Year |
Citation |
Score |
2023 |
Sutherland JH, Holloman WK. Determinants governing BRC function evaluated by mutational analysis of Brh2 in Ustilago maydis. Dna Repair. 127: 103511. PMID 37141696 DOI: 10.1016/j.dnarep.2023.103511 |
0.437 |
|
2022 |
Zahid S, Aloe S, Sutherland JH, Holloman WK, Lue NF. Ustilago maydis telomere protein Pot1 harbors an extra N-terminal OB fold and regulates homology-directed DNA repair factors in a dichotomous and context-dependent manner. Plos Genetics. 18: e1010182. PMID 35587917 DOI: 10.1371/journal.pgen.1010182 |
0.478 |
|
2020 |
Yu EY, Zahid SS, Ganduri S, Sutherland JH, Hsu M, Holloman WK, Lue NF. Structurally distinct telomere-binding proteins in Ustilago maydis execute non-overlapping functions in telomere replication, recombination, and protection. Communications Biology. 3: 777. PMID 33328546 DOI: 10.1038/s42003-020-01505-z |
0.354 |
|
2019 |
Sutherland JH, Holloman WK. Characterization of a potent dominant negative mutant variant of Rad51 in Ustilago maydis. Dna Repair. 78: 91-101. PMID 31005682 DOI: 10.1016/J.Dnarep.2019.04.003 |
0.646 |
|
2018 |
Sutherland JH, Holloman WK. Loss of Cohesin Subunit Rec8 Switches Rad51 Mediator Dependence in Resistance to Formaldehyde Toxicity in . Genetics. PMID 30082279 DOI: 10.1534/Genetics.118.301439 |
0.614 |
|
2018 |
Zhou Q, Holloman WK, Kojic M. Approaches to Understanding the Mediator Function of Brh2 in Ustilago maydis. Methods in Enzymology. 600: 513-525. PMID 29458772 DOI: 10.1016/Bs.Mie.2017.11.019 |
0.431 |
|
2018 |
Kojic M, Milisavljevic M, Holloman WK. Collaboration in the actions of Brh2 with resolving functions during DNA repair and replication stress in Ustilago maydis. Dna Repair. 63: 47-55. PMID 29414053 DOI: 10.1016/J.Dnarep.2018.01.010 |
0.611 |
|
2017 |
Yu EY, Hsu M, Holloman WK, Lue NF. Contributions of recombination and repair proteins to telomere maintenance in telomerase-positive and negative Ustilago maydis. Molecular Microbiology. PMID 29052918 DOI: 10.1111/Mmi.13866 |
0.489 |
|
2017 |
Zhou Q, Holloman WK. Dss1 regulates association of Brh2 with Rad51. Biochemistry. PMID 28616972 DOI: 10.1021/Acs.Biochem.7B00184 |
0.596 |
|
2017 |
Lim PX, Sutherland J, Noonan R, Dananberg A, Holloman W, Smogorzewska A, Jasin M. Abstract A27: Assessing somatic tumor-associated RAD51 mutations and screening for novel dominant-interfering RAD51 proteins Molecular Cancer Research. 15. DOI: 10.1158/1557-3125.Dnarepair16-A27 |
0.48 |
|
2015 |
Yu EY, Pérez-Martín J, Holloman WK, Lue NF. Mre11 and Blm-Dependent Formation of ALT-Like Telomeres in Ku-Deficient Ustilago maydis. Plos Genetics. 11: e1005570. PMID 26492073 DOI: 10.1371/Journal.Pgen.1005570 |
0.473 |
|
2015 |
de Sena-Tomás C, Sutherland JH, Milisavljevic M, Nikolic DB, Pérez-Martín J, Kojic M, Holloman WK. LAMMER kinase contributes to genome stability in Ustilago maydis. Dna Repair. 33: 70-7. PMID 26176563 DOI: 10.1016/J.Dnarep.2015.05.011 |
0.488 |
|
2015 |
de Sena-Tomás C, Yu EY, Calzada A, Holloman WK, Lue NF, Pérez-Martín J. Fungal Ku prevents permanent cell cycle arrest by suppressing DNA damage signaling at telomeres. Nucleic Acids Research. 43: 2138-51. PMID 25653166 DOI: 10.1093/Nar/Gkv082 |
