M
Michael B. Mathews
Researcher at Rutgers University
Publications - 182
Citations - 19433
Michael B. Mathews is an academic researcher from Rutgers University. The author has contributed to research in topics: RNA & Transcription (biology). The author has an hindex of 72, co-authored 180 publications receiving 18981 citations. Previous affiliations of Michael B. Mathews include University of Medicine and Dentistry of New Jersey & State University of New York System.
Papers
More filters
Book
Translational control of gene expression
TL;DR: Origins and Principles of Translational Control, Genetic Approaches to Translation Initiation in Saccharomyces cerevisiae, and Programmed translational Frameshifting, Hopping, an
Journal ArticleDOI
Functional identity of proliferating cell nuclear antigen and a DNA polymerase-δ auxiliary protein
Gregory Prelich,Cheng-Keat Tan,Matthew Kostura,Michael B. Mathews,Antero G. So,Kathleen M. Downey,Bruce Stillman +6 more
TL;DR: It is shown that PCNA and the polyrnerase-δ auxiliary protein have similar electrophoretic behaviour and are both recognized by anti-PCNA human autoantibodies, and both proteins are functionally equivalent; they stimulate SV40 DNA replication in vitro and increase the processivity of calf thymus DNA polymerase- δ.
Journal ArticleDOI
Transcription elongation factor P-TEFb is required for HIV-1 Tat transactivation in vitro
Yuerong Zhu,T Pe'ery,Junmin Peng,Yegnanarayana Ramanathan,Nick F. Marshall,Tricia K. Marshall,Brad A. Amendt,Michael B. Mathews,David H. Price +8 more
TL;DR: The cloning of the small subunit of Drosophila P-TEFb and the finding that it encodes a Cdc2-related protein kinase is reported, indicating that P- TEFb is a Tat-associated kinase (TAK) and PITALRE associated with the activation domain of HIV-1 Tat.
Journal ArticleDOI
Identity of the proliferating cell nuclear antigen and cyclin.
TL;DR: It is established here that PCNA and cyclin are identical, and it is shown thatPCNA is an acidic nuclear protein of apparent molecular weight 35,000, which is similar to ‘cyclin’.
Journal ArticleDOI
Interactions between double-stranded RNA regulators and the protein kinase DAI.
TL;DR: Analysis of complexes between dsRNA and DAI suggests that at maximal packing the enzyme interacts with as little as a single helical turn of ds RNA (11 bp) but under conditions that allow activation the binding site protects about 80 bp of duplex.