Multimodal fusion models for pulmonary embolism mortality prediction.

Pulmonary embolism (PE) is a common, life threatening cardiovascular emergency. Risk stratification is one of the core principles of acute PE management and determines the choice of diagnostic and therapeutic strategies. In routine clinical practice, clinicians rely on the patient's electronic health record (EHR) to provide a context for their medical imaging interpretation.

Reliability and validity of the Hebrew version of the International Spinal Cord Injury Activities and Participation Basic Data Set.

Background: The International Spinal Cord Injury (SCI) Activities and Participation Basic Data Set (APBDS) was created to facilitate comparisons of levels of function and disability in SCI individuals worldwide.

Aim: Evaluating the reliability and validity of the APBDS's Hebrew translation was our goal.

Design: Observational, cross-sectional study.

Reactions of granulocytic lineage of hemopoiesis and mechanisms of their development in combined treatment with adriablastin and taxotere.

We studied myelotoxic effects of adriablastin and taxotere combination on granulocytic lineage cells and processes of their recovery in patients with stage III-IV breast cancer. Intensive maturation of granulocytic CFU provided regeneration of the hemopoiesis even under conditions of reduced proliferative activity of these cells, which, in turn, led to accumulation of mature and immature neutrophilic granulocytes in the bone marrow and improved reserve capacities of the neutrophil pool in the bone marrow.

[The mechanisms of the proteolytic degradation of native globular proteins. The role of local and global fluctuations of the native structure].

Analysis of the proteolytic degradation of the native protein structure carried out by the comparison of the temperature dependence of the hydrogen exchange and proteolytic splitting rates of the hen egg-white lysozyme and human Hb and apoHb. Acceleration of the burst-like (all or none) proteolytic degradation in the high temperature range is provided by the intensification of the global fluctuations with overall unfolding revealed by hydrogen exchange. For Hb and apoHb the rate of burst-like proteolytic degradation and hydrogen exchange weakly depends on temperature in the range, where hydrogen exchange reveals only local fluctuations of the native protein structure.

[The principles of analysis on multicomponent fluorescence spectra of proteins. Temperature and pH-induced transitions in tetrameric melittin].

Structural transitions in the tetrameric melittin from bee venom in 2 M KCl induced by variations of pH (from 0.7 to 12.0) and temperature (from 2 to 95 degrees C) have been studied.

[The component analysis of tryptophan fluorescence spectra of melittin during its oligomerization].

The oligomerization of melittin with increasing ionic strength and protein concentration was investigated using the methods of decomposition of its tryptophan fluorescence spectra into "elementary" log-normal components. At high ionic strength (up to 2 M KCl), the emission spectra of tetrameric melittin are well described as the sum of two log-normal components, suggesting the presence of tryptophan residues in two sorts of environment with greatly differing polarity. Measurements of fluorescence spectra by iodide showed that these two spectral components possess different Stern-Volmer constants, that is, the tryptophans emitting them have different solvent accessibility, which does not correlate with the crystallographic structure of tetrameric melittin.

[Analysis of log-normal components of fluorescence spectra of prodan and acrylodan bound to proteins].

Steady-state fluorescence spectra of prodan and acrylodan covalently bound to cystein residue of Lys-Cys-Phe tripeptide in solvents of different polarity were analyzed. It was shown that the shape of spectral bands is well described by a log-normal function. Linear relations between three shape-determining parameters of the log-normal function (namely, the positions of spectral maximum and two half-maximum amplitudes) were revealed and evaluated for both fluorophores.

[Assignment of a component of serine proteinase fluorescence spectrum to a cluster of tryptophan residues].

The two log-normal spectral components in, alpha-chymotrypsin, trypsinogen and beta-trypsin fluorescence and the single component of chymotrypsinogen A emission were analyzed using characteristics of microenvironment of atoms of indolic fluorophores of individual tryptophan residues in the three-dimensional structures of the proteins. Tryptophan residues (eight ones in chymotrypsinogen A and alpha-chymotrypsin and four ones in trypsinogen and beta-trypsin) in these homologous proteins form three clusters with resonance excitation energy exchange between fluorophores within each of them. In all the proteins, Trp51 and 141 determine the shorter-wavelength spectral components (ca.

[Assignment of a component of protein fluorescence spectra to tryptophan residues by their three-dimensional microoenvironmental properties].

Parameters of fluorescence of three single-tryptophan-containing proteins and of two log-normal components of proteinase K (2 tryptophans) were analyzed in relation to the microenvironment characteristics of indolic atoms in crystal structures of the proteins. For this purpose, it was constructed a system of microenvironment description including accessibility of the atoms to the bulk and bound water; the density, polarity and mobility of environment within radii of 5.5 and 7.

[Resolution of fluorescence spectra by degree of quenching accessibility].

The novel algorithm QUENCH is described which resolves fluorescence spectra onto two components differing in the accessibility (the Stern-Volmer constants) for small quenchers. In contrast to the known algorithms, the QUENCH first estimates Stern-Volmer constants using the total arrow of spectra measured at different quencher concentrations and, then, calculates contributions of each component into the emission intensities at every wavelength value. The component spectra, resolved with QUENCH from the tryptophan fluorescence of ribosomal S7 protein, were very similar to the log-normal components revealed using the SIMS program [16].

[Decomposition fluorescence spectra of tryptophan residues in proteins based on log-normal components by a least squares method].

An algorithm of decomposition of protein tryptophan spectra into components was developed. The spectral shape of components is described by a uniparametric log-normal function. Rise of certainty and accuracy of resolution of widely overlapping smooth spectral components (a typical uncorrect reverse problem) was achieved using several regularizing factors: (i) the set of experimental spectra used were measured at several quencher concentrations; (ii) the functional being minimized, along with the root mean square residuals of intensities, the term depending on the obedience to the Stern-Volmer law; (iii) an extra information is used--the number of experimental values greatly exceeds the number of parameters to be estimated.

