Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Christine Fagotto-Kaufmann"'
Autor:
Christine Fagotto-Kaufmann, Anne Debant, Amandine Falco, Freddy Jeanneteau, Marion Bonhomme, Jérôme Boudeau, Niels Galjart, Jeffrey van Haren, Carlos Sánchez-Huertas
Publikováno v:
Journal of Cell Biology
Journal of Cell Biology, Rockefeller University Press, 2020, 219 (9), ⟨10.1083/jcb.201905199⟩
The Journal of Cell Biology
Digital.CSIC. Repositorio Institucional del CSIC
instname
Journal of Cell Biology, 219(9):e201905199. Rockefeller University Press
Journal of Cell Biology, Rockefeller University Press, 2020, 219 (9), ⟨10.1083/jcb.201905199⟩
The Journal of Cell Biology
Digital.CSIC. Repositorio Institucional del CSIC
instname
Journal of Cell Biology, 219(9):e201905199. Rockefeller University Press
Trabajo presentado al 17th Meeting of the Spanish Society for Developmental Biology (SEBD), celebrado de forma virtual del 18 al 20 de noviembre de 2020.
The microtubule plus-end tracking proteins (+TIPs) are central players in the coordination
The microtubule plus-end tracking proteins (+TIPs) are central players in the coordination
Autor:
Marcie A. Steeves, Marjorlaine Willems, Siddharth Banka, Yline Capri, Michael J. Parker, Stephanie Greville-Heygate, Emma Clement, David Goudie, Vincent Cantagrel, Diana Rodriguez, Marlène Rio, Matthew Guille, Htoo A Wai, Anne Debant, Ajoy Sarkar, Fleur Vansenne, Frédéric Tran Mau-Them, Peter D Turnpenny, Audrey Putoux, Christine Fagotto-Kaufmann, Karine Siquier-Pernet, Bert B.A. de Vries, Boris Keren, Maxime Bonnet, Lydie Burglen, Sébastien Moutton, Marion Gérard, Susanne Schmidt, Diana Baralle, Sónia Barbosa, Benjamin Cogné, Damien Laouteouet, Amélie Piton, Helen Cox, Rebecca Mawby, Marie Vincent, Annie Godwin, Andrey V. Kajava, Sarju G. Mehta, Alexander J. M. Dingemans, Jozef Hertecant, Jayne Y. Hehir-Kwa, Gaetan Lesca
Publikováno v:
C4RCD Research Group 2020, ' Opposite Modulation of RAC1 by Mutations in TRIO Is Associated with Distinct, Domain-Specific Neurodevelopmental Disorders ', American Journal of Human Genetics . https://doi.org/10.1016/j.ajhg.2020.01.018
American Journal of Human Genetics, 106(3), 338-355. CELL PRESS
American Journal of Human Genetics, 106, 338-355
Barbosa, S, Greville-Heygate, S, Bonnet, M, Godwin, A L, Fagotto-Kaufmann, C, Kajava, A V, Laouteouet, D, Mawby, R, Wai, H A, Dingemans, A, De Vries, B, Willems, M, Capri, Y, Mehta, S G, Cox, H, Goudie, D, Vansenne, F, Turnpenny, P, Vincent, M, Lesca, G, Hertecant, J, Rodriguez, D, Marion, G, Putoux, A, Ramsey, K, Cantagrel, V, Banka, S, Sarkar, A, Steeves, M, Parker, M, Clement, E, Moutton, S, Tran-Mau-Them, F, Piton, A, Guille, M, Debant, A, Schmidt, S & Baralle, D 2020, ' Opposite modulation of RAC1 by mutations in TRIO is associated with distinct, domain specific neurodevelopmental disorders ', American Journal of Human Genetics, vol. 106, no. 3, pp. 338-355 . https://doi.org/10.1016/j.ajhg.2020.01.018
American Journal of Human Genetics, 106, 3, pp. 338-355
American Journal of Human Genetics
American Journal of Human Genetics, Elsevier (Cell Press), 2020, 106 (3), pp.338-355. ⟨10.1016/j.ajhg.2020.01.018⟩
American Journal of Human Genetics, 106(3), 338-355. CELL PRESS
American Journal of Human Genetics, 106, 338-355
Barbosa, S, Greville-Heygate, S, Bonnet, M, Godwin, A L, Fagotto-Kaufmann, C, Kajava, A V, Laouteouet, D, Mawby, R, Wai, H A, Dingemans, A, De Vries, B, Willems, M, Capri, Y, Mehta, S G, Cox, H, Goudie, D, Vansenne, F, Turnpenny, P, Vincent, M, Lesca, G, Hertecant, J, Rodriguez, D, Marion, G, Putoux, A, Ramsey, K, Cantagrel, V, Banka, S, Sarkar, A, Steeves, M, Parker, M, Clement, E, Moutton, S, Tran-Mau-Them, F, Piton, A, Guille, M, Debant, A, Schmidt, S & Baralle, D 2020, ' Opposite modulation of RAC1 by mutations in TRIO is associated with distinct, domain specific neurodevelopmental disorders ', American Journal of Human Genetics, vol. 106, no. 3, pp. 338-355 . https://doi.org/10.1016/j.ajhg.2020.01.018
American Journal of Human Genetics, 106, 3, pp. 338-355
American Journal of Human Genetics
