Author pages are created from data sourced from our academic publisher partnerships and public sources.
Share This Author
An Enzymatic Activity in the Yeast Sir2 Protein that Is Essential for Gene Silencing
Cyclic-AMP-dependent protein kinase type II is associated with the Golgi complex and with centrosomes
DNA fragmentation and NAD depletion. Their relation to the turnover of endogenous mono(ADP-ribosyl) and poly(ADP-ribosyl) proteins.
Specific inhibition of poly adpribose polymerase by thymidine and nicotinamide in HeLa cells
Rapid isolation of mouse Leydig cells by centrifugation in Percoll density gradients with complete retention of morphological and biochemical integrity.
Stimulation of proteinase K action by denaturing agents: application to the isolation of nucleic acids and the degradation of 'masked' proteins.
The combined action of the detergent and proteinase K was effective in degrading "masked" proteins in a poly(adenosine diphosphoribose) preparation which could not be attacked by the proteinase alone.
Cellular recovery of dividing and confluent C3H10T1/2 cells from N-methyl-N'-nitro-N-nitrosoguanidine in the presence of ADP-ribosylation inhibitors.
- E. Jacobson, J. Y. Smith, K. Wielckens, H. Hilz, M. Jacobson
- Biology, ChemistryCarcinogenesis
- 1 May 1985
It is suggested that ADP-ribosylation is required for normal cell cycle progression following DNA damage in dividing cells.
Molecular Heterogeneity of Free PSA in Sera of Patients with Benign and Malignant Prostate Tumors
- H. Hilz, J. Noldus, P. Hammerer, F. Buck, Martina Lück, H. Huland
- Biology, MedicineEuropean Urology
- 2 September 1999
Free prostate-specific antigen as obtained from BPH and PCa sera represents a heterogeneous fraction and Diagnostic potential could arise from the quantitative differences of the smaller PSA derivatives seen between PCa and BPH sera.
Poly(ADP-ribose) and ADP-ribosylation of proteins.
Rapid and reversible translocation of the catalytic subunit of cAMP‐dependent protein kinase type II from the Golgi complex to the nucleus.
The results suggest that nuclear translocation of activated protein kinase subunits may represent an important link between hormonal stimuli and physiological responses in unstimulated interphase bovine epithelial cells.