| Year |
Citation |
Score |
| 2018 |
Grunstein M, Allis CD. Genetics, Biochemistry, and "Simple" Organisms Converge to Unlock Secrets in Histone Biology: The 2018 Albert Lasker Basic Medical Research Award. Jama. PMID 30208392 DOI: 10.1001/Jama.2018.12437 |
0.349 |
|
| 2015 |
Grunstein M, Bird A. Max Birnstiel 1933-2014: Gene pioneer. Proceedings of the National Academy of Sciences of the United States of America. 112: 302-3. PMID 25556180 DOI: 10.1073/Pnas.1423755112 |
0.554 |
|
| 2013 |
Grunstein M, Gasser SM. Epigenetics in Saccharomyces cerevisiae. Cold Spring Harbor Perspectives in Biology. 5. PMID 23818500 DOI: 10.1101/cshperspect.a017491 |
0.609 |
|
| 2013 |
Tan Y, Xue Y, Song C, Grunstein M. Acetylated histone H3K56 interacts with Oct4 to promote mouse embryonic stem cell pluripotency. Proceedings of the National Academy of Sciences of the United States of America. 110: 11493-8. PMID 23798425 DOI: 10.1073/pnas.1309914110 |
0.547 |
|
| 2012 |
Kitada T, Kuryan BG, Tran NN, Song C, Xue Y, Carey M, Grunstein M. Mechanism for epigenetic variegation of gene expression at yeast telomeric heterochromatin. Genes & Development. 26: 2443-55. PMID 23124068 DOI: 10.1101/Gad.201095.112 |
0.756 |
|
| 2012 |
Yu Y, Song C, Zhang Q, DiMaggio PA, Garcia BA, York A, Carey MF, Grunstein M. Histone H3 lysine 56 methylation regulates DNA replication through its interaction with PCNA. Molecular Cell. 46: 7-17. PMID 22387026 DOI: 10.1016/J.Molcel.2012.01.019 |
0.57 |
|
| 2012 |
Chen XF, Kuryan B, Kitada T, Tran N, Li JY, Kurdistani S, Grunstein M, Li B, Carey M. The Rpd3 core complex is a chromatin stabilization module. Current Biology : Cb. 22: 56-63. PMID 22177115 DOI: 10.1016/J.Cub.2011.11.042 |
0.767 |
|
| 2011 |
Sperling AS, Jeong KS, Kitada T, Grunstein M. Topoisomerase II binds nucleosome-free DNA and acts redundantly with topoisomerase I to enhance recruitment of RNA Pol II in budding yeast. Proceedings of the National Academy of Sciences of the United States of America. 108: 12693-8. PMID 21771901 DOI: 10.1073/Pnas.1106834108 |
0.788 |
|
| 2011 |
Kitada T, Schleker T, Sperling AS, Xie W, Gasser SM, Grunstein M. γH2A is a component of yeast heterochromatin required for telomere elongation. Cell Cycle (Georgetown, Tex.). 10: 293-300. PMID 21212735 DOI: 10.4161/Cc.10.2.14536 |
0.819 |
|
| 2010 |
Sinha I, Buchanan L, Rönnerblad M, Bonilla C, Durand-Dubief M, Shevchenko A, Grunstein M, Stewart AF, Ekwall K. Genome-wide mapping of histone modifications and mass spectrometry reveal H4 acetylation bias and H3K36 methylation at gene promoters in fission yeast. Epigenomics. 2: 377-93. PMID 22121899 DOI: 10.2217/Epi.10.18 |
0.541 |
|
| 2009 |
Sperling AS, Grunstein M. Histone H3 N-terminus regulates higher order structure of yeast heterochromatin. Proceedings of the National Academy of Sciences of the United States of America. 106: 13153-9. PMID 19666585 DOI: 10.1073/Pnas.0906866106 |
0.728 |
|
| 2009 |
Chin MH, Mason MJ, Xie W, Volinia S, Singer M, Peterson C, Ambartsumyan G, Aimiuwu O, Richter L, Zhang J, Khvorostov I, Ott V, Grunstein M, Lavon N, Benvenisty N, et al. Induced pluripotent stem cells and embryonic stem cells are distinguished by gene expression signatures. Cell Stem Cell. 5: 111-23. PMID 19570518 DOI: 10.1016/J.Stem.2009.06.008 |
0.434 |
|
| 2009 |
Sun W, Xie W, Xu F, Grunstein M, Li KC. Dissecting nucleosome free regions by a segmental semi-Markov model. Plos One. 4: e4721. PMID 19266098 DOI: 10.1371/Journal.Pone.0004721 |
0.606 |
|
| 2009 |
