Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Manuel Gimenez-Andres"'
Autor:
Kai-En Chen, Edmund R. R. Moody, Peter J. Cullen, Ashley J. Evans, Boris Simonetti, Tom A. Williams, Manuel Gimenez-Andres, Brett M. Collins, Qian Guo, Chris M. Danson
Sorting nexin-27 (SNX27)-Retromer is an endosomal sorting complex that orchestrates endosome-to-plasma membrane recycling of hundreds of internalized receptors, channels and transporters, enzymes and adhesion molecules. While SNX27-Retromer is essent
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::67a3ea989047b957f9014c48e2406cc0
https://doi.org/10.1101/2021.08.28.457928
https://doi.org/10.1101/2021.08.28.457928
Autor:
Bruno Antonny, Manuel Gimenez-Andres, Tadej Emeršič, Sandra Antoine-Bally, Alenka Čopič, Juan Martín D'Ambrosio, Jure Derganc
Publikováno v:
eLife
eLife, eLife Sciences Publication, 2021, ⟨10.7554/eLife.61401⟩
eLife, Vol 10 (2021)
eLife, eLife Sciences Publication, 2021, ⟨10.7554/eLife.61401⟩
eLife, Vol 10 (2021)
Numerous proteins target lipid droplets (LDs) through amphipathic helices (AHs). It is generally assumed that AHs insert bulky hydrophobic residues in packing defects at the LD surface. However, this model does not explain the targeting of perilipins
Autor:
Sandra Antoine-Bally, Tadej Emeršič, Bruno Antonny, Jure Derganc, Alenka Čopič, Manuel Gimenez-Andres
Numerous proteins target lipid droplets (LDs) through amphipathic helices (AHs). It is generally assumed that AHs insert bulky hydrophobic residues in packing defects at the LD surface. However, this model does not explain the targeting of perilipins
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::18f5cda7933a7628cadbf8c8721b731e
https://doi.org/10.1101/2020.07.30.228353
https://doi.org/10.1101/2020.07.30.228353
Autor:
Manuel Gimenez-Andres, Sophie Pagnotta, Cesar La Torre Garay, Bruno Antonny, Sandra Antoine-Bally, Alenka Čopič, Jeanne Guihot, Marco M. Manni, Catherine L. Jackson
Publikováno v:
Nature Communications
Nature Communications, Nature Publishing Group, 2018, 9 (1), ⟨10.1038/s41467-018-03717-8⟩
Nature Communications, Vol 9, Iss 1, Pp 1-16 (2018)
Nature Communications, Nature Publishing Group, 2018, 9 (1), ⟨10.1038/s41467-018-03717-8⟩
Nature Communications, Vol 9, Iss 1, Pp 1-16 (2018)
How proteins are targeted to lipid droplets (LDs) and distinguish the LD surface from the surfaces of other organelles is poorly understood, but many contain predicted amphipathic helices (AHs) that are involved in targeting. We have focused on human
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b2552554e710f5074b64a440e509620c
https://doi.org/10.1101/276238
https://doi.org/10.1101/276238
Autor:
Boris Simonetti, Qian Guo, Manuel Giménez-Andrés, Kai-En Chen, Edmund R R Moody, Ashley J Evans, Mintu Chandra, Chris M Danson, Tom A Williams, Brett M Collins, Peter J Cullen
Publikováno v:
PLoS Biology, Vol 20, Iss 4, p e3001601 (2022)
Coat complexes coordinate cargo recognition through cargo adaptors with biogenesis of transport carriers during integral membrane protein trafficking. Here, we combine biochemical, structural, and cellular analyses to establish the mechanistic basis
Externí odkaz:
https://doaj.org/article/844881cd71af4ba98857830ac0cd310b
Autor:
Manuel Giménez-Andrés, Tadej Emeršič, Sandra Antoine-Bally, Juan Martin D'Ambrosio, Bruno Antonny, Jure Derganc, Alenka Čopič
Publikováno v:
eLife, Vol 10 (2021)
Numerous proteins target lipid droplets (LDs) through amphipathic helices (AHs). It is generally assumed that AHs insert bulky hydrophobic residues in packing defects at the LD surface. However, this model does not explain the targeting of perilipins
Externí odkaz:
https://doaj.org/article/feb96be726824530b92c9c9c35541f93
Autor:
Alenka Čopič, Sandra Antoine-Bally, Manuel Giménez-Andrés, César La Torre Garay, Bruno Antonny, Marco M. Manni, Sophie Pagnotta, Jeanne Guihot, Catherine L. Jackson
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-16 (2018)
Lipid droplets are cellular organelles important for cellular homeostasis and their disruption has been implicated in many diseases. Here the authors use a large amphipathic helix from perilipin 4 to uncover parameters important for specific lipid dr
Externí odkaz:
https://doaj.org/article/492f328f8d8144b1b134824fe07962c6
Publikováno v:
Biomolecules, Vol 8, Iss 3, p 45 (2018)
Amphipathic helices (AHs), a secondary feature found in many proteins, are defined by their structure and by the segregation of hydrophobic and polar residues between two faces of the helix. This segregation allows AHs to adsorb at polar–apolar int
Externí odkaz:
https://doaj.org/article/52784150ae0b48738d4cc6fcca07d547