Year |
Citation |
Score |
2021 |
Guberovic I, Hurtado-Bagès S, Rivera-Casas C, Knobloch G, Malinverni R, Valero V, Leger MM, García J, Basquin J, Gómez de Cedrón M, Frigolé-Vivas M, Cheema MS, Pérez A, Ausió J, Ramírez de Molina A, ... ... Ladurner AG, et al. Evolution of a histone variant involved in compartmental regulation of NAD metabolism. Nature Structural & Molecular Biology. 28: 1009-1019. PMID 34887560 DOI: 10.1038/s41594-021-00692-5 |
0.318 |
|
2021 |
Murawska M, Greenstein RA, Schauer T, Olsen KCF, Ng H, Ladurner AG, Al-Sady B, Braun S. The histone chaperone FACT facilitates heterochromatin spreading by regulating histone turnover and H3K9 methylation states. Cell Reports. 37: 109944. PMID 34731638 DOI: 10.1016/j.celrep.2021.109944 |
0.766 |
|
2021 |
Lüscher B, Ahel I, Altmeyer M, Ashworth A, Bai P, Chang P, Cohen M, Corda D, Dantzer F, Daugherty MD, Dawson TM, Dawson VL, Deindl S, Fehr AR, Feijs KLH, ... ... Ladurner A, et al. ADP-ribosyltransferases, an update on function and nomenclature. The Febs Journal. PMID 34323016 DOI: 10.1111/febs.16142 |
0.746 |
|
2020 |
Margulies CE, Ladurner AG. PARP-1 Flips the Epigenetic Switch on Obesity. Molecular Cell. 79: 874-875. PMID 32946760 DOI: 10.1016/J.Molcel.2020.08.019 |
0.766 |
|
2020 |
Blessing C, Knobloch G, Ladurner AG. Restraining and unleashing chromatin remodelers - structural information guides chromatin plasticity. Current Opinion in Structural Biology. 65: 130-138. PMID 32693313 DOI: 10.1016/J.Sbi.2020.06.008 |
0.509 |
|
2020 |
Blessing C, Ladurner AG. Tickling PARPs into serine action. Nature Structural & Molecular Biology. PMID 32231290 DOI: 10.1038/S41594-020-0412-X |
0.462 |
|
2020 |
Hurtado-Bagès S, Knobloch G, Ladurner AG, Buschbeck M. The taming of PARP1 and its impact on NAD metabolism. Molecular Metabolism. 100950. PMID 32199820 DOI: 10.1016/J.Molmet.2020.01.014 |
0.306 |
|
2020 |
Murawska M, Ladurner AG. Bromodomain AAA+ ATPases get into shape. Nucleus (Austin, Tex.). 11: 32-34. PMID 32191554 DOI: 10.1080/19491034.2020.1741304 |
0.408 |
|
2019 |
Murawska M, Schauer T, Matsuda A, Wilson MD, Pysik T, Wojcik F, Muir TW, Hiraoka Y, Straub T, Ladurner AG. The Chaperone FACT and Histone H2B Ubiquitination Maintain S. pombe Genome Architecture through Genic and Subtelomeric Functions. Molecular Cell. PMID 31837996 DOI: 10.1016/J.Molcel.2019.11.016 |
0.788 |
|
2018 |
Kozlowski M, Corujo D, Hothorn M, Guberovic I, Mandemaker IK, Blessing C, Sporn J, Gutierrez-Triana A, Smith R, Portmann T, Treier M, Scheffzek K, Huet S, Timinszky G, Buschbeck M, ... Ladurner AG, et al. MacroH2A histone variants limit chromatin plasticity through two distinct mechanisms. Embo Reports. PMID 30177554 DOI: 10.15252/Embr.201744445 |
0.839 |
|
2017 |
Singh HR, Nardozza AP, Möller IR, Knobloch G, Kistemaker HAV, Hassler M, Harrer N, Blessing C, Eustermann S, Kotthoff C, Huet S, Mueller-Planitz F, Filippov DV, Timinszky G, Rand KD, ... Ladurner AG, et al. A Poly-ADP-Ribose Trigger Releases the Auto-Inhibition of a Chromatin Remodeling Oncogene. Molecular Cell. 68: 860-871.e7. PMID 29220653 DOI: 10.1016/J.Molcel.2017.11.019 |
