Year |
Citation |
Score |
2016 |
Sleven H, Welsh SJ, Yu J, Churchill ME, Wright CF, Henderson A, Horvath R, Rankin J, Vogt J, Magee A, McConnell V, Green A, King MD, Cox H, Armstrong L, et al. De Novo Mutations in EBF3 Cause a Neurodevelopmental Syndrome. American Journal of Human Genetics. PMID 28017370 DOI: 10.1016/J.Ajhg.2016.11.020 |
0.321 |
|
2016 |
Malarkey CS, Gustafson CE, Saifee JF, Torres RM, Churchill ME, Janoff EN. Mechanism of Mitochondrial Transcription Factor A Attenuation of CpG-Induced Antibody Production. Plos One. 11: e0157157. PMID 27280778 DOI: 10.1371/Journal.Pone.0157157 |
0.34 |
|
2016 |
Malarkey CS, Lionetti C, Deceglie S, Roberti M, Churchill ME, Cantatore P, Polosa PL. The sea urchin mitochondrial transcription factor A binds and bends DNA efficiently despite its unusually short C-terminal tail. Mitochondrion. PMID 27101895 DOI: 10.1016/J.Mito.2016.04.004 |
0.508 |
|
2016 |
Horita H, Wysoczynski CL, Walker LA, Moulton KS, Li M, Ostriker A, Tucker R, McKinsey TA, Churchill ME, Nemenoff RA, Weiser-Evans MC. Nuclear PTEN functions as an essential regulator of SRF-dependent transcription to control smooth muscle differentiation. Nature Communications. 7: 10830. PMID 26940659 DOI: 10.1038/Ncomms10830 |
0.324 |
|
2015 |
Sánchez-Giraldo R, Acosta-Reyes FJ, Malarkey CS, Saperas N, Churchill ME, Campos JL. Two high-mobility group box domains act together to underwind and kink DNA. Acta Crystallographica. Section D, Biological Crystallography. 71: 1423-32. PMID 26143914 DOI: 10.1107/S1399004715007452 |
0.566 |
|
2015 |
Miknis GF, Stevens SJ, Smith LE, Ostrov DA, Churchill ME. Development of novel Asf1-H3/H4 inhibitors. Bioorganic & Medicinal Chemistry Letters. 25: 963-8. PMID 25582598 DOI: 10.1016/J.Bmcl.2014.11.067 |
0.322 |
|
2014 |
Das C, Roy S, Namjoshi S, Malarkey CS, Jones DN, Kutateladze TG, Churchill ME, Tyler JK. Binding of the histone chaperone ASF1 to the CBP bromodomain promotes histone acetylation. Proceedings of the National Academy of Sciences of the United States of America. 111: E1072-81. PMID 24616510 DOI: 10.1073/Pnas.1319122111 |
0.36 |
|
2013 |
Wysoczynski CL, Roemer SC, Dostal V, Barkley RM, Churchill ME, Malarkey CS. Reversed-phase ion-pair liquid chromatography method for purification of duplex DNA with single base pair resolution. Nucleic Acids Research. 41: e194. PMID 24013567 DOI: 10.1093/Nar/Gkt815 |
0.515 |
|
2013 |
Razzaghi H, Tempczyk-Russell A, Haubold K, Santorico SA, Shokati T, Christians U, Churchill ME. Genetic and structure-function studies of missense mutations in human endothelial lipase. Plos One. 8: e55716. PMID 23536757 DOI: 10.1371/Journal.Pone.0055716 |
0.305 |
|
2013 |
Dennehey BK, Noone S, Liu WH, Smith L, Churchill ME, Tyler JK. The C terminus of the histone chaperone Asf1 cross-links to histone H3 in yeast and promotes interaction with histones H3 and H4. Molecular and Cellular Biology. 33: 605-21. PMID 23184661 DOI: 10.1128/Mcb.01053-12 |
0.348 |
|
2012 |
Malarkey CS, Churchill ME. The high mobility group box: the ultimate utility player of a cell. Trends in Biochemical Sciences. 37: 553-62. PMID 23153957 DOI: 10.1016/J.Tibs.2012.09.003 |
0.545 |
|
2012 |
Liu WH, Roemer SC, Port AM, Churchill ME. CAF-1-induced oligomerization of histones H3/H4 and mutually exclusive interactions with Asf1 guide H3/H4 transitions among histone chaperones and DNA. Nucleic Acids Research. 40: 11229-39. PMID 23034810 DOI: 10.1093/Nar/Gks906 |
