منابع مشابه
Session: 5A
ACOUSTIC WAVES MEASUREMENTS ON SNGS CRYSTALS AND DETERMINATION OF MATERIAL CONSTANTS E. CHILLA*1, R. KUNZE2, A. SOTNIKOV2, M. WEIHNACHT2, J. BOHM3, R. B. HEIMANN4, M. HENGST4, and U. STRAUBE5, 1VI Tele Filter GmbH, Teltow, Germany, 2Leibniz Institute for Solid State and Materials Research, Dresden, Germany, 3Institute for Crystal Growth, Berlin, Germany, 4Freiberg University of Mining and Techn...
متن کاملSession 5a: Acoustic Modeling
The session focused on acoustic modeling for speech recognition ; which can be segmented into three broad sub-areas: (1) feature extraction, (2) modeling the features for the speech source, and (3) estimation of the model parameters. The papers in this session touched on all of these areas. Huang focuses on the feature representation. Furui et al., Austin et al., and Kimbal et al. discuss new m...
متن کاملOral Session 03: CNS Risk
Exposure to space radiation may have impacts on brain function, either during or following missions. It is most important to determine how low doses of protons and high-LET irradiation elicit changes in brain function. Within this framework, the role of oxidative stress should also be assessed, as well as other possible interaction mechanisms involving, e.g., genetic, environmental, and sex-dep...
متن کاملInteraction of hHR23 with S5a. The ubiquitin-like domain of hHR23 mediates interaction with S5a subunit of 26 S proteasome.
hHR23B is one of two human homologs of the Saccharomyces cerevisiae nucleotide excision repair (NER) gene product RAD23 and a component of a protein complex that specifically complements the NER defect of xeroderma pigmentosum group C (XP-C) cell extracts in vitro. Although a small proportion of hHR23B is tightly complexed with the XP-C responsible gene product, XPC protein, a vast majority exi...
متن کاملDefining how ubiquitin receptors hHR23a and S5a bind polyubiquitin.
Ubiquitin receptors connect substrate ubiquitylation to proteasomal degradation. HHR23a binds proteasome subunit 5a (S5a) through a surface that also binds ubiquitin. We report that UIM2 of S5a binds preferentially to hHR23a over polyubiquitin, and we provide a model for the ternary complex that we expect represents one of the mechanisms used by the proteasome to capture ubiquitylated substrate...
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ژورنال
عنوان ژورنال: Plastic and Reconstructive Surgery - Global Open
سال: 2019
ISSN: 2169-7574
DOI: 10.1097/01.gox.0000583076.47468.d4