[Ricin structure: the study by the fluorescence quenching method].

To elucidate the details of pH-induced conformational transformation of ricin [I] in the region surrounding tryptophan residues, we studied parameters of fluorescence of the native toxin and its isolated A- and B-subunits at pH 4.0, 5.0 and 7.

[Analysis of the causes of fatal outcome in fractures of the upper third of the femur].

Analysis of 5-year mortality of 1348 patients with fractures of the proximal end of the femur is presented. The effectiveness of measures aimed at the prevention of developing complications has been assessed. The data obtained demonstrate the effectiveness of these measures.

[Effect of the medium on functional and structural properties of serum albumins. IV. The state of human serum albumin in the pH range from 5 to 10].

In order to investigate the effects of temperature and ionic strength on the N-B-transition and the alkaline denaturation of the human serum albumin, the pH-dependences of fluorescence position and relative yield of Trp-24 and of protein bound dye ANS were measured. The measurements were carried out at temperatures from 10 to 45 degrees C and ionic strengths (NaCl) from 0.001 to 0.

[The effect of the medium on the functional and structural properties of serum albumins. III. Relation between the N-F1-, F1-F2- and F2-E transitions of human serum albumin and temperature and ionic strength].

Using fluorescence parameters of tryptophanyl and bound ANS, the acid-induced structural transitions of defatted monomeric human serum albumin were measured as pH-dependences from 6 to 2.5 in the wide range of temperature (10 to 45 degrees C) and ionic strength (from 0.001 to 0.

[The effect of medium on functional and structural properties of serum albumins. II. The effect of temperature on the N-form of human serum albumin].

In order to investigate effects of temperature in the physiological range (from 10 to 50 degrees C) on structural, physical and functional properties of the N-form of human serum albumin (HSA), the temperature dependences of fluorescence parameters of Trp-214 residue of HSA and of the specifically bound dye ANS, as well as of association constants of ANS binding in the primary and secondary binding sites on HSA molecule were measured. The temperature-induced changes of these properties of HSA are essentially dependent on pH (7.0 or 5,6) and ionic strength (0.

[Effect of the medium on the functional and structural properties of serum albumins. I. Effect of ionic strength on N-variant of human serum albumin].

The effect of ionic strength on the 1-anilino-8- naphtalene sulfonate (ANS) binding sites of the N-form of human serum albumin (HSA) was studied by means of the protein and ligand fluorescence. The parameters of the binding of ANS to HSA (the number of sites and the binding constants) were determined by two methods: by measuring the ANS fluorescence either (i) at increasing protein concentrations and constant ANS concentration, or (ii) at increasing ANS concentration and two constant protein concentrations (9.6 and 2.

[Human immune interferon: production and action].

The most marked production of immune interferon by human peripheral blood leukocytes and splenocytes stimulated with phytohemagglutinin (PHA) and staphylococcal enterotoxin A (SEA) was shown to be achieved when lymphoid cells are propagated under conditions of constant sparing mixing on roller apparatus at a temperature of 37 degrees +/- 0.5 degrees C. The resulting interferon was sensitive to low pH, thermolabile, inactivated by treatment with trypsin, and not neutralised by antisera to human alpha- and beta-interferons.

[Intrinsic luminescence of protein as a tool for studying fast structural dynamics].

The photoexcitation of Trp, Tyr or Phe chromophore in a protein is analogous to the instant (10(-15) to 10(-14) s) introduction of a local probe carrying strong electronic and protonic donor and acceptor moieties and, moreover, having a significant dipole moment (4 to 11 D). Depending on the protein structure mobility during the excited state lifetime, the intra-macromolecular complexes (the exciplexes) with polar groups can be formed and some reversible charge transfer processes, which qaench the fluorescence, can take place with greater or lesser probability. The shifts of Trp fluorescence spectra from 307 to 316 nm (due to the 1:1 exciplex formation) and to 325-330 nm (2:1 exciplex) are typical for many proteins.

[Effect of calcium binding on the quenching time of self-fluorescence of Ca-binding proteins].

Lifetimes of phenylalanine, tyrosine and tryptophan self-fluorescence of three Ca2+-binding proteins (parvalbumins pI 4.47 and 3.95 and bovine alpha-lactalbumin) in the Ca2+-saturated state and without Ca2+ were measured on a device functioning in a channel of synchrotron radiation of the Lebedev Physical Institute electron accelerator C-60 with a single photon counting system.

[Binding of Mg ions with alpha-lactalbumin studied by fluorescent spectroscopy].

Titration of metal-freed bovine alpha-lactalbumin with Mg2+ ions causes a two-stepped decrease in the fluorescence quantum yield and a pronounced spectral shift towards shorter wavelengths. It seems to reflect conformational changes induced by the binding of two Mg2+ ions to the protein molecule which results in a transfer of some tryptophan residues from the protein surface into an interior part of the protein in rigid unpolar environment. The Mg2+ association constants evaluated from the fluorimetric Mg2+-titration are 2x10(3) and 2x10(2) M-1.

[Binding of Ca2+ ions to bovine alpha-lactalbumin. Intrinsic protein fluorescence changes].

Binding of Ca2+ ion to bovine alpha-lactalbumin molecule causes a conformational change reflected in an almost two-fold decrease of the fluorescence quantum yield and a rather pronounced spectral shift towards shorter wavelengths (by ca. 20 nm). The changes could be interpreted as a result of a transfer of highly exposed tryptophan residue(s) into a rigid internal part of the protein molecule containing effective quenching groups (probably, vicinal disulphide bridges).