Výsledky vyhledávání

Determination of Key Parameters for a Mechanism-Based Model to Predict Doxorubicin Release from Actively Loaded Liposomes

Autor: Tian-Xiang Xiang, Bradley D. Anderson, Paul M. Bummer, Sogol Kangarlou, Eva Csuhai, Duhyung Choi, Andrei Ponta

Publikováno v: Journal of Pharmaceutical Sciences. 104:1087-1098

Despite extensive study of liposomal drug formulations, reliable predictive models of release kinetics in vitro and in vivo are still lacking. Progress in the development of robust, predictive release models has been hindered by a lack of systematic,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3229c1d00a53ec68a57398a0a92fe47b
https://doi.org/10.1002/jps.24307

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Design, selection, and characterization of a split chorismate mutase

Autor: Peter Kast, Manuel M. Müller, Donald Hilvert, Eva Csuhai, Hajo Kries

Publikováno v: Protein Science. 19:1000-1010

Split proteins are versatile tools for detecting protein–protein interactions and studying protein folding. Here, we report a new, particularly small split enzyme, engineered from a thermostable chorismate mutase (CM). Upon dissecting the helical-b

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::ef444885c44f42c0bc4476278e37d80b
https://doi.org/10.1002/pro.377

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Design, selection, and characterization of a split chorismate mutase

Autor: Manuel M, Müller, Hajo, Kries, Eva, Csuhai, Peter, Kast, Donald, Hilvert

Publikováno v: Protein Science

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::59d0fffb37bb7b89ad2de0c4e5278af6

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The use of proteolysis to study the structure of nardilysin

Autor: K. Martin Chow, Zhangliang Ma, Louis B. Hersh, Eva Csuhai

Publikováno v: Archives of Biochemistry and Biophysics. 401:198-204

Treatment of a 128 kDa mouse nardilysin with trypsin initially produced an active 105 kDa N-terminally cleaved form. Continued trypsin digestion occurred at the C-terminus, producing inactive core species of approximately 92, 76.5, and 62 kDa. Protea

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b95910d64884c0eec02fbd5612217710
https://doi.org/10.1016/s0003-9861(02)00020-6

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Kinetic Analysis of Spermine Binding to NRD Convertase

Autor: Maria A. Juliano, Eva Csuhai, Louis B. Hersh, Luiz Juliano

Publikováno v: Archives of Biochemistry and Biophysics. 362:291-300

N-arginine dibasic convertase cleaves polypeptides between paired basic residues containing the sequence Arg-Arg or Arg-Lys. The enzyme contains a large anionic domain, which in the rat enzyme consists of 57 acidic residues out of a stretch of 76 ami

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d8b4a41e8f539fad6e909ac6c57ab6ea
https://doi.org/10.1006/abbi.1998.1029

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Regulation of N-Arginine Dibasic Convertase Activity by Amines: Putative Role of a Novel Acidic Domain as an Amine Binding Site

Autor: Guojin Chen, Louis B. Hersh, Eva Csuhai

Publikováno v: Biochemistry. 37:3787-3794

Peptide sequence analysis and cDNA cloning indicate that a previously described mouse arginine-specific dibasic cleaving enzyme (dynorphin converting enzyme) [Csuhai et al. (1995) Biochemistry 34, 12411] is the homologue of N-arginine dibasic convert

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e02406e19e1cd954d6118c68cd06ef92
https://doi.org/10.1021/bi971969b

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