0.744 |
|
2017 |
Marjanović MP, Hurtado-Bagès S, Lassi M, Valero V, Malinverni R, Delage H, Navarro M, Corujo D, Guberovic I, Douet J, Gama-Perez P, Garcia-Roves PM, Ahel I, Ladurner AG, Yanes O, et al. MacroH2A1.1 regulates mitochondrial respiration by limiting nuclear NAD(+) consumption. Nature Structural & Molecular Biology. PMID 28991266 DOI: 10.1038/Nsmb.3481 |
0.68 |
|
2017 |
Singh HR, Murawska M, Ladurner AG. Remodelers tap into nucleosome plasticity. Nature Structural & Molecular Biology. 24: 341-343. PMID 28384136 DOI: 10.1038/Nsmb.3394 |
0.746 |
|
2017 |
Bowman A, Koide A, Goodman JS, Colling ME, Zinne D, Koide S, Ladurner AG. sNASP and ASF1A function through both competitive and compatible modes of histone binding. Nucleic Acids Research. 45: 643-656. PMID 28123037 DOI: 10.1093/Nar/Gkw892 |
0.731 |
|
2016 |
Sellou H, Lebeaupin T, Chapuis C, Smith R, Hegele A, Singh HR, Kozlowski M, Bultmann S, Ladurner AG, Timinszky G, Huet S. The poly(ADP-ribose)-dependent chromatin remodeler Alc1 induces local chromatin relaxation upon DNA damage. Molecular Biology of the Cell. PMID 27733626 DOI: 10.1091/Mbc.E16-05-0269 |
0.804 |
|
2016 |
Nardozza AP, Ladurner AG. Nick Your DNA, Mark Your Chromatin. Molecular Cell. 64: 7-9. PMID 27716488 DOI: 10.1016/J.Molcel.2016.09.023 |
0.449 |
|
2016 |
Murawska M, Ladurner AG. CENPs and Sweet Nucleosomes Face the FACT. Trends in Biochemical Sciences. 41: 736-738. PMID 27499233 DOI: 10.1016/J.Tibs.2016.07.010 |
0.491 |
|
2016 |
Kistemaker HA, Nardozza AP, Overkleeft HS, van der Marel GA, Ladurner AG, Filippov DV. Synthesis and Macrodomain Binding of Mono-ADP-Ribosylated Peptides. Angewandte Chemie (International Ed. in English). 55: 10634-8. PMID 27464500 DOI: 10.1002/Anie.201604058 |
0.377 |
|
2016 |
Peleg S, Feller C, Ladurner AG, Imhof A. The Metabolic Impact on Histone Acetylation and Transcription in Ageing. Trends in Biochemical Sciences. 41: 700-11. PMID 27283514 DOI: 10.1016/J.Tibs.2016.05.008 |
0.392 |
|
2016 |
Dell'Orso S, Wang AH, Shih HY, Saso K, Berghella L, Gutierrez-Cruz G, Ladurner AG, O'Shea JJ, Sartorelli V, Zare H. The Histone Variant MacroH2A1.2 Is Necessary for the Activation of Muscle Enhancers and Recruitment of the Transcription Factor Pbx1. Cell Reports. PMID 26832413 DOI: 10.1016/J.Celrep.2015.12.103 |
0.482 |
|
2016 |
Peleg S, Feller C, Forne I, Schiller E, Sévin DC, Schauer T, Regnard C, Straub T, Prestel M, Klima C, Schmitt Nogueira M, Becker L, Klopstock T, Sauer U, Becker PB, ... ... Ladurner AG, et al. Life span extension by targeting a link between metabolism and histone acetylation in Drosophila. Embo Reports. PMID 26781291 DOI: 10.15252/Embr.201541132 |
0.763 |
|
2015 |
Bowman A, Lercher L, Singh HR, Zinne D, Timinszky G, Carlomagno T, Ladurner AG. The histone chaperone sNASP binds a conserved peptide motif within the globular core of histone H3 through its TPR repeats. Nucleic Acids Research. PMID 26673727 DOI: 10.1093/Nar/Gkv1372 |
