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Vania M.M. Braga

Researcher at National Institutes of Health

Publications -  69
Citations -  10537

Vania M.M. Braga is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Cadherin & Cell adhesion. The author has an hindex of 35, co-authored 67 publications receiving 9826 citations. Previous affiliations of Vania M.M. Braga include Universidade Federal de Minas Gerais & Federal University of Rio de Janeiro.

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Journal ArticleDOI

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.
Journal ArticleDOI

The Small GTPases Rho and Rac Are Required for the Establishment of Cadherin-dependent Cell–Cell Contacts

TL;DR: The data showed that the concerted action of Rho and Rac modulate the establishment of cadherin adhesion: a constitutively active form of Rac was not sufficient to stabilize cadherindependent cell–cell contacts when endogenous Rho was inhibited.
Journal ArticleDOI

Cell-cell adhesion and signalling.

TL;DR: Signalling pathways activated by Rho small GTPases have recently been identified that coordinate junction assembly, stability and function, as well as interactions of adhesive complexes with the underlying cortical cytoskeleton, which points to a more integrated view of signalling processes.
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Regulation of Cadherin Function by Rho and Rac: Modulation by Junction Maturation and Cellular Context

TL;DR: The results suggest that the same stimuli may have different activity in regulating the paracellular activity in endothelial and epithelial cells, and uncovered possible roles for the small GTPases during the establishment of E-cadherin-dependent contacts.
Journal ArticleDOI

Rap1 Regulates the Formation of E-Cadherin-Based Cell-Cell Contacts

TL;DR: It is reported here that the cytoplasmic domain of E-cadherin interacts with C3G, a guanine nucleotide exchange factor for Rap1, and suggested that Cdc42 functions downstream of Rap1 in this process.