| Year |
Citation |
Score |
| 2019 |
Sivapragasam S, Grove A. The Link between Purine Metabolism and Production of Antibiotics in . Antibiotics (Basel, Switzerland). 8. PMID 31174282 DOI: 10.3390/Antibiotics8020076 |
0.302 |
|
| 2019 |
Deochand DK, Pande A, Meariman JK, Grove A. Redox Sensing by PecS from the Plant Pathogen Pectobacterium atrosepticum and Its Effect on Gene Expression and the Conformation of PecS-Bound Promoter DNA. Biochemistry. PMID 31046241 DOI: 10.1021/Acs.Biochem.9B00288 |
0.482 |
|
| 2019 |
Bhattacharyya N, Lemon TL, Grove A. A role for Vibrio vulnificus PecS during hypoxia. Scientific Reports. 9: 2797. PMID 30808913 DOI: 10.1038/S41598-019-39095-4 |
0.382 |
|
| 2018 |
Pande A, Veale TC, Grove A. Gene regulation by redox-sensitive OhrR and its role in bacterial killing of . Infection and Immunity. PMID 29967095 DOI: 10.1128/Iai.00322-18 |
0.396 |
|
| 2017 |
Sivapragasam S, Deochand DK, Meariman JK, Grove A. Stringent response induced by phosphate limitation promotes purine salvage in Agrobacterium fabrum. Biochemistry. PMID 29027458 DOI: 10.1021/Acs.Biochem.7B00844 |
0.369 |
|
| 2017 |
Grove A. Control of RNA polymerase II-transcribed genes by direct binding of TOR kinase. Current Genetics. PMID 28831551 DOI: 10.1007/S00294-017-0738-Z |
0.398 |
|
| 2017 |
Panday A, Gupta A, Srinivasa K, Xiao L, Smith MD, Grove A. DNA damage regulates direct association of TOR kinase with the RNA polymerase II-transcribed HMO1 gene. Molecular Biology of the Cell. PMID 28701348 DOI: 10.1091/Mbc.E17-01-0024 |
0.433 |
|
| 2017 |
Grove A. Regulation of Metabolic Pathways by MarR Family Transcription Factors. Computational and Structural Biotechnology Journal. 15: 366-371. PMID 28694934 DOI: 10.1016/J.Csbj.2017.06.001 |
0.327 |
|
| 2017 |
Gupta A, Fuentes SM, Grove A. Redox-sensitive MarR homolog BifR from Burkholderia thailandensis regulates biofilm formation. Biochemistry. PMID 28406615 DOI: 10.1021/Acs.Biochem.7B00103 |
0.329 |
|
| 2017 |
Panday A, Xiao L, Gupta A, Grove A. Control of DNA end resection by yeast Hmo1p affects efficiency of DNA end-joining. Dna Repair. PMID 28336179 DOI: 10.1016/J.Dnarep.2017.03.002 |
0.503 |
|
| 2017 |
Panday A, Grove A. Yeast HMO1: Linker Histone Reinvented. Microbiology and Molecular Biology Reviews : Mmbr. 81. PMID 27903656 DOI: 10.1128/Mmbr.00037-16 |
0.497 |
|
| 2016 |
Deochand DK, Perera IC, Crochet RB, Gilbert NC, Newcomer ME, Grove A. Histidine switch controlling pH-dependent protein folding and DNA binding in a transcription factor at the core of synthetic network devices. Molecular Biosystems. PMID 27282811 DOI: 10.1039/C6Mb00304D |
0.448 |
|
| 2016 |
Deochand DK, Meariman JK, Grove A. pH-Dependent DNA Distortion and Repression of Gene Expression by Pectobacterium atrosepticum PecS. Acs Chemical Biology. PMID 27213700 DOI: 10.1021/Acschembio.6B00168 |
0.506 |
|
| 2016 |
Panday A, Grove A. The high mobility group protein HMO1 functions as a linker histone in yeast. Epigenetics & Chromatin. 9: 13. PMID 27030801 DOI: 10.1186/S13072-016-0062-8 |