Xie W, Song C, Young NL, Sperling AS, Xu F, Sridharan R, Conway AE, Garcia BA, Plath K, Clark AT, Grunstein M. Histone h3 lysine 56 acetylation is linked to the core transcriptional network in human embryonic stem cells. Molecular Cell. 33: 417-27. PMID 19250903 DOI: 10.1016/J.Molcel.2009.02.004 |
0.804 |
|
| 2008 |
Houseley J, Rubbi L, Grunstein M, Tollervey D, Vogelauer M. A ncRNA modulates histone modification and mRNA induction in the yeast GAL gene cluster. Molecular Cell. 32: 685-95. PMID 19061643 DOI: 10.1016/J.Molcel.2008.09.027 |
0.819 |
|
| 2008 |
Kaplan T, Liu CL, Erkmann JA, Holik J, Grunstein M, Kaufman PD, Friedman N, Rando OJ. Cell cycle- and chaperone-mediated regulation of H3K56ac incorporation in yeast. Plos Genetics. 4: e1000270. PMID 19023413 DOI: 10.1371/Journal.Pgen.1000270 |
0.463 |
|
| 2008 |
Horwitz GA, Zhang K, McBrian MA, Grunstein M, Kurdistani SK, Berk AJ. Adenovirus small e1a alters global patterns of histone modification. Science (New York, N.Y.). 321: 1084-5. PMID 18719283 DOI: 10.1126/Science.1155544 |
0.56 |
|
| 2007 |
Xu F, Zhang Q, Zhang K, Xie W, Grunstein M. Sir2 deacetylates histone H3 lysine 56 to regulate telomeric heterochromatin structure in yeast. Molecular Cell. 27: 890-900. PMID 17889663 DOI: 10.1016/J.Molcel.2007.07.021 |
0.661 |
|
| 2007 |
Durand-Dubief M, Sinha I, Fagerström-Billai F, Bonilla C, Wright A, Grunstein M, Ekwall K. Specific functions for the fission yeast Sirtuins Hst2 and Hst4 in gene regulation and retrotransposon silencing. The Embo Journal. 26: 2477-88. PMID 17446861 DOI: 10.1038/Sj.Emboj.7601690 |
0.501 |
|
| 2007 |
Shahbazian MD, Grunstein M. Functions of site-specific histone acetylation and deacetylation. Annual Review of Biochemistry. 76: 75-100. PMID 17362198 DOI: 10.1146/annurev.biochem.76.052705.162114 |
0.615 |
|
| 2006 |
Ahn SH, Diaz RL, Grunstein M, Allis CD. Histone H2B deacetylation at lysine 11 is required for yeast apoptosis induced by phosphorylation of H2B at serine 10. Molecular Cell. 24: 211-20. PMID 17052455 DOI: 10.1016/J.Molcel.2006.09.008 |
0.539 |
|
| 2006 |
Millar CB, Grunstein M. Genome-wide patterns of histone modifications in yeast. Nature Reviews. Molecular Cell Biology. 7: 657-66. PMID 16912715 DOI: 10.1038/nrm1986 |
0.592 |
|
| 2006 |
Millar CB, Xu F, Zhang K, Grunstein M. Acetylation of H2AZ Lys 14 is associated with genome-wide gene activity in yeast. Genes & Development. 20: 711-22. PMID 16543223 DOI: 10.1101/Gad.1395506 |
0.576 |
|
| 2005 |
Keogh MC, Kurdistani SK, Morris SA, Ahn SH, Podolny V, Collins SR, Schuldiner M, Chin K, Punna T, Thompson NJ, Boone C, Emili A, Weissman JS, Hughes TR, Strahl BD, ... Grunstein M, et al. Cotranscriptional set2 methylation of histone H3 lysine 36 recruits a repressive Rpd3 complex. Cell. 123: 593-605. PMID 16286008 DOI: 10.1016/J.Cell.2005.10.025 |
0.614 |
|
| 2005 |
Wirén M, Silverstein RA, Sinha I, Walfridsson J, Lee HM, Laurenson P, Pillus L, Robyr D, Grunstein M, Ekwall K. Genomewide analysis of nucleosome density histone acetylation and HDAC function in fission yeast. The Embo Journal. 24: 2906-18. PMID 16079916 DOI: 10.1038/Sj.Emboj.7600758 |
0.576 |
|
| 2005 |
Shahbazian MD, Zhang K, Grunstein M. Histone H2B ubiquitylation controls processive methylation but not monomethylation by Dot1 and Set1. Molecular Cell. 19: 271-7. PMID 16039595 DOI: 10.1016/J.Molcel.2005.06.010 |
0.546 |
|
| 2005 |
Seligson DB, Horvath S, Shi T, Yu H, Tze S, Grunstein M, Kurdistani SK. Global histone modification patterns predict risk of prostate cancer recurrence. Nature. 435: 1262-6. PMID 15988529 DOI: 10.1038/Nature03672 |
0.489 |
|
| 2005 |
