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Träfflista för sökning "WFRF:(Deak L) srt2:(2001-2004)"

Sökning: WFRF:(Deak L) > (2001-2004)

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1.
  • Adler, SS, et al. (författare)
  • Double helicity asymmetry in inclusive midrapidity pi(0) production for polarized p+p collisions at root s=200 GeV
  • 2004
  • Ingår i: Physical Review Letters. - 1079-7114. ; 93:20: 202002
  • Tidskriftsartikel (refereegranskat)abstract
    • We present a measurement of the double longitudinal spin asymmetry in inclusive pi(0) production in polarized proton-proton collisions at roots=200 GeV. The data were taken at the Relativistic Heavy Ion Collider with average beam polarizations of 0.27. The measurements are the first in a program to study the longitudinal spin structure of the proton, using strongly interacting probes, at collider energies. The asymmetry is presented for transverse momenta 1-5 GeV/c at midrapidity, where next-to-leading-order perturbative quantum chromodynamic (NLO pQCD) calculations well describe the unpolarized cross section. The observed asymmetry is small and is compared to a NLO pQCD calculation with a range of polarized gluon distributions.
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3.
  • Beuchat, L. R., et al. (författare)
  • Performance of mycological media in enumerating desiccated food spoilage yeasts : an interlaboratory study
  • 2001
  • Ingår i: International Journal of Food Microbiology. - : Elsevier. - 0168-1605 .- 1879-3460. ; 70:1-2, s. 89-96
  • Tidskriftsartikel (refereegranskat)abstract
    • Dichloran 18% glycerol agar (DG18) was originally formulated to enumerate nonfastidious xerophilic moulds in foods containing rapidly growing Eurotium species. Some laboratories are now using DG18 as a general purpose medium for enumerating yeasts and moulds, although its performance in recovering yeasts from dry foods has not been evaluated. An interlaboratory study compared DG18 with dichloran rose bengal chloramphenicol agar (DRBC), plate count agar supplemented with chloramphenicol (PCAC), tryptone glucose yeast extract chloramphenicol agar (TGYC), acidified potato dextrose agar (APDA), and orange serum agar (OSA) for their suitability to enumerate 14 species of lyophilized yeasts. The coefficient of variation for among-laboratories repeatability within yeast was 1.39% and reproducibility of counts among laboratories was 7.1%. The order of performance of media for recovering yeasts was TGYC > PCAC = OSA > APDA > DRBC > DG18. A second study was done to determine the combined effects of storage time and temperature on viability of yeasts and suitability of media for recovery. Higher viability was retained at - 18 degreesC than at 5 degreesC or 25 degreesC for up to 42 weeks, although the difference in mean counts of yeasts stored at - 18 degreesC and 25 degreesC was only 0.78 log(10) cfu/ml of rehydrated suspension. TGYC was equal to PCAC and superior to the other four media in recovering yeasts stored at - 18 degreesC, 5 degreesC, or 25 degreesC for up to 42 weeks. Results from both the interlaboratory study and the storage study support the use of TGYC for enumerating desiccated yeasts. DG18 is not recommended as a general purpose medium for recovering yeasts from a desiccated condition.
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4.
  • Mates, L, et al. (författare)
  • Comparative analysis of the mouse and human genes (Matn2 and MATN2) for matrilin-2, a filament-forming protein widely distributed in extracellular matrices
  • 2002
  • Ingår i: Matrix Biology. - 1569-1802. ; 21:2, s. 163-174
  • Tidskriftsartikel (refereegranskat)abstract
    • We previously identified matrilin-2 (MATN2), the largest member of the novel family of matrilins. These filament-forming adapter proteins expressed in a distinct, but partially overlapping, pattern in all tissues were implicated in the organization of the extracellular matrix. Matrilin-2 functions in a great variety of tissues. Here, we present the genomic organization of the highly conserved mouse and human MATN2 loci, which cover > 100 kb and 167.167 kb genomic regions, respectively, and are composed of 19 exons. RT-PCR analysis revealed that alternative transcripts with identical protein coding regions are transcribed from two promoters in both species. The upstream, housekeeping type promoter is functional in all tissues and cell types tested. The activity of the downstream, TATA-like promoter preceded with putative motifs for the homeobox transcription factor PRRX2 is restricted to embryonic fibroblasts and certain cell lines. The oligomerization module is split by an U12-type AT-AC intron found in conserved position in all four matrilin genes. We assigned Matn2 to mouse chromosome 15, linked to Trhr and Sntb1 in a region synthenic to human chromosome 8q22-24.
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5.
  • Mates, L, et al. (författare)
  • Mice lacking the extracellular matrix adaptor protein matrilin-2 develop without obvious abnormalities
  • 2004
  • Ingår i: Matrix Biology. - : Elsevier BV. - 1569-1802 .- 0945-053X. ; 23:3, s. 195-204
  • Tidskriftsartikel (refereegranskat)abstract
    • Matrilins are putative adaptor proteins of the extracellular matrix (ECM) which can form both collagen-dependent and collagen-independent filamentous networks. While all known matrilins (matrilin-1, -2, -3, and -4) are expressed in cartilage, only matrilin-2 and matrilin-4 are abundant in non-skeletal tissues. To clarify the biological role of matrilin-2, we have developed a matrilin-2-deficient mouse strain. Matrilin-2 null mice show no gross abnormalities during embryonic or adult development, are fertile, and have a normal lifespan. Histological and ultrastructural analyses indicate apparently normal structure of all organs and tissues where matrilin-2 is expressed. Although matrilin-2 co-localizes with matrilin-4 in many tissues, Northern hybridization, semiquantitative RT-PCR, immunohistochemistry and biochemical analysis reveal no significant alteration in the steady-state level of matrilin-4 expression in homozygous mutant mice. Immunostaining of wild-type and mutant skin samples indicate no detectable differences in the expression and deposition of matrilin-2 binding partners including collagen I, laminin-nidogen complexes, fibrillin-2 and fibronectin. In addition, electron microscopy reveals an intact basement membrane at the epidermal-dermal junction and normal organization of the dermal collagen fibrils in mutant skin. These data suggest that either matrilin-2 and matrilin-2-mediated matrix-matrix interactions are dispensable for proper ECM assembly and function, or that they are efficiently compensated by other matrix components including wild-type levels of matrilin-4.
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