0.823 |
|
2015 |
Kozlowski M, Ladurner AG. ATM, MacroH2A.1, and SASP: The Checks and Balances of Cellular Senescence. Molecular Cell. 59: 713-5. PMID 26340421 DOI: 10.1016/J.Molcel.2015.08.010 |
0.805 |
|
2015 |
Ali AA, Timinszky G, Arribas-Bosacoma R, Kozlowski M, Hassa PO, Hassler M, Ladurner AG, Pearl LH, Oliver AW. Corrigendum: The zinc-finger domains of PARP1 cooperate to recognize DNA strand breaks. Nature Structural & Molecular Biology. 22: 645. PMID 26243658 DOI: 10.1038/Nsmb0815-645A |
0.773 |
|
2015 |
Handley A, Schauer T, Ladurner AG, Margulies CE. Designing Cell-Type-Specific Genome-wide Experiments. Molecular Cell. 58: 621-31. PMID 26000847 DOI: 10.1016/J.Molcel.2015.04.024 |
0.763 |
|
2015 |
Handley A, Schauer T, Ladurner AG, Margulies CE. Designing Cell-Type-Specific Genome-wide Experiments Molecular Cell. 58: 621-631. DOI: 10.1016/j.molcel.2015.04.024 |
0.746 |
|
2014 |
Timinszky G, Ladurner AG. PARP1 and CBP lose their footing in cancer. Nature Structural & Molecular Biology. 21: 947-8. PMID 25372309 DOI: 10.1038/Nsmb.2913 |
0.445 |
|
2014 |
Singh HR, Ladurner AG. ACF takes the driver's seat. Molecular Cell. 55: 345-6. PMID 25105485 DOI: 10.1016/J.Molcel.2014.07.014 |
0.706 |
|
2013 |
Hondele M, Ladurner AG. Catch me if you can: how the histone chaperone FACT capitalizes on nucleosome breathing. Nucleus (Austin, Tex.). 4: 443-9. PMID 24413069 DOI: 10.4161/Nucl.27235 |
0.812 |
|
2013 |
Schauer T, Schwalie PC, Handley A, Margulies CE, Flicek P, Ladurner AG. CAST-ChIP maps cell-type-specific chromatin states in the Drosophila central nervous system. Cell Reports. 5: 271-82. PMID 24095734 DOI: 10.1016/J.Celrep.2013.09.001 |
0.798 |
|
2013 |
Czarna A, Berndt A, Singh HR, Grudziecki A, Ladurner AG, Timinszky G, Kramer A, Wolf E. Structures of Drosophila cryptochrome and mouse cryptochrome1 provide insight into circadian function. Cell. 153: 1394-405. PMID 23746849 DOI: 10.1016/J.Cell.2013.05.011 |
0.721 |
|
2013 |
Barkauskaite E, Jankevicius G, Ladurner AG, Ahel I, Timinszky G. The recognition and removal of cellular poly(ADP-ribose) signals. The Febs Journal. 280: 3491-507. PMID 23711178 DOI: 10.1111/Febs.12358 |
0.804 |
|
2013 |
Hondele M, Stuwe T, Hassler M, Halbach F, Bowman A, Zhang ET, Nijmeijer B, Kotthoff C, Rybin V, Amlacher S, Hurt E, Ladurner AG. Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Nature. 499: 111-4. PMID 23698368 DOI: 10.1038/Nature12242 |
0.822 |
|
2013 |
Sharifi R, Morra R, Appel CD, Tallis M, Chioza B, Jankevicius G, Simpson MA, Matic I, Ozkan E, Golia B, Schellenberg MJ, Weston R, Williams JG, Rossi MN, Galehdari H, ... ... Ladurner AG, et al. Deficiency of terminal ADP-ribose protein glycohydrolase TARG1/C6orf130 in neurodegenerative disease. The Embo Journal. 32: 1225-37. PMID 23481255 DOI: 10.1038/Emboj.2013.51 |
0.802 |
|
2013 |
Jankevicius G, Hassler M, Golia B, Rybin V, Zacharias M, Timinszky G, Ladurner AG. A family of macrodomain proteins reverses cellular mono-ADP-ribosylation. Nature Structural & Molecular Biology. 20: 508-14. PMID 23474712 DOI: 10.1038/Nsmb.2523 |
