Home > Publications database > Conformational Polymorphism in Autophagy-Related Protein GATE-16 > print

001     276569
005     20210129220914.0
024 7 _ |a 10.1021/acs.biochem.5b00366
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024 7 _ |a 1520-4995
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100 1 _ |a Ma, Peixiang
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245 _ _ |a Conformational Polymorphism in Autophagy-Related Protein GATE-16
260 _ _ |a Columbus, Ohio
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520 _ _ |a Autophagy is a fundamental homeostatic process in eukaryotic organisms, fulfilling essential roles in development and adaptation to stress. Among other factors, formation of autophagosomes critically depends on proteins of the Atg8 (autophagy-related protein 8) family, which are reversibly conjugated to membrane lipids. We have applied Xray crystallography, nuclear magnetic resonance spectroscopy, and molecular dynamics simulations to study the conformational dynamics of Atg8-type proteins, using GATE-16 (Golgiassociated ATPase enhancer of 16 kDa), also known as GABARAPL2, as a model system. This combination of complementary approaches provides new insight into a structural transition centered on the C-terminus, which is crucial for the biological activity of these proteins.
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700 1 _ |a Schillinger, Oliver
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700 1 _ |a Schwarten, Melanie
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700 1 _ |a Lecher, Justin
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700 1 _ |a Hartmann, Rudolf
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700 1 _ |a Stoldt, Matthias
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700 1 _ |a Mohrlüder, Jeannine
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700 1 _ |a Olubiyi, Olujide
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700 1 _ |a Strodel, Birgit
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700 1 _ |a Willbold, Dieter
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700 1 _ |a Weiergräber, Oliver H.
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773 _ _ |a 10.1021/acs.biochem.5b00366
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