0.345 |
|
2012 |
Scorgie JK, Donham DC, Churchill ME. Analysis of histone chaperone antisilencing function 1 interactions. Methods in Enzymology. 512: 223-41. PMID 22910209 DOI: 10.1016/B978-0-12-391940-3.00010-X |
0.419 |
|
2012 |
Zan J, Cicirelli EM, Mohamed NM, Sibhatu H, Kroll S, Choi O, Choi O, Uhlson CL, Wysoczynski CL, Wysoczinski CL, Murphy RC, Churchill ME, Hill RT, Fuqua C. A complex LuxR-LuxI type quorum sensing network in a roseobacterial marine sponge symbiont activates flagellar motility and inhibits biofilm formation. Molecular Microbiology. 85: 916-33. PMID 22742196 DOI: 10.1111/J.1365-2958.2012.08149.X |
0.308 |
|
2012 |
Liu WH, Churchill ME. Histone transfer among chaperones. Biochemical Society Transactions. 40: 357-63. PMID 22435812 DOI: 10.1042/Bst20110737 |
0.334 |
|
2012 |
Malarkey CS, Bestwick M, Kuhlwilm JE, Shadel GS, Churchill ME. Transcriptional activation by mitochondrial transcription factor A involves preferential distortion of promoter DNA. Nucleic Acids Research. 40: 614-24. PMID 21948790 DOI: 10.1093/Nar/Gkr787 |
0.528 |
|
2012 |
Hill KK, Roemer SC, Churchill ME, Edwards DP. Structural and functional analysis of domains of the progesterone receptor. Molecular and Cellular Endocrinology. 348: 418-29. PMID 21803119 DOI: 10.1016/J.Mce.2011.07.017 |
0.493 |
|
2011 |
Pollock DD, de Koning AP, Kim H, Castoe TA, Churchill ME, Kechris KJ. Bayesian analysis of high-throughput quantitative measurement of protein-DNA interactions. Plos One. 6: e26105. PMID 22069446 DOI: 10.1371/Journal.Pone.0026105 |
0.468 |
|
2011 |
Lintz MJ, Oinuma K, Wysoczynski CL, Greenberg EP, Churchill ME. Crystal structure of QscR, a Pseudomonas aeruginosa quorum sensing signal receptor. Proceedings of the National Academy of Sciences of the United States of America. 108: 15763-8. PMID 21911405 DOI: 10.1073/Pnas.1112398108 |
0.475 |
|
2011 |
Donham DC, Scorgie JK, Churchill ME. The activity of the histone chaperone yeast Asf1 in the assembly and disassembly of histone H3/H4-DNA complexes. Nucleic Acids Research. 39: 5449-58. PMID 21447559 DOI: 10.1093/Nar/Gkr097 |
0.41 |
|
2011 |
Pascreau G, Churchill ME, Maller JL. Centrosomal localization of cyclins E and A: structural similarities and functional differences. Cell Cycle (Georgetown, Tex.). 10: 199-205. PMID 21217199 DOI: 10.4161/Cc.10.2.14444 |
0.409 |
|
2011 |
Churchill ME, Chen L. Structural basis of acyl-homoserine lactone-dependent signaling. Chemical Reviews. 111: 68-85. PMID 21125993 DOI: 10.1021/Cr1000817 |
0.392 |
|
2011 |
Churchill ME, Sibhatu HM, Uhlson CL. Defining the structure and function of acyl-homoserine lactone autoinducers. Methods in Molecular Biology (Clifton, N.J.). 692: 159-71. PMID 21031311 DOI: 10.1007/978-1-60761-971-0_12 |
0.3 |
|
2010 |
Churchill ME, Klass J, Zoetewey DL. Structural analysis of HMGD-DNA complexes reveals influence of intercalation on sequence selectivity and DNA bending. Journal of Molecular Biology. 403: 88-102. PMID 20800069 DOI: 10.1016/J.Jmb.2010.08.031 |
0.58 |
|
2010 |
Das C, Tyler JK, Churchill ME. The histone shuffle: histone chaperones in an energetic dance. Trends in Biochemical Sciences. 35: 476-89. PMID 20444609 DOI: 10.1016/J.Tibs.2010.04.001 |
0.328 |
|
2010 |
Pascreau G, Eckerdt F, Churchill ME, Maller JL. Discovery of a distinct domain in cyclin A sufficient for centrosomal localization independently of Cdk binding. Proceedings of the National Academy of Sciences of the United States of America. 107: 2932-7. PMID 20133761 DOI: 10.1073/Pnas.0914874107 |
