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Jose Luis Rosa

Researcher at University of Barcelona

Publications -  122
Citations -  11114

Jose Luis Rosa is an academic researcher from University of Barcelona. The author has contributed to research in topics: Ubiquitin ligase & Transcription factor. The author has an hindex of 41, co-authored 117 publications receiving 9976 citations. Previous affiliations of Jose Luis Rosa include Bristol-Myers Squibb.

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Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)

Daniel J. Klionsky, +2522 more
- 21 Jan 2016 - 
TL;DR: In this paper, the authors present a set of guidelines for the selection and interpretation of methods for use by investigators who aim to examine macro-autophagy and related processes, as well as for reviewers who need to provide realistic and reasonable critiques of papers that are focused on these processes.
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Direct binding of Smad1 and Smad4 to two distinct motifs mediates bone morphogenetic protein-specific transcriptional activation of Id1 gene.

Teresa López-Rovira, +4 more
- 01 Feb 2002 - 
TL;DR: The simultaneous requirement of two independent DNA binding elements to allow functional cooperativity of B MP-regulated Smads and Smad4 in BMP-activated gene promoters is suggested.
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Phosphorylation‐dependent and constitutive activation of Rho proteins by wild‐type and oncogenic Vav‐2

Kornel E. Schuebel, +3 more
- 16 Nov 1998 - 
TL;DR: Vav‐2, a member of the Vav family of oncoproteins, acts as a guanosine nucleotide exchange factor (GEF) for RhoG and RhoA‐like GTPases in a phosphotyrosine‐dependent manner and is identified as a regulated GEF for the RHoA subfamily.
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6-Phosphofructo-2-kinase (pfkfb3) gene promoter contains hypoxia-inducible factor-1 binding sites necessary for transactivation in response to hypoxia

Mercè Obach, +9 more
- 17 Dec 2004 - 
TL;DR: It is demonstrated that pfkfb3 is a hypoxia-inducible gene that is stimulated through HIF interaction with the consensus HRE site in its promoter region, and that HIF-1 protein was critically involved for hypoxic transactivation of this gene.
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TSC1 stabilizes TSC2 by inhibiting the interaction between TSC2 and the HERC1 ubiquitin ligase.

Huira Chong-Kopera, +6 more
- 31 Mar 2006 - 
TL;DR: A potential molecular mechanism of how TSC1 stabilizes TSC2 by excluding the HERC1 ubiquitin ligase from the T SC2 complex is revealed and a possible biochemical basis of how certain disease mutations inactivate TSC 2 is revealed.