0.57 |
|
2014 |
Zhou Q, Holloman WK. Dual DNA-binding domains shape the interaction of Brh2 with DNA. Dna Repair. 22: 104-11. PMID 25128760 DOI: 10.1016/J.Dnarep.2014.07.013 |
0.595 |
|
2013 |
Kojic M, Sutherland JH, Pérez-Martín J, Holloman WK. Initiation of meiotic recombination in Ustilago maydis. Genetics. 195: 1231-40. PMID 24077302 DOI: 10.1534/Genetics.113.156752 |
0.429 |
|
2013 |
Yu EY, Kojic M, Holloman WK, Lue NF. Brh2 and Rad51 promote telomere maintenance in Ustilago maydis, a new model system of DNA repair proteins at telomeres. Dna Repair. 12: 472-9. PMID 23726221 DOI: 10.1016/J.Dnarep.2013.04.027 |
0.592 |
|
2012 |
Zhou Q, Kojic M, Holloman WK. Dss1 release activates DNA binding potential in Brh2. Biochemistry. 51: 9137-46. PMID 23094644 DOI: 10.1021/Bi3011187 |
0.526 |
|
2012 |
Kojic M, Holloman WK. Brh2 domain function distinguished by differential cellular responses to DNA damage and replication stress. Molecular Microbiology. 83: 351-61. PMID 22171788 DOI: 10.1111/J.1365-2958.2011.07935.X |
0.581 |
|
2011 |
Holloman WK. Unraveling the mechanism of BRCA2 in homologous recombination. Nature Structural & Molecular Biology. 18: 748-54. PMID 21731065 DOI: 10.1038/Nsmb.2096 |
0.613 |
|
2011 |
de Sena-Tomás C, Fernández-Álvarez A, Holloman WK, Pérez-Martín J. The DNA damage response signaling cascade regulates proliferation of the phytopathogenic fungus Ustilago maydis in planta. The Plant Cell. 23: 1654-65. PMID 21478441 DOI: 10.1105/Tpc.110.082552 |
0.441 |
|
2011 |
Kojic M, Zhou Q, Fan J, Holloman WK. Mutational analysis of Brh2 reveals requirements for compensating mediator functions. Molecular Microbiology. 79: 180-91. PMID 21166902 DOI: 10.1111/J.1365-2958.2010.07440.X |
0.635 |
|
2009 |
Mazloum N, Holloman WK. Brh2 promotes a template-switching reaction enabling recombinational bypass of lesions during DNA synthesis. Molecular Cell. 36: 620-30. PMID 19941822 DOI: 10.1016/J.Molcel.2009.09.033 |
0.575 |
|
2009 |
Zhou Q, Mazloum N, Mao N, Kojic M, Holloman WK. Dss1 regulates interaction of Brh2 with DNA. Biochemistry. 48: 11929-38. PMID 19919104 DOI: 10.1021/Bi901775J |
0.557 |
|
2009 |
Mao N, Kojic M, Holloman WK. Role of Blm and collaborating factors in recombination and survival following replication stress in Ustilago maydis. Dna Repair. 8: 752-9. PMID 19349216 DOI: 10.1016/J.Dnarep.2009.02.006 |
0.588 |
|
2009 |
Mazloum N, Holloman WK. Second-end capture in DNA double-strand break repair promoted by Brh2 protein of Ustilago maydis. Molecular Cell. 33: 160-70. PMID 19187759 DOI: 10.1016/J.Molcel.2008.12.023 |
0.604 |
|
2009 |
Zhou Q, Kojic M, Holloman WK. DNA-binding Domain within the Brh2 N Terminus Is the Primary Interaction Site for Association with DNA. The Journal of Biological Chemistry. 284: 8265-73. PMID 19182269 DOI: 10.1074/Jbc.M809226200 |
0.58 |
|
2008 |
Holloman WK, Schirawski J, Holliday R. The homologous recombination system of Ustilago maydis. Fungal Genetics and Biology : Fg & B. 45: S31-9. PMID 18502156 DOI: 10.1016/J.Fgb.2008.04.006 |
