Zobrazeno 1 - 10
of 24
pro vyhledávání: '"Paola Llinas"'
Autor:
The Quyen Nguyen, Mélanie Chenon, Fernando Vilela, Christophe Velours, Magali Aumont-Nicaise, Jessica Andreani, Paloma F Varela, Paola Llinas, Julie Ménétrey
Publikováno v:
PLoS ONE, Vol 13, Iss 5, p e0197193 (2018)
[This corrects the article DOI: 10.1371/journal.pone.0186354.].
Externí odkaz:
https://doaj.org/article/f2e5b460a92a44a083ccb24a0e9bc7e6
Autor:
The Quyen Nguyen, Mélanie Chenon, Fernando Vilela, Christophe Velours, Magali Aumont-Nicaise, Jessica Andreani, Paloma F Varela, Paola Llinas, Julie Ménétrey
Publikováno v:
PLoS ONE, Vol 12, Iss 10, p e0186354 (2017)
Kinesin1 plays a major role in neuronal transport by recruiting many different cargos through its kinesin light chain (KLC). Various structurally unrelated cargos interact with the conserved tetratricopeptide repeat (TPR) domain of KLC. The N-termina
Externí odkaz:
https://doaj.org/article/662176ad3f3a4691a98914922c6f1ed9
Autor:
Fernando Vilela, Mélanie Chenon, Christophe Velours, Jessica Andreani, Paola Llinas, Julie Ménétrey
Whereas our understanding of kinesin auto-inhibition mechanisms is improving faster, important insights into kinesin activation mechanisms such as those controlled by cargo-motor adaptors are still missing. JIP3 and JIP4 are versatile motor-cargo ada
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::337718bbf772111086459613079f2778
https://doi.org/10.1101/2022.09.09.507386
https://doi.org/10.1101/2022.09.09.507386
Autor:
Julie Ménétrey, Aurélien Thureau, Christophe Velours, Magali Aumont-Nicaise, Fernando Vilela, Valérie Campanacci, Paola Llinas, Olena Pylypenko, Mélanie Chenon, Jessica Andreani
Publikováno v:
Scientific Reports
Scientific Reports, Nature Publishing Group, 2019, 9 (1), ⟨10.1038/s41598-019-52537-3⟩
Scientific Reports, Vol 9, Iss 1, Pp 1-15 (2019)
Scientific Reports, 2019, 9 (1), ⟨10.1038/s41598-019-52537-3⟩
Scientific Reports, Nature Publishing Group, 2019, 9 (1), ⟨10.1038/s41598-019-52537-3⟩
Scientific Reports, Vol 9, Iss 1, Pp 1-15 (2019)
Scientific Reports, 2019, 9 (1), ⟨10.1038/s41598-019-52537-3⟩
JIP3 and JIP4 (JNK-interacting proteins 3 and 4) are adaptors for cargo recruitment by dynein/dynactin and kinesin1 motors. Both are dimers that are stabilised by two sections of leucine zipper coiled coils. The N-terminal Leucine Zipper I (LZI) belo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2ceeea1295f01b47049a55146c6abf01
https://hal.archives-ouvertes.fr/hal-02349800
https://hal.archives-ouvertes.fr/hal-02349800
Autor:
T Quyen, Nguyen, Magali, Aumont-Nicaise, Jessica, Andreani, Christophe, Velours, Mélanie, Chenon, Fernando, Vilela, Clémentine, Geneste, Paloma F, Varela, Paola, Llinas, Julie, Ménétrey
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2018, 293 (36), pp.13946--13960. ⟨10.1074/jbc.RA118.003916⟩
Journal of Biological Chemistry, 2018, 293 (36), pp.13946--13960. ⟨10.1074/jbc.RA118.003916⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2018, 293 (36), pp.13946--13960. ⟨10.1074/jbc.RA118.003916⟩
Journal of Biological Chemistry, 2018, 293 (36), pp.13946--13960. ⟨10.1074/jbc.RA118.003916⟩
JIP1 was first identified as scaffold protein for the MAP kinase JNK and is a cargo protein for the kinesin1 molecular motor. JIP1 plays significant and broad roles in neurons, mainly as a regulator of kinesin1-dependent transport, and is associated
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::0ae2bc6991b4476f675141c56e5a348f
https://hal.archives-ouvertes.fr/hal-02183096
https://hal.archives-ouvertes.fr/hal-02183096
Autor:
Julie Ménétrey, Paola Llinas, Annélie de Régibus, Mélanie Chenon, Cátia Moreira, Pedro A. Fernandes, T. Quyen Nguyen, Maria J. Ramos, Raphael Guerois, Aline Coquard
Publikováno v:
Acta crystallographica. Section F, Structural biology communications
Acta crystallographica. Section F, Structural biology communications, John Wiley & Sons Ltd, 2016, pp.198-206. ⟨10.1107/S2053230X16001576⟩
Acta crystallographica. Section F, Structural biology communications, John Wiley & Sons Ltd, 2016, pp.198-206. 〈10.1107/S2053230X16001576〉
Acta crystallographica Section F : Structural biology communications [2014-...]
Acta crystallographica Section F : Structural biology communications [2014-..], 2016, pp.198-206. ⟨10.1107/S2053230X16001576⟩
Acta crystallographica. Section F, Structural biology communications, John Wiley & Sons Ltd, 2016, pp.198-206. ⟨10.1107/S2053230X16001576⟩
Acta crystallographica. Section F, Structural biology communications, John Wiley & Sons Ltd, 2016, pp.198-206. 〈10.1107/S2053230X16001576〉
Acta crystallographica Section F : Structural biology communications [2014-...]
Acta crystallographica Section F : Structural biology communications [2014-..], 2016, pp.198-206. ⟨10.1107/S2053230X16001576⟩
International audience; JIP3 and JIP4, two highly related scaffolding proteins for MAP kinases, are binding partners for two molecular motors as well as for the small G protein ARF6. The leucine zipper II (LZII) region of JIP3/4 is the binding site f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f0893bc1f8ae40cb11b2669939786237
https://hal.archives-ouvertes.fr/hal-01457789
https://hal.archives-ouvertes.fr/hal-01457789
Publikováno v:
FEBS Journal. 279:551-562
Molecular motors such as myosins are allosteric enzymes that power essential motility functions in the cell and structural biology is an important tool to decipher how these motors work. Force is produced by myosins upon the actin-driven conformation
Autor:
Clara Franzini-Armstrong, H. Lee Sweeney, HyeongJun Kim, Paola Llinas, Mirko Travaglia, Daniel Safer, Paul R. Selvin, Monalisa Mukherjea, Anne Houdusse, Julie Ménétrey
Publikováno v:
Molecular Cell. 35(3):305-315
Myosin VI challenges the prevailing theory of how myosin motors move on actin: the lever arm hypothesis. While the reverse directionality and large powerstroke of myosin VI can be attributed to unusual properties of a subdomain of the motor (converte
Autor:
Anne Houdusse, J. Cicolari, H. Lee Sweeney, Xiaoyan Liu, Julie Ménétrey, Anna Li, Paola Llinas, Gaelle Squires
Publikováno v:
The EMBO Journal. 27:244-252
Myosin VI has an unexpectedly large swing of its lever arm (powerstroke) that optimizes its unique reverse direction movement. The basis for this is an unprecedented rearrangement of the subdomain to which the lever arm is attached, referred to as th
Publikováno v:
Cell. 131(2):300-308
SummaryDue to a unique addition to the lever arm-positioning region (converter), class VI myosins move in the opposite direction (toward the minus-end of actin filaments) compared to other characterized myosin classes. However, the large size of the