Zobrazeno 1 - 10
of 44
pro vyhledávání: '"Margarida Gairí"'
Autor:
João M. C. Teixeira, Héctor Fuentes, Stasė Bielskutė, Margarida Gairi, Szymon Żerko, Wiktor Koźmiński, Miquel Pons
Publikováno v:
Molecules, Vol 23, Iss 11, p 2731 (2018)
The function of the intrinsically disordered Unique domain of the Src family of tyrosine kinases (SFK), where the largest differences between family members are concentrated, remains poorly understood. Recent studies in c-Src have demonstrated that t
Externí odkaz:
https://doaj.org/article/4b9a952b4a5440e49cc28c86ab8ed240
Autor:
Andras Lang, Alejandro Fernández, Mireia Diaz-Lobo, Mar Vilanova, Francisco Cárdenas, Margarida Gairí, Miquel Pons
Publikováno v:
Molecules, Vol 28, Iss 12, p 4686 (2023)
In contrast to the well-studied canonical regulatory mechanisms, the way by which the recently discovered Src N-terminal regulatory element (SNRE) modulates Src activity is not yet well understood. Phosphorylation of serine and threonine residues mod
Externí odkaz:
https://doaj.org/article/c4336f8608b841058599b6a0e1369ca8
Autor:
Albert Escobedo, Busra Topal, Micha B. A. Kunze, Juan Aranda, Giulio Chiesa, Daniele Mungianu, Ganeko Bernardo-Seisdedos, Bahareh Eftekharzadeh, Margarida Gairí, Roberta Pierattelli, Isabella C. Felli, Tammo Diercks, Oscar Millet, Jesús García, Modesto Orozco, Ramon Crehuet, Kresten Lindorff-Larsen, Xavier Salvatella
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-11 (2019)
Polyglutamine (polyQ) tracts are low-complexity regions and their expansion is linked to certain neurodegenerative diseases. Here the authors combine experimental and computational approaches to find that the length of the androgen receptor polyQ tra
Externí odkaz:
https://doaj.org/article/1f190bc76aba4d9fb248940a644fa9a9
Autor:
Anabel-Lise Le Roux, Irrem-Laareb Mohammad, Borja Mateos, Miguel Arbesú, Margarida Gairí, Farman Ali Khan, João M.C. Teixeira, Miquel Pons
Publikováno v:
iScience, Vol 12, Iss , Pp 194-203 (2019)
Summary: The c-Src oncogene is anchored to the cytoplasmic membrane through its N-terminal myristoylated SH4 domain. This domain is part of an intramolecular fuzzy complex with the SH3 and Unique domains. Here we show that the N-terminal myristoyl gr
Externí odkaz:
https://doaj.org/article/1c963853cb6c4b0ba24b5f945472944a
Autor:
Pons, Andras Lang, Alejandro Fernández, Mireia Diaz-Lobo, Mar Vilanova, Francisco Cárdenas, Margarida Gairí, Miquel
Publikováno v:
Molecules; Volume 28; Issue 12; Pages: 4686
In contrast to the well-studied canonical regulatory mechanisms, the way by which the recently discovered Src N-terminal regulatory element (SNRE) modulates Src activity is not yet well understood. Phosphorylation of serine and threonine residues mod
Autor:
Miguel Arbesú, Borja Mateos, João M.C. Teixeira, Miquel Pons, Margarida Gairí, Irrem-Laareb Mohammad, Farman Ali Khan, Anabel-Lise Le Roux
Publikováno v:
Dipòsit Digital de la UB
Universidad de Barcelona
iScience, Vol 12, Iss, Pp 194-203 (2019)
iScience
Universidad de Barcelona
iScience, Vol 12, Iss, Pp 194-203 (2019)
iScience
Summary The c-Src oncogene is anchored to the cytoplasmic membrane through its N-terminal myristoylated SH4 domain. This domain is part of an intramolecular fuzzy complex with the SH3 and Unique domains. Here we show that the N-terminal myristoyl gro
Autor:
