Paraprosthetic Complications After Endoprosthesis Replacement of Pelvis Joint with Implants.

PURPOSE: The purpose of the paper is shaping of ideas about possible ways of decreasing complications of the analyzed types of operations and identification of opportunities of the impact on the socio-economic environment among the Afro-American population of USA. The paper demonstrates that the issue of coxofemoral prosthesis is not only a purely medical but also a social problem. In particular, availability of timely aid, as well as insurance in the form of surgery, refer to relevance of the range of problems. METHODOLOGY: The experimental method was used in the study. Patients were implanted different types of endoprostheses. 90 patients were implanted customized endoprostheses, 27 patients were implanted foreign module endoprostheses. The research subject is prediction of complications after endoprosthesis replacement surgeries depending on methods, types and forms. RESULTS: As a result, we can see that available health insurance is more acceptable understanding of the need for endoprosthesis replacement. Post-operative care issues fall into the range of social policy problems. A comparative aspect of a country with general insurance and differentiated coverage among the Afro-America population appears innovative. CONCLUSIONS: In the context of the current situation it can be concluded that surgery is the last stage for already established support system of the population. For this reason, it's worth mentioning that state bodies of the U.S. should put a greater emphasis on the health care of the Afro-American population.

Structural analysis of influenza A virus matrix protein M1 and its self-assemblies at low pH.

Influenza A virus matrix protein M1 is one of the most important and abundant proteins in the virus particles broadly involved in essential processes of the viral life cycle. The absence of high-resolution data on the full-length M1 makes the structural investigation of the intact protein particularly important. We employed synchrotron small-angle X-ray scattering (SAXS), analytical ultracentrifugation and atomic force microscopy (AFM) to study the structure of M1 at acidic pH. The low-resolution structural models built from the SAXS data reveal a structurally anisotropic M1 molecule consisting of a compact NM-fragment and an extended and partially flexible C-terminal domain. The M1 monomers co-exist in solution with a small fraction of large clusters that have a layered architecture similar to that observed in the authentic influenza virions. AFM analysis on a lipid-like negatively charged surface reveals that M1 forms ordered stripes correlating well with the clusters observed by SAXS. The free NM-domain is monomeric in acidic solution with the overall structure similar to that observed in previously determined crystal structures. The NM-domain does not spontaneously self assemble supporting the key role of the C-terminus of M1 in the formation of supramolecular structures. Our results suggest that the flexibility of the C-terminus is an essential feature, which may be responsible for the multi-functionality of the entire protein. In particular, this flexibility could allow M1 to structurally organise the viral membrane to maintain the integrity and the shape of the intact influenza virus.

The in situ structural characterization of the influenza A virus matrix M1 protein within a virion.

The first attempt has been made to suggest a model of influenza A virus matrix M1 protein spatial structure and molecule orientation within a virion on the basis of tritium planigraphy data and theoretical prediction results. Limited in situ proteolysis of the intact virions with bromelain and surface plasmon resonance spectroscopy study of the M1 protein interaction with lipid coated surfaces were used for independent confirmation of the proposed model.