0.414 |
|
| 2016 |
Sivapragasam S, Grove A. Streptomyces coelicolor XdhR is a direct target of (p)ppGpp that controls expression of genes encoding xanthine dehydrogenase to promote purine salvage. Molecular Microbiology. PMID 26833627 DOI: 10.1111/Mmi.13342 |
0.465 |
|
| 2015 |
Panday A, Xiao L, Grove A. Yeast high mobility group protein HMO1 stabilizes chromatin and is evicted during repair of DNA double strand breaks. Nucleic Acids Research. 43: 5759-70. PMID 25979266 DOI: 10.1093/Nar/Gkv498 |
0.51 |
|
| 2015 |
Sivapragasam S, Pande A, Grove A. A recommended workflow for DNase I footprinting using a capillary electrophoresis genetic analyzer. Analytical Biochemistry. 481: 1-3. PMID 25908559 DOI: 10.1016/J.Ab.2015.04.013 |
0.444 |
|
| 2015 |
Huang H, Sivapragasam S, Grove A. The regulatory role of Streptomyces coelicolor TamR in central metabolism. The Biochemical Journal. 466: 347-58. PMID 25494937 DOI: 10.1042/Bj20130838 |
0.479 |
|
| 2015 |
Kushwaha AK, Deochand DK, Grove A. A moonlighting function of Mycobacterium smegmatis Ku in zinc homeostasis? Protein Science : a Publication of the Protein Society. 24: 253-63. PMID 25450225 DOI: 10.1002/Pro.2612 |
0.555 |
|
| 2014 |
Gupta A, Grove A. Ligand-binding pocket bridges DNA-binding and dimerization domains of the urate-responsive MarR homologue MftR from Burkholderia thailandensis. Biochemistry. 53: 4368-80. PMID 24955985 DOI: 10.1021/Bi500219T |
0.498 |
|
| 2013 |
Kushwaha AK, Grove A. Mycobacterium smegmatis Ku binds DNA without free ends. The Biochemical Journal. 456: 275-82. PMID 24059867 DOI: 10.1042/Bj20130749 |
0.561 |
|
| 2013 |
Huang H, Mackel BJ, Grove A. Streptomyces coelicolor encodes a urate-responsive transcriptional regulator with homology to PecS from plant pathogens. Journal of Bacteriology. 195: 4954-65. PMID 23995633 DOI: 10.1128/Jb.00854-13 |
0.442 |
|
| 2013 |
Grove A. MarR family transcription factors. Current Biology : Cb. 23: R142-3. PMID 23428319 DOI: 10.1016/J.Cub.2013.01.013 |
0.329 |
|
| 2013 |
Huang H, Grove A. The transcriptional regulator TamR from Streptomyces coelicolor controls a key step in central metabolism during oxidative stress. Molecular Microbiology. 87: 1151-66. PMID 23320788 DOI: 10.1111/Mmi.12156 |
0.379 |
|
| 2013 |
Kushwaha AK, Grove A. C-terminal low-complexity sequence repeats of Mycobacterium smegmatis Ku modulate DNA binding. Bioscience Reports. 33: 175-84. PMID 23167261 DOI: 10.1042/Bsr20120105 |
0.584 |
|
| 2012 |
Reon BJ, Nguyen KH, Bhattacharyya G, Grove A. Functional comparison of Deinococcus radiodurans Dps proteins suggests distinct in vivo roles. The Biochemical Journal. 447: 381-91. PMID 22857940 DOI: 10.1042/Bj20120902 |
0.52 |
|
| 2012 |
Nguyen KH, Grove A. Metal binding at the Deinococcus radiodurans Dps-1 N-terminal metal site controls dodecameric assembly and DNA binding. Biochemistry. 51: 6679-89. PMID 22846100 DOI: 10.1021/Bi300703X |
