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Athar Ansari

Researcher at Wayne State University

Publications -  37
Citations -  2088

Athar Ansari is an academic researcher from Wayne State University. The author has contributed to research in topics: RNA polymerase II & Transcription (biology). The author has an hindex of 19, co-authored 36 publications receiving 1944 citations. Previous affiliations of Athar Ansari include University of Medicine and Dentistry of New Jersey & Rutgers University.

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Dual role of TFIIH in DNA excision repair and in transcription by RNA polymerase II

TL;DR: It is found thatTFIIH has a dual role, being required for basal transcription of class II genes and for participation in DNA-excision repair, and the general transcription factor IIE negatively modulates the helicase activity of TFIIH through a direct interaction between TFIIE and the ERCC3 subunit of TF IIH.
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A role for the CPF 3′-end processing machinery in RNAP II-dependent gene looping

TL;DR: A model for RNAP II transcription is proposed in which promoter and terminator regions are juxtaposed, and that the resulting gene loops facilitate transcription reinitiation by the same molecule ofRNAP II in a manner dependent upon Ssu72-mediated CTD dephosphorylation.
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Characterization of the Protein Kinase Activity of TRPM7/ChaK1, a Protein Kinase Fused to the Transient Receptor Potential Ion Channel

TL;DR: Considering intracellular ion concentrations, the results suggest that, among divalent metal ions, only Mg2+ can directly modulate TRPM7/ChaK1 kinase activity in vivo.
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Esc1, a Nuclear Periphery Protein Required for Sir4-Based Plasmid Anchoring and Partitioning

TL;DR: The data suggest that Esc1 is a component of a redundant pathway that functions to localize silencing complexes to the nuclear periphery, and that Sir protein-mediated partitioning of a telomere-based plasmid also required ESC1.
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SLU7 and a novel activity, SSF1, act during the PRP16-dependent step of yeast pre-mRNA splicing.

TL;DR: It is shown that SLU7 protein and a novel activity that is named SSF1 (second‐step factor 1) were required in concert with PRP16 to promote progression through the second catalytic step of splicing.