Xu F, Zhang K, Grunstein M. Acetylation in histone H3 globular domain regulates gene expression in yeast. Cell. 121: 375-85. PMID 15882620 DOI: 10.1016/J.Cell.2005.03.011 |
0.662 |
|
| 2004 |
Millar CB, Kurdistani SK, Grunstein M. Acetylation of yeast histone H4 lysine 16: a switch for protein interactions in heterochromatin and euchromatin. Cold Spring Harbor Symposia On Quantitative Biology. 69: 193-200. PMID 16117649 DOI: 10.1101/Sqb.2004.69.193 |
0.539 |
|
| 2004 |
Kurdistani SK, Tavazoie S, Grunstein M. Mapping global histone acetylation patterns to gene expression. Cell. 117: 721-33. PMID 15186774 DOI: 10.1016/J.Cell.2004.05.023 |
0.628 |
|
| 2004 |
Robyr D, Kurdistani SK, Grunstein M. Analysis of genome-wide histone acetylation state and enzyme binding using DNA microarrays. Methods in Enzymology. 376: 289-304. PMID 14975313 DOI: 10.1016/S0076-6879(03)76019-4 |
0.627 |
|
| 2003 |
Mellone BG, Ball L, Suka N, Grunstein MR, Partridge JF, Allshire RC. Centromere silencing and function in fission yeast is governed by the amino terminus of histone H3. Current Biology : Cb. 13: 1748-57. PMID 14561399 DOI: 10.1016/J.Cub.2003.09.031 |
0.527 |
|
| 2003 |
Kurdistani SK, Grunstein M. In vivo protein-protein and protein-DNA crosslinking for genomewide binding microarray. Methods (San Diego, Calif.). 31: 90-5. PMID 12893178 DOI: 10.1016/S1046-2023(03)00092-6 |
0.449 |
|
| 2003 |
Robyr D, Grunstein M. Genomewide histone acetylation microarrays. Methods (San Diego, Calif.). 31: 83-9. PMID 12893177 DOI: 10.1016/S1046-2023(03)00091-4 |
0.625 |
|
| 2003 |
Kurdistani SK, Grunstein M. Histone acetylation and deacetylation in yeast. Nature Reviews. Molecular Cell Biology. 4: 276-84. PMID 12671650 DOI: 10.1038/Nrm1075 |
0.664 |
|
| 2003 |
Thompson JS, Snow ML, Giles S, McPherson LE, Grunstein M. Identification of a functional domain within the essential core of histone H3 that is required for telomeric and HM silencing in Saccharomyces cerevisiae. Genetics. 163: 447-52. PMID 12586729 |
0.426 |
|
| 2002 |
Vogelauer M, Rubbi L, Lucas I, Brewer BJ, Grunstein M. Histone acetylation regulates the time of replication origin firing. Molecular Cell. 10: 1223-33. PMID 12453428 DOI: 10.1016/S1097-2765(02)00702-5 |
0.812 |
|
| 2002 |
Wang A, Kurdistani SK, Grunstein M. Requirement of Hos2 histone deacetylase for gene activity in yeast. Science (New York, N.Y.). 298: 1412-4. PMID 12434058 DOI: 10.1126/Science.1077790 |
0.728 |
|
| 2002 |
Kristjuhan A, Walker J, Suka N, Grunstein M, Roberts D, Cairns BR, Svejstrup JQ. Transcriptional inhibition of genes with severe histone h3 hypoacetylation in the coding region. Molecular Cell. 10: 925-33. PMID 12419235 DOI: 10.1016/S1097-2765(02)00647-0 |
0.634 |
|
| 2002 |
Suka N, Luo K, Grunstein M. Sir2p and Sas2p opposingly regulate acetylation of yeast histone H4 lysine16 and spreading of heterochromatin. Nature Genetics. 32: 378-83. PMID 12379856 DOI: 10.1038/Ng1017 |
0.7 |
|
| 2002 |
Kurdistani SK, Robyr D, Tavazoie S, Grunstein M. Genome-wide binding map of the histone deacetylase Rpd3 in yeast. Nature Genetics. 31: 248-54. PMID 12089521 DOI: 10.1038/Ng907 |
0.563 |
|
| 2002 |
Robyr D, Suka Y, Xenarios I, Kurdistani SK, Wang A, Suka N, Grunstein M. Microarray deacetylation maps determine genome-wide functions for yeast histone deacetylases. Cell. 109: 437-46. PMID 12086601 DOI: 10.1016/S0092-8674(02)00746-8 |
0.728 |
|
| 2002 |
Luo K, Vega-Palas MA, Grunstein M. Rap1-Sir4 binding independent of other Sir, yKu, or histone interactions initiates the assembly of telomeric heterochromatin in yeast. Genes & Development. 16: 1528-39. PMID 12080091 DOI: 10.1101/Gad.988802 |
0.711 |
|
| 2002 |