0.771 |
|
2013 |
Forst AH, Karlberg T, Herzog N, Thorsell AG, Gross A, Feijs KL, Verheugd P, Kursula P, Nijmeijer B, Kremmer E, Kleine H, Ladurner AG, Schüler H, Lüscher B. Recognition of mono-ADP-ribosylated ARTD10 substrates by ARTD8 macrodomains. Structure (London, England : 1993). 21: 462-75. PMID 23473667 DOI: 10.1016/J.Str.2012.12.019 |
0.633 |
|
2013 |
Oppikofer M, Kueng S, Keusch JJ, Hassler M, Ladurner AG, Gut H, Gasser SM. Dimerization of Sir3 via its C-terminal winged helix domain is essential for yeast heterochromatin formation. The Embo Journal. 32: 437-49. PMID 23299941 DOI: 10.1038/Emboj.2012.343 |
0.501 |
|
2013 |
Oliver AW, Ali AAE, Timinszky G, Arribas-Bosacoma R, Kozlowski M, Hassa PO, Hassler M, Ladurner AG, Pearl LH. Cooperation of the PARP1 zinc-finger domains in recognising DNA strand breaks Acta Crystallographica Section a Foundations of Crystallography. 69: s69-s69. DOI: 10.1107/S0108767313099418 |
0.792 |
|
2012 |
Hassler M, Ladurner AG. Towards a structural understanding of PARP1 activation and related signalling ADP-ribosyl-transferases. Current Opinion in Structural Biology. 22: 721-9. PMID 22985748 DOI: 10.1016/J.Sbi.2012.08.005 |
0.454 |
|
2012 |
Ali AAE, Timinszky G, Arribas-Bosacoma R, Kozlowski M, Hassa PO, Hassler M, Ladurner AG, Pearl LH, Oliver AW. The zinc-finger domains of PARP1 cooperate to recognize DNA strand breaks. Nature Structural & Molecular Biology. 19: 685-692. PMID 22683995 DOI: 10.1038/Nsmb.2335 |
0.809 |
|
2012 |
Talbert PB, Ahmad K, Almouzni G, Ausió J, Berger F, Bhalla PL, Bonner WM, Cande WZ, Chadwick BP, Chan SW, Cross GA, Cui L, Dimitrov SI, Doenecke D, Eirin-López JM, ... ... Ladurner AG, et al. A unified phylogeny-based nomenclature for histone variants. Epigenetics & Chromatin. 5: 7. PMID 22650316 DOI: 10.1186/1756-8935-5-7 |
0.417 |
|
2011 |
Hondele M, Ladurner AG. The chaperone-histone partnership: for the greater good of histone traffic and chromatin plasticity. Current Opinion in Structural Biology. 21: 698-708. PMID 22054910 DOI: 10.1016/J.Sbi.2011.10.003 |
0.805 |
|
2011 |
Hassler M, Jankevicius G, Ladurner AG. PARG: a macrodomain in disguise. Structure (London, England : 1993). 19: 1351-3. PMID 22000507 DOI: 10.1016/J.Str.2011.09.007 |
0.76 |
|
2011 |
Ehrentraut S, Hassler M, Oppikofer M, Kueng S, Weber JM, Mueller JW, Gasser SM, Ladurner AG, Ehrenhofer-Murray AE. Structural basis for the role of the Sir3 AAA+ domain in silencing: interaction with Sir4 and unmethylated histone H3K79. Genes & Development. 25: 1835-46. PMID 21896656 DOI: 10.1101/Gad.17175111 |
0.475 |
|
2011 |
Murawska M, Hassler M, Renkawitz-Pohl R, Ladurner A, Brehm A. Stress-induced PARP activation mediates recruitment of Drosophila Mi-2 to promote heat shock gene expression. Plos Genetics. 7. PMID 21829383 DOI: 10.1371/Journal.Pgen.1002206 |
0.441 |
|
2010 |
Hondele M, Ladurner A. A mitotic beacon reveals its nucleosome anchor. Molecular Cell. 39: 829-30. PMID 20864028 DOI: 10.1016/J.Molcel.2010.09.001 |