American Journal of Human Genetics, Elsevier (Cell Press), 2020, 106 (3), pp.338-355. ⟨10.1016/j.ajhg.2020.01.018⟩
The Rho-guanine nucleotide exchange factor (RhoGEF) TRIO acts as a key regulator of neuronal migration, axonal outgrowth, axon guidance, and synaptogenesis by activating the GTPase RAC1 and modulating actin cytoskeleton remodeling. Pathogenic variant
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3e6feb0d914090bef0d0a94f376bcc6f
https://eprints.soton.ac.uk/438435/
https://eprints.soton.ac.uk/438435/
Autor:
Stephanie Greville-Heygate, Susanne Schmidt, Diana Baralle, Eleanor G. Seaby, Anne Debant, Sarah Ennis, M. Reza Jabalameli, Sarju G. Mehta, Reuben J. Pengelly, Christine Fagotto-Kaufmann, Michael J. Parker, David Goudie, Catherine Mercer
Publikováno v:
Journal of Medical Genetics
Journal of Medical Genetics, BMJ Publishing Group, 2016, 53 (11), pp.735--742. ⟨10.1136/jmedgenet-2016-103942⟩
Journal of Medical Genetics, BMJ Publishing Group, 2016, 53 (11), pp.735--742. ⟨10.1136/jmedgenet-2016-103942⟩
Background: Neurodevelopmental disorders have challenged clinical genetics for decades, with over 700 genes implicated and many whose function remains unknown. The application of whole-exome sequencing is proving pivotal in closing the genotype/pheno
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ccb013cda5f2da0e87a1fe211e6d836
https://hal.archives-ouvertes.fr/hal-01878037
https://hal.archives-ouvertes.fr/hal-01878037
Autor:
Christine Fagotto-Kaufmann, Marian Chen, Douglas S. Annis, Deane F. Mosher, Laetitia Sabatier, Dieter P. Reinhardt, Jelena Djokic
Publikováno v:
Biochemical Journal. 456:283-295
Fibrillins constitute the backbone of extracellular multifunctional assemblies present in elastic and non-elastic matrices, termed microfibrils. Assembly of fibrillins into microfibrils and their homoeostasis is poorly understood and is often comprom
Autor:
Jelena Djokic, Valentin Nelea, Christine Fagotto-Kaufmann, Dieter P. Reinhardt, Rainer Bartels
Publikováno v:
Journal of Biological Chemistry. 288:22821-22835
Extracellular short fibulins, fibulin-3, -4, and -5, are components of the elastic fiber/microfibril system and are implicated in the formation and homeostasis of elastic tissues. In this study, we report new structural and functional properties of t
Autor:
Dirk Hubmacher, Christine Fagotto-Kaufmann, Lynn Y. Sakai, Eric Bergeron, Dieter P. Reinhardt
Publikováno v:
Biomacromolecules. 15(4)
Fibrillin proteins constitute the backbone of extra-cellular macromolecular microfibrils. Mutations in fibrillins cause heritable connective tissue disorders, including Marfan syndrome, dominant Weill-Marchesani syndrome, and stiff skin syndrome. Fib
Autor:
Dirk Hubmacher, Christine Fagotto-Kaufmann, Dieter P. Reinhardt, Ryan Kirschner, Rainer Bartels, Jasvir Kaur, Garud Iyengar, Dieter Brömme
Publikováno v:
The Journal of biological chemistry. 286(37)
Mutations in fibrillin-1 give rise to Marfan syndrome (MFS) characterized by vascular, skeletal, and ocular abnormalities. Fibrillins form the backbone of extracellular matrix microfibrils in tissues including blood vessels, bone, and skin. They are
Autor:
Dieter P. Reinhardt, Christine Fagotto-Kaufmann, Laetitia Sabatier, Daliang Chen, Deane F. Mosher, Douglas S. Annis
Publikováno v:
The FASEB Journal. 24
Autor:
Laetitia Sabatier, Daliang Chen, Douglas S. Annis, Dirk Hubmacher, Christine Fagotto-Kaufmann, Deane F. Mosher, Marc D. McKee, Dieter P. Reinhardt
Publikováno v:
Molecular biology of the cell. 20(3)
Fibrillins constitute the major backbone of multifunctional microfibrils in elastic and nonelastic extracellular matrices. Proper assembly mechanisms are central to the formation and function of these microfibrils, and their properties are often comp
Autor:
Christine Fagotto-Kaufmann, Meghan Elliott, Emilie Dumontier, Renu Heir, Fiona Bedford, Celine Ablasou
Publikováno v:
EMBO reports. 7(12)
Defects in protein folding and the proteasomal pathway have been linked with many neurodegenerative diseases. PLIC-1 (protein linking IAP to the cytoskeleton) is a ubiquitin-like protein that binds to the ubiquitin-interacting motif (UIM) of the prot