| Year | Citation | Score | |||
|---|---|---|---|---|---|
| 2022 | Malinina DK, Sivkina AL, Korovina AN, McCullough LL, Formosa T, Kirpichnikov MP, Studitsky VM, Feofanov AV. Hmo1 Protein Affects the Nucleosome Structure and Supports the Nucleosome Reorganization Activity of Yeast FACT. Cells. 11. PMID 36230893 DOI: 10.3390/cells11192931 | 0.402 | |||
| 2021 | Connell Z, Parnell TJ, McCullough LL, Hill CP, Formosa T. The interaction between the Spt6-tSH2 domain and Rpb1 affects multiple functions of RNA Polymerase II. Nucleic Acids Research. PMID 34967414 DOI: 10.1093/nar/gkab1262 | 0.302 | |||
| 2020 | Formosa T, Winston F. The role of FACT in managing chromatin: disruption, assembly, or repair? Nucleic Acids Research. PMID 33104782 DOI: 10.1093/nar/gkaa912 | 0.399 | |||
| 2019 | Chang HW, Nizovtseva EV, Razin SV, Formosa T, Gurova KV, Studitsky VM. Histone Chaperone FACT and Curaxins: Effects on Genome Structure and Function. Journal of Cancer Metastasis and Treatment. 5. PMID 31853507 DOI: 10.20517/2394-4722.2019.31 | 0.391 | |||
| 2019 | Nune M, Morgan MT, Connell Z, McCullough L, Jbara M, Sun H, Brik A, Formosa T, Wolberger C. FACT and Ubp10 collaborate to modulate H2B deubiquitination and nucleosome dynamics. Elife. 8. PMID 30681413 DOI: 10.7554/Elife.40988 | 0.488 | |||
| 2019 | McCullough LL, Pham TH, Parnell TJ, Connell Z, Chandrasekharan MB, Stillman DJ, Formosa T. Establishment and Maintenance of Chromatin Architecture Are Promoted Independent of Transcription by the Histone Chaperone FACT and H3-K56 Acetylation in . Genetics. PMID 30679261 DOI: 10.1534/Genetics.118.301853 | 0.398 | |||
| 2018 | Shen Z, Formosa T, Tantin D. FACT Inhibition Blocks Induction but not Maintenance of Pluripotency. Stem Cells and Development. PMID 30319048 DOI: 10.1089/Scd.2018.0150 | 0.397 | |||
| 2018 | McCullough LL, Connell Z, Xin H, Studitsky VM, Feofanov AV, Valieva ME, Formosa T. Functional roles of the DNA-binding HMGB domain in the histone chaperone FACT in nucleosome reorganization. The Journal of Biological Chemistry. PMID 29514976 DOI: 10.1074/Jbc.Ra117.000199 | 0.512 | |||
| 2017 | Sdano MA, Fulcher JM, Palani S, Chandrasekharan MB, Parnell TJ, Whitby FG, Formosa T, Hill CP. A novel SH2 recognition mechanism recruits Spt6 to the doubly phosphorylated RNA polymerase II linker at sites of transcription. Elife. 6. PMID 28826505 DOI: 10.7554/Elife.28723 | 0.353 | |||
| 2017 | Hsieh FK, Kozlova AL, Gerasimova NS, Kotova EY, Formosa T, Studitsky VM. Role of the Nhp6 Protein in In Vitro Transcription through the Nucleosome Moscow University Biological Sciences Bulletin. 72: 218-221. DOI: 10.3103/S009639251704006X | 0.511 | |||
| 2016 | Valieva ME, Armeev GA, Kudryashova KS, Gerasimova NS, Shaytan AK, Kulaeva OI, McCullough LL, Formosa T, Georgiev PG, Kirpichnikov MP, Studitsky VM, Feofanov AV. Large-scale ATP-independent nucleosome unfolding by a histone chaperone. Nature Structural & Molecular Biology. PMID 27820806 DOI: 10.1038/Nsmb.3321 | 0.534 | |||
