Asymmetric Nodal expression in the mouse is governed by the combinatorial activities of two distinct regulatory elements

Autor: J. Ann Le Good, Elizabeth J. Robertson, Daniel B. Constam, Dominic P. Norris, Stéphane D. Vincent

Publikováno v: Mechanisms of Development
Mechanisms of Development, Elsevier, 2004, 121 (11), pp.1403-1415. ⟨10.1016/j.mod.2004.06.002⟩

International audience; In all vertebrates, invariant left/right (L/R) positioning and organization of the internal viscera is controlled by a conserved pathway. Nodal, a member of the TGFbeta superfamily is a critical upstream component responsible

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2973c3517a5ea8cd37f578bfc543f5f5
https://doi.org/10.1016/j.mod.2004.06.002

High-Affinity Transport of Choline- O -Sulfate and Its Use as a Compatible Solute in Bacillus subtilis

Autor: J. Ann Le Good, Erhard Bremer, Gabriele Nau-Wagner, Jens Boch

Publikováno v: Applied and Environmental Microbiology. 65:560-568

We report here that the naturally occurring choline ester choline- O -sulfate serves as an effective compatible solute for Bacillus subtilis , and we have identified a high-affinity ATP-binding cassette (ABC) transport system responsible for its upta

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::786789c261d987fb25668b4584a0f6e8
https://doi.org/10.1128/aem.65.2.560-568.1999

Molecular mechanisms regulating protein kinase Czeta turnover and cellular transformation

Autor: David N. Brindley, J. Ann Le Good

Publikováno v: The Biochemical journal. 378(Pt 1)

The regulation of protein kinase C (PKC)zeta in relation to its turnover, cell growth and transformation was investigated in Rat2 fibroblasts by over-expressing wild-type or mutant forms of PKCzeta. Deletion of the pseudosubstrate site (PSS) produced

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::79a09fa36d274de9c3ea6a303186dce8
https://pubmed.ncbi.nlm.nih.gov/14580237

Activation of PRK1 by phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate. A comparison with protein kinase C isotypes

Autor: R H, Palmer, L V, Dekker, R, Woscholski, J A, Le Good, R, Gigg, P J, Parker

Publikováno v: The Journal of biological chemistry. 270(38)

As potential targets for polyphosphoinositides, activation of protein kinase C (PKC) isotypes (beta 1, epsilon, zeta, nu) and a member of the PKC-related kinase (PRK) family, PRK1, has been compared in vitro. PRK1 is shown to be activated by both pho

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::35aa863b05dc9c963b18c91bd12be833
https://pubmed.ncbi.nlm.nih.gov/7673228

Cripto localizes nodal at the limiting membrane of early endosomes

Autor: Stéphane Baflast, Judith Klumperman, Daniel B. Constam, Viola Oorschot, Marie-Hélène Blanchet, Gabriella Minchiotti, J. Ann Le Good

Publikováno v: Science signaling 1 (2008): ra13. doi:10.1126/scisignal.1165027
info:cnr-pdr/source/autori:Blanchet M.H.; Le Good J.A.; Oorschot V.; Baflast S.; Minchiotti G.; Klumperman J.; Constam D.B./titolo:Cripto localizes Nodal at the limiting membrane of early endosomes/doi:10.1126%2Fscisignal.1165027/rivista:Science signaling/anno:2008/pagina_da:ra13/pagina_a:/intervallo_pagine:ra13/volume:1

Cripto is a glycosylphosphatidylinositol (GPI)-anchored co-receptor of Nodal and several other transforming growth factor-beta (TGF-beta) family ligands. It contains an epidermal growth factor (EGF)-like motif and a Cripto-FRL1-Cryptic (CFC) domain,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::112873b419113eaa0c93f2a90e40f25f
https://infoscience.epfl.ch/record/130137