2016 - Gruber Prize in Genetics
2008 - Member of the National Academy of Sciences
2001 - Fellow of the American Academy of Arts and Sciences
His primary scientific interests are in Molecular biology, Histone H2A, Histone code, Genetics and SAP30. His Molecular biology research is multidisciplinary, relying on both ColE1, Histone deacetylase complex and DNA. His research integrates issues of Chromatin immunoprecipitation, Histone methyltransferase and Histone H1 in his study of Histone H2A.
His work deals with themes such as Histone acetylation and deacetylation and Cell biology, which intersect with Histone H1. His study in Histone, Heterochromatin and Heterochromatin protein 1 is done as part of Genetics. His SAP30 research is multidisciplinary, incorporating elements of Histone H4 and Histone deacetylase 2.
His primary areas of study are Histone, Genetics, Histone H2A, Histone code and Molecular biology. His Histone study combines topics from a wide range of disciplines, such as Chromatin, Heterochromatin and Saccharomyces cerevisiae. His study in Genetics concentrates on Histone H4, Regulation of gene expression and Chromatin immunoprecipitation.
His Histone H2A research is multidisciplinary, incorporating perspectives in Histone deacetylase 2, Histone methyltransferase and Histone H1. The Histone code study combines topics in areas such as Histone H3, Histone octamer, Epigenomics, Cell biology and Histone methylation. His Molecular biology research includes themes of Cell cycle, Transcription and TATA box.
Michael Grunstein mainly investigates Histone, Genetics, Histone H2A, Nucleosome and Histone H3. His studies deal with areas such as Cancer, Acetylation, Chromatin, Heterochromatin and Regulation of gene expression as well as Histone. His work on Gene and Heterochromatin protein 1 as part of general Genetics study is frequently connected to Function, therefore bridging the gap between diverse disciplines of science and establishing a new relationship between them.
His Histone H2A study combines topics in areas such as Histone H1 and Histone code. His biological study spans a wide range of topics, including Histone octamer, Histone methylation and Cell biology. His study looks at the relationship between Histone H3 and fields such as Molecular biology, as well as how they intersect with chemical problems.
His scientific interests lie mostly in Histone H3, Molecular biology, Histone H2A, Histone code and Histone. His Molecular biology study integrates concerns from other disciplines, such as Embryonic stem cell, Cell culture, Reprogramming and Stem cell, Cell biology. His Cell biology research focuses on subjects like SAP30, which are linked to Histone octamer and Cancer epigenetics.
His studies in Histone H2A integrate themes in fields like Histone methyltransferase, Histone methylation and Histone H1. His work in Histone methylation addresses issues such as Nucleosome, which are connected to fields such as Heterochromatin, Telomeric heterochromatin and EZH2. His study in Histone is interdisciplinary in nature, drawing from both Chromatin, Transcription and Acetylation.
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Histone acetylation in chromatin structure and transcription
Michael Grunstein.
Nature (1997)
Colony hybridization: a method for the isolation of cloned DNAs that contain a specific gene
Michael Grunstein;David S. Hogness.
Proceedings of the National Academy of Sciences of the United States of America (1975)
Functions of site-specific histone acetylation and deacetylation.
Mona D. Shahbazian;Michael Grunstein.
Annual Review of Biochemistry (2007)
Induced Pluripotent Stem Cells and Embryonic Stem Cells Are Distinguished by Gene Expression Signatures
Mark H. Chin;Mike J. Mason;Wei Xie;Stefano Volinia.
Cell Stem Cell (2009)
Global histone modification patterns predict risk of prostate cancer recurrence
David B. Seligson;Steve Horvath;Tao Shi;Hong Yu.
Nature (2005)
SIR2 and SIR4 interactions differ in core and extended telomeric heterochromatin in yeast.
S Strahl-Bolsinger;A Hecht;K Luo;M Grunstein.
Genes & Development (1997)
Histone H3 and H4 N-termini interact with SIR3 and SIR4 proteins: A molecular model for the formation of heterochromatin in yeast
Andreas Hecht;Thierry Laroche;Sabine Strahl-Bolsinger;Susan M Gasser.
Cell (1995)
Cotranscriptional set2 methylation of histone H3 lysine 36 recruits a repressive Rpd3 complex.
Michael Christopher Keogh;Siavash K. Kurdistani;Stephanie A. Morris;Seong Hoon Ahn.
Cell (2005)
HDA1 and RPD3 are members of distinct yeast histone deacetylase complexes that regulate silencing and transcription.
Stephen E. Rundlett;Andrew A. Carmen;Ryuji Kobayashi;Sergei Bavykin.
Proceedings of the National Academy of Sciences of the United States of America (1996)
Histone acetylation and deacetylation in yeast
Siavash K Kurdistani;Michael Grunstein.
Nature Reviews Molecular Cell Biology (2003)
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