0.759 |
|
2009 |
Timinszky G, Till S, Hassa PO, Hothorn M, Kustatscher G, Nijmeijer B, Colombelli J, Altmeyer M, Stelzer EH, Scheffzek K, Hottiger MO, Ladurner AG. A macrodomain-containing histone rearranges chromatin upon sensing PARP1 activation. Nature Structural & Molecular Biology. 16: 923-9. PMID 19680243 DOI: 10.1038/Nsmb.1664 |
0.824 |
|
2009 |
Gottschalk AJ, Timinszky G, Kong SE, Jin J, Cai Y, Swanson SK, Washburn MP, Florens L, Ladurner AG, Conaway JW, Conaway RC. Poly(ADP-ribosyl)ation directs recruitment and activation of an ATP-dependent chromatin remodeler Proceedings of the National Academy of Sciences of the United States of America. 106: 13770-13774. PMID 19666485 DOI: 10.1073/Pnas.0906920106 |
0.535 |
|
2009 |
Sporn JC, Kustatscher G, Hothorn T, Collado M, Serrano M, Muley T, Schnabel P, Ladurner AG. Histone macroH2A isoforms predict the risk of lung cancer recurrence. Oncogene. 28: 3423-8. PMID 19648962 DOI: 10.1038/Onc.2009.26 |
0.727 |
|
2009 |
Ladurner AG. Chromatin places metabolism center stage. Cell. 138: 18-20. PMID 19596230 DOI: 10.1016/J.Cell.2009.06.025 |
0.384 |
|
2009 |
Hothorn M, Neumann H, Lenherr ED, Wehner M, Rybin V, Hassa PO, Uttenweiler A, Reinhardt M, Schmidt A, Seiler J, Ladurner AG, Herrmann C, Scheffzek K, Mayer A. Catalytic core of a membrane-associated eukaryotic polyphosphate polymerase. Science (New York, N.Y.). 324: 513-6. PMID 19390046 DOI: 10.1126/Science.1168120 |
0.666 |
|
2009 |
Till S, Ladurner AG. Sensing NAD metabolites through macro domains. Frontiers in Bioscience (Landmark Edition). 14: 3246-58. PMID 19273270 DOI: 10.2741/3448 |
0.815 |
|
2009 |
Dani N, Stilla A, Marchegiani A, Tamburro A, Till S, Ladurner AG, Corda D, Di Girolamo M. Combining affinity purification by ADP-ribose-binding macro domains with mass spectrometry to define the mammalian ADP-ribosyl proteome. Proceedings of the National Academy of Sciences of the United States of America. 106: 4243-8. PMID 19246377 DOI: 10.1073/Pnas.0900066106 |
0.8 |
|
2009 |
Wu WH, Wu CH, Ladurner A, Mizuguchi G, Wei D, Xiao H, Luk E, Ranjant A, Wu C. N terminus of Swr1 binds to histone H2AZ and provides a platform for subunit assembly in the chromatin remodeling complex Journal of Biological Chemistry. 284: 6200-6207. PMID 19088068 DOI: 10.1074/Jbc.M808830200 |
0.513 |
|
2008 |
Till S, Diamantara K, Ladurner AG. PARP: a transferase by any other name. Nature Structural & Molecular Biology. 15: 1243-4. PMID 19050719 DOI: 10.1038/Nsmb1208-1243 |
0.792 |
|
2008 |
Stuwe T, Hothorn M, Lejeune E, Rybin V, Bortfeld M, Scheffzek K, Ladurner AG. The FACT Spt16 "peptidase" domain is a histone H3-H4 binding module. Proceedings of the National Academy of Sciences of the United States of America. 105: 8884-9. PMID 18579787 DOI: 10.1073/Pnas.0712293105 |
0.787 |
|
2008 |
Timinszky G, Bortfeld M, Ladurner AG. Repression of RNA polymerase II transcription by a Drosophila oligopeptide. Plos One. 3: e2506. PMID 18575576 DOI: 10.1371/Journal.Pone.0002506 |