0.392 |
|
2009 |
Hill KK, Roemer SC, Jones DN, Churchill ME, Edwards DP. A progesterone receptor co-activator (JDP2) mediates activity through interaction with residues in the carboxyl-terminal extension of the DNA binding domain. The Journal of Biological Chemistry. 284: 24415-24. PMID 19553667 DOI: 10.1074/Jbc.M109.003244 |
0.453 |
|
2009 |
Gangelhoff TA, Mungalachetty PS, Nix JC, Churchill ME. Structural analysis and DNA binding of the HMG domains of the human mitochondrial transcription factor A. Nucleic Acids Research. 37: 3153-64. PMID 19304746 DOI: 10.1093/Nar/Gkp157 |
0.527 |
|
2008 |
Roemer SC, Adelman J, Churchill ME, Edwards DP. Mechanism of high-mobility group protein B enhancement of progesterone receptor sequence-specific DNA binding. Nucleic Acids Research. 36: 3655-66. PMID 18474528 DOI: 10.1093/Nar/Gkn249 |
0.555 |
|
2007 |
Kao DJ, Churchill ME, Irvin RT, Hodges RS. Animal protection and structural studies of a consensus sequence vaccine targeting the receptor binding domain of the type IV pilus of Pseudomonas aeruginosa. Journal of Molecular Biology. 374: 426-42. PMID 17936788 DOI: 10.1016/J.Jmb.2007.09.032 |
0.326 |
|
2006 |
English CM, Adkins MW, Carson JJ, Churchill ME, Tyler JK. Structural basis for the histone chaperone activity of Asf1. Cell. 127: 495-508. PMID 17081973 DOI: 10.1016/J.Cell.2006.08.047 |
0.317 |
|
2006 |
Roemer SC, Donham DC, Sherman L, Pon VH, Edwards DP, Churchill ME. Structure of the progesterone receptor-deoxyribonucleic acid complex: novel interactions required for binding to half-site response elements. Molecular Endocrinology (Baltimore, Md.). 20: 3042-52. PMID 16931575 DOI: 10.1210/Me.2005-0511 |
0.512 |
|
2006 |
Gould TA, Herman J, Krank J, Murphy RC, Churchill ME. Specificity of acyl-homoserine lactone synthases examined by mass spectrometry. Journal of Bacteriology. 188: 773-83. PMID 16385066 DOI: 10.1128/Jb.188.2.773-783.2006 |
0.313 |
|
2005 |
English CM, Maluf NK, Tripet B, Churchill ME, Tyler JK. ASF1 binds to a heterodimer of histones H3 and H4: a two-step mechanism for the assembly of the H3-H4 heterotetramer on DNA. Biochemistry. 44: 13673-82. PMID 16229457 DOI: 10.1021/Bi051333H |
0.325 |
|
2005 |
Eyers PA, Churchill ME, Maller JL. The Aurora A and Aurora B protein kinases: a single amino acid difference controls intrinsic activity and activation by TPX2. Cell Cycle (Georgetown, Tex.). 4: 784-9. PMID 15908779 DOI: 10.4161/Cc.4.6.1693 |
0.334 |
|
2004 |
Gould TA, Schweizer HP, Churchill ME. Structure of the Pseudomonas aeruginosa acyl-homoserinelactone synthase LasI. Molecular Microbiology. 53: 1135-46. PMID 15306017 DOI: 10.1111/J.1365-2958.2004.04211.X |
0.399 |
|
2004 |
Melvin VS, Harrell C, Adelman JS, Kraus WL, Churchill M, Edwards DP. The role of the C-terminal extension (CTE) of the estrogen receptor alpha and beta DNA binding domain in DNA binding and interaction with HMGB. The Journal of Biological Chemistry. 279: 14763-71. PMID 14739282 DOI: 10.1074/Jbc.M313335200 |
0.515 |
|
2003 |
Klass J, Murphy FV, Fouts S, Serenil M, Changela A, Siple J, Churchill ME. The role of intercalating residues in chromosomal high-mobility-group protein DNA binding, bending and specificity. Nucleic Acids Research. 31: 2852-64. PMID 12771212 DOI: 10.1093/Nar/Gkg389 |
0.752 |
|
2003 |
