Cargando…
The N-Terminal Region of the Human Autophagy Protein ATG16L1 Contains a Domain That Folds into a Helical Structure Consistent with Formation of a Coiled-Coil
Autophagy is a fundamental cellular process required for organelle degradation and removal of invasive pathogens. Autophagosome formation involves the recruitment of, and interaction between, multiple proteins produced from autophagy-related (ATG) genes. One of the key complexes in autophagosome for...
Autores principales: | Parkhouse, Rhiannon, Ebong, Ima-Obong, Robinson, Carol V., Monie, Tom P. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2013
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3782427/ https://www.ncbi.nlm.nih.gov/pubmed/24086718 http://dx.doi.org/10.1371/journal.pone.0076237 |
Ejemplares similares
-
Coiled-coil-mediated dimerization of Atg16 is required for binding to the PROPPIN Atg21
por: Bueno-Arribas, Miranda, et al.
Publicado: (2023) -
The Structure and Topology of α-Helical Coiled Coils
por: Lupas, Andrei N., et al.
Publicado: (2017) -
The ATG5-binding and coiled coil domains of ATG16L1 maintain autophagy and tissue homeostasis in mice independently of the WD domain required for LC3-associated phagocytosis
por: Rai, Shashank, et al.
Publicado: (2018) -
Blau syndrome polymorphisms in NOD2 identify nucleotide hydrolysis and helical domain 1 as signalling regulators
por: Parkhouse, Rhiannon, et al.
Publicado: (2014) -
Mapping Critical Residues in ATG11’s Coiled-Coil 2 Domain that Block Multiple Interactions and Disrupt Selective Autophagy
por: Meyer, Mitchell D., et al.
Publicado: (2022)