Publications by authors named "Nadia P Allen"
Article Synopsis
- The IGRA QuantiFERON-TB Gold Plus (QFT-Plus) has been updated to include two antigen tubes, TB1 and TB2, targeting specific T-cell responses to Mycobacterium tuberculosis.
- TB1 primarily stimulates CD4 T-cells for cell-mediated responses, while TB2 is designed to also engage CD8 T-cells by utilizing newly developed peptides.
- Research demonstrated that specific CD4 T-cell clones responded to both tubes, but CD8 T-cell clones showed a much stronger response (>140-fold difference) primarily to TB2, confirming its effectiveness in detecting CD8 T-cell activity.
Article Synopsis
- RASSF1A is a tumor suppressor that is often silenced in tumors due to promoter methylation, affecting important cellular functions like cell cycle regulation and apoptosis.
- The study reveals a new pathway where RASSF1A interacts with the protein MOAP-1, which is crucial for activating Bax, a protein that promotes cell death, particularly when K-Ras is activated.
- Tumor-derived mutations in RASSF1A disrupt its interaction with MOAP-1 and impair Bax activation, highlighting a critical pro-apoptotic pathway involving K-Ras, RASSF1A, and Bax that is compromised in some cancers.
A thorough analysis of the protein interaction partners of the yeast GTPase Gsp1p was carried out by a multidimensional chromatography strategy of strong cation exchange fractionation of peptides followed by reverse phase LC-ESI-MSMS using a QSTAR instrument. This dataset was then analyzed using the latest developmental version of Protein Prospector. The Prospector search results were also compared with results from the search engine "Mascot" using a new results comparison program within Prospector named "SearchCompare.
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- An in-depth analysis was performed on a dataset from a QqTOF instrument, focusing on 3269 CID spectra.
- Through manual verification, 2368 spectra were identified as predicted tryptic peptides, showcasing the reliability of the results.
- The study also examined non-matching spectra, providing insights into their composition and illustrating the capability of QqTOF instruments to produce highly interpretable data.
Deciphering networks of protein interactions at the nuclear pore complex.
Mol Cell Proteomics
December 2002
The nuclear pore complex (NPC) gates the only known conduit for molecular exchange between the nucleus and cytoplasm of eukaryotic cells. Macromolecular transport across the NPC is mediated by nucleocytoplasmic shuttling receptors termed karyopherins (Kaps). Kaps interact with NPC proteins (nucleoporins) that contain FG peptide repeats (FG Nups) and altogether carry hundreds of different cargoes across the NPC.
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