Zobrazeno 1 - 10
of 24
pro vyhledávání: '"Marta Marin-Argany"'
Autor:
Bahareh Eftekharzadeh, Varuna C. Banduseela, Giulio Chiesa, Paula Martínez-Cristóbal, Jennifer N. Rauch, Samir R. Nath, Daniel M. C. Schwarz, Hao Shao, Marta Marin-Argany, Claudio Di Sanza, Elisa Giorgetti, Zhigang Yu, Roberta Pierattelli, Isabella C. Felli, Isabelle Brun-Heath, Jesús García, Ángel R. Nebreda, Jason E. Gestwicki, Andrew P. Lieberman, Xavier Salvatella
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-14 (2019)
Hsp chaperones stabilize the inactive conformation of androgen receptor (AR) and are released upon hormone-induced AR activation. Here, the authors locate the Hsp binding region on AR, and show that Hsp70 reduces AR aggregation and promotes AR degrad
Externí odkaz:
https://doaj.org/article/6c6c515e273b446cb66da2f55b7b3d95
Autor:
Bahareh Eftekharzadeh, Varuna C. Banduseela, Giulio Chiesa, Paula Martínez-Cristóbal, Jennifer N. Rauch, Samir R. Nath, Daniel M. C. Schwarz, Hao Shao, Marta Marin-Argany, Claudio Di Sanza, Elisa Giorgetti, Zhigang Yu, Roberta Pierattelli, Isabella C. Felli, Isabelle Brun-Heath, Jesús García, Ángel R. Nebreda, Jason E. Gestwicki, Andrew P. Lieberman, Xavier Salvatella
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-1 (2019)
An amendment to this paper has been published and can be accessed via a link at the top of the paper.
Externí odkaz:
https://doaj.org/article/d1198cecc1114d42ba57e2c691ec211c
Publikováno v:
PLoS ONE, Vol 9, Iss 5, p e98124 (2014)
The modulation of binding affinities and specificities by post-translational modifications located out from the binding pocket of the third PDZ domain of PSD-95 (PDZ3) has been reported recently. It is achieved through an intra-domain electrostatic n
Externí odkaz:
https://doaj.org/article/97f4479b097c4efa96bddfa1219c7835
Autor:
David L. Murray, Christopher J. Ward, Angela Dispenzieri, Marta Marin-Argany, Surendra Dasari, Samih H. Nasr, Marina Ramirez-Alvarado, Nelson Leung, David R. Barnidge, Christopher J. Dick, Victor H Jimenez-Zepeda, Shawna A. Cooper
Publikováno v:
American Journal of Hematology. 92:536-541
Immunoglobulin light chain (AL) amyloidosis is a fatal complication of B-cell proliferation secondary to deposition of amyloid fibrils in various organs. Urinary exosomes (UEX) are the smallest of the microvesicles excreted in the urine. Previously,
Autor:
Isabella C. Felli, Jesús García, Roberta Pierattelli, Samir R. Nath, Paula Martínez-Cristóbal, Giulio Chiesa, Andrew P. Lieberman, Zhigang Yu, Xavier Salvatella, Daniel M. C. Schwarz, Claudio Di Sanza, Bahareh Eftekharzadeh, Jennifer N. Rauch, Elisa Giorgetti, Varuna C. Banduseela, Marta Marin-Argany, Isabelle Brun-Heath, Angel R. Nebreda, Jason E. Gestwicki, Hao Shao
Publikováno v:
Nature communications, vol 10, iss 1
Nature Communications, Vol 10, Iss 1, Pp 1-1 (2019)
Nature Communications
Nature Communications, Vol 10, Iss 1, Pp 1-1 (2019)
Nature Communications
Molecular chaperones such as Hsp40 and Hsp70 hold the androgen receptor (AR) in an inactive conformation. They are released in the presence of androgens, enabling transactivation and causing the receptor to become aggregation-prone. Here we show that
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1e3006d7de3e115a9649d8bf1c63fb04
https://escholarship.org/uc/item/1s17d7p6
https://escholarship.org/uc/item/1s17d7p6
Autor:
Marta Marin-Argany, Megan McClure, Marina Ramirez-Alvarado, Jonathan S. Wall, Laura R. Elsbernd, Yi Lin, Angela Williams, Kyle G. Howell, Pinaki Misra
Publikováno v:
Journal of Biological Chemistry. 291:19813-19825
Light chain (AL) amyloidosis is an incurable human disease characterized by the misfolding, aggregation, and systemic deposition of amyloid composed of immunoglobulin light chains (LC). This work describes our studies on potential mechanisms of AL cy
Autor:
Luis M. Blancas-Mejia, Marta Marin-Argany, Matthew Auton, Alexander Tischer, Marina Ramirez-Alvarado, Timothy J. Horn
Publikováno v:
Biophysical Chemistry. 207:13-20
Light chain (AL) amyloidosis is a fatal disease where monoclonal immunoglobulin light chains deposit as insoluble amyloid fibrils. For many years it has been considered that AL amyloid deposits are formed primarily by the variable domain, while its c
Autor:
Pinaki Misra, Marta Marin-Argany, Shawna A. Cooper, Keely R. Redhage, Christopher J. Dick, Luis M. Blancas-Mejia, Marina Ramirez-Alvarado
Publikováno v:
Methods in Molecular Biology ISBN: 9781493988198
Common biophysical techniques like absorption and fluorescence spectroscopy, microscopy, and light scattering studies have been in use to investigate fibril assembly for a long time. However, there is sometimes a lack of consensus from the findings o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7563d46898f5c5e073e3ab7da23f0dae
https://doi.org/10.1007/978-1-4939-8820-4_8
https://doi.org/10.1007/978-1-4939-8820-4_8
Autor:
Marta Marin-Argany, Jofre Güell-Bosch, Luis M. Blancas-Mejia, Sandra Villegas, Marina Ramirez-Alvarado
Publikováno v:
Protein Science. 24:1829-1840
Light chain (AL) amyloidosis is an incurable human disease, where the amyloid precursor is a misfolding-prone immunoglobulin light-chain. Here, we identify the role of somatic mutations in the structure, stability and in vitro fibril formation for an
Publikováno v:
Journal of Biological Chemistry. 290:4953-4965
Amyloid light chain (AL) amyloidosis is a protein misfolding disease where immunoglobulin light chains sample partially folded states that lead to misfolding and amyloid formation, resulting in organ dysfunction and death. In vivo, amyloid deposits a