0.568 |
|
2008 |
Kojic M, Mao N, Zhou Q, Lisby M, Holloman WK. Compensatory role for Rad52 during recombinational repair in Ustilago maydis. Molecular Microbiology. 67: 1156-68. PMID 18208529 DOI: 10.1111/J.1365-2958.2008.06116.X |
0.565 |
|
2008 |
Mazloum N, Zhou Q, Holloman WK. D-loop formation by Brh2 protein of Ustilago maydis. Proceedings of the National Academy of Sciences of the United States of America. 105: 524-9. PMID 18174332 DOI: 10.1073/Pnas.0707031105 |
0.608 |
|
2007 |
Holloman WK, Schirawski J, Holliday R. Towards understanding the extreme radiation resistance of Ustilago maydis. Trends in Microbiology. 15: 525-9. PMID 17997098 DOI: 10.1016/J.Tim.2007.10.007 |
0.375 |
|
2007 |
Mao N, Zhou Q, Kojic M, Pérez-Martín J, Holloman WK. Ortholog of BRCA2-interacting protein BCCIP controls morphogenetic responses during DNA replication stress in Ustilago maydis. Dna Repair. 6: 1651-60. PMID 17627904 DOI: 10.1016/J.Dnarep.2007.05.012 |
0.622 |
|
2007 |
Mazloum N, Zhou Q, Holloman WK. DNA binding, annealing, and strand exchange activities of Brh2 protein from Ustilago maydis. Biochemistry. 46: 7163-73. PMID 17523678 DOI: 10.1021/Bi700399M |
0.633 |
|
2007 |
Zhou Q, Kojic M, Cao Z, Lisby M, Mazloum NA, Holloman WK. Dss1 interaction with Brh2 as a regulatory mechanism for recombinational repair. Molecular and Cellular Biology. 27: 2512-26. PMID 17261595 DOI: 10.1128/Mcb.01907-06 |
0.486 |
|
2006 |
Kojic M, Zhou Q, Lisby M, Holloman WK. Rec2 interplay with both Brh2 and Rad51 balances recombinational repair in Ustilago maydis. Molecular and Cellular Biology. 26: 678-88. PMID 16382157 DOI: 10.1128/Mcb.26.2.678-688.2006 |
0.426 |
|
2005 |
Kojic M, Zhou Q, Lisby M, Holloman WK. Brh2-Dss1 interplay enables properly controlled recombination in Ustilago maydis. Molecular and Cellular Biology. 25: 2547-57. PMID 15767662 DOI: 10.1128/Mcb.25.7.2547-2557.2005 |
0.584 |
|
2005 |
Yang H, Li Q, Fan J, Holloman WK, Pavletich NP. The BRCA2 homologue Brh2 nucleates RAD51 filament formation at a dsDNA-ssDNA junction. Nature. 433: 653-7. PMID 15703751 DOI: 10.1038/Nature03234 |
0.608 |
|
2004 |
Kojic M, Holloman WK. BRCA2-RAD51-DSS1 interplay examined from a microbial perspective. Cell Cycle (Georgetown, Tex.). 3: 247-8. PMID 14726651 DOI: 10.4161/Cc.3.3.701 |
0.526 |
|
2004 |
Symington LS, Holloman WK. Molecular biology. New Year's resolution--resolving resolvases. Science (New York, N.Y.). 303: 184-5. PMID 14716002 DOI: 10.1126/Science.1093959 |
0.606 |
|
2003 |
Kojic M, Yang H, Kostrub CF, Pavletich NP, Holloman WK. The BRCA2-interacting protein DSS1 is vital for DNA repair, recombination, and genome stability in Ustilago maydis. Molecular Cell. 12: 1043-9. PMID 14580353 DOI: 10.1016/S1097-2765(03)00367-8 |
0.55 |
|
2003 |
Zan H, Wu X, Komori A, Holloman WK, Casali P. AID-dependent generation of resected double-strand DNA breaks and recruitment of Rad52/Rad51 in somatic hypermutation. Immunity. 18: 727-38. PMID 12818155 DOI: 10.1016/S1074-7613(03)00151-1 |
0.568 |
|
2002 |