Verdone L, Wu J, van Riper K, Kacherovsky N, Vogelauer M, Young ET, Grunstein M, Di Mauro E, Caserta M. Hyperacetylation of chromatin at the ADH2 promoter allows Adr1 to bind in repressed conditions. The Embo Journal. 21: 1101-11. PMID 11867538 DOI: 10.1093/Emboj/21.5.1101 |
0.811 |
|
| 2002 |
Carmen AA, Milne L, Grunstein M. Acetylation of the yeast histone H4 N terminus regulates its binding to heterochromatin protein SIR3. The Journal of Biological Chemistry. 277: 4778-81. PMID 11714726 DOI: 10.1074/jbc.M110532200 |
0.546 |
|
| 2001 |
Suka N, Suka Y, Carmen AA, Wu J, Grunstein M. Highly specific antibodies determine histone acetylation site usage in yeast heterochromatin and euchromatin. Molecular Cell. 8: 473-9. PMID 11545749 DOI: 10.1016/S1097-2765(01)00301-X |
0.391 |
|
| 2001 |
Wu J, Carmen AA, Kobayashi R, Suka N, Grunstein M. HDA2 and HDA3 are related proteins that interact with and are essential for the activity of the yeast histone deacetylase HDA1. Proceedings of the National Academy of Sciences of the United States of America. 98: 4391-6. PMID 11287668 DOI: 10.1073/pnas.081560698 |
0.452 |
|
| 2001 |
Wu J, Suka N, Carlson M, Grunstein M. TUP1 utilizes histone H3/H2B-specific HDA1 deacetylase to repress gene activity in yeast. Molecular Cell. 7: 117-26. PMID 11172717 DOI: 10.1016/S1097-2765(01)00160-5 |
0.643 |
|
| 2000 |
Wu J, Grunstein M. 25 years after the nucleosome model: chromatin modifications. Trends in Biochemical Sciences. 25: 619-23. PMID 11116189 DOI: 10.1016/S0968-0004(00)01718-7 |
0.594 |
|
| 2000 |
Vogelauer M, Wu J, Suka N, Grunstein M. Global histone acetylation and deacetylation in yeast. Nature. 408: 495-8. PMID 11100734 DOI: 10.1038/35044127 |
0.835 |
|
| 1999 |
Hecht A, Strahl-Bolsinger S, Grunstein M. Mapping DNA interaction sites of chromosomal proteins. Crosslinking studies in yeast. Methods in Molecular Biology (Clifton, N.J.). 119: 469-79. PMID 10804533 DOI: 10.1385/1-59259-681-9:469 |
0.344 |
|
| 1999 |
Wyrick JJ, Holstege FC, Jennings EG, Causton HC, Shore D, Grunstein M, Lander ES, Young RA. Chromosomal landscape of nucleosome-dependent gene expression and silencing in yeast. Nature. 402: 418-21. PMID 10586882 DOI: 10.1038/46567 |
0.607 |
|
| 1999 |
Carmen AA, Griffin PR, Calaycay JR, Rundlett SE, Suka Y, Grunstein M. Yeast HOS3 forms a novel trichostatin A-insensitive homodimer with intrinsic histone deacetylase activity. Proceedings of the National Academy of Sciences of the United States of America. 96: 12356-61. PMID 10535926 DOI: 10.1073/pnas.96.22.12356 |
0.562 |
|
| 1999 |
Hecht A, Grunstein M. Mapping DNA interaction sites of chromosomal proteins using immunoprecipitation and polymerase chain reaction. Methods in Enzymology. 304: 399-414. PMID 10372373 DOI: 10.1016/S0076-6879(99)04024-0 |
0.448 |
|
| 1999 |
Martin SG, Laroche T, Suka N, Grunstein M, Gasser SM. Relocalization of telomeric Ku and SIR proteins in response to DNA strand breaks in yeast. Cell. 97: 621-33. PMID 10367891 DOI: 10.1016/S0092-8674(00)80773-4 |
0.418 |
|
| 1999 |
Kadonaga JT, Grunstein M. Chromatin: The packaging is the message Current Opinion in Genetics and Development. 9: 129-131. DOI: 10.1016/S0959-437X(99)80019-7 |
0.55 |
|
| 1998 |
Suka N, Carmen AA, Rundlett SE, Grunstein M. The regulation of gene activity by histones and the histone deacetylase RPD3. Cold Spring Harbor Symposia On Quantitative Biology. 63: 391-9. PMID 10384304 DOI: 10.1101/Sqb.1998.63.391 |
0.619 |
|
| 1998 |
