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Insect Molecular Biology|October 3, 2008
Environmental conditions impinge on dragline silk protein compositionK-H Guehrs, B Schlott, F Grosse, et al.
The Review of Scientific Instruments|October 31, 2021
Breakthrough instruments and products: Lattice Lightsheet 7-Non-invasive imaging of the subcellular dynamics of lifeK Elgass, D Hartmann, J Siebenmorgen, et al.
Journal of Virology|January 1, 1993
The extreme C terminus of herpes simplex virus DNA polymerase is crucial for functional interaction with processivity factor UL42 and for viral replicationP Digard, W R Bebrin, K Weisshart, et al.
Molecular and Cellular Biology|May 1, 1994
Species-specific functional interactions of DNA polymerase alpha-primase with simian virus 40 (SV40) T antigen require SV40 origin DNAC Schneider, K Weisshart, L A Guarino, et al.
Journal of Virology|August 17, 2001
Amino acids 257 to 288 of mouse p48 control the cooperation of polyomavirus large T antigen, replication protein A, and DNA polymerase alpha-primase to synthesize DNA in vitroA R Kautz, K Weisshart, A Schneider, et al.
Journal of Virology|February 13, 2001
Different regions of primase subunit p48 control mouse polyomavirus and simian virus 40 DNA replication in vitroA R Kautz, A Schneider, K Weisshart, et al.
FEBS Letters|January 12, 1999
Alternative conformations of human replication protein A are detected by crosslinks with primers carrying a photoreactive group at the 3'-endO I Lavrik, D M Kolpashchikov, H P Nasheuer, et al.
The Journal of Biological Chemistry|September 9, 1994
Structural and functional organization of herpes simplex virus DNA polymerase investigated by limited proteolysisK Weisshart, A A Kuo, C B Hwang, et al.
The Journal of Biological Chemistry|April 5, 2000
Protein-protein interactions of the primase subunits p58 and p48 with simian virus 40 T antigen are required for efficient primer synthesis in a cell-free systemK Weisshart, H Förster, E Kremmer, et al.
Journal of Virology|February 11, 1999
Two regions of simian virus 40 T antigen determine cooperativity of double-hexamer assembly on the viral origin of DNA replication and promote hexamer interactions during bidirectional origin DNA unwindingK Weisshart, P Taneja, A Jenne, et al.
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