Kojic M, Kostrub CF, Buchman AR, Holloman WK. BRCA2 homolog required for proficiency in DNA repair, recombination, and genome stability in Ustilago maydis. Molecular Cell. 10: 683-91. PMID 12408834 DOI: 10.1016/S1097-2765(02)00632-9 |
0.542 |
|
2001 |
Kojic M, Thompson CW, Holloman WK. Disruptions of the Ustilago maydis REC2 gene identify a protein domain important in directing recombinational repair of DNA. Molecular Microbiology. 40: 1415-26. PMID 11442839 DOI: 10.1046/J.1365-2958.2001.02490.X |
0.533 |
|
2001 |
Bennett RL, Holloman WK. A RecA homologue in Ustilago maydis that is distinct and evolutionarily distant from Rad51 actively promotes DNA pairing reactions in the absence of auxiliary factors. Biochemistry. 40: 2942-53. PMID 11258906 DOI: 10.1021/Bi002494I |
0.634 |
|
2001 |
Sanz MM, Proytcheva M, Ellis NA, Holloman WK, German J. BLM, the Bloom's syndrome protein, varies during the cell cycle in its amount, distribution, and co-localization with other nuclear proteins. Cytogenetics and Cell Genetics. 91: 217-23. PMID 11173860 DOI: 10.1159/000056848 |
0.427 |
|
2000 |
van Brabant AJ, Ye T, Sanz M, German III JL, Ellis NA, Holloman WK. Binding and melting of D-loops by the Bloom syndrome helicase. Biochemistry. 39: 14617-25. PMID 11087418 DOI: 10.1021/Bi0018640 |
0.563 |
|
2000 |
Kojic M, Holloman WK. Shuttle vectors for genetic manipulations in Ustilago maydis. Canadian Journal of Microbiology. 46: 333-338. PMID 10779869 DOI: 10.1139/W00-002 |
0.388 |
|
1999 |
Naureckiene S, Holloman WK. DNA hydrolytic activity associated with the Ustilago maydis REC1 gene product analyzed on hairpin oligonucleotide substrates. Biochemistry. 38: 14379-14386. PMID 10572012 DOI: 10.1021/Bi991495B |
0.609 |
|
1999 |
Cole-Strauss A, Gamper H, Holloman WK, Muñoz M, Cheng N, Kmiec EB. Targeted gene repair directed by the chimeric RNA/DNA oligonucleotide in a mammalian cell-free extract. Nucleic Acids Research. 27: 1323-30. PMID 9973621 DOI: 10.1093/Nar/27.5.1323 |
0.491 |
|
1997 |
Onel K, Holloman WK. Molecular cloning of a gene required for DNA replication in Ustilago maydis Molecular and General Genetics. 253: 463-468. PMID 9037106 DOI: 10.1007/S004380050344 |
0.602 |
|
1996 |
Cole-Strauss A, Yoon K, Xiang Y, Byrne BC, Rice MC, Gryn J, Holloman WK, Kmiec EB. Correction of the mutation responsible for sickle cell anemia by an RNA-DNA oligonucleotide. Science (New York, N.Y.). 273: 1386-9. PMID 8703073 DOI: 10.1126/Science.273.5280.1386 |
0.423 |
|
1996 |
Ferguson DO, Holloman WK. Recombinational repair of gaps in DNA is asymmetric in Ustilago maydis and can be explained by a migrating D-loop model Proceedings of the National Academy of Sciences of the United States of America. 93: 5419-5424. PMID 8643590 DOI: 10.1073/Pnas.93.11.5419 |
0.595 |
|
1995 |
Onel K, Thelen MP, Ferguson DO, Bennett RL, Holloman WK. Mutation avoidance and DNA repair proficiency in Ustilago maydis are differentially lost with progressive truncation of the REC1 gene product. Molecular and Cellular Biology. 15: 5329-38. PMID 7565682 DOI: 10.1128/Mcb.15.10.5329 |
0.491 |
|
1994 |