Kresten Lindorff-Larsen, Juan Aranda, Jesús T. García, Ganeko Bernardo-Seisdedos, Giulio Chiesa, Ramon Crehuet, Oscar Millet, Margarida Gairí, Micha B. A. Kunze, Busra Topal, Xavier Salvatella, Daniele Mungianu, Albert Escobedo, Bahareh Eftekharzadeh, Roberta Pierattelli, Isabella C. Felli, Tammo Diercks, Modesto Orozco
Publikováno v:
Nature Communications
Digital.CSIC. Repositorio Institucional del CSIC
instname
Nature Communications, Vol 10, Iss 1, Pp 1-11 (2019)
Escobedo, A, Topal, B, Kunze, M B A, Aranda, J, Chiesa, G, Mungianu, D, Bernardo-Seisdedos, G, Eftekharzadeh, B, Gairí, M, Pierattelli, R, Felli, I C, Diercks, T, Millet, O, García, J, Orozco, M, Crehuet, R, Lindorff-Larsen, K & Salvatella, X 2019, ' Side chain to main chain hydrogen bonds stabilize a polyglutamine helix in a transcription factor ', Nature Communications, vol. 10, 2034 . https://doi.org/10.1038/s41467-019-09923-2
Digital.CSIC. Repositorio Institucional del CSIC
instname
Nature Communications, Vol 10, Iss 1, Pp 1-11 (2019)
Escobedo, A, Topal, B, Kunze, M B A, Aranda, J, Chiesa, G, Mungianu, D, Bernardo-Seisdedos, G, Eftekharzadeh, B, Gairí, M, Pierattelli, R, Felli, I C, Diercks, T, Millet, O, García, J, Orozco, M, Crehuet, R, Lindorff-Larsen, K & Salvatella, X 2019, ' Side chain to main chain hydrogen bonds stabilize a polyglutamine helix in a transcription factor ', Nature Communications, vol. 10, 2034 . https://doi.org/10.1038/s41467-019-09923-2
Polyglutamine (polyQ) tracts are regions of low sequence complexity frequently found in transcription factors. Tract length often correlates with transcriptional activity and expansion beyond specific thresholds in certain human proteins is the cause
Autor:
Victor Guallar, Abraham Lopez, Oscar Millet, Fátima Herranz-Trillo, Pau Bernadó, Ernest Giralt, Margarida Gairí, Teresa Tarragó, Martin Kotev
Publikováno v:
Recercat. Dipósit de la Recerca de Catalunya
instname
Dipòsit Digital de la UB
Universidad de Barcelona
UPCommons. Portal del coneixement obert de la UPC
Universitat Politècnica de Catalunya (UPC)
instname
Dipòsit Digital de la UB
Universidad de Barcelona
UPCommons. Portal del coneixement obert de la UPC
Universitat Politècnica de Catalunya (UPC)
Deciphering conformational dynamics is crucial for understanding the biological functions of proteins and for designing compounds targeting them. In particular, providing an accurate description of microsecond–millisecond motions opens the opportun
Autor:
Oscar Millet, Giulio Chiesa, Busra Topal, Jesús García, Roberta Pierattelli, Tammo Diercks, Micha B. A. Kunze, Isabella C. Felli, Juan Aranda, Xavier Salvatella, Daniele Mungianu, Modesto Orozco, Bahareh Eftekharzadeh, Margarida Gairí, Ramon Crehuet, Kresten Lindorff-Larsen, Ganeko Bernardo-Seisdedos, Albert Escobedo
Polyglutamine (polyQ) tracts are regions of low sequence complexity of variable length found in more than one hundred human proteins. These tracts are frequent in activation domains of transcription factors and their length often correlates with tran
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f0cd28275f996d7110ef2696a9179794
https://doi.org/10.1101/447896
https://doi.org/10.1101/447896
Autor:
Montserrat, Serra-Batiste, Martí, Ninot-Pedrosa, Eduard, Puig, Sonia, Ciudad, Margarida, Gairí, Natàlia, Carulla
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1779
The formation of amyloid-β peptide (Aβ) oligomers at the cellular membrane is considered a crucial process that underlies neurotoxicity in Alzheimer's disease (AD). To obtain structural information on this type of oligomers, we were inspired by mem