Christian Speck - Publications

Affiliations: 
Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 
 Imperial College, London, London, England, United Kingdom 
Website:
http://www.imperial.ac.uk/people/chris.speck

42 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2022 Saleh A, Noguchi Y, Aramayo R, Ivanova ME, Stevens KM, Montoya A, Sunidhi S, Carranza NL, Skwark MJ, Speck C. The structural basis of Cdc7-Dbf4 kinase dependent targeting and phosphorylation of the MCM2-7 double hexamer. Nature Communications. 13: 2915. PMID 35614055 DOI: 10.1038/s41467-022-30576-1  0.335
2021 Feng X, Noguchi Y, Barbon M, Stillman B, Speck C, Li H. The structure of ORC-Cdc6 on an origin DNA reveals the mechanism of ORC activation by the replication initiator Cdc6. Nature Communications. 12: 3883. PMID 34162887 DOI: 10.1038/s41467-021-24199-1  0.755
2020 Yuan Z, Schneider S, Dodd T, Riera A, Bai L, Yan C, Magdalou I, Ivanov I, Stillman B, Li H, Speck C. Structural mechanism of helicase loading onto replication origin DNA by ORC-Cdc6. Proceedings of the National Academy of Sciences of the United States of America. PMID 32669428 DOI: 10.1073/Pnas.2006231117  0.764
2020 Roman-Trufero M, Ito CM, Pedebos C, Magdalou I, Wang YF, Karimi MM, Moyon B, Webster Z, di Gregorio A, Azuara V, Khalid S, Speck C, Rodriguez T, Dillon N. Evolution of an amniote-specific mechanism for modulating ubiquitin signalling via phosphoregulation of the E2 enzyme UBE2D3. Molecular Biology and Evolution. PMID 32145025 DOI: 10.1093/Molbev/Msaa060  0.329
2017 Noguchi Y, Yuan Z, Bai L, Schneider S, Zhao G, Stillman B, Speck C, Li H. Cryo-EM structure of Mcm2-7 double hexamer on DNA suggests a lagging-strand DNA extrusion model. Proceedings of the National Academy of Sciences of the United States of America. PMID 29078375 DOI: 10.1073/Pnas.1712537114  0.749
2017 Riera A, Barbon M, Noguchi Y, Reuter LM, Schneider S, Speck C. From structure to mechanism-understanding initiation of DNA replication. Genes & Development. 31: 1073-1088. PMID 28717046 DOI: 10.1101/Gad.298232.117  0.645
2017 Yuan Z, Riera A, Bai L, Sun J, Nandi S, Spanos C, Chen ZA, Barbon M, Rappsilber J, Stillman B, Speck C, Li H. Structural basis of Mcm2-7 replicative helicase loading by ORC-Cdc6 and Cdt1. Nature Structural & Molecular Biology. PMID 28191893 DOI: 10.1038/Nsmb.3372  0.811
2016 Tognetti S, Speck C. Replicating repetitive DNA. Nature Cell Biology. 18: 593-4. PMID 27230530 DOI: 10.1038/Ncb3367  0.544
2015 Herrera MC, Tognetti S, Riera A, Zech J, Clarke P, Fernández-Cid A, Speck C. A reconstituted system reveals how activating and inhibitory interactions control DDK dependent assembly of the eukaryotic replicative helicase. Nucleic Acids Research. 43: 10238-50. PMID 26338774 DOI: 10.1093/Nar/Gkv881  0.509
2015 Chang F, Riera A, Evrin C, Sun J, Li H, Speck C, Weinreich M. Cdc6 ATPase activity disengages Cdc6 from the pre-replicative complex to promote DNA replication. Elife. 4. PMID 26305410 DOI: 10.7554/Elife.05795  0.773
2015 Riera A, Speck C. Opening the gate to DNA replication. Cell Cycle (Georgetown, Tex.). 14: 6-8. PMID 25483056 DOI: 10.4161/15384101.2014.987624  0.665
2015 Tognetti S, Riera A, Speck C. Switch on the engine: how the eukaryotic replicative helicase MCM2-7 becomes activated. Chromosoma. 124: 13-26. PMID 25308420 DOI: 10.1007/S00412-014-0489-2  0.61
2015 Herrera MC, Tognetti S, Riera A, Zech J, Clarke P, Fernández-Cid A, Speck C. A reconstituted system reveals how activating and inhibitory interactions control DDK dependent assembly of the eukaryotic replicative helicase Nucleic Acids Research. 43: 10238-10250. DOI: 10.1093/nar/gkv881  0.417
2014 Silva N, Ferrandiz N, Barroso C, Tognetti S, Lightfoot J, Telecan O, Encheva V, Faull P, Hanni S, Furger A, Snijders AP, Speck C, Martinez-Perez E. The fidelity of synaptonemal complex assembly is regulated by a signaling mechanism that controls early meiotic progression. Developmental Cell. 31: 503-11. PMID 25455309 DOI: 10.1016/J.Devcel.2014.10.001  0.394
