Zobrazeno 1 - 10 of 31 pro vyhledávání: '"Pablo Christian Echeverria"'
1
Nucleocytoplasmic shuttling of the glucocorticoid receptor is influenced by tetratricopeptide repeat-containing proteins
Autor: Gisela Ileana Mazaira, Pablo Christian Echeverria, Mario D. Galigniana
Publikováno v: Journal of Cell Science, Vol. 133, No jcs238873 (2020) pp. 1-12
It has been demonstrated that tetratricopeptide repeats (TPR)-domain proteins regulate the subcellular localization of the glucocorticoid receptor (GR). This study analyses the influence of the TPR-domain of high molecular weight immunophilins in the
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33f5a003df37dfe323c8cad85d803205
https://archive-ouverte.unige.ch/unige:138332
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2
Vps11 and Vps18 of Vps-C membrane traffic complexes are E3 ubiquitin ligases and fine-tune signalling
Autor: Robert K. Maeda, Didier Picard, François Karch, Marcela A. Bennesch, Gregory Segala, Deo Prakash Pandey, Pablo Christian Echeverria, Nastaran Mohammadi Ghahhari
Publikováno v: Nature Communications, Vol 10, Iss 1, Pp 1-15 (2019)
Nature Communications, Vol. 10, No 1833 (2019)
Nature Communications
In response to extracellular signals, many signalling proteins associated with the plasma membrane are sorted into endosomes. This involves endosomal fusion, which depends on the complexes HOPS and CORVET. Whether and how their subunits themselves mo
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::14bfcfc9e289d1a088b52e15a7ebae0f
https://doi.org/10.1038/s41467-019-09800-y
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3
The Hsp70/Hsp90 Co-Chaperone Hop/Stip1 Shifts the Proteostatic Balance from Folding Towards Degradation
Autor: Didier Picard, S. G. D. Rüdiger, Lorenz Weidenauer, Kaushik Bhattacharya, Diana Wider, Christoph Ruediger Bauer, Lilia Bernasconi, Pablo Christian Echeverria, Manfredo Quadroni, M. Villemin, T. Moran Luengo
SUMMARYHop/Stip1/Sti1 is thought to be essential as a co-chaperone to facilitate substrate transfer between the Hsp70 and Hsp90 molecular chaperones. Despite this proposed key function for protein folding and maturation, it is not essential in a numb
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d38c20ca7fec2711578ee7976a6564f6
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4
Differential regulation of the glucocorticoid receptor nucleocytoplasmic shuttling by TPR-domain proteins
Autor: Martin Monte, Gisela Ileana Mazaira, Alejandra G. Erlejman, Luciana Gallo, Pablo Christian Echeverria, Mario D. Galigniana, Sol M. Ciucci
Publikováno v: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1868:119000
A dimer of the heat-shock protein of 90-kDa (Hsp90) represents the critical core of the chaperone complex associated to the glucocorticoid receptor (GR) oligomer. The C-terminal end of the Hsp90 dimer shapes a functional acceptor site for co-chaperon
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::331bcfaf39af3462c21134c7a32cadf6
https://doi.org/10.1016/j.bbamcr.2021.119000
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5
The sensitivity to Hsp90 inhibitors of both normal and oncogenically transformed cells is determined by the equilibrium between cellular quiescence and activity
Autor: Abhinav Joshi, Kaushik Bhattacharya, Tai Wang, Didier Picard, Pablo Christian Echeverria
Publikováno v: PLoS ONE
PLOS One, Vol. 14, No 2 (2019) P. e0208287
PLoS ONE, Vol 14, Iss 2, p e0208287 (2019)
The molecular chaperone Hsp90 is an essential and highly abundant central node in the interactome of eukaryotic cells. Many of its large number of client proteins are relevant to cancer. A hallmark of Hsp90-dependent proteins is that their accumulati
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::022bd10e8fceabcc305b8a71b4c67c03
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6
A remodeled Hsp90 molecular chaperone ensemble with the novel co-chaperone Aarsd1 is required for muscle differentiation
Autor: Pablo Christian Echeverria, Pierre André Briand, Didier Picard
Publikováno v: Molecular and Cellular Biology, Vol. 36 (2016) pp. 1310-1321
Hsp90 is the ATP-consuming core component of a very abundant molecular chaperone machine that handles a substantial portion of the cytosolic proteome. Rather than one machine, it is in fact an ensemble of molecular machines, since most mammalian cell
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::917e7d9c437c1c60ad675421a46e396d
https://archive-ouverte.unige.ch/unige:82275
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7
Unusual Suspects in the Twilight Zone Between the Hsp90 Interactome and Carcinogenesis
Autor: Evangelia Vartholomaiou, Didier Picard, Pablo Christian Echeverria
Publikováno v: Hsp90 in Cancer: Beyond the Usual Suspects pp. 1-30
Hsp90 in Cancer: Beyond the Usual Suspects
The molecular chaperone Hsp90 has attracted a lot of interest in cancer research ever since cancer cells were found to be more sensitive to Hsp90 inhibition than normal cells. Why that is has remained a matter of debate and is still unclear. In addit
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef381df73128f049e616335edace9e65
https://archive-ouverte.unige.ch/unige:81886
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8
RUNX1 and FOXP3 interplay regulates expression of breast cancer related genes
Autor: Johanna M. Tocci, Natalia Rubinstein, Esteban Grasso, Lucio H. Castilla, Luciana Rocha-Viegas, Edith C. Kordon, Pablo Christian Echeverria, María Sol Recouvreux, Carolina Schere-Levy
Publikováno v: Oncotarget, Vol. 7, No 6 (2015) pp. 6552-6565
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Oncotarget
Runx1 participation in epithelial mammary cells is still under review. Emerging data indicates that Runx1 could be relevant for breast tumor promotion. However, to date no studies have specifically evaluated the functional contribution of Runx1 to co
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::01a2c9d195bb84973fceed6816c48523
https://archive-ouverte.unige.ch/unige:81859
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10
Differential Subcellular Localization of Members of the Toxoplasma gondii Small Heat Shock Protein Family
Autor: Sergio O. Angel, Pablo Christian Echeverria, N. de Miguel
Publikováno v: Eukaryotic Cell. 4:1990-1997
The results of this study describe the identification and characterization of the Toxoplasma gondii α-crystallin/small heat shock protein (sHsp) family. By database ( www.toxodb.org ) search, five parasite sHsps (Hsp20, Hsp21, Hsp28, Hsp29, and the
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3ef379386762a4f2fb1a215b876e27d5
https://doi.org/10.1128/ec.4.12.1990-1997.2005
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