Zobrazeno 1 - 7
of 7
pro vyhledávání: '"M. Christine Bruce"'
Autor:
M Christine Bruce, Steven Weger, Pratima Basak, Afshin Raouf, Leigh C. Murphy, Sumanta Chatterjee
Publikováno v:
Endocrine-Related Cancer
Although the role of estrogen signaling in breast cancer development has been extensively studied, the mechanisms that regulate the indispensable role of estrogen in normal mammary gland development have not been well studied. Because of the unavaila
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5f51575526bbf9e4f59c60e88742999d
https://doi.org/10.1530/erc-15-0105
https://doi.org/10.1530/erc-15-0105
Publikováno v:
Endocrine Related Cancer. 21:R357-R370
Estrogen receptor alpha (ERα) regulates and is regulated by kinases involved in several functions associated with the hallmarks of cancer. The following literature review strongly suggests that distinct kinomes exist for ERα-positive and -negative
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::613c48c52fb104209c7efbd0cacef023
https://doi.org/10.1530/erc-14-0232
https://doi.org/10.1530/erc-14-0232
Publikováno v:
The Journal of Cell Biology
LAPTM5 is a lysosomal transmembrane protein expressed in immune cells. We show that LAPTM5 binds the ubiquitin-ligase Nedd4 and GGA3 to promote LAPTM5 sorting from the Golgi to the lysosome, an event that is independent of LAPTM5 ubiquitination. LAPT
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::386c7ae7659adb2497723243bec1b87a
https://doi.org/10.1083/jcb.200603001
https://doi.org/10.1083/jcb.200603001
Publikováno v:
Structure. 14:543-553
SummaryInteractions between the WW domains of Drosophila Nedd4 (dNedd4) and Commissureless (Comm) PY motifs promote axon crossing at the CNS midline and muscle synaptogenesis. Here we report the solution structure of the dNedd4 WW3∗ domain complexe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0254a8b5cc8352644307eb9b14ea815b
https://doi.org/10.1016/j.str.2005.11.018
https://doi.org/10.1016/j.str.2005.11.018
Autor:
Marion Berenguer, Andrey A. Gurtovenko, Jinzhong Zhang, Yannick Le Marchand-Brustel, Laurène Martinez, Roland Govers, Teresa Gonzalez, Tao Xu, M. Christine Bruce
Publikováno v:
Biochimie
Biochimie, Elsevier, 2011, 93 (4), pp.697-709. ⟨10.1016/j.biochi.2010.12.013⟩
Biochimie, Elsevier, 2011, 93 (4), pp.697-709
Biochimie, 2011, 93 (4), pp.697-709. ⟨10.1016/j.biochi.2010.12.013⟩
Biochimie, Elsevier, 2011, 93 (4), pp.697-709. ⟨10.1016/j.biochi.2010.12.013⟩
Biochimie, Elsevier, 2011, 93 (4), pp.697-709
Biochimie, 2011, 93 (4), pp.697-709. ⟨10.1016/j.biochi.2010.12.013⟩
International audience; Insulin increases muscle and fat cell glucose uptake by inducing the translocation of glucose transporter GLUT4 from intracellular compartments to the plasma membrane. Here, we have demonstrated that in 3T3-L1 adipocytes, DMSO
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fb64590c601571698cf87e2d6f2dd773
https://hal.archives-ouvertes.fr/hal-01478348
https://hal.archives-ouvertes.fr/hal-01478348
Autor:
Yannick Le Marchand-Brustel, Roland Govers, Laurène Martinez, Marion Berenguer, M. Christine Bruce
Publikováno v:
Biochemical Pharmacology
Biochemical Pharmacology, Elsevier, 2010, 79 (9), pp.1300-1309. ⟨10.1016/j.bcp.2009.12.013⟩
Biochemical Pharmacology, 2010, 79 (9), pp.1300-1309. ⟨10.1016/j.bcp.2009.12.013⟩
Biochemical Pharmacology, Elsevier, 2010, 79 (9), pp.1300-1309. ⟨10.1016/j.bcp.2009.12.013⟩
Biochemical Pharmacology, 2010, 79 (9), pp.1300-1309. ⟨10.1016/j.bcp.2009.12.013⟩
Insulin induces a translocation of the glucose transporter GLUT4 from intracellular storage compartments towards the cell surface in adipocytes and skeletal muscle cells, allowing the cells to take up glucose. In type 2 diabetes-associated insulin re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e0e842cec047a88c38181dd96a54a7e3
https://hal.archives-ouvertes.fr/hal-01478364
https://hal.archives-ouvertes.fr/hal-01478364
Autor:
Bruno Gavillet, Olivier Staub, M. Christine Bruce, Florine Apothéloz, Thomas Jespersen, Sophie Cordonier, Hugues Abriel, Jean-Sébastien Rougier, Daniela Rotin, Miguel X. van Bemmelen
Publikováno v:
American journal of physiology. Cell physiology. 288(3)
The voltage-gated Na+ channels (Nav) form a family composed of 10 genes. The COOH termini of Nav contain a cluster of amino acids that are nearly identical among 7 of the 10 members. This COOH-terminal sequence, PPSYDSV, is a PY motif known to bind t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7be3362118ff2984b8994ae9581493f6
https://pubmed.ncbi.nlm.nih.gov/15548568
https://pubmed.ncbi.nlm.nih.gov/15548568