Ma XJ, Wu J, Altheim BA, Schultz MC, Grunstein M. Deposition-related sites K5/K12 in histone H4 are not required for nucleosome deposition in yeast. Proceedings of the National Academy of Sciences of the United States of America. 95: 6693-8. PMID 9618474 DOI: 10.1073/pnas.95.12.6693 |
0.41 |
|
| 1998 |
Grunstein M. Yeast heterochromatin: regulation of its assembly and inheritance by histones. Cell. 93: 325-8. PMID 9590166 DOI: 10.1016/S0092-8674(00)81160-5 |
0.568 |
|
| 1998 |
Rundlett SE, Carmen AA, Suka N, Turner BM, Grunstein M. Transcriptional repression by UME6 involves deacetylation of lysine 5 of histone H4 by RPD3. Nature. 392: 831-5. PMID 9572144 DOI: 10.1038/33952 |
0.642 |
|
| 1997 |
Grunstein M. Histone acetylation in chromatin structure and transcription. Nature. 389: 349-52. PMID 9311776 DOI: 10.1038/38664 |
0.625 |
|
| 1997 |
Gotta M, Strahl-Bolsinger S, Renauld H, Laroche T, Kennedy BK, Grunstein M, Gasser SM. Localization of Sir2p: the nucleolus as a compartment for silent information regulators. The Embo Journal. 16: 3243-55. PMID 9214640 DOI: 10.1093/Emboj/16.11.3243 |
0.372 |
|
| 1997 |
Grunstein M. Molecular model for telomeric heterochromatin in yeast. Current Opinion in Cell Biology. 9: 383-7. PMID 9159071 DOI: 10.1016/S0955-0674(97)80011-7 |
0.564 |
|
| 1997 |
Strahl-Bolsinger S, Hecht A, Luo K, Grunstein M. SIR2 and SIR4 interactions differ in core and extended telomeric heterochromatin in yeast. Genes & Development. 11: 83-93. PMID 9000052 DOI: 10.1101/Gad.11.1.83 |
0.68 |
|
| 1996 |
Rundlett SE, Carmen AA, Kobayashi R, Bavykin S, Turner BM, Grunstein M. HDA1 and RPD3 are members of distinct yeast histone deacetylase complexes that regulate silencing and transcription. Proceedings of the National Academy of Sciences of the United States of America. 93: 14503-8. PMID 8962081 DOI: 10.1073/pnas.93.25.14503 |
0.667 |
|
| 1996 |
Hecht A, Strahl-Bolsinger S, Grunstein M. Spreading of transcriptional repressor SIR3 from telomeric heterochromatin. Nature. 383: 92-6. PMID 8779721 DOI: 10.1038/383092a0 |
0.633 |
|
| 1996 |
Lenfant F, Mann RK, Thomsen B, Ling X, Grunstein M. All four core histone N-termini contain sequences required for the repression of basal transcription in yeast. The Embo Journal. 15: 3974-85. PMID 8670902 DOI: 10.1002/J.1460-2075.1996.Tb00771.X |
0.599 |
|
| 1996 |
Carmen AA, Rundlett SE, Grunstein M. HDA1 and HDA3 are components of a yeast histone deacetylase (HDA) complex. The Journal of Biological Chemistry. 271: 15837-44. PMID 8663039 DOI: 10.1074/jbc.271.26.15837 |
0.525 |
|
| 1996 |
Ma XJ, Lu Q, Grunstein M. A search for proteins that interact genetically with histone H3 and H4 amino termini uncovers novel regulators of the Swe1 kinase in Saccharomyces cerevisiae. Genes & Development. 10: 1327-40. PMID 8647431 |
0.456 |
|
| 1996 |
Ling X, Harkness TA, Schultz MC, Fisher-Adams G, Grunstein M. Yeast histone H3 and H4 amino termini are important for nucleosome assembly in vivo and in vitro: redundant and position-independent functions in assembly but not in gene regulation. Genes & Development. 10: 686-99. PMID 8598296 DOI: 10.1101/Gad.10.6.686 |
0.568 |
|
| 1995 |
Grunstein M, Hecht A, Fisher-Adams G, Wan J, Mann RK, Strahl-Bolsinger S, Laroche T, Gasser S. The regulation of euchromatin and heterochromatin by histones in yeast. Journal of Cell Science. Supplement. 19: 29-36. PMID 8655644 DOI: 10.1242/Jcs.1995.Supplement_19.4 |
0.534 |
|
| 1995 |
Marsolier MC, Tanaka S, Livingstone-Zatchej M, Grunstein M, Thoma F, Sentenac A. Reciprocal interferences between nucleosomal organization and transcriptional activity of the yeast SNR6 gene. Genes & Development. 9: 410-22. PMID 7883166 DOI: 10.1101/Gad.9.4.410 |
0.553 |
|
| 1995 |
