153 research outputs found
O-linked glycoproteins of the nuclear pore complex interact with a cytosolic factor required for nuclear protein import.
Impact of the Siena College Tech Valley Scholars Program on Student Outcomes
The experimental group for this study included 38 students who entered the Tech Valley Scholars (TVS) program over the course of three academic years, from 2009-10 through 2011-12. Two groups of controls were used: a randomly selected sample of STEM students who matriculated in the same time frame; and a matched sample. The TVS students and controls were compared on two primary outcome variables: graduation (or retention to senior year), and final cumulative GPA. The major findings of this study are that (1) the TVS students had better outcomes than both the randomly selected comparison group and the matched control group, (2) unmet financial need is an important risk factor for non-retention, (3) students with moderately high unmet need can be academically successful if retained, and (4) the TVS program is having a positive impact on at-risk students. Recommendations for effective and efficient allocation of scholarship funds are given and future statistical studies are recommended
Nuclear protein import in permeabilized mammalian cells requires soluble cytoplasmic factors
Abstract. We have developed an in vitro system involving digitonin-permeabilized vertebrate cells to study biochemical events in the transport of macromolecules across the nuclear envelope. While treatment of cultured cells with digitonin permeabilizes the plasma membranes to macromolecules, the nuclear envelopes remain structurally intact and nuclei retain the ability to transport and accumulate proteins containing the SV40 large T antigen nuclear location sequence. Transport requires addition of exogenous cytosol to permeabilized cells, indicating the soluble cytoplasmic factor(s) required for nuclear import are released during digitonin treatment. In this reconstituted import system, a protein containing a nuclear location signal is rapidly accumulated in nuclei, wher
Opioid Receptor Types Selectively Cointernalize with G Protein-Coupled Receptor Kinases 2 and 3
The structure of the GRK2–Gβγ complex: intimate association of G-protein signaling modules
Cell Imaging Assays for G Protein‐Coupled Receptor Internalization: Application to High‐Throughput Screening
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