Thomas CB, Scavetta RD, Gumport RI, Churchill ME. Structures of liganded and unliganded RsrI N6-adenine DNA methyltransferase: a distinct orientation for active cofactor binding. The Journal of Biological Chemistry. 278: 26094-101. PMID 12732637 DOI: 10.1074/Jbc.M303751200 |
0.456 |
|
2002 |
Melvin VS, Roemer SC, Churchill ME, Edwards DP. The C-terminal extension (CTE) of the nuclear hormone receptor DNA binding domain determines interactions and functional response to the HMGB-1/-2 co-regulatory proteins. The Journal of Biological Chemistry. 277: 25115-24. PMID 12006575 DOI: 10.1074/Jbc.M110400200 |
0.486 |
|
2002 |
Watson WT, Minogue TD, Val DL, von Bodman SB, Churchill ME. Structural basis and specificity of acyl-homoserine lactone signal production in bacterial quorum sensing. Molecular Cell. 9: 685-94. PMID 11931774 DOI: 10.1016/S1097-2765(02)00480-X |
0.373 |
|
2001 |
Watson WT, Murphy FV, Gould TA, Jambeck P, Val DL, Cronan JE, Beck von Bodman S, Churchill ME. Crystallization and rhenium MAD phasing of the acyl-homoserinelactone synthase EsaI. Acta Crystallographica. Section D, Biological Crystallography. 57: 1945-9. PMID 11717525 DOI: 10.1107/S0907444901014512 |
0.642 |
|
2000 |
Scavetta RD, Thomas CB, Walsh MA, Szegedi S, Joachimiak A, Gumport RI, Churchill ME. Structure of RsrI methyltransferase, a member of the N6-adenine beta class of DNA methyltransferases. Nucleic Acids Research. 28: 3950-61. PMID 11024175 DOI: 10.1093/Nar/28.20.3950 |
0.496 |
|
2000 |
Dow LK, Jones DN, Wolfe SA, Verdine GL, Churchill ME. Structural studies of the high mobility group globular domain and basic tail of HMG-D bound to disulfide cross-linked DNA. Biochemistry. 39: 9725-36. PMID 10933789 DOI: 10.1021/Bi000723V |
0.578 |
|
2000 |
Murphy FV, Churchill ME. Nonsequence-specific DNA recognition: a structural perspective. Structure (London, England : 1993). 8: R83-9. PMID 10801483 DOI: 10.1016/S0969-2126(00)00126-X |
0.737 |
|
1999 |
Murphy FV, Sweet RM, Churchill ME. The structure of a chromosomal high mobility group protein-DNA complex reveals sequence-neutral mechanisms important for non-sequence-specific DNA recognition. The Embo Journal. 18: 6610-8. PMID 10581235 DOI: 10.1093/Emboj/18.23.6610 |
0.752 |
|
1999 |
Murphy FV, Sehy JV, Dow LK, Gao YG, Churchill ME. Co-crystallization and preliminary crystallographic analysis of the high mobility group domain of HMG-D bound to DNA. Acta Crystallographica. Section D, Biological Crystallography. 55: 1594-7. PMID 10489457 DOI: 10.1107/S0907444999008240 |
0.732 |
|
1999 |
Churchill ME, Changela A, Dow LK, Krieg AJ. Interactions of high mobility group box proteins with DNA and chromatin. Methods in Enzymology. 304: 99-133. PMID 10372358 DOI: 10.1016/S0076-6879(99)04009-4 |
0.517 |
|
1998 |
Kuo MH, Zhou J, Jambeck P, Churchill ME, Allis CD. Histone acetyltransferase activity of yeast Gcn5p is required for the activation of target genes in vivo. Genes & Development. 12: 627-39. PMID 9499399 DOI: 10.1101/Gad.12.5.627 |
0.306 |
|
1997 |
Dow LK, Changela A, Hefner HE, Churchill ME. Oxidation of a critical methionine modulates DNA binding of the Drosophila melanogaster high mobility group protein, HMG-D. Febs Letters. 414: 514-20. PMID 9323026 DOI: 10.1016/S0014-5793(97)01059-4 |
0.535 |
|
1996 |
Churchill ME. The latest on DNA form and function. Chemistry & Biology. 3: 729-30. PMID 8939688 DOI: 10.1016/S1074-5521(96)90248-3 |
0.476 |
|
1995 |
