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John C W Randell

Showing results (1-10 of 8) with videos related to

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Journal of Molecular Biology|December 16, 2003
The herpes simplex virus processivity factor, UL42, binds DNA as a monomerJohn C W Randell, Donald M Coen
Molecular Cell|December 22, 2004
ATP hydrolysis by ORC catalyzes reiterative Mcm2-7 assembly at a defined origin of replicationJayson L Bowers, John C W Randell, Shuyan Chen, et al.
Molecular Cell|January 3, 2006
Sequential ATP hydrolysis by Cdc6 and ORC directs loading of the Mcm2-7 helicaseJohn C W Randell, Jayson L Bowers, Heather K Rodríguez, et al.
Genes & Development|March 10, 2009
Incorporation into the prereplicative complex activates the Mcm2-7 helicase for Cdc7-Dbf4 phosphorylationLaura I Francis, John C W Randell, Thomas J Takara, et al.
Journal of Virology|September 6, 2005
Effects of substitutions of arginine residues on the basic surface of herpes simplex virus UL42 support a role for DNA binding in processive DNA synthesisJohn C W Randell, Gloria Komazin, Changying Jiang, et al.
Journal of Virology|January 19, 2007
Mutations that decrease DNA binding of the processivity factor of the herpes simplex virus DNA polymerase reduce viral yield, alter the kinetics of viral DNA replication, and decrease the fidelity of DNA replicationChangying Jiang, Ying T Hwang, John C W Randell, et al.
Journal of Virology|August 24, 2007
Herpes simplex virus mutants with multiple substitutions affecting DNA binding of UL42 are impaired for viral replication and DNA synthesisChangying Jiang, Ying T Hwang, Guangliang Wang, et al.
Molecular Cell|November 13, 2010
Mec1 is one of multiple kinases that prime the Mcm2-7 helicase for phosphorylation by Cdc7John C W Randell, Andy Fan, Clara Chan, et al.
Pageof 1

Showing results (1-10 of 8) with videos related to

Sort By:
Pageof 1
Journal of Molecular Biology|December 16, 2003
The herpes simplex virus processivity factor, UL42, binds DNA as a monomerJohn C W Randell, Donald M Coen
Molecular Cell|December 22, 2004
ATP hydrolysis by ORC catalyzes reiterative Mcm2-7 assembly at a defined origin of replicationJayson L Bowers, John C W Randell, Shuyan Chen, et al.
Molecular Cell|January 3, 2006
Sequential ATP hydrolysis by Cdc6 and ORC directs loading of the Mcm2-7 helicaseJohn C W Randell, Jayson L Bowers, Heather K Rodríguez, et al.
Genes & Development|March 10, 2009
Incorporation into the prereplicative complex activates the Mcm2-7 helicase for Cdc7-Dbf4 phosphorylationLaura I Francis, John C W Randell, Thomas J Takara, et al.
Journal of Virology|September 6, 2005
Effects of substitutions of arginine residues on the basic surface of herpes simplex virus UL42 support a role for DNA binding in processive DNA synthesisJohn C W Randell, Gloria Komazin, Changying Jiang, et al.
Journal of Virology|January 19, 2007
Mutations that decrease DNA binding of the processivity factor of the herpes simplex virus DNA polymerase reduce viral yield, alter the kinetics of viral DNA replication, and decrease the fidelity of DNA replicationChangying Jiang, Ying T Hwang, John C W Randell, et al.
Journal of Virology|August 24, 2007
Herpes simplex virus mutants with multiple substitutions affecting DNA binding of UL42 are impaired for viral replication and DNA synthesisChangying Jiang, Ying T Hwang, Guangliang Wang, et al.
Molecular Cell|November 13, 2010
Mec1 is one of multiple kinases that prime the Mcm2-7 helicase for phosphorylation by Cdc7John C W Randell, Andy Fan, Clara Chan, et al.
Pageof 1