0.351 |
|
2008 |
Grummt I, Ladurner AG. A metabolic throttle regulates the epigenetic state of rDNA. Cell. 133: 577-80. PMID 18485866 DOI: 10.1016/J.Cell.2008.04.026 |
0.452 |
|
2007 |
Till S, Ladurner AG. RNA Pol IV plays catch with Argonaute 4. Cell. 131: 643-5. PMID 18022355 DOI: 10.1016/J.Cell.2007.10.044 |
0.788 |
|
2007 |
Li AG, Piluso LG, Cai X, Gadd BJ, Ladurner AG, Liu X. An acetylation switch in p53 mediates holo-TFIID recruitment. Molecular Cell. 28: 408-21. PMID 17996705 DOI: 10.1016/J.Molcel.2007.09.006 |
0.373 |
|
2007 |
Kustatscher G, Ladurner AG. Modular paths to 'decoding' and 'wiping' histone lysine methylation. Current Opinion in Chemical Biology. 11: 628-35. PMID 17988933 DOI: 10.1016/J.Cbpa.2007.09.011 |
0.791 |
|
2007 |
Till S, Lejeune E, Thermann R, Bortfeld M, Hothorn M, Enderle D, Heinrich C, Hentze MW, Ladurner AG. A conserved motif in Argonaute-interacting proteins mediates functional interactions through the Argonaute PIWI domain. Nature Structural & Molecular Biology. 14: 897-903. PMID 17891150 DOI: 10.1038/Nsmb1302 |
0.779 |
|
2007 |
Alonso A, Fritz B, Hasson D, Abrusan G, Cheung F, Yoda K, Radlwimmer B, Ladurner AG, Warburton PE. Co-localization of CENP-C and CENP-H to discontinuous domains of CENP-A chromatin at human neocentromeres. Genome Biology. 8: R148. PMID 17651496 DOI: 10.1186/Gb-2007-8-7-R148 |
0.482 |
|
2007 |
Lejeune E, Bortfeld M, White SA, Pidoux AL, Ekwall K, Allshire RC, Ladurner AG. The chromatin-remodeling factor FACT contributes to centromeric heterochromatin independently of RNAi. Current Biology : Cb. 17: 1219-24. PMID 17614284 DOI: 10.1016/J.Cub.2007.06.028 |
0.815 |
|
2006 |
Ladurner AG. Rheostat control of gene expression by metabolites. Molecular Cell. 24: 1-11. PMID 17018288 DOI: 10.1016/J.Molcel.2006.09.002 |
0.417 |
|
2005 |
Kustatscher G, Hothorn M, Pugieux C, Scheffzek K, Ladurner AG. Splicing regulates NAD metabolite binding to histone macroH2A. Nature Structural & Molecular Biology. 12: 624-5. PMID 15965484 DOI: 10.1038/Nsmb956 |
0.823 |
|
2005 |
Karras GI, Kustatscher G, Buhecha HR, Allen MD, Pugieux C, Sait F, Bycroft M, Ladurner AG. The macro domain is an ADP-ribose binding module. The Embo Journal. 24: 1911-20. PMID 15902274 DOI: 10.1038/Sj.Emboj.7600664 |
0.808 |
|
2005 |
Lejeune E, Ladurner AG. Hitting transcription in all the right places. Nature Structural & Molecular Biology. 12: 390-2. PMID 15870728 DOI: 10.1038/Nsmb0505-390 |
0.811 |
|
2003 |
Ladurner AG. Inactivating chromosomes: a macro domain that minimizes transcription. Molecular Cell. 12: 1-3. PMID 12887886 DOI: 10.1016/S1097-2765(03)00284-3 |
0.439 |
|
2003 |
Ladurner AG, Inouye C, Jain R, Tjian R. Bromodomains mediate an acetyl-histone encoded antisilencing function at heterochromatin boundaries. Molecular Cell. 11: 365-76. PMID 12620225 DOI: 10.1016/S1097-2765(03)00035-2 |
0.665 |
|
2003 |
Ladurner AG. Tick-tock goes the acetylation clock. Nature Structural Biology. 10: 83. PMID 12555082 DOI: 10.1038/Nsb0203-83 |
0.32 |
|
