2015 - Member of the National Academy of Sciences
2009 - Fellow of the American Academy of Arts and Sciences
2008 - Fellow of the American Association for the Advancement of Science (AAAS)
Alan G. Hinnebusch focuses on Biochemistry, Initiation factor, Genetics, Eukaryotic translation and Eukaryotic initiation factor. Biochemistry is represented through his Saccharomyces cerevisiae, Protein biosynthesis, eIF2B, Phosphorylation and Translation research. His Initiation factor research includes themes of Translational regulation, EIF1, Protein subunit, G alpha subunit and Molecular biology.
He has included themes like Guanine nucleotide exchange factor and Computational biology in his Eukaryotic translation study. His Eukaryotic initiation factor research is multidisciplinary, incorporating perspectives in Eukaryotic translation initiation factor 4 gamma, Prokaryotic initiation factor, Internal ribosome entry site, Eukaryotic Ribosome and Cell biology. His study in Cell biology is interdisciplinary in nature, drawing from both eIF2, Eukaryotic Initiation Factor-2, EIF4A1 and Transfer RNA, Eukaryotic Large Ribosomal Subunit.
His scientific interests lie mostly in Cell biology, Eukaryotic translation, Biochemistry, Genetics and Translation. The concepts of his Cell biology study are interwoven with issues in Molecular biology, Messenger RNA, EIF4E, Ribosome and Transcription preinitiation complex. His research in Molecular biology intersects with topics in RNA polymerase II and Protein subunit.
His Eukaryotic translation study combines topics from a wide range of disciplines, such as EIF1, Eukaryotic Small Ribosomal Subunit, eIF4A, Polysome and Initiation factor. Alan G. Hinnebusch has researched Initiation factor in several fields, including Eukaryotic translation initiation factor 4 gamma, Translational regulation, eIF2, Eukaryotic Ribosome and Eukaryotic initiation factor. The various areas that Alan G. Hinnebusch examines in his Translation study include Open reading frame and Transfer RNA.
Alan G. Hinnebusch mainly investigates Cell biology, Start codon, Eukaryotic translation, Translation and Messenger RNA. His Cell biology research incorporates themes from Eukaryotic Ribosome, Ribosome, eIF4A, Initiation factor and Transcription preinitiation complex. His Eukaryotic translation research is multidisciplinary, incorporating elements of Eukaryotic Small Ribosomal Subunit and Eukaryotic initiation factor.
Eukaryotic initiation factor is a subfield of Genetics that Alan G. Hinnebusch investigates. His Translation research includes elements of Open reading frame, Reprogramming and Saccharomyces cerevisiae. The Messenger RNA study combines topics in areas such as Molecular biology and Yeast.
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Regulation of Translation Initiation in Eukaryotes: Mechanisms and Biological Targets
Nahum Sonenberg;Alan G. Hinnebusch.
Translational regulation of GCN4 and the general amino acid control of yeast.
Alan G Hinnebusch.
Annual Review of Microbiology (2005)
Transcriptional Profiling Shows that Gcn4p Is a Master Regulator of Gene Expression during Amino Acid Starvation in Yeast
Krishnamurthy Natarajan;Michael R. Meyer;Belinda M. Jackson;David Slade.
Molecular and Cellular Biology (2001)
Phosphorylation of initiation factor 2α by protein kinase GCN2 mediates gene-specific translational control of GCN4 in yeast
Thomas E. Dever;Lan Feng;Ronald C. Wek;A.Mark Cigan.
The Scanning Mechanism of Eukaryotic Translation Initiation
Alan G Hinnebusch.
Annual Review of Biochemistry (2014)
Translational Regulation of Yeast GCN4 A WINDOW ON FACTORS THAT CONTROL INITIATOR-tRNA BINDING TO THE RIBOSOME
Alan G. Hinnebusch.
Journal of Biological Chemistry (1997)
Translational control by 5′-untranslated regions of eukaryotic mRNAs
Alan G. Hinnebusch;Ivaylo P. Ivanov;Nahum Sonenberg.
Multiple upstream AUG codons mediate translational control of GCN4
Peter P. Mueller;Alan G. Hinnebusch.
Evidence for translational regulation of the activator of general amino acid control in yeast.
Alan G. Hinnebusch.
Proceedings of the National Academy of Sciences of the United States of America (1984)
Uncharged tRNA activates GCN2 by displacing the protein kinase moiety from a bipartite tRNA-binding domain.
Jinsheng Dong;Hongfang Qiu;Minerva Garcia-Barrio;James T. Anderson.
Molecular Cell (2000)
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