Hecht A, Laroche T, Strahl-Bolsinger S, Gasser SM, Grunstein M. Histone H3 and H4 N-termini interact with SIR3 and SIR4 proteins: a molecular model for the formation of heterochromatin in yeast. Cell. 80: 583-92. PMID 7867066 DOI: 10.1016/0092-8674(95)90512-X |
0.52 |
|
| 1995 |
Wan JS, Mann RK, Grunstein M. Yeast histone H3 and H4 N termini function through different GAL1 regulatory elements to repress and activate transcription. Proceedings of the National Academy of Sciences of the United States of America. 92: 5664-8. PMID 7777566 DOI: 10.1073/pnas.92.12.5664 |
0.504 |
|
| 1995 |
Fisher-Adams G, Grunstein M. Yeast histone H4 and H3 N-termini have different effects on the chromatin structure of the GAL1 promoter. The Embo Journal. 14: 1468-77. PMID 7729422 DOI: 10.1002/J.1460-2075.1995.Tb07133.X |
0.505 |
|
| 1994 |
Thompson JS, Johnson LM, Grunstein M. Specific repression of the yeast silent mating locus HMR by an adjacent telomere. Molecular and Cellular Biology. 14: 446-55. PMID 8264612 DOI: 10.1128/Mcb.14.1.446 |
0.493 |
|
| 1994 |
Thompson JS, Ling X, Grunstein M. Histone H3 amino terminus is required for telomeric and silent mating locus repression in yeast. Nature. 369: 245-7. PMID 8183346 DOI: 10.1038/369245a0 |
0.618 |
|
| 1993 |
Thompson JS, Hecht A, Grunstein M. Histones and the regulation of heterochromatin in yeast Cold Spring Harbor Symposia On Quantitative Biology. 58: 247-256. PMID 7956035 DOI: 10.1101/Sqb.1993.058.01.029 |
0.606 |
|
| 1992 |
Johnson LM, Fisher-Adams G, Grunstein M. Identification of a non-basic domain in the histone H4 N-terminus required for repression of the yeast silent mating loci Embo Journal. 11: 2201-2209. PMID 1600945 DOI: 10.1002/J.1460-2075.1992.Tb05279.X |
0.537 |
|
| 1992 |
Wan J, Xu H, Grunstein M. CDC14 of Saccharomyces cerevisiae. Cloning, sequence analysis, and transcription during the cell cycle Journal of Biological Chemistry. 267: 11274-11280. PMID 1597462 |
0.472 |
|
| 1992 |
Durrin LK, Mann RK, Grunstein M. Nucleosome loss activates CUP1 and HIS3 promoters to fully induced levels in the yeast Saccharomyces cerevisiae Molecular and Cellular Biology. 12: 1621-1629. PMID 1549116 DOI: 10.1128/Mcb.12.4.1621 |
0.472 |
|
| 1992 |
Roth SY, Shimizu M, Johnson L, Grunstein M, Simpson RT. Stable nucleosome positioning and complete repression by the yeast alpha 2 repressor are disrupted by amino-terminal mutations in histone H4. Genes & Development. 6: 411-25. PMID 1547940 DOI: 10.1101/Gad.6.3.411 |
0.429 |
|
| 1992 |
Mann RK, Grunstein M. Histone H3 N-terminal mutations allow hyperactivation of the yeast GAL 1 gene in vivo Embo Journal. 11: 3297-3306. PMID 1505519 DOI: 10.1002/J.1460-2075.1992.Tb05408.X |
0.524 |
|
| 1992 |
Grunstein M, Hogness DS. Colony hybridization: a method for the isolation of cloned DNAs that contain a specific gene. 1975. Biotechnology (Reading, Mass.). 24: 117-21. PMID 1422005 |
0.616 |
|
| 1992 |
Grunstein M. Histones as regulators of genes Scientific American. 267: 68-74+74B. PMID 1411455 DOI: 10.1038/Scientificamerican1092-68 |
0.613 |
|
| 1992 |
Xu H, Kim UJ, Schuster T, Grunstein M. Identification of a new set of cell cycle-regulatory genes that regulate S-phase transcription of histone genes in Saccharomyces cerevisiae Molecular and Cellular Biology. 12: 5249-5259. PMID 1406694 DOI: 10.1128/Mcb.12.11.5249 |
0.583 |
|
| 1992 |
Grunstein M, Durrin LK, Mann RK, Fisher-Adams G, Johnson LM. 48 Histones: Regulators of Transcription in Yeast Cold Spring Harbor Monograph Archive. 1295-1315. DOI: 10.1101/087969425.22B.1295 |
0.657 |
|
| 1991 |
