Substrate recruitment via eIF2γ enhances catalytic efficiency of a holophosphatase that terminates the integrated stress response.

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Title: Substrate recruitment via eIF2γ enhances catalytic efficiency of a holophosphatase that terminates the integrated stress response.
Authors: Yan Y; Cambridge Institute for Medical Research, Department of Clinical Biochemistry, University of Cambridge, Cambridge CB2 0XY, United Kingdom., Shetty M; Cambridge Institute for Medical Research, Department of Clinical Biochemistry, University of Cambridge, Cambridge CB2 0XY, United Kingdom., Harding HP; Cambridge Institute for Medical Research, Department of Clinical Biochemistry, University of Cambridge, Cambridge CB2 0XY, United Kingdom., George G; Cambridge Institute for Medical Research, Department of Clinical Biochemistry, University of Cambridge, Cambridge CB2 0XY, United Kingdom., Zyryanova A; Cambridge Institute for Medical Research, Department of Clinical Biochemistry, University of Cambridge, Cambridge CB2 0XY, United Kingdom., Labbé K; Calico Life Sciences, South San Francisco, CA 94080., Mafi A; Calico Life Sciences, South San Francisco, CA 94080., Hao Q; Calico Life Sciences, South San Francisco, CA 94080., Sidrauski C; Calico Life Sciences, South San Francisco, CA 94080., Ron D; Cambridge Institute for Medical Research, Department of Clinical Biochemistry, University of Cambridge, Cambridge CB2 0XY, United Kingdom.
Source: Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2024 Apr 02; Vol. 121 (14), pp. e2320013121. Date of Electronic Publication: 2024 Mar 28.
Publication Type: Journal Article
Journal Info: Publisher: National Academy of Sciences Country of Publication: United States NLM ID: 7505876 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1091-6490 (Electronic) Linking ISSN: 00278424 NLM ISO Abbreviation: Proc Natl Acad Sci U S A Subsets: MEDLINE
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  Data: Substrate recruitment via eIF2γ enhances catalytic efficiency of a holophosphatase that terminates the integrated stress response.
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  Data: <searchLink fieldCode="AU" term="%22Yan+Y%22">Yan Y</searchLink>; Cambridge Institute for Medical Research, Department of Clinical Biochemistry, University of Cambridge, Cambridge CB2 0XY, United Kingdom.<br /><searchLink fieldCode="AU" term="%22Shetty+M%22">Shetty M</searchLink>; Cambridge Institute for Medical Research, Department of Clinical Biochemistry, University of Cambridge, Cambridge CB2 0XY, United Kingdom.<br /><searchLink fieldCode="AU" term="%22Harding+HP%22">Harding HP</searchLink>; Cambridge Institute for Medical Research, Department of Clinical Biochemistry, University of Cambridge, Cambridge CB2 0XY, United Kingdom.<br /><searchLink fieldCode="AU" term="%22George+G%22">George G</searchLink>; Cambridge Institute for Medical Research, Department of Clinical Biochemistry, University of Cambridge, Cambridge CB2 0XY, United Kingdom.<br /><searchLink fieldCode="AU" term="%22Zyryanova+A%22">Zyryanova A</searchLink>; Cambridge Institute for Medical Research, Department of Clinical Biochemistry, University of Cambridge, Cambridge CB2 0XY, United Kingdom.<br /><searchLink fieldCode="AU" term="%22Labbé+K%22">Labbé K</searchLink>; Calico Life Sciences, South San Francisco, CA 94080.<br /><searchLink fieldCode="AU" term="%22Mafi+A%22">Mafi A</searchLink>; Calico Life Sciences, South San Francisco, CA 94080.<br /><searchLink fieldCode="AU" term="%22Hao+Q%22">Hao Q</searchLink>; Calico Life Sciences, South San Francisco, CA 94080.<br /><searchLink fieldCode="AU" term="%22Sidrauski+C%22">Sidrauski C</searchLink>; Calico Life Sciences, South San Francisco, CA 94080.<br /><searchLink fieldCode="AU" term="%22Ron+D%22">Ron D</searchLink>; Cambridge Institute for Medical Research, Department of Clinical Biochemistry, University of Cambridge, Cambridge CB2 0XY, United Kingdom.
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              Text: 2024 Apr 02
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