Detalhe da pesquisa
1.
Reversible cryo-arrest for imaging molecules in living cells at high spatial resolution.
Nat Methods
; 13(8): 665-672, 2016 08.
Artigo
em Inglês
| MEDLINE | ID: mdl-27400419
2.
Cytoplasmic relaxation of active Eph controls ephrin shedding by ADAM10.
PLoS Biol
; 7(10): e1000215, 2009 Oct.
Artigo
em Inglês
| MEDLINE | ID: mdl-19823572
3.
Contact inhibitory Eph signaling suppresses EGF-promoted cell migration by decoupling EGFR activity from vesicular recycling.
Sci Signal
; 11(541)2018 07 31.
Artigo
em Inglês
| MEDLINE | ID: mdl-30065026
4.
Correction: Subcellular Partitioning of Protein Tyrosine Phosphatase 1B to the Endoplasmic Reticulum and Mitochondria Depends Sensitively on the Composition of Its Tail Anchor.
PLoS One
; 11(4): e0154908, 2016.
Artigo
em Inglês
| MEDLINE | ID: mdl-27124743
5.
Ubiquitination switches EphA2 vesicular traffic from a continuous safeguard to a finite signalling mode.
Nat Commun
; 6: 8047, 2015 Aug 21.
Artigo
em Inglês
| MEDLINE | ID: mdl-26292967
6.
Subcellular Partitioning of Protein Tyrosine Phosphatase 1B to the Endoplasmic Reticulum and Mitochondria Depends Sensitively on the Composition of Its Tail Anchor.
PLoS One
; 10(10): e0139429, 2015.
Artigo
em Inglês
| MEDLINE | ID: mdl-26431424
7.
EGF-dependent re-routing of vesicular recycling switches spontaneous phosphorylation suppression to EGFR signaling.
Elife
; 42015 Nov 26.
Artigo
em Inglês
| MEDLINE | ID: mdl-26609808
8.
The composition of EphB2 clusters determines the strength in the cellular repulsion response.
J Cell Biol
; 204(3): 409-22, 2014 Feb 03.
Artigo
em Inglês
| MEDLINE | ID: mdl-24469634
9.
Regulation of signaling at regions of cell-cell contact by endoplasmic reticulum-bound protein-tyrosine phosphatase 1B.
PLoS One
; 7(5): e36633, 2012.
Artigo
em Inglês
| MEDLINE | ID: mdl-22655028
10.
Clasp-mediated microtubule bundling regulates persistent motility and contact repulsion in Drosophila macrophages in vivo.
J Cell Biol
; 189(4): 681-9, 2010 May 17.
Artigo
em Inglês
| MEDLINE | ID: mdl-20457764