Rubin BP, Li D, Holloman WK. The LEU1 gene of Ustilago maydis. Gene. 140: 131-135. PMID 8125330 DOI: 10.1016/0378-1119(94)90743-9 |
0.325 |
|
1994 |
Kmiec EB, Holloman WK. ATP-dependent DNA renaturation and DNA-dependent ATPase reactions catalyzed by the Ustilago maydis homologous pairing protein. European Journal of Biochemistry. 219: 865-75. PMID 8112338 DOI: 10.1111/J.1432-1033.1994.Tb18568.X |
0.49 |
|
1994 |
Rubin BP, Ferguson DO, Holloman WK. Structure of REC2, a recombinational repair gene of Ustilago maydis, and its function in homologous recombination between plasmid and chromosomal sequences. Molecular and Cellular Biology. 14: 6287-6296. PMID 8065360 DOI: 10.1128/Mcb.14.9.6287 |
0.56 |
|
1994 |
Kmiec EB, Cole A, Holloman WK. The REC2 gene encodes the homologous pairing protein of Ustilago maydis. Molecular and Cellular Biology. 14: 7163-72. PMID 7935431 DOI: 10.1128/Mcb.14.11.7163 |
0.565 |
|
1993 |
Thiyagarajan MM, Kotani H, Holloman WK, Kmiec EB. DNA relaxation mediated by Ustilago maydis type I topoisomerase; modulation by chromatin associated proteins. Biochimica Et Biophysica Acta. 1173: 155-64. PMID 8389206 DOI: 10.1016/0167-4781(93)90176-E |
0.566 |
|
1993 |
Kotani H, Kmiec EB, Holloman WK. Purification and properties of a cruciform DNA binding protein from Ustilago maydis. Chromosoma. 102: 348-54. PMID 8325166 DOI: 10.1007/Bf00661278 |
0.5 |
|
1990 |
Bauchwitz R, Holloman WK. Isolation of the REC2 gene controlling recombination in Ustilago maydis. Gene. 96: 285-288. PMID 2269439 DOI: 10.1016/0378-1119(90)90265-S |
0.54 |
|
1989 |
Fotheringham S, Holloman WK. Cloning and disruption of Ustilago maydis genes. Molecular and Cellular Biology. 9: 4052-4055. PMID 2779577 DOI: 10.1128/Mcb.9.9.4052 |
0.351 |
|
1989 |
Tsukuda T, Bauchwitz R, Holloman WK. Isolation of the REC1 gene controlling recombination in Ustilago maydis Gene. 85: 335-341. PMID 2628171 DOI: 10.1016/0378-1119(89)90426-5 |
0.544 |
|
1988 |
Tsukuda T, Carleton S, Fotheringham S, Holloman WK. Isolation and characterization of an autonomously replicating sequence from Ustilago maydis. Molecular and Cellular Biology. 8: 3703-3709. PMID 2851726 DOI: 10.1128/Mcb.8.9.3703 |
0.382 |
|
1986 |
Kmiec EB, Holloman WK. Homologous pairing of DNA molecules by Ustilago rec1 protein is promoted by sequences of Z-DNA. Cell. 44: 545-54. PMID 3948243 DOI: 10.1016/0092-8674(86)90264-3 |
0.573 |
|
1986 |
Brougham MJ, Rowe TC, Holloman WK. Topoisomerase from Ustilago maydis forms a covalent complex with single-stranded DNA through a phosphodiester bond to tyrosine. Biochemistry. 25: 7362-8. PMID 3026452 DOI: 10.1021/Bi00371A018 |
0.558 |
|
1985 |
Holliday R, Taylor SY, Kmiec EB, Holloman WK. Biochemical characterization of rec1 mutants and the genetic control of recombination in Ustilago maydis. Cold Spring Harbor Symposia On Quantitative Biology. 49: 669-73. PMID 6597760 DOI: 10.1101/Sqb.1984.049.01.075 |
0.315 |
|
1985 |
Kmiec EB, Angelides KJ, Holloman WK. Left-handed DNA and the synaptic pairing reaction promoted by Ustilago rec1 protein. Cell. 40: 139-45. PMID 3967291 DOI: 10.1016/0092-8674(85)90317-4 |