0.523 |
|
| 2012 |
Ray S, Grove A. Interaction of Saccharomyces cerevisiae HMO2 domains with distorted DNA. Biochemistry. 51: 1825-35. PMID 22329404 DOI: 10.1021/Bi201700H |
0.582 |
|
| 2012 |
Nguyen KH, Smith LT, Xiao L, Bhattacharyya G, Grove A. On the stoichiometry of Deinococcus radiodurans Dps-1 binding to duplex DNA. Proteins. 80: 713-21. PMID 22114047 DOI: 10.1002/Prot.23228 |
0.585 |
|
| 2011 |
Xiao L, Kamau E, Donze D, Grove A. Expression of yeast high mobility group protein HMO1 is regulated by TOR signaling. Gene. 489: 55-62. PMID 21924331 DOI: 10.1016/J.Gene.2011.08.017 |
0.603 |
|
| 2011 |
Perera IC, Grove A. MarR homologs with urate-binding signature. Protein Science : a Publication of the Protein Society. 20: 621-9. PMID 21432936 DOI: 10.1002/Pro.588 |
0.523 |
|
| 2011 |
Grove A. Functional evolution of bacterial histone-like HU proteins. Current Issues in Molecular Biology. 13: 1-12. PMID 20484776 |
0.495 |
|
| 2010 |
Grove A. Urate-responsive MarR homologs from Burkholderia. Molecular Biosystems. 6: 2133-42. PMID 20730247 DOI: 10.1039/C0Mb00086H |
0.486 |
|
| 2010 |
Perera IC, Grove A. Molecular mechanisms of ligand-mediated attenuation of DNA binding by MarR family transcriptional regulators. Journal of Molecular Cell Biology. 2: 243-54. PMID 20716550 DOI: 10.1093/Jmcb/Mjq021 |
0.482 |
|
| 2010 |
Perera IC, Grove A. Urate is a ligand for the transcriptional regulator PecS. Journal of Molecular Biology. 402: 539-51. PMID 20678501 DOI: 10.1016/J.Jmb.2010.07.053 |
0.502 |
|
| 2010 |
Wowor AJ, Datta K, Brown HS, Thompson GS, Ray S, Grove A, LiCata VJ. Thermodynamics of the DNA structural selectivity of the Pol I DNA polymerases from Escherichia coli and Thermus aquaticus. Biophysical Journal. 98: 3015-24. PMID 20550914 DOI: 10.1016/J.Bpj.2010.03.021 |
0.572 |
|
| 2010 |
Xiao L, Williams AM, Grove A. The C-terminal domain of yeast high mobility group protein HMO1 mediates lateral protein accretion and in-phase DNA bending. Biochemistry. 49: 4051-9. PMID 20402481 DOI: 10.1021/Bi1003603 |
0.577 |
|
| 2009 |
Meades G, Benson BK, Grove A, Waldrop GL. A tale of two functions: Enzymatic activity and translational repression by carboxyltransferase Nucleic Acids Research. 38: 1217-1227. PMID 19965770 DOI: 10.1093/Nar/Gkp1079 |
0.355 |
|
| 2009 |
Xiao L, Grove A. Coordination of Ribosomal Protein and Ribosomal RNA Gene Expression in Response to TOR Signaling. Current Genomics. 10: 198-205. PMID 19881913 DOI: 10.2174/138920209788185261 |
0.341 |
|
| 2009 |
Ray S, Grove A. The yeast high mobility group protein HMO2, a subunit of the chromatin-remodeling complex INO80, binds DNA ends. Nucleic Acids Research. 37: 6389-99. PMID 19726587 DOI: 10.1093/Nar/Gkp695 |
0.581 |
|
| 2009 |
Perera IC, Lee YH, Wilkinson SP, Grove A. Mechanism for attenuation of DNA binding by MarR family transcriptional regulators by small molecule ligands. Journal of Molecular Biology. 390: 1019-29. PMID 19501097 DOI: 10.1016/J.Jmb.2009.06.002 |
