A network of hydrophobic residues impeding helix alphaC rotation maintains latency of kinase Gcn2, which phosphorylates the alpha subunit of translation initiation factor 2. (Q37110590)

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scientific article published on 29 December 2008

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English	A network of hydrophobic residues impeding helix alphaC rotation maintains latency of kinase Gcn2, which phosphorylates the alpha subunit of translation initiation factor 2.	scientific article published on 29 December 2008

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19 January 2020

A network of hydrophobic residues impeding helix alphaC rotation maintains latency of kinase Gcn2, which phosphorylates the alpha subunit of translation initiation factor 2 (English)

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19 January 2020

phosphorylation

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5

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19 January 2020

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Andrés Gárriz

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19 January 2020

Hongfang Qiu

2

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19 January 2020

Madhusudan Dey

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19 January 2020

Eun-Joo Seo

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19 January 2020

Alan G Hinnebusch

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19 January 2020

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29 December 2008

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19 January 2020

Molecular and Cellular Biology

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19 January 2020

29

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19 January 2020

6

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19 January 2020

1592-1607

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Uncharged tRNA activates GCN2 by displacing the protein kinase moiety from a bipartite tRNA-binding domain

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Mutations in the Double-stranded RNA-activated Protein Kinase Insert Region That Uncouple Catalysis from eIF2α Binding

1 reference

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1128/MCB.01446-08

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19 January 2020

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19 January 2020

1 reference

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19 January 2020

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