| 2015 | Kemble DJ, McCullough LL, Whitby FG, Formosa T, Hill CP. FACT Disrupts Nucleosome Structure by Binding H2A-H2B with Conserved Peptide Motifs. Molecular Cell. 60: 294-306. PMID 26455391 DOI: 10.1016/J.Molcel.2015.09.008 | 0.385 | |||
| 2015 | McCullough L, Connell Z, Petersen C, Formosa T. The Abundant Histone Chaperones Spt6 and FACT Collaborate to Assemble, Inspect, and Maintain Chromatin Structure in Saccharomyces cerevisiae. Genetics. PMID 26416482 DOI: 10.1534/Genetics.115.180794 | 0.43 | |||
| 2014 | Lee M, Lee CH, Demin AA, Munashingha PR, Amangyeld T, Kwon B, Formosa T, Seo YS. Rad52/Rad59-dependent recombination as a means to rectify faulty Okazaki fragment processing. The Journal of Biological Chemistry. 289: 15064-79. PMID 24711454 DOI: 10.1074/Jbc.M114.548388 | 0.503 | |||
| 2013 | Formosa T. The role of FACT in making and breaking nucleosomes. Biochimica Et Biophysica Acta. 1819: 247-55. PMID 24459727 DOI: 10.1016/j.bbagrm.2011.07.009 | 0.366 | |||
| 2013 | McCullough L, Poe B, Connell Z, Xin H, Formosa T. The FACT histone chaperone guides histone H4 into its nucleosomal conformation in Saccharomyces cerevisiae. Genetics. 195: 101-13. PMID 23833181 DOI: 10.1534/Genetics.113.153080 | 0.451 | |||
| 2013 | Kemble DJ, Whitby FG, Robinson H, McCullough LL, Formosa T, Hill CP. Structure of the Spt16 middle domain reveals functional features of the histone chaperone FACT. The Journal of Biological Chemistry. 288: 10188-94. PMID 23417676 DOI: 10.1074/Jbc.C113.451369 | 0.384 | |||
| 2012 | Stadtmueller BM, Kish-Trier E, Ferrell K, Petersen CN, Robinson H, Myszka DG, Eckert DM, Formosa T, Hill CP. Structure of a proteasome Pba1-Pba2 complex: implications for proteasome assembly, activation, and biological function. The Journal of Biological Chemistry. 287: 37371-82. PMID 22930756 DOI: 10.1074/Jbc.M112.367003 | 0.363 | |||
| 2012 | Formosa T. The role of FACT in making and breaking nucleosomes. Biochimica Et Biophysica Acta. 1819: 247-55. PMID 21807128 DOI: 10.1016/J.Bbagrm.2011.07.009 | 0.46 | |||
| 2011 | McCullough L, Rawlins R, Olsen A, Xin H, Stillman DJ, Formosa T. Insight into the mechanism of nucleosome reorganization from histone mutants that suppress defects in the FACT histone chaperone. Genetics. 188: 835-46. PMID 21625001 DOI: 10.1534/Genetics.111.128769 | 0.502 | |||
| 2011 | Close D, Johnson SJ, Sdano MA, McDonald SM, Robinson H, Formosa T, Hill CP. Crystal structures of the S. cerevisiae Spt6 core and C-terminal tandem SH2 domain. Journal of Molecular Biology. 408: 697-713. PMID 21419780 DOI: 10.1016/J.Jmb.2011.03.002 | 0.414 | |||
| 2011 | Formosa T. A kinase's work is never done: Rad53 monitors chromatin near replication origins. Cell Cycle (Georgetown, Tex.). 10: 573-4. PMID 21311236 DOI: 10.4161/Cc.10.4.14843 | 0.314 | |||
| 2010 | McDonald SM, Close D, Xin H, Formosa T, Hill CP. Structure and biological importance of the Spn1-Spt6 interaction, and its regulatory role in nucleosome binding. Molecular Cell. 40: 725-35. PMID 21094070 DOI: 10.1016/J.Molcel.2010.11.014 | 0.434 | |||