Durrin LK, Mann RK, Kayne PS, Grunstein M. Yeast histone H4 N-terminal sequence is required for promoter activation in vivo Cell. 65: 1023-1031. PMID 2044150 DOI: 10.1016/0092-8674(91)90554-C |
0.566 |
|
| 1990 |
Grunstein M. Histone function in transcription Annual Review of Cell Biology. 6: 643-678. PMID 2275823 DOI: 10.1146/Annurev.Cb.06.110190.003235 |
0.609 |
|
| 1990 |
Saunders MJ, Yeh E, Grunstein M, Bloom K. Nucleosome depletion alters the chromatin structure of Saccharomyces cerevisiae centromeres Molecular and Cellular Biology. 10: 5721-5727. PMID 2233714 DOI: 10.1128/Mcb.10.11.5721 |
0.489 |
|
| 1990 |
Johnson LM, Kayne PS, Kahn ES, Grunstein M. Genetic evidence for an interaction between SIR3 and histone H4 in the repression of the silent mating loci in Saccharomyces cerevisiae Proceedings of the National Academy of Sciences of the United States of America. 87: 6286-6290. PMID 2201024 DOI: 10.1073/Pnas.87.16.6286 |
0.505 |
|
| 1990 |
Xu H, Johnson L, Grunstein M. Coding and noncoding sequences at the 3' end of yeast histone H2B mRNA confer cell cycle regulation Molecular and Cellular Biology. 10: 2687-2694. PMID 2188095 DOI: 10.1128/Mcb.10.6.2687 |
0.474 |
|
| 1990 |
Grunstein M. Nucleosomes: regulators of transcription Trends in Genetics. 6: 395-400. PMID 2087781 DOI: 10.1016/0168-9525(90)90299-L |
0.586 |
|
| 1989 |
Mullen JR, Kayne PS, Moerschell RP, Tsunasawa S, Gribskov M, Colavito-Shepanski M, Grunstein M, Sherman F, Sternglanz R. Identification and characterization of genes and mutants for an N-terminal acetyltransferase from yeast Embo Journal. 8: 2067-2075. PMID 2551674 DOI: 10.1002/J.1460-2075.1989.Tb03615.X |
0.349 |
|
| 1988 |
Kayne PS, Kim UJ, Han M, Mullen JR, Yoshizaki F, Grunstein M. Extremely conserved histone H4 N terminus is dispensable for growth but essential for repressing the silent mating loci in yeast Cell. 55: 27-39. PMID 3048701 DOI: 10.1016/0092-8674(88)90006-2 |
0.54 |
|
| 1988 |
Han M, Kim UJ, Kayne P, Grunstein M. Depletion of histone H4 and nucleosomes activates the PHO5 gene in Saccharomyces cerevisiae Embo Journal. 7: 2221-2228. PMID 3046934 DOI: 10.1002/J.1460-2075.1988.Tb03061.X |
0.632 |
|
| 1988 |
Kim UJ, Han M, Kayne P, Grunstein M. Effects of histone H4 depletion on the cell cycle and transcription of Saccharomyces cerevisiae Embo Journal. 7: 2211-2219. PMID 3046933 DOI: 10.1002/J.1460-2075.1988.Tb03060.X |
0.538 |
|
| 1988 |
Han M, Grunstein M. Nucleosome loss activates yeast downstream promoters in vivo Cell. 55: 1137-1145. PMID 2849508 DOI: 10.1016/0092-8674(88)90258-9 |
0.522 |
|
| 1988 |
Lishanskaya AI, Bavykin SG, Schuster T, Grunstein M, Mirzabekov AD. Structure of nucleosomes containing deleted histone H2B Doklady Biochemistry. 300: 134-138. |
0.478 |
|
| 1987 |
Han M, Chang M, Kim UJ, Grunstein M. Histone H2B repression causes cell-cycle-specific arrest in yeast: Effects on chromosomal segregation, replication, and transcription Cell. 48: 589-597. PMID 3815518 DOI: 10.1016/0092-8674(87)90237-6 |
0.601 |
|
| 1987 |
Masson JM, Meuris P, Grunstein M, Abelson J, Miller JH. Expression of a set of synthetic suppressor tRNA(Phe) genes in Saccharomyces cerevisiae Proceedings of the National Academy of Sciences of the United States of America. 84: 6815-6819. PMID 3309948 DOI: 10.1073/Pnas.84.19.6815 |
0.307 |
|
| 1986 |
Schuster T, Han M, Grunstein M. Yeast histone H2A and H2B amino termini have interchangeable functions Cell. 45: 445-451. PMID 3516414 DOI: 10.1016/0092-8674(86)90330-2 |
0.495 |
|
| 1985 |
