PubMed · 7942497
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R Cataldo. 1994. Residencies database.. https://doi.org/10.1016/s0160-3450(15)30359-7
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BACKGROUND: Discernible improvements have taken place in soft tissue sarcoma patient survivorship and quality of life over the past 20 years, with overall 5-year survival currently at approximately 50%. Shifts in treatment have taken place over the past decade, from single-modality treatment involving radical surgery to sophisticated limb-salvage strategies combined with radiation therapy and protocol-administered chemotherapy. METHODS: To identify patterns of treatment and outcome, all soft tissue sarcoma cases diagnosed in 1988 and 1993 as recorded in the National Cancer Data Base were analyzed on the basis of histology and anatomic site. RESULTS: There was an increase in sarcomas originating in the pleura with a concurrent increase in mesotheliomas. A shift toward more advanced disease was also noted. Limb-sparing surgical procedures are now standard. However, it appears from stage subset analysis that many Stage II and III patients are undertreated due to lack of multimodality therapy usage. CONCLUSIONS: Use of pretreatment multimodality planning conferences will increase the likelihood that stage-appropriate combinations of surgery, radiation therapy, and chemotherapy will be used. In turn, election of multimodality approaches should increase the possibility of improved overall and disease free survival in the future.
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The question of whether proteins originate from random sequences of amino acids is addressed. A statistical analysis is performed in terms of blocked and random walk values formed by binary hydrophobic assignments of the amino acids along the protein chains. Theoretical expectations of these variables from random distributions of hydrophobicities are compared with those obtained from functional proteins. The results, which are based upon proteins in the SWISS-PROT data base, convincingly show that the amino acid sequences in proteins differ from what is expected from random sequences in a statistically significant way. By performing Fourier transforms on the random walks, one obtains additional evidence for nonrandomness of the distributions. We have also analyzed results from a synthetic model containing only two amino acid types, hydrophobic and hydrophilic. With reasonable criteria on good folding properties in terms of thermodynamical and kinetic behavior, sequences that fold well are isolated. Performing the same statistical analysis on the sequences that fold well indicates similar deviations from randomness as for the functional proteins. The deviations from randomness can be interpreted as originating from anticorrelations in terms of an Ising spin model for the hydrophobicities. Our results, which differ from some previous investigations using other methods, might have impact on how permissive with respect to sequence specificity protein folding process is-only sequences with nonrandom hydrophobicity distributions fold well. Other distributions give rise to energy landscapes with poor folding properties and hence did not survive the evolution.