| 2010 | Han J, Li Q, McCullough L, Kettelkamp C, Formosa T, Zhang Z. Ubiquitylation of FACT by the cullin-E3 ligase Rtt101 connects FACT to DNA replication. Genes & Development. 24: 1485-90. PMID 20634314 DOI: 10.1101/Gad.1887310 | 0.547 | |||
| 2010 | Formosa T. Avoiding a fatal attraction: properties of nucleosomes and a histone chaperone revealed under physiological conditions. Molecular Cell. 37: 747-8. PMID 20347417 DOI: 10.1016/J.Molcel.2010.02.016 | 0.367 | |||
| 2010 | Sadre-Bazzaz K, Whitby FG, Robinson H, Formosa T, Hill CP. Structure of a Blm10 complex reveals common mechanisms for proteasome binding and gate opening. Molecular Cell. 37: 728-35. PMID 20227375 DOI: 10.1016/J.Molcel.2010.02.002 | 0.337 | |||
| 2009 | Xin H, Takahata S, Blanksma M, McCullough L, Stillman DJ, Formosa T. yFACT induces global accessibility of nucleosomal DNA without H2A-H2B displacement. Molecular Cell. 35: 365-76. PMID 19683499 DOI: 10.1016/J.Molcel.2009.06.024 | 0.459 | |||
| 2008 | Formosa T. FACT and the reorganized nucleosome. Molecular Biosystems. 4: 1085-93. PMID 18931784 DOI: 10.1039/B812136B | 0.486 | |||
| 2008 | Biswas D, Takahata S, Xin H, Dutta-Biswas R, Yu Y, Formosa T, Stillman DJ. A role for Chd1 and Set2 in negatively regulating DNA replication in Saccharomyces cerevisiae. Genetics. 178: 649-59. PMID 18245327 DOI: 10.1534/Genetics.107.084202 | 0.502 | |||
| 2008 | VanDemark AP, Xin H, McCullough L, Rawlins R, Bentley S, Heroux A, Stillman DJ, Hill CP, Formosa T. Structural and functional analysis of the Spt16p N-terminal domain reveals overlapping roles of yFACT subunits. The Journal of Biological Chemistry. 283: 5058-68. PMID 18089575 DOI: 10.1074/Jbc.M708682200 | 0.402 | |||
| 2007 | VanDemark AP, Blanksma M, Ferris E, Heroux A, Hill CP, Formosa T. The Structure of the yFACT Pob3-M Domain, Its Interaction with the DNA Replication Factor RPA, and a Potential Role in Nucleosome Deposition (DOI:10.1016/j.molcel.2006.03.025) Molecular Cell. 27: 171-172. DOI: 10.1016/J.Molcel.2007.06.007 | 0.407 | |||
| 2006 | McCullock S, Kinard T, McCullough L, Formosa T. blm3-1 is an allele of UBP3, a ubiquitin protease that appears to act during transcription of damaged DNA. Journal of Molecular Biology. 363: 660-72. PMID 16997324 DOI: 10.1016/J.Jmb.2006.08.073 | 0.514 | |||
| 2006 | Biswas D, Dutta-Biswas R, Mitra D, Shibata Y, Strahl BD, Formosa T, Stillman DJ. Opposing roles for Set2 and yFACT in regulating TBP binding at promoters. The Embo Journal. 25: 4479-89. PMID 16977311 DOI: 10.1038/Sj.Emboj.7601333 | 0.406 | |||
| 2006 | Iwanczyk J, Sadre-Bazzaz K, Ferrell K, Kondrashkina E, Formosa T, Hill CP, Ortega J. Structure of the Blm10-20 S proteasome complex by cryo-electron microscopy. Insights into the mechanism of activation of mature yeast proteasomes. Journal of Molecular Biology. 363: 648-59. PMID 16952374 DOI: 10.1016/J.Jmb.2006.08.010 | 0.391 | |||