0.517 |
|
| 2009 |
Jain T, Roper BJ, Grove A. A functional type I topoisomerase from Pseudomonas aeruginosa. Bmc Molecular Biology. 10: 23. PMID 19317906 DOI: 10.1186/1471-2199-10-23 |
0.402 |
|
| 2009 |
Mukherjee A, DiMario PJ, Grove A. Mycobacterium smegmatis histone-like protein Hlp is nucleoid associated. Fems Microbiology Letters. 291: 232-40. PMID 19146577 DOI: 10.1111/J.1574-6968.2008.01458.X |
0.459 |
|
| 2008 |
Mukherjee A, Bhattacharyya G, Grove A. The C-terminal domain of HU-related histone-like protein Hlp from Mycobacterium smegmatis mediates DNA end-joining. Biochemistry. 47: 8744-53. PMID 18656956 DOI: 10.1021/Bi800010S |
0.535 |
|
| 2008 |
Mukherjee A, Sokunbi AO, Grove A. DNA protection by histone-like protein HU from the hyperthermophilic eubacterium Thermotoga maritima. Nucleic Acids Research. 36: 3956-68. PMID 18515342 DOI: 10.1093/Nar/Gkn348 |
0.581 |
|
| 2008 |
Benson BK, Meades G, Grove A, Waldrop GL. DNA inhibits catalysis by the carboxyltransferase subunit of acetyl-CoA carboxylase: Implications for active site communication Protein Science. 17: 34-42. PMID 18156466 DOI: 10.1110/Ps.073186408 |
0.553 |
|
| 2007 |
Bhattacharyya G, Grove A. The N-terminal extensions of Deinococcus radiodurans Dps-1 mediate DNA major groove interactions as well as assembly of the dodecamer. The Journal of Biological Chemistry. 282: 11921-30. PMID 17331944 DOI: 10.1074/Jbc.M611255200 |
0.558 |
|
| 2007 |
Bhattacharyya G, Grove A. The N‐terminal extension of Dps‐1 from
Deinococcus radiodurans
is required for assembly of the dodecamer as well as for DNA binding The Faseb Journal. 21. DOI: 10.1096/Fasebj.21.5.A660-D |
0.539 |
|
| 2007 |
Williams AM, Grove A. The yeast high mobility group protein, HMO1, facilitates DNA end‐joining The Faseb Journal. 21. DOI: 10.1096/Fasebj.21.5.A291 |
0.568 |
|
| 2006 |
Tsihlis ND, Grove A. The Saccharomyces cerevisiae RNA polymerase III recruitment factor subunits Brf1 and Bdp1 impose a strict sequence preference for the downstream half of the TATA box. Nucleic Acids Research. 34: 5585-93. PMID 17028095 DOI: 10.1093/Nar/Gkl534 |
0.448 |
|
| 2006 |
Kim SG, Bhattacharyya G, Grove A, Lee YH. Crystal structure of Dps-1, a functionally distinct Dps protein from Deinococcus radiodurans. Journal of Molecular Biology. 361: 105-14. PMID 16828801 DOI: 10.1016/J.Jmb.2006.06.010 |
0.427 |
|
| 2006 |
Bordelon T, Wilkinson SP, Grove A, Newcomer ME. The Crystal Structure of the Transcriptional Regulator HucR from Deinococcus radiodurans Reveals a Repressor Preconfigured for DNA Binding Journal of Molecular Biology. 360: 168-177. PMID 16750221 DOI: 10.1016/J.Jmb.2006.05.005 |
0.576 |
|
| 2006 |
Bauerle KT, Kamau E, Grove A. Interactions between N- and C-terminal domains of the Saccharomyces cerevisiae high-mobility group protein HMO1 are required for DNA bending. Biochemistry. 45: 3635-45. PMID 16533046 DOI: 10.1021/Bi0522798 |
0.676 |
|
| 2006 |