2003 |
Bianco A, Ladurner AG. The Meaning (of Structure) in Life Cell. 115: 7-8. DOI: 10.1016/S0092-8674(03)00770-0 |
0.439 |
|
2002 |
Ladurner AG. The origin of silence. Nature Structural Biology. 9: 718. PMID 12352952 DOI: 10.1038/Nsb1002-718 |
0.304 |
|
2000 |
Jacobson RH, Ladurner AG, King DS, Tjian R. Structure and function of a human TAFII250 double bromodomain module. Science (New York, N.Y.). 288: 1422-5. PMID 10827952 DOI: 10.1126/Science.288.5470.1422 |
0.656 |
|
1999 |
Andel F, Ladurner AG, Inouye C, Tjian R, Nogales E. Three-dimensional structure of the human TFIID-IIA-IIB complex. Science (New York, N.Y.). 286: 2153-6. PMID 10591646 DOI: 10.1126/Science.286.5447.2153 |
0.585 |
|
1999 |
Ryu S, Zhou S, Ladurner AG, Tjian R. The transcriptional cofactor complex CRSP is required for activity of the enhancer-binding protein Sp1. Nature. 397: 446-50. PMID 9989412 DOI: 10.1038/17141 |
0.615 |
|
1998 |
Ladurner AG, Itzhaki LS, Daggett V, Fersht AR. Synergy between simulation and experiment in describing the energy landscape of protein folding. Proceedings of the National Academy of Sciences of the United States of America. 95: 8473-8. PMID 9671702 DOI: 10.1073/Pnas.95.15.8473 |
0.475 |
|
1998 |
Ladurner AG, Itzhaki LS, Fersht AR. Strain in the folding nucleus of chymotrypsin inhibitor 2. Folding & Design. 2: 363-8. PMID 9427010 DOI: 10.1016/S1359-0278(97)00050-3 |
0.496 |
|
1997 |
Ladurner AG, Fersht AR. Glutamine, alanine or glycine repeats inserted into the loop of a protein have minimal effects on stability and folding rates. Journal of Molecular Biology. 273: 330-7. PMID 9367765 DOI: 10.1006/Jmbi.1997.1304 |
0.533 |
|
1997 |
Ladurner AG, Itzhaki LS, de Prat Gay G, Fersht AR. Complementation of peptide fragments of the single domain protein chymotrypsin inhibitor 2. Journal of Molecular Biology. 273: 317-29. PMID 9367764 DOI: 10.1006/Jmbi.1997.1303 |
0.507 |
|
1997 |
Neira JL, Itzhaki LS, Ladurner AG, Davis B, de Prat Gay G, Fersht AR. Following co-operative formation of secondary and tertiary structure in a single protein module. Journal of Molecular Biology. 268: 185-97. PMID 9149151 DOI: 10.1006/Jmbi.1997.0932 |
0.513 |
|
1997 |
Neira JL, Davis B, Ladurner AG, Buckle AM, Gay Gde P, Fersht AR. Towards the complete structural characterization of a protein folding pathway: the structures of the denatured, transition and native states for the association/folding of two complementary fragments of cleaved chymotrypsin inhibitor 2. Direct evidence for a nucleation-condensation mechanism. Folding & Design. 1: 189-208. PMID 9079381 DOI: 10.1016/S1359-0278(96)00031-4 |
0.487 |
|
1996 |
de Prat Gay G, Ruiz-Sanz J, Neira JL, Corrales FJ, Otzen DE, Ladurner AG, Fersht AR. Conformational pathway of the polypeptide chain of chymotrypsin inhibitor-2 growing from its N terminus in vitro. Parallels with the protein folding pathway. Journal of Molecular Biology. 254: 968-79. PMID 7500364 DOI: 10.1006/Jmbi.1995.0669 |
0.516 |
|
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