Certa U, Colavito-Shepanski M, Grunstein M. Yeast may not contain histone H1: the only known 'histone H1-like' protein in Saccharomyces cerevisiae is a mitochondrial protein. Nucleic Acids Research. 12: 7975-85. PMID 6390339 DOI: 10.1093/NAR/12.21.7975 |
0.517 |
|
| 1985 |
Choe J, Schuster T, Grunstein M. Organization, primary structure, and evolution of histone H2A and H2B genes of the fission yeast Schizosaccharomyces pombe Molecular and Cellular Biology. 5: 3261-3269. PMID 3018512 DOI: 10.1128/Mcb.5.11.3261 |
0.477 |
|
| 1984 |
Wallis JW, Rykowski M, Grunstein M. Yeast histone H2B containing large amino terminus deletions can function in vivo. Cell. 35: 711-9. PMID 6360379 DOI: 10.1016/0092-8674(83)90104-6 |
0.523 |
|
| 1984 |
Travis GH, Colavito-Shepanski M, Grunstein M. Extensive purification and characterization of chromatin-bound histone acetyltransferase from Saccharomyces cerevisiae. Journal of Biological Chemistry. 259: 14406-14412. DOI: 10.1016/s0021-9258(17)42614-7 |
0.523 |
|
| 1983 |
Kolodrubetz D, Rykowski MC, Grunstein M. Histone H2A subtypes associate interchangeably in vivo with histone H2B subtypes. Proceedings of the National Academy of Sciences of the United States of America. 79: 7814-8. PMID 6760203 DOI: 10.1073/Pnas.79.24.7814 |
0.527 |
|
| 1982 |
Choe J, Kolodrubetz D, Grunstein M. The two yeast histone H2A genes encode similar protein subtypes Proceedings of the National Academy of Sciences of the United States of America. 79: 1484-1487. PMID 7041122 DOI: 10.1073/Pnas.79.5.1484 |
0.535 |
|
| 1981 |
Rykowski MC, Wallis JW, Choe J, Grunstein M. Histone H2B subtypes are dispensable during the yeast cell cycle. Cell. 25: 477-87. PMID 7026046 DOI: 10.1016/0092-8674(81)90066-0 |
0.479 |
|
| 1981 |
Grunstein M, Diamond KE, Knoppel E, Grunstein JE. Comparison of the early histone H4 gene sequence of Strongylocentrotus purpuratus with maternal, early, and late histone H4 mRNA sequences. Biochemistry. 20: 1216-23. PMID 7013789 DOI: 10.1021/Bi00508A025 |
0.395 |
|
| 1981 |
Wallis JW, Hereford L, Grunstein M. Histone H2B genes of yeast encode two different proteins. Cell. 22: 799-805. PMID 7006833 DOI: 10.1016/0092-8674(80)90556-5 |
0.446 |
|
| 1978 |
Grunstein M. Hatching in the sea urchin Lytechinus pictus is accompanied by a shift in histone H4 gene activity. Proceedings of the National Academy of Sciences of the United States of America. 75: 4135-9. PMID 279903 DOI: 10.1073/PNAS.75.9.4135 |
0.505 |
|
| 1976 |
Grunstein M, Schedl P, Kedes L. Sequence analysis and evolution of sea urchin (Lytechinus pictus and Strongylocentrotus purpuratus) histone H4 messenger RNAs Journal of Molecular Biology. 104: 351-369. PMID 950666 DOI: 10.1016/0022-2836(76)90276-X |
0.307 |
|
| 1976 |
Grunstein M, Schedl P. Isolation and sequence analysis of sea urchin (Lytechinus pictus) histone H4 messenger RNA. Journal of Molecular Biology. 104: 323-49. PMID 950665 DOI: 10.1016/0022-2836(76)90275-8 |
0.313 |
|
| 1975 |
Levy S, Wood P, Grunstein M, Kedes L. Individual histone messenger RNAs: Identification by template activity Cell. 4: 239-248. PMID 1122555 DOI: 10.1016/0092-8674(75)90171-3 |
0.325 |
|
| 1975 |
Grunstein M, Hogness DS. Colony hybridization: a method for the isolation of cloned DNAs that contain a specific gene. Proceedings of the National Academy of Sciences of the United States of America. 72: 3961-5. PMID 1105573 DOI: 10.1073/Pnas.72.10.3961 |
0.637 |
|
| 1974 |
Grunstein M, Levy S, Schedl P, Kedes L. Messenger RNAs for individual histone proteins: fingerprint analysis and in vitro translation Cold Spring Harbor Symposia On Quantitative Biology. 38: 717-724. PMID 4524784 |
0.323 |
|
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