Wolfe SA, Ferentz AE, Grantcharova V, Churchill ME, Verdine GL. Modifying the helical structure of DNA by design: recruitment of an architecture-specific protein to an enforced DNA bend. Chemistry & Biology. 2: 213-21. PMID 9383423 DOI: 10.1016/1074-5521(95)90271-6 |
0.556 |
|
1995 |
Churchill ME, Jones DN, Glaser T, Hefner H, Searles MA, Travers AA. HMG-D is an architecture-specific protein that preferentially binds to DNA containing the dinucleotide TG. The Embo Journal. 14: 1264-75. PMID 7720717 |
0.451 |
|
1995 |
Wang AH, Churchill ME. Bite-size DNA Nature Structural & Molecular Biology. 2: 934-936. DOI: 10.1038/Nsb1195-934 |
0.441 |
|
1994 |
Travers AA, Ner SS, Churchill ME. DNA chaperones: a solution to a persistence problem? Cell. 77: 167-9. PMID 8168125 DOI: 10.1016/0092-8674(94)90306-9 |
0.516 |
|
1994 |
Ner SS, Travers AA, Churchill ME. Harnessing the writhe: a role for DNA chaperones in nucleoprotein-complex formation. Trends in Biochemical Sciences. 19: 185-7. PMID 8048157 DOI: 10.1016/0968-0004(94)90017-5 |
0.462 |
|
1994 |
Jones DN, Searles MA, Shaw GL, Churchill ME, Ner SS, Keeler J, Travers AA, Neuhaus D. The solution structure and dynamics of the DNA-binding domain of HMG-D from Drosophila melanogaster. Structure (London, England : 1993). 2: 609-27. PMID 7922039 DOI: 10.1016/S0969-2126(00)00063-0 |
0.432 |
|
1993 |
Ner SS, Churchill ME, Searles MA, Travers AA. dHMG-Z, a second HMG-1-related protein in Drosophila melanogaster. Nucleic Acids Research. 21: 4369-71. PMID 8414994 DOI: 10.1093/Nar/21.18.4369 |
0.362 |
|
1991 |
Churchill ME, Travers AA. Protein motifs that recognize structural features of DNA. Trends in Biochemical Sciences. 16: 92-7. PMID 1647556 DOI: 10.1016/0968-0004(91)90040-3 |
0.477 |
|
1990 |
Churchill ME, Schmitz AM, Peak JG, Peak MJ. Photosensitized damage to supercoiled plasmid DNA induced by 334-nm radiation in the presence of 2-thiouracil consists of alkali- and piperidine-labile sites as well as frank strand breaks. Photochemistry and Photobiology. 52: 1017-23. PMID 2287632 DOI: 10.1111/j.1751-1097.1990.tb01819.x |
0.303 |
|
1990 |
Guo Q, Lu M, Churchill ME, Tullius TD, Kallenbach NR. Asymmetric structure of a three-arm DNA junction. Biochemistry. 29: 10927-34. PMID 2176888 DOI: 10.1021/Bi00501A010 |
0.662 |
|
1990 |
Churchill ME, Tullius TD, Klug A. Mode of interaction of the zinc finger protein TFIIIA with a 5S RNA gene of Xenopus. Proceedings of the National Academy of Sciences of the United States of America. 87: 5528-32. PMID 2164687 DOI: 10.1073/Pnas.87.14.5528 |
0.743 |
|
1989 |
Churchill M, Suzuki M. ‘SPKK’ motifs prefer to bind to DNA at A/T-rich sites. The Embo Journal. 8: 4189-4195. DOI: 10.1002/J.1460-2075.1989.Tb08604.X |
0.503 |
|
1988 |
Churchill ME, Tullius TD, Kallenbach NR, Seeman NC. A Holliday recombination intermediate is twofold symmetric. Proceedings of the National Academy of Sciences of the United States of America. 85: 4653-6. PMID 3387432 DOI: 10.1073/Pnas.85.13.4653 |
0.665 |
|
1988 |
Chen JH, Churchill ME, Tullius TD, Kallenbach NR, Seeman NC. Construction and analysis of monomobile DNA junctions. Biochemistry. 27: 6032-8. PMID 3191106 DOI: 10.1021/Bi00416A031 |
0.648 |
|
1988 |
Vrana KE, Churchill ME, Tullius TD, Brown DD. Mapping functional regions of transcription factor TFIIIA. Molecular and Cellular Biology. 8: 1684-96. PMID 2837652 DOI: 10.1128/Mcb.8.4.1684 |
0.681 |
|
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