Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Liane M. Mende-Mueller"'
Autor:
Thomas Toneff, Richard A. Bundey, Marie-Françoise Chesselet, Liane M. Mende-Mueller, Vivian Hook, Leslie M. Thompson, Ying Wu, Shin-Rong Hwang
Publikováno v:
Journal of Neurochemistry. 82:84-92
Proteolytic fragments of huntingtin (htt) in human lymphoblast cell lines from HD and control cases were compared to those in human HD striatal and cortical brain regions, by western blots with epitope-specific antibodies. HD lymphoblast cell lines w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ec67fb634fa846c5089e95139e865962
https://doi.org/10.1046/j.1471-4159.2002.00940.x
https://doi.org/10.1046/j.1471-4159.2002.00940.x
Autor:
Vivian Hook, Liane M. Mende-Mueller, Marie-Françoise Chesselet, Thomas Toneff, Shin-Rong Hwang
Publikováno v:
The Journal of Neuroscience. 21:1830-1837
Proteolysis of mutant huntingtin (htt) has been hypothesized to occur in Huntington's disease (HD) brains. Therefore, this in vivo study examined htt fragments in cortex and striatum of adult HD and control human brains by Western blots, using domain
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::37aac495c7578189981d9e91b66762e2
https://doi.org/10.1523/jneurosci.21-06-01830.2001
https://doi.org/10.1523/jneurosci.21-06-01830.2001
Autor:
Anthony A. Paiva, Lee Huang, Liane M. Mende-Mueller, Ravi Kambampati, Carla B. Pellegrino, Kalpana Chakraburtty
Publikováno v:
Journal of Biological Chemistry. 275:16963-16968
Elongation factor 3 (EF-3) is an ATPase essential for polypeptide chain synthesis in a variety of yeasts and fungi. We used limited proteolysis to study the organization of the subdomains of EF-3. Trypsinolysis of EF-3 at 30 °C resulted in the forma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3b545b71e2c96cb333f953976b144e77
https://doi.org/10.1074/jbc.m001157200
https://doi.org/10.1074/jbc.m001157200
Publikováno v:
Journal of Bacteriology. 179:7165-7168
Extracellular protein profiles from wild-type and regulatory or secretory isogenic mutants of the Pseudomonas aeruginosa exoenzyme S regulon were compared to identify proteins coordinately secreted with ExoS. Data from amino-terminal sequence analysi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6bc1d0042cd61121bafc349e46dda656
https://doi.org/10.1128/jb.179.22.7165-7168.1997
https://doi.org/10.1128/jb.179.22.7165-7168.1997
Autor:
Liane M. Mende-Mueller, Jeanine P. Wiener-Kronish, Lei Zhu, Christine Wu, Suzanne M. J. Fleiszig, Dara W. Frank, Joanne Goranson, Viviane Finck-Barbançon, Teiji Sawa
Publikováno v:
Scopus-Elsevier
The production of exoenzyme S is correlated with the ability of Pseudomonas aeruginosa to disseminate from epithelial colonization sites and cause a fatal sepsis in burn injury and acute lung infection models. Exoenzyme S is purified from culture sup
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8d7000c6c4736cffbca9842bdffb74f9
https://doi.org/10.1046/j.1365-2958.1997.4891851.x
https://doi.org/10.1046/j.1365-2958.1997.4891851.x
Publikováno v:
FEBS Letters. 382:6-10
The preference of the ‘prohormone thiol protease’ (PTP), a candidate prohormone processing enzyme, for different peptide precursors was assessed in vitro with recombinant prohormones near estimated in vivo levels. Pro-neuropeptide Y (pro-NPY), pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b09311bef79926f934158add8145ccf8
https://doi.org/10.1016/0014-5793(96)00083-x
https://doi.org/10.1016/0014-5793(96)00083-x
Autor:
Vivian Hook, Stephen C. Noctor, Liane M. Mende-Mueller, Rama Kannan, Timothy J. Krieger, Nikolaos Tezapsidis
Publikováno v:
Journal of Biological Chemistry. 270:13285-13290
Proenkephalin and other prohormones require proteolytic processing at paired basic and monobasic residues for the biosynthesis of active neuropeptides. The novel “prohormone thiol protease” (PTP) has been proposed as a candidate proenkephalin pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::27e197633294188355910ee6617b9be6
https://doi.org/10.1074/jbc.270.22.13285
https://doi.org/10.1074/jbc.270.22.13285
Publikováno v:
Journal of Biological Chemistry. 269:10431-10437
We report the purification and proteolytic characterization of the 49-kDa form of exoenzyme S and the cloning of the structural gene for the 49-kDa form of exoenzyme S (exoS). The 49-kDa form of exoenzyme S was purified from SDS-polyacrylamide gels.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7f7e18b9cba3b55c7a04a90d5e8b25f5
https://doi.org/10.1016/s0021-9258(17)34078-4
https://doi.org/10.1016/s0021-9258(17)34078-4
Publikováno v:
Journal of Biological Chemistry. 266:8122-8128
Trypsin digestion of pertussis toxin (PT) preferentially cleaved the S1 subunit at Arg-218 without detectable degradation of the B oligomer. The fragment produced, termed the tryptic S1 fragment, appears to remain associated with the B oligomer. Chym
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ccaecf667f746ead69dabbca20d0e217
https://doi.org/10.1016/s0021-9258(18)92950-9
https://doi.org/10.1016/s0021-9258(18)92950-9
Publikováno v:
Archives of Biochemistry and Biophysics. 283:523-529
Full length cDNA (1.85 kb) coding for an avian liver 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA) synthase has been isolated and sequenced. The cDNA isolation relied on hybridization to a 32P-labeled oligonucleotide coding for a portion of the active sit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8a6929d2895cd2efc9312af34bda31fd
https://doi.org/10.1016/0003-9861(90)90677-q
https://doi.org/10.1016/0003-9861(90)90677-q