| 2006 | VanDemark AP, Blanksma M, Ferris E, Heroux A, Hill CP, Formosa T. The structure of the yFACT Pob3-M domain, its interaction with the DNA replication factor RPA, and a potential role in nucleosome deposition. Molecular Cell. 22: 363-74. PMID 16678108 DOI: 10.1016/J.Molcel.2006.03.025 | 0.545 | |||
| 2005 | Biswas D, Yu Y, Prall M, Formosa T, Stillman DJ. The yeast FACT complex has a role in transcriptional initiation. Molecular and Cellular Biology. 25: 5812-22. PMID 15987999 DOI: 10.1128/Mcb.25.14.5812-5822.2005 | 0.496 | |||
| 2004 | Rhoades AR, Ruone S, Formosa T. Structural features of nucleosomes reorganized by yeast FACT and its HMG box component, Nhp6. Molecular and Cellular Biology. 24: 3907-17. PMID 15082784 DOI: 10.1128/Mcb.24.9.3907-3917.2004 | 0.521 | |||
| 2003 | Ruone S, Rhoades AR, Formosa T. Multiple Nhp6 molecules are required to recruit Spt16-Pob3 to form yFACT complexes and to reorganize nucleosomes. The Journal of Biological Chemistry. 278: 45288-95. PMID 12952948 DOI: 10.1074/Jbc.M307291200 | 0.506 | |||
| 2003 | Formosa T. Changing the DNA landscape: Putting a SPN on chromatin Current Topics in Microbiology and Immunology. 274: 171-201. PMID 12596908 DOI: 10.1007/978-3-642-55747-7_7 | 0.47 | |||
| 2002 | Formosa T, Ruone S, Adams MD, Olsen AE, Eriksson P, Yu Y, Rhoades AR, Kaufman PD, Stillman DJ. Defects in SPT16 or POB3 (yFACT) in Saccharomyces cerevisiae cause dependence on the Hir/Hpc pathway: polymerase passage may degrade chromatin structure. Genetics. 162: 1557-71. PMID 12524332 | 0.396 | |||
| 2001 | Formosa T, Eriksson P, Wittmeyer J, Ginn J, Yu Y, Stillman DJ. Spt16-Pob3 and the HMG protein Nhp6 combine to form the nucleosome-binding factor SPN Embo Journal. 20: 3506-3517. PMID 11432837 DOI: 10.1093/Emboj/20.13.3506 | 0.561 | |||
| 2000 | Schlesinger MB, Formosa T. POB3 is required for both transcription and replication in the yeast Saccharomyces cerevisiae. Genetics. 155: 1593-606. PMID 10924459 | 0.693 | |||
| 1999 | Wittmeyer J, Joss L, Formosa T. Spt16 and Pob3 of Saccharomyces cerevisiae form an essential, abundant heterodimer that is nuclear, chromatin-associated, and copurifies with DNA polymerase α Biochemistry. 38: 8961-8971. PMID 10413469 DOI: 10.1021/Bi982851D | 0.522 | |||
| 1999 | Formosa T, Nittis T. Dna2 mutants reveal interactions with Dna polymerase α and Ctf4, a Pol α accessory factor, and show that full Dna2 helicase activity is not essential for growth Genetics. 151: 1459-1470. PMID 10101169 | 0.404 | |||
| 1998 | Formosa T, Nittis T. Suppressors of the temperature sensitivity of DNA polymerase α mutations in Saccharomyces cerevisiae Molecular and General Genetics. 257: 461-468. PMID 9529527 DOI: 10.1007/s004380050670 | 0.386 | |||
| 1997 | Wittmeyer J, Formosa T. The Saccharomyces cerevisiae DNA polymerase α catalytic subunit interacts with Cdc68/Spt16 and with Pob3, a protein similar to an HMG1-like protein Molecular and Cellular Biology. 17: 4178-4190. PMID 9199353 DOI: 10.1128/Mcb.17.7.4178 | 0.524 | |||
| 1996 | Singer JD, Manning BM, Formosa T. Coordinating DNA replication to produce one copy of the genome requires genes that act in ubiquitin metabolism. Molecular and Cellular Biology. 16: 1356-66. PMID 8657109 DOI: 10.1128/Mcb.16.4.1356 | 0.477 | |||
