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V N Podust

Showing results (1-10 of 43) with videos related to

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The Journal of Biological Chemistry|March 7, 1997
Assembly of functional replication factor C expressed using recombinant baculovirusesV N Podust, E Fanning
Nucleic Acids Research|February 25, 1993
Lagging strand DNA synthesis by calf thymus DNA polymerases alpha, beta, delta and epsilon in the presence of auxiliary proteinsV N Podust, U Hübscher
Biochemistry International|April 1, 1991
Human placenta DNA primase: purification of enzyme and analysis of RNA primer synthesisV N Podust, O V Vladimirova, O I Lavrik
The Journal of Biological Chemistry|May 28, 1998
Functional interactions among the subunits of replication factor C potentiate and modulate its ATPase activityV N Podust, N Tiwari, R Ott, et al.
Nucleic Acids Research|August 25, 1992
Calf thymus RF-C as an essential component for DNA polymerase delta and epsilon holoenzymes functionV N Podust, A Georgaki, B Strack, et al.
The Journal of Biological Chemistry|November 21, 1998
Replication factor C disengages from proliferating cell nuclear antigen (PCNA) upon sliding clamp formation, and PCNA itself tethers DNA polymerase delta to DNAV N Podust, N Tiwari, S Stephan, et al.
Nucleic Acids Research|August 11, 1994
Assembly of DNA polymerase delta and epsilon holoenzymes depends on the geometry of the DNA templateL M Podust, V N Podust, C Floth, et al.
Biochemistry|April 18, 1995
DNA polymerase delta holoenzyme: action on single-stranded DNA and on double-stranded DNA in the presence of replicative DNA helicasesV N Podust, L M Podust, F Müller, et al.
The EMBO Journal|November 15, 1995
Tyrosine 114 is essential for the trimeric structure and the functional activities of human proliferating cell nuclear antigenZ O Jónsson, V N Podust, L M Podust, et al.
Molecular and Cellular Biology|June 1, 1995
Mammalian DNA polymerase auxiliary proteins: analysis of replication factor C-catalyzed proliferating cell nuclear antigen loading onto circular double-stranded DNAL M Podust, V N Podust, J M Sogo, et al.
Pageof 5

Showing results (1-10 of 43) with videos related to

Sort By:
Pageof 5
The Journal of Biological Chemistry|March 7, 1997
Assembly of functional replication factor C expressed using recombinant baculovirusesV N Podust, E Fanning
Nucleic Acids Research|February 25, 1993
Lagging strand DNA synthesis by calf thymus DNA polymerases alpha, beta, delta and epsilon in the presence of auxiliary proteinsV N Podust, U Hübscher
Biochemistry International|April 1, 1991
Human placenta DNA primase: purification of enzyme and analysis of RNA primer synthesisV N Podust, O V Vladimirova, O I Lavrik
The Journal of Biological Chemistry|May 28, 1998
Functional interactions among the subunits of replication factor C potentiate and modulate its ATPase activityV N Podust, N Tiwari, R Ott, et al.
Nucleic Acids Research|August 25, 1992
Calf thymus RF-C as an essential component for DNA polymerase delta and epsilon holoenzymes functionV N Podust, A Georgaki, B Strack, et al.
The Journal of Biological Chemistry|November 21, 1998
Replication factor C disengages from proliferating cell nuclear antigen (PCNA) upon sliding clamp formation, and PCNA itself tethers DNA polymerase delta to DNAV N Podust, N Tiwari, S Stephan, et al.
Nucleic Acids Research|August 11, 1994
Assembly of DNA polymerase delta and epsilon holoenzymes depends on the geometry of the DNA templateL M Podust, V N Podust, C Floth, et al.
Biochemistry|April 18, 1995
DNA polymerase delta holoenzyme: action on single-stranded DNA and on double-stranded DNA in the presence of replicative DNA helicasesV N Podust, L M Podust, F Müller, et al.
The EMBO Journal|November 15, 1995
Tyrosine 114 is essential for the trimeric structure and the functional activities of human proliferating cell nuclear antigenZ O Jónsson, V N Podust, L M Podust, et al.
Molecular and Cellular Biology|June 1, 1995
Mammalian DNA polymerase auxiliary proteins: analysis of replication factor C-catalyzed proliferating cell nuclear antigen loading onto circular double-stranded DNAL M Podust, V N Podust, J M Sogo, et al.
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