2014 Sun J, Fernandez-Cid A, Riera A, Tognetti S, Yuan Z, Stillman B, Speck C, Li H. Structural and mechanistic insights into Mcm2-7 double-hexamer assembly and function. Genes & Development. 28: 2291-303. PMID 25319829 DOI: 10.1101/Gad.242313.114  0.768
2014 Samel SA, Fernández-Cid A, Sun J, Riera A, Tognetti S, Herrera MC, Li H, Speck C. A unique DNA entry gate serves for regulated loading of the eukaryotic replicative helicase MCM2-7 onto DNA. Genes & Development. 28: 1653-66. PMID 25085418 DOI: 10.1101/Gad.242404.114  0.623
2014 Riera A, Tognetti S, Speck C. Helicase loading: how to build a MCM2-7 double-hexamer. Seminars in Cell & Developmental Biology. 30: 104-9. PMID 24637008 DOI: 10.1016/J.Semcdb.2014.03.008  0.592
2014 Evrin C, Fernández-Cid A, Riera A, Zech J, Clarke P, Herrera MC, Tognetti S, Lurz R, Speck C. The ORC/Cdc6/MCM2-7 complex facilitates MCM2-7 dimerization during prereplicative complex formation Nucleic Acids Research. 42: 2257-2269. PMID 24234446 DOI: 10.1093/Nar/Gkt1148  0.48
2013 Riera A, Li H, Speck C. Seeing is believing: the MCM2-7 helicase trapped in complex with its DNA loader. Cell Cycle (Georgetown, Tex.). 12: 2917-8. PMID 23974098 DOI: 10.4161/Cc.26132  0.682
2013 Sun J, Evrin C, Samel SA, Fernández-Cid A, Riera A, Kawakami H, Stillman B, Speck C, Li H. Cryo-EM structure of a helicase loading intermediate containing ORC-Cdc6-Cdt1-MCM2-7 bound to DNA. Nature Structural & Molecular Biology. 20: 944-51. PMID 23851460 DOI: 10.1038/Nsmb.2629  0.81
2013 Riera A, Fernández-Cid A, Speck C. The ORC/Cdc6/MCM2–7 complex, a new power player for regulated helicase loading. Cell Cycle (Georgetown, Tex.). 12: 2155-6. PMID 23803736 DOI: 10.4161/Cc.25336  0.582
2013 Fernández-Cid A, Riera A, Tognetti S, Herrera MC, Samel S, Evrin C, Winkler C, Gardenal E, Uhle S, Speck C. An ORC/Cdc6/MCM2-7 complex is formed in a multistep reaction to serve as a platform for MCM double-hexamer assembly. Molecular Cell. 50: 577-88. PMID 23603117 DOI: 10.1016/J.Molcel.2013.03.026  0.605
2013 Evrin C, Fernández-Cid A, Zech J, Herrera MC, Riera A, Clarke P, Brill S, Lurz R, Speck C. In the absence of ATPase activity, pre-RC formation is blocked prior to MCM2-7 hexamer dimerization. Nucleic Acids Research. 41: 3162-72. PMID 23376927 DOI: 10.1093/Nar/Gkt043  0.646
2012 Sun J, Kawakami H, Zech J, Speck C, Stillman B, Li H. Cdc6-induced conformational changes in ORC bound to origin DNA revealed by cryo-electron microscopy. Structure (London, England : 1993). 20: 534-44. PMID 22405012 DOI: 10.1016/J.Str.2012.01.011  0.821
2011 Johansson E, Speck C, Chabes A. A top-down view on DNA replication and recombination from 9,000 feet above sea level. Genome Biology. 12: 304. PMID 21554750 DOI: 10.1186/Gb-2011-12-4-304  0.744
2009 Evrin C, Clarke P, Zech J, Lurz R, Sun J, Uhle S, Li H, Stillman B, Speck C. A double-hexameric MCM2-7 complex is loaded onto origin DNA during licensing of eukaryotic DNA replication. Proceedings of the National Academy of Sciences of the United States of America. 106: 20240-5. PMID 19910535 DOI: 10.1073/Pnas.0911500106  0.741
2008 Chen Z, Speck C, Wendel P, Tang C, Stillman B, Li H. The architecture of the DNA replication origin recognition complex in Saccharomyces cerevisiae. Proceedings of the National Academy of Sciences of the United States of America. 105: 10326-31. PMID 18647841 DOI: 10.1073/Pnas.0803829105  0.719
2007 Speck C, Stillman B. Cdc6 ATPase activity regulates ORC x Cdc6 stability and the selection of specific DNA sequences as origins of DNA replication. The Journal of Biological Chemistry. 282: 11705-14. PMID 17314092 DOI: 10.1074/Jbc.M700399200  0.735
