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Robert A. Sclafani

Researcher at University of Colorado Denver

Publications -  73
Citations -  4688

Robert A. Sclafani is an academic researcher from University of Colorado Denver. The author has contributed to research in topics: Origin recognition complex & Cell cycle. The author has an hindex of 33, co-authored 73 publications receiving 4493 citations. Previous affiliations of Robert A. Sclafani include Anschutz Medical Campus & University of Colorado Boulder.

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Cell Cycle Regulation of DNA Replication

TL;DR: Cell cycle regulation by protein phosphorylation ensures that pre-RC assembly can only occur in G1 phase, whereas helicase activation and loading canonly occur in S phase, and checkpoint regulation maintains high fidelity by stabilizing replication forks and preventing cell cycle progression during replication stress or damage.
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The structure and function of MCM from archaeal M.Thermoautotrophicum

TL;DR: The structure of a fragment of MCM from Methanobacterium thermoautotrophicum, a model system for eukaryotic MCM, is determined, revealing a novel dodecameric architecture with a remarkably long central channel and a common architecture for a similar task: gripping/remodeling DNA and regulating MCM activity.
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mcm5/cdc46-bob1 bypasses the requirement for the S phase activator Cdc7p

TL;DR: The characterization in S. cerevisiae of a recessive mutation in a member of the MCM family, MCM5/CDC46, which bypasses the requirement for Cdc7p and its interacting factor Dbf4p is reported.
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Biphasic Regulation of Breast Cancer Cell Growth by Progesterone: Role of the Cyclin-Dependent Kinase Inhibitors, p21 and p27Kip1

TL;DR: It is concluded that progesterone is neither inherently proliferative nor antiproliferative, but that it is capable of stimulating or inhibiting cell growth depending on whether treatment is transient or continuous.
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Cell cycle regulation of the yeast Cdc7 protein kinase by association with the Dbf4 protein.

TL;DR: It is proposed that Dbf4 may represent a cyclin-like molecule specific for the activation of Cdc7 kinase, which is consistent with CDC7 function in the cell cycle.