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Katherine A. Jones

Researcher at Salk Institute for Biological Studies

Publications -  81
Citations -  13077

Katherine A. Jones is an academic researcher from Salk Institute for Biological Studies. The author has contributed to research in topics: Transcription (biology) & RNA polymerase II. The author has an hindex of 46, co-authored 79 publications receiving 12710 citations. Previous affiliations of Katherine A. Jones include Howard Hughes Medical Institute & University of California, Berkeley.

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A Novel CDK9-Associated C-Type Cyclin Interacts Directly with HIV-1 Tat and Mediates Its High-Affinity, Loop-Specific Binding to TAR RNA

TL;DR: It is proposed that Tat directs cyclin T-CDK9 to RNAPII through cooperative binding to TAR RNA, and confers a requirement for sequences in the loop of TAR that are not recognized by Tat alone.
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Promoter-specific activation of RNA polymerase II transcription by Sp1

TL;DR: The RNA polymerase II transcription factor Sp1 is a protein that binds to specific DNA sequences and activates RNA synthesis from a select group of promoters and appears to be important for modulation of gene expression in higher organisms.
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A cellular DNA-binding protein that activates eukaryotic transcription and DNA replication

TL;DR: It is concluded that CTF/NF-I can serve both as a transcription selectivity factor for RNA polymerase II and as an initiation factor for adenovirus DNA replication.
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Activation of the AIDS retrovirus promoter by the cellular transcription factor, Sp1

TL;DR: Findings suggest that one important component of the AIDS virus transcriptional control region interacts with a cellular transcription factor, Sp1, and that this factor must function in conjunction with transcriptional elements located downstream of the RNA cap site to mediate the response of the LTR to viral trans-activation.
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Two distinct transcription factors bind to the HSV thymidine kinase promoter in vitro.

TL;DR: An in vitro transcription system derived from uninfected HeLa cells that accurately initiates RNA synthesis at the herpes virus thymidine kinase (TK) promoter is characterized and three distinctive protein binding sites are identified.