| 1995 | Wittmeyer J, Formosa T. Identifying DNA replication complex components using protein affinity chromatography Methods in Enzymology. 262: 415-430. PMID 8594365 DOI: 10.1016/0076-6879(95)62033-8 | 0.455 | |||
| 1992 | Miles J, Formosa T. Protein affinity chromatography with purified yeast DNA polymerase α detects proteins that bind to DNA polymerase Proceedings of the National Academy of Sciences of the United States of America. 89: 1276-1280. PMID 1741381 DOI: 10.1073/Pnas.89.4.1276 | 0.503 | |||
| 1992 | Miles J, Formosa T. Evidence that POB1, a Saccharomyces cerevisiae protein that binds to DNA polymerase α, acts in DNA metabolism in vivo Molecular and Cellular Biology. 12: 5724-5735. PMID 1448101 DOI: 10.1128/Mcb.12.12.5724 | 0.515 | |||
| 1991 | Formosa T, Barry J, Alberts BM, Greenblatt J. Using protein affinity chromatography to probe structure of protein machines Methods in Enzymology. 208: 24-45. PMID 1779837 DOI: 10.1016/0076-6879(91)08005-3 | 0.501 | |||
| 1986 | Formosa T, Alberts BM. DNA synthesis dependent on genetic recombination: Characterization of a reaction catalyzed by purified bacteriophage T4 proteins Cell. 47: 793-806. PMID 3022939 DOI: 10.1016/0092-8674(86)90522-2 | 0.616 | |||
| 1986 | Formosa T, Alberts BM. Purification and characterization of the T4 bacteriophage uvsX protein Journal of Biological Chemistry. 261: 6107-6118. PMID 2939071 | 0.427 | |||
| 1985 | Griffith J, Formosa T. The uvsX protein of bacteriophage T4 arranges single-stranded and double-stranded DNA into similar helical nucleoprotein filaments Journal of Biological Chemistry. 260: 4484-4491. PMID 3156858 | 0.403 | |||
| 1985 | Formosa T, Alberts BM. Recombination-dependent initiation of DNA synthesis in vitro by a novel mechanism Federation Proceedings. 44: No. 1431. | 0.325 | |||
| 1984 | Formosa T, Alberts BM. The use of affinity chromatography to study proteins involved in bacteriophage T4 genetic recombination Cold Spring Harbor Symposia On Quantitative Biology. 363-370. PMID 6335687 DOI: 10.1101/Sqb.1984.049.01.043 | 0.53 | |||
| 1984 | Jongeneel CV, Formosa T, Munn M, Alberts BM. Enzymological studies of the T4 replication proteins Advances in Experimental Medicine and Biology. 179: 17-33. PMID 6098151 DOI: 10.1007/978-1-4684-8730-5_2 | 0.602 | |||
| 1984 | Jongeneel CV, Formosa T, Alberts BM. Purification and characterization of the bacteriophage T4 dda protein. A DNA helicase that associates with the viral helix-destabilizing protein Journal of Biological Chemistry. 259: 12925-12932. PMID 6092351 | 0.434 | |||
| 1983 | Formosa T, Burke RL, Alberts BM. Affinity purification of bacteriophage T4 proteins essential for DNA replication and genetic recombination Proceedings of the National Academy of Sciences of the United States of America. 80: 2442-2446. PMID 6302682 DOI: 10.1073/Pnas.80.9.2442 | 0.602 | |||