0.565 |
|
1984 |
Kmiec E, Kroeger P, Holliday R, Holloman W. Homologous pairing promoted by Ustilago RecI protein. Cold Spring Harbor Symposia On Quantitative Biology. 49: 675-682. PMID 6597761 DOI: 10.1101/Sqb.1984.049.01.076 |
0.386 |
|
1984 |
Kmiec EB, Holloman WK. Synapsis promoted by Ustilago rec1 protein. Cell. 36: 593-8. PMID 6321036 DOI: 10.1016/0092-8674(84)90338-6 |
0.589 |
|
1983 |
Kmiec EB, Holloman WK. Heteroduplex formation and polarity during strand transfer promoted by Ustilago rec 1 protein. Cell. 33: 857-64. PMID 6871997 DOI: 10.1016/0092-8674(83)90028-4 |
0.491 |
|
1983 |
Ross CF, Brougham MJ, Holloman WK, Ross WE. Properties of a purified nuclear topoisomerase from L1210 cells. Biochimica Et Biophysica Acta. 741: 230-6. PMID 6317036 DOI: 10.1016/0167-4781(83)90063-5 |
0.421 |
|
1983 |
Kmiec EB, Kroeger PE, Brougham MJ, Holloman WK. Topological linkage of circular DNA molecules promoted by Ustilago rec 1 protein and topoisomerase. Cell. 34: 919-29. PMID 6313215 DOI: 10.1016/0092-8674(83)90549-4 |
0.574 |
|
1982 |
Kmiec E, Holloman WK. Homologous pairing of DNA molecules promoted by a protein from Ustilago. Cell. 29: 367-74. PMID 6214313 DOI: 10.1016/0092-8674(82)90153-2 |
0.615 |
|
1977 |
Radding CM, Beattie KL, Holloman WK, Wiegand RC. Uptake of homologous single-stranded fragments by superhelical DNA. IV. Branch migration. Journal of Molecular Biology. 116: 825-39. PMID 592403 DOI: 10.1016/0022-2836(77)90273-X |
0.543 |
|
1977 |
Wiegand RC, Beattie KL, Holloman WK, Radding CM. Uptake of homologous single-stranded fragments by superhelical DNA. III. The product and its enzymic conversion to a recombinant molecule Journal of Molecular Biology. 116: 805-824. PMID 592402 DOI: 10.1016/0022-2836(77)90272-8 |
0.562 |
|
1976 |
Banks GR, Holloman WK, Kairis MV, Spanos A, Yarranton GT. A DNA polymerase from Ustilago maydis. 1. Purification and properties of the polymerase activity European Journal of Biochemistry. 62: 131-142. PMID 1248475 DOI: 10.1111/J.1432-1033.1976.Tb10106.X |
0.571 |
|
1976 |
Ahmad A, Holloman WK, Holliday R. Nuclease that preferentially inactivates DNA containing mismatched bases. Nature. 258: 54-6. PMID 810727 DOI: 10.1038/258054A0 |
0.577 |
|
1976 |
Holloman WK, Radding CM. Recombination promoted by superhelical DNA and the recA gene of Escherichia coli Proceedings of the National Academy of Sciences of the United States of America. 73: 3910-3914. PMID 792876 DOI: 10.1073/Pnas.73.11.3910 |
0.594 |
|
1975 |
Holloman WK, Wiegand R, Hoessli C, Radding CM. Uptake of homologous single stranded fragments by superhelical DNA: a possible mechanism for initiation of genetic recombination Proceedings of the National Academy of Sciences of the United States of America. 72: 2394-2398. PMID 1094467 DOI: 10.1073/Pnas.72.6.2394 |
0.559 |
|
1973 |
HOLLIDAY R, HOLLOMAN WK. The Possible Role of Deoxyribonucleases in Recombination in Eukaryotes: Hypotheses and Observations Biochemical Society Transactions. 1: 245-245. DOI: 10.1042/Bst0010245 |
0.355 |
|
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