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Alejandro Holgado-Rodriguez de,Alberto Izquierdo-Fernandez,Jesus Manuel Mendez-Sanchez,Jose Carlos Diaz-Minarro 대한견주관절의학회 2022 대한견주관절의학회지 Vol.25 No.3
The objective of this article is to describe intraoperative pulmonary embolism during shoulder arthroscopy in a patient with previous severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection. Further, we describe how the pandemic has influenced the population by increasing the rate of embolisms. Awareness of such cases will help to increase knowledge regarding SARS-Cov-2 and to determine if such patients should receive routine antithrombotic prophylaxis.
Refined topology model of the STT3/Stt3 protein subunit of the oligosaccharyltransferase complex
Lara, Patricia,Ojemalm, Karin,Reithinger, Johannes,Holgado, Aurora,Maojun, You,Hammed, Abdessalem,Mattle, Daniel,Kim, Hyun,Nilsson, IngMarie American Society for Biochemistry and Molecular Bi 2017 The Journal of biological chemistry Vol.292 No.27
<P>The oligosaccharyltransferase complex, localized in the endoplasmic reticulum (ER) of eukaryotic cells, is responsible for the N-linked glycosylation of numerous protein substrates. The membrane protein STT3 is a highly conserved part of the oligosaccharyltransferase and likely contains the active site of the complex. However, understanding the catalytic determinants of this system has been challenging, in part because of a discrepancy in the structural topology of the bacterial versus eukaryotic proteins and incomplete information about the mechanism of membrane integration. Here, we use a glycosylation mapping approach to investigate these questions. We measured the membrane integration efficiency of the mouse STT3-A and yeast Stt3p transmembrane domains (TMDs) and report a refined topology of the N-terminal half of the mouse STT3-A. Our results show that most of the STT3 TMDs are well inserted into the ER membrane on their own or in the presence of the natural flanking residues. However, for the mouse STT3-A hydrophobic domains 4 and 6 and yeast Stt3p domains 2, 3a, 3c, and 6 we measured reduced insertion efficiency into the ER membrane. Furthermore, we mapped the first half of the STT3-A protein, finding two extra hydrophobic domains between the third and the fourthTMD. This result indicates that the eukaryotic STT3 has 13 transmembrane domains, consistent with the structure of the bacterial homolog of STT3 and setting the stage for future combined efforts to interrogate this fascinating system.</P>
PROPAGATION OF NUCLEAR DATA UNCERTAINTIES FOR PWR CORE ANALYSIS
Cabellos, O.,Castro, E.,Ahnert, C.,Holgado, C. Korean Nuclear Society 2014 Nuclear Engineering and Technology Vol.46 No.3
An uncertainty propagation methodology based on the Monte Carlo method is applied to PWR nuclear design analysis to assess the impact of nuclear data uncertainties. The importance of the nuclear data uncertainties for $^{235,238}U$, $^{239}Pu$, and the thermal scattering library for hydrogen in water is analyzed. This uncertainty analysis is compared with the design and acceptance criteria to assure the adequacy of bounding estimates in safety margins.
Propagation of Nuclear Data Uncertainties for PWR Core Analysis
O. CABELLOS,E. CASTRO,C. AHNERT,C. HOLGADO 한국원자력학회 2014 Nuclear Engineering and Technology Vol.46 No.3
An uncertainty propagation methodology based on the Monte Carlo method is applied to PWR nuclear design analysis toassess the impact of nuclear data uncertainties. The importance of the nuclear data uncertainties for 235,238U, 239Pu, and thethermal scattering library for hydrogen in water is analyzed. This uncertainty analysis is compared with the design andacceptance criteria to assure the adequacy of bounding estimates in safety margins.