| 1982 | Alberts BM, Barry J, Bedinger P, Formosa T, Jongeneel CV, Kreuzer KN. Studies on DNA replication in the bacteriophage T4 in vitro system Cold Spring Harbor Symposia On Quantitative Biology. 47: 655-668. PMID 6305581 DOI: 10.1101/Sqb.1983.047.01.077 | 0.588 | |||
| Low-probability matches (unlikely to be authored by this person) | |||||
| 2017 | Sdano MA, Fulcher JM, Palani S, Chandrasekharan MB, Parnell TJ, Whitby FG, Formosa T, Hill CP. Author response: A novel SH2 recognition mechanism recruits Spt6 to the doubly phosphorylated RNA polymerase II linker at sites of transcription Elife. DOI: 10.7554/Elife.28723.033 | 0.288 | |||
| 2018 | Formosa T, Spies M. Decision letter: Dissociation rate compensation mechanism for budding yeast pioneer transcription factors Elife. DOI: 10.7554/Elife.43008.030 | 0.285 | |||
| 2019 | Chun Y, Joo YJ, Suh H, Batot G, Hill CP, Formosa T, Buratowski S. Selective kinase inhibition shows that Bur1 (Cdk9) phosphorylates the Rpb1 linker in vivo. Molecular and Cellular Biology. PMID 31085683 DOI: 10.1128/Mcb.00602-18 | 0.283 | |||
| 2019 | Formosa T, Gartenberg M. Decision letter: Epigenetic memory independent of symmetric histone inheritance Elife. DOI: 10.7554/Elife.51421.029 | 0.281 | |||
| 2018 | Nune M, Morgan MT, Connell Z, McCullough L, Jbara M, Sun H, Brik A, Formosa T, Wolberger C. Author response: FACT and Ubp10 collaborate to modulate H2B deubiquitination and nucleosome dynamics Elife. DOI: 10.7554/Elife.40988.022 | 0.243 | |||
| 2020 | Formosa T, Kamakaka RT, Moazed D. Decision letter: S-phase-independent silencing establishment in Saccharomyces cerevisiae Elife. DOI: 10.7554/Elife.58910.Sa1 | 0.239 | |||
| 1996 | Demianova M, Formosa TG, Ellis SR. Yeast proteins related to the p40/laminin receptor precursor are essential components of the 40 S ribosomal subunit Journal of Biological Chemistry. 271: 11383-11391. PMID 8626693 DOI: 10.1074/jbc.271.19.11383 | 0.227 | |||
| 2006 | Ortega J, Iwanczyk J, Sadre-Bazzaz K, Ferrell K, Kondrashkina E, Formosa T, Hill CP. Structure of the Blm10-20S proteasome complex by single particle cryo electron microscopy Microscopy and Microanalysis. 12: 372-373. DOI: 10.1017/S1431927606061484 | 0.223 | |||
| 2019 | McCullough LL, Pham TH, Parnell TJ, Connell Z, Chandrasekharan MB, Stillman DJ, Formosa T. Supplemental Material for McCullough et al., 2019 Genetics. DOI: 10.25386/Genetics.7586207.V3 | 0.177 | |||
| 2022 | Colbert-Getz JM, Lindsley J, Moore KB, Formosa T, Pippitt K. Promotion of a Mastery Orientation to Learning in Medical School: Implementation of the Not Yet Pass Grade. Academic Medicine : Journal of the Association of American Medical Colleges. 98: 52-56. PMID 36576767 DOI: 10.1097/ACM.0000000000005002 | 0.026 | |||
| 2022 | Pippitt KA, Moore KB, Lindsley JE, Cariello PF, Smith AG, Formosa T, Moser K, Morton DA, Colbert-Getz JM, Chow CJ. Assessment for Learning with Ungraded and Graded Assessments. Medical Science Educator. 32: 1045-1054. PMID 36276764 DOI: 10.1007/s40670-022-01612-y | 0.012 | |||
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