Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Hue Anh Luu"'
Autor:
Charles F.B. Holmes, Barbara J. Ballermann, Marya Obeidat, Hue-Anh Luu, Laiji Li, Micheal J. Shopik
Publikováno v:
Biochemical and Biophysical Research Communications. 435:567-573
TIMAP is an endothelial-cell predominant member of the MYPT family of PP1c regulatory subunits. This study explored the TIMAP-PP1c interaction and substrate specificity in vitro. TIMAP associated with all three PP1c isoforms, but endogenous endotheli
Autor:
T. L. Mccready, Charles F.B. Holmes, Dudley H. Williams, Hue Anh Luu, Marcia Craig, Raymond J. Andersen
Publikováno v:
Biochemistry and Cell Biology. 74:569-578
Heptapeptide microcystin and pentapeptide motuporin (nodularin-V) are equipotent inhibitors of type-1 and type-2A protein phosphatase catalytic subunits (PP-1c and PP-2Ac). Herein we describe elucidation of the molecular mechanisms involved in the in
Autor:
Tamara D. Skene-Arnold, Jason T. Maynes, Michael N.G. James, Andrea Fong, Laura Trinkle-Mulcahy, R. Glen Uhrig, Hue Anh Luu, Greg B. G. Moorhead, Veerle De Wever, Charles F.B. Holmes, Mhairi Nimick
Publikováno v:
The Biochemical journal. 449(3)
The serine/threonine PP-1c (protein phosphatase-1 catalytic subunit) is regulated by association with multiple regulatory subunits. Human ASPPs (apoptosis-stimulating proteins of p53) comprise three family members: ASPP1, ASPP2 and iASPP (inhibitory
Publikováno v:
Current Genetics. 20:17-23
It has previously been shown that the yeast ubiquitin genes UBI1, 2 and 3 are strongly expressed during the log-phase of batch culture growth, whereas the UBI4 gene is weakly expressed. We found that heat shock, treatment with DNA-damaging agents, st
Autor:
Maia M. Cherney, Kathleen R. Perreault, Michael N.G. James, Jason T. Maynes, Hue Anh Luu, Charles F.B. Holmes
Publikováno v:
The Journal of biological chemistry. 279(41)
Protein phosphatase-1 and protein phosphatase-2B (calcineurin) are eukaryotic serine/threonine phosphatases that share 40% sequence identity in their catalytic subunits. Despite the similarities in sequence, these phosphatases are widely divergent wh
Autor:
Hue Anh Luu, Katherine S. Bateman, Amit Das, Charles F.B. Holmes, Maia M. Cherney, Michael N.G. James, Jason T. Maynes
Publikováno v:
The Journal of biological chemistry. 276(47)
Protein phosphatase-1 (PP1) plays a key role in dephosphorylation in numerous biological processes such as glycogen metabolism, cell cycle regulation, smooth muscle contraction, and protein synthesis. Microorganisms produce a variety of inhibitors of
Publikováno v:
Biochemical and biophysical research communications. 270(2)
The catalytic cores of PP-1c and PP-2B (calcineurin) are structurally conserved. However, PP-2B is resistant to inhibition by toxins of the okadaic acid and cyclic peptide classes, while PP-1c is potently inhibited. Molecular docking of the structure
Autor:
M. O’Connor-McCourt, J. Magoon, H. Klix, Hue Anh Luu, Charles F.B. Holmes, Marion P. Boland, K. Wang, Marcia Craig, Raymond J. Andersen, T. L. Mccready, Dawn Z.X. Chen, J. F. Dawson
Publikováno v:
Peptides ISBN: 9789401042956
Peptides
Peptides
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::da6270dbdd9248e78aa0e391a912dda1
https://doi.org/10.1007/978-94-011-0683-2_190
https://doi.org/10.1007/978-94-011-0683-2_190
Liquid chromatography (LC)-linked protein phosphatase 1/2A (PP-1/PP2A) bioassay was used to quantitatively identify diarrhetic shellfish toxins in marine phytoplankton (cultured and natural assemblages) and commercially available mussels. Using this
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ebc2f7502148d56583164c51d1cd5451
https://doi.org/10.1016/0041-0101(93)90359-q
https://doi.org/10.1016/0041-0101(93)90359-q
Autor:
Hue Anh Luu, Jack A. Kornblatt
Publikováno v:
European journal of biochemistry. 159(2)
Cytochrome c oxidase forms tight binding complexes with the cytochrome c analog, porphyrin cytochrome c. The behaviour of the reduced and pulsed forms of the oxidase with porphyrin cytochrome c have been followed as functions of ionic strength; this