2007 Majka J, Speck C. Analysis of protein-DNA interactions using surface plasmon resonance. Advances in Biochemical Engineering/Biotechnology. 104: 13-36. PMID 17290817 DOI: 10.1007/10_026  0.509
2005 Speck C, Chen Z, Li H, Stillman B. ATPase-dependent cooperative binding of ORC and Cdc6 to origin DNA. Nature Structural & Molecular Biology. 12: 965-71. PMID 16228006 DOI: 10.1038/Nsmb1002  0.78
2004 de la Hoz AB, Pratto F, Misselwitz R, Speck C, Weihofen W, Welfle K, Saenger W, Welfle H, Alonso JC. Recognition of DNA by omega protein from the broad-host range Streptococcus pyogenes plasmid pSM19035: analysis of binding to operator DNA with one to four heptad repeats. Nucleic Acids Research. 32: 3136-47. PMID 15190131 DOI: 10.1093/Nar/Gkh633  0.592
2002 Pieper U, Groll DH, Wünsch S, Gast FU, Speck C, Mücke N, Pingoud A. The GTP-dependent restriction enzyme McrBC from Escherichia coli forms high-molecular mass complexes with DNA and produces a cleavage pattern with a characteristic 10-base pair repeat. Biochemistry. 41: 5245-54. PMID 11955074 DOI: 10.1021/Bi015687U  0.529
2002 Berenstein D, Olesen K, Speck C, Skovgaard O. Genetic organization of the Vibrio harveyi DnaA gene region and analysis of the function of the V. harveyi DnaA protein in Escherichia coli. Journal of Bacteriology. 184: 2533-8. PMID 11948168 DOI: 10.1128/Jb.184.9.2533-2538.2002  0.414
2002 Skarstad K, Lueder G, Lurz R, Speck C, Messer W. The Escherichia coli SeqA protein binds specifically and co‐operatively to two sites in hemimethylated and fully methylated oriC Molecular Microbiology. 36: 1319-1326. PMID 10931282 DOI: 10.1046/J.1365-2958.2000.01943.X  0.706
2001 Messer W, Blaesing F, Jakimowicz D, Krause M, Majka J, Nardmann J, Schaper S, Seitz H, Speck C, Weigel C, Wegrzyn G, Welzeck M, Zakrzewska-Czerwinska J. Bacterial replication initiator DnaA. Rules for DnaA binding and roles of DnaA in origin unwinding and helicase loading. Biochimie. 83: 5-12. PMID 11254968 DOI: 10.1016/S0300-9084(00)01216-5  0.723
2001 Speck C, Messer W. Mechanism of origin unwinding: sequential binding of DnaA to double- and single-stranded DNA. The Embo Journal. 20: 1469-76. PMID 11250912 DOI: 10.1093/Emboj/20.6.1469  0.734
2000 Schaper S, Nardmann J, Lüder G, Lurz R, Speck C, Messer W. Identification of the chromosomal replication origin from Thermus thermophilus and its interaction with the replication initiator DnaA Journal of Molecular Biology. 299: 655-665. PMID 10835275 DOI: 10.1006/Jmbi.2000.3764  0.724
2000 Messer W, Blaesing F, Majka J, Nardmann J, Schaper S, Schmidt A, Seitz H, Speck C, Tüngler D, Wegrzyn G, Weigel C, Welzeck M, Zakrzewska-Czerwinska J. Functional domains of DnaA proteins. Biochimie. 81: 819-25. PMID 10572294 DOI: 10.1016/S0300-9084(99)00215-1  0.723
2000 Speck C, Weigel C, Messer W. ATP- and ADP-dnaA protein, a molecular switch in gene regulation. The Embo Journal. 18: 6169-76. PMID 10545126 DOI: 10.1093/Emboj/18.21.6169  0.694
1998 Szalewska-Palasz A, Weigel C, Speck C, Srutkowska S, Konopa G, Lurz R, Marszalek J, Taylor K, Messer W, Wegrzyn G. Interaction of the Escherichia coli DnaA protein with bacteriophage λ DNA Molecular and General Genetics. 259: 679-688. PMID 9819062 DOI: 10.1007/S004380050863  0.766
1998 Jakimowicz D, Majka J, Messer W, Speck C, Fernandez M, Cruz Martin M, Sanchez J, Schauwecker F, Keller U, Schrempf H, Zakrzewska-Czerwinńska J. Structural elements of the Streptomyces oriC region and their interactions with the DnaA protein. Microbiology (Reading, England). 144: 1281-1290. PMID 9611803 DOI: 10.1099/00221287-144-5-1281  0.653
1997 Speck C, Weigel C, Messer W. From footprint to toeprint: a close-up of the DnaA box, the binding site for the bacterial initiator protein DnaA. Nucleic Acids Research. 25: 3242-7. PMID 9297181 DOI: 10.1093/Nar/25.16.3242  0.689
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