurgia , Órbita/cirurgia , Seios Paranasais/cirurgia , Fótons/uso terapêutico , Radioterapia Adjuvante , Radioterapia de Alta Energia , Sarcoma Sinovial/química , Sarcoma Sinovial/complicações , Sarcoma Sinovial/diagnóstico , Sarcoma Sinovial/radioterapia , Sarcoma Sinovial/cirurgia , Tomografia Computadorizada por Raios X , Transtornos da Visão/etiologia
2.
Phys Rev E Stat Nonlin Soft Matter Phys ; 80(5 Pt 1): 051909, 2009 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-20365008

RESUMO

We subject the primary sequence of proteins gathered from the Structural Classification of Proteins (SCOP) database to a discrete wavelet transform (DWT) analysis to search for predictors of secondary structures. We use proteins with both alpha helices and beta sheets (the A/B , A+B databases from SCOP). The amino acids composing the protein are converted to their hydrophobicity values using three hydrophobicity scales. Results prove to be independent of the scale used. Using a DWT multiresolution decomposition, each protein is coarse grained, in effect, creating snapshots of each protein at multiple scales. For each protein, a control data set is formed by generating random realizations that remove the positional informational in the sequence but still contain the same amino acid frequencies. Regions of salient hydrophobicity in the protein sequence are identified by comparing the transforms of the original sequence with those of the control set, at each resolution. We find significant matching between regions of salient hydrophobicity and the locations of secondary structure along the amino acid chains. We calculate the sensitivity, specificity, and Matthews correlation to quantify the agreement between the wavelet detected structures and the real protein. In addition we are able to distinguish between the morphologically different subsets, A/B and A+B. We also construct a correlation function based on the DWT that correlates quasilocalized structures at lengths in wavelet space. Through a similar comparison to the control data sets, features in this space-scale correlation are identified that show correspondence to the typical lengths of the secondary structures.


Assuntos
Algoritmos , Modelos Químicos , Modelos Moleculares , Proteínas/química , Proteínas/ultraestrutura , Análise de Sequência de Proteína/métodos , Processamento de Sinais Assistido por Computador , Sequência de Aminoácidos , Simulação por Computador , Dados de Sequência Molecular , Estrutura Secundária de Proteína
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