Ghosh S, Grove A. The Deinococcus radiodurans-encoded HU protein has two DNA-binding domains. Biochemistry. 45: 1723-33. PMID 16460019 DOI: 10.1021/Bi0514010 |
0.7 |
|
| 2006 |
Wilkinson SP, Grove A. Ligand-responsive transcriptional regulation by members of the MarR family of winged helix proteins. Current Issues in Molecular Biology. 8: 51-62. PMID 16450885 |
0.437 |
|
| 2005 |
Wilkinson SP, Grove A. Negative cooperativity of uric acid binding to the transcriptional regulator HucR from Deinococcus radiodurans. Journal of Molecular Biology. 350: 617-30. PMID 15967460 DOI: 10.1016/J.Jmb.2005.05.027 |
0.54 |
|
| 2005 |
Kamau E, Tsihlis ND, Simmons LA, Grove A. Surface salt bridges modulate the DNA site size of bacterial histone-like HU proteins. The Biochemical Journal. 390: 49-55. PMID 15845027 DOI: 10.1042/Bj20050274 |
0.718 |
|
| 2005 |
Grove A, Wilkinson SP. Differential DNA binding and protection by dimeric and dodecameric forms of the ferritin homolog Dps from Deinococcus radiodurans. Journal of Molecular Biology. 347: 495-508. PMID 15755446 DOI: 10.1016/J.Jmb.2005.01.055 |
0.543 |
|
| 2004 |
Kamau E, Bauerle KT, Grove A. The Saccharomyces cerevisiae high mobility group box protein HMO1 contains two functional DNA binding domains. The Journal of Biological Chemistry. 279: 55234-40. PMID 15507436 DOI: 10.1074/Jbc.M409459200 |
0.729 |
|
| 2004 |
Wilkinson SP, Grove A. HucR, a novel uric acid-responsive member of the MarR family of transcriptional regulators from Deinococcus radiodurans. The Journal of Biological Chemistry. 279: 51442-50. PMID 15448166 DOI: 10.1074/Jbc.M405586200 |
0.501 |
|
| 2004 |
Kamau E, Grove A. Fluoroquinolone-dependent DNA supercoiling by Vaccinia topoisomerase I. Journal of Molecular Biology. 342: 479-87. PMID 15327948 DOI: 10.1016/J.Jmb.2004.06.082 |
0.699 |
|
| 2004 |
Chen C, Ghosh S, Grove A. Substrate specificity of Helicobacter pylori histone-like HU protein is determined by insufficient stabilization of DNA flexure points. The Biochemical Journal. 383: 343-51. PMID 15255779 DOI: 10.1042/Bj20040938 |
0.678 |
|
| 2004 |
Ghosh S, Grove A. Histone-like protein HU from Deinococcus radiodurans binds preferentially to four-way DNA junctions. Journal of Molecular Biology. 337: 561-71. PMID 15019777 DOI: 10.1016/J.Jmb.2004.02.010 |
0.69 |
|
| 2003 |
Grove A. Surface salt bridges modulate DNA wrapping by the type II DNA-binding protein TF1. Biochemistry. 42: 8739-47. PMID 12873134 DOI: 10.1021/Bi034551O |
0.583 |
|
| 2002 |
Kassavetis GA, Grove A, Geiduschek EP. Effects of DNA strand breaks on transcription by RNA polymerase III: Insights into the role of TFIIIB and the polarity of promoter opening Embo Journal. 21: 5508-5515. PMID 12374751 DOI: 10.1093/Emboj/Cdf533 |
0.478 |
|
| 2002 |
Grove A, Saavedra TC. The role of surface-exposed lysines in wrapping DNA about the bacterial histone-like protein HU. Biochemistry. 41: 7597-603. PMID 12056890 DOI: 10.1021/Bi016095E |
0.565 |
|
| 2002 |
Grove A, Adessa MS, Geiduschek EP, Kassavetis GA. Marking the start site of RNA polymerase III transcription: the role of constraint, compaction and continuity of the transcribed DNA strand. The Embo Journal. 21: 704-14. PMID 11847118 DOI: 10.1093/Emboj/21.4.704 |
0.448 |
|
| 2001 |
Grove A, Lim L. High-affinity DNA binding of HU protein from the hyperthermophile Thermotoga maritima Journal of Molecular Biology. 311: 491-502. PMID 11493003 DOI: 10.1006/Jmbi.2001.4763 |
0.581 |
|
| 2000 |
Vu HM, Liu W, Grove A, Geiduschek EP, Kearns DR. Mechanisms for the enhanced thermal stability of a mutant of transcription factor 1 as explained by (1)H, (15)N and (13)C NMR chemical shifts and secondary structure analysis. Biochimica Et Biophysica Acta. 1478: 113-24. PMID 10719180 DOI: 10.1016/S0167-4838(99)00252-6 |
0.384 |
|
| 1999 |
Grove A, Kassavetis GA, Johnson TE, Geiduschek EP. The RNA polymerase III-recruiting factor TFIIIB induces a DNA bend between the TATA box and the transcriptional start site. Journal of Molecular Biology. 285: 1429-40. PMID 9917387 DOI: 10.1006/Jmbi.1998.2347 |
0.554 |
|
| 1998 |
Kumar A, Grove A, Kassavetis GA, Geiduschek EP. Transcription factor IIIB: The architecture of its DNA complex, and its roles in initiation of transcription by RNA polymerase III Cold Spring Harbor Symposia On Quantitative Biology. 63: 121-129. PMID 10384276 DOI: 10.1101/Sqb.1998.63.121 |
0.407 |
|
| 1998 |
Grove A, Galeone A, Yu E, Mayol L, Geiduschek EP. Affinity, stability and polarity of binding of the TATA binding protein governed by flexure at the TATA box Journal of Molecular Biology. 282: 731-739. PMID 9743622 DOI: 10.1006/Jmbi.1998.2058 |
0.578 |
|
| 1997 |
Grove A, Figueiredo ML, Galeone A, Mayol L, Geiduschek EP. Twin hydroxymethyluracil-A base pair steps define the binding site for the DNA-binding protein TF1. The Journal of Biological Chemistry. 272: 13084-7. PMID 9148920 DOI: 10.1074/Jbc.272.20.13084 |
0.531 |
|
| 1997 |
Grove A, Geiduschek EP. Localizing flexibility within the target site of DNA-bending proteins Techniques in Protein Chemistry. 8: 585-592. DOI: 10.1016/S1080-8914(97)80058-0 |
0.585 |
|
| 1996 |
Jia X, Grove A, Ivancic M, Hsu VL, Geiduscheck EP, Kearns DR. Structure of the Bacillus subtilis phage SPO1-encoded type II DNA-binding protein TF1 in solution. Journal of Molecular Biology. 263: 259-68. PMID 8913305 DOI: 10.1006/Jmbi.1996.0573 |
0.386 |
|
| 1996 |
Grove A, Galeone A, Mayol L, Geiduschek EP. On the connection between inherent DNA flexure and preferred binding of hydroxymethyluracil-containing DNA by the type II DNA-binding protein TF1 Journal of Molecular Biology. 260: 196-206. PMID 8764400 DOI: 10.1006/Jmbi.1996.0392 |
0.585 |
|
| 1996 |
Grove A, Galeone A, Mayol L, Geiduschek EP. Localized DNA flexibility contributes to target site selection by DNA-bending proteins Journal of Molecular Biology. 260: 120-125. PMID 8764394 DOI: 10.1